NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|392871558|ref|NP_001255215|]
View 

receptor-type tyrosine-protein phosphatase C isoform 3 precursor [Mus musculus]

Protein Classification

R-PTPc-C-1 and R-PTP-C-2 domain-containing protein( domain architecture ID 13781589)

protein containing domains PTP_N, CD45, R-PTPc-C-1, and R-PTP-C-2

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 533-733 1.55e-148

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 1.


:

Pssm-ID: 350405 [Multi-domain]  Cd Length: 201  Bit Score: 442.34  E-value: 1.55e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  533 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFKDIVVTINDH 612
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  613 KRCPDYIIQKLNVAHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 692
Cdd:cd14557    81 KICPDYIIRKLNINNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIGI 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 392871558  693 DAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 733
Cdd:cd14557   161 DAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 843-1048 3.23e-116

PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 2.


:

Pssm-ID: 350406 [Multi-domain]  Cd Length: 203  Bit Score: 357.86  E-value: 3.23e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  843 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYWGEGKQTYGDMEVEMKDTNRA 922
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIEVELKDTEKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  923 SAYTLRTFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVSMIQDLKQKLPKASpegMKYHKHASILVHCRDGSQQTG 1002
Cdd:cd14558    81 PTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKN---SKHGRSVPIVVHCSDGSSRTG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 392871558 1003 LFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYD 1048
Cdd:cd14558   158 IFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
CD45 pfam12567
Leukocyte receptor CD45; This family of proteins is found in eukaryotes. Proteins in this ...
 49-102 1.30e-16

Leukocyte receptor CD45; This family of proteins is found in eukaryotes. Proteins in this family are typically between 77 and 1130 amino acids in length. The family is found in association with pfam00041. CD45 plays a critical role in T-cell receptor (TCR)-mediated signaling. CD45 interacts with SKAP55 which is a transcriptional activator of IL-2.


:

Pssm-ID: 432641  Cd Length: 59  Bit Score: 74.71  E-value: 1.30e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 392871558    49 VNYTYESSNQTFKADLKDVQNAKCGNEDCE-NVLNNLEECSQIkNISVSNDSCAP 102
Cdd:pfam12567    1 VEYTYNSENKSFTAKLNVNDNVECENNDCEnNELHNLQECEQI-NVSISHNSCTS 54
PTP_N pfam12453
Protein tyrosine phosphatase N terminal; This domain family is found in eukaryotes, and is ...
 7-31 4.41e-08

Protein tyrosine phosphatase N terminal; This domain family is found in eukaryotes, and is approximately 30 amino acids in length. The family is found in association with pfam00041. There is a single completely conserved residue L that may be functionally important. This family consists of various protein tyrosine phosphatase haematopoietic receptors, e.g. CD45, which dephosphorylate growth stimulating proteins. This limits growth signalling in haematopoietic cells.


:

Pssm-ID: 403599  Cd Length: 26  Bit Score: 49.85  E-value: 4.41e-08
                           10        20
                   ....*....|....*....|....*
gi 392871558     7 LKLLAFGFALLDTEVFVTGQTPTPS 31
Cdd:pfam12453    1 LKLLAFGFAFLDTEVFVTGESLTSS 25
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 311-390 1.97e-06

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 47.11  E-value: 1.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  311 PDKVNGMKTSRPTDNSINVTCGPPYETNGPKTFYILVVRSGGS----FVTKYNKTNCQFYVDNLYYSTDYEFLVSFHNGV 386
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSgdwkEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80


                  ....
gi 392871558  387 YEGD 390
Cdd:cd00063    81 GESP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 230-288 7.38e-05

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 42.48  E-value: 7.38e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392871558  230 LVSWPEPvskPESASKPHGYVLCYK----NNSEKCKSLPNNVTSFEVESLKPYKYYEVSLLAY 288
Cdd:cd00063    18 TLSWTPP---EDDGGPITGYVVEYRekgsGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAV 77
 
Name Accession Description Interval E-value
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 533-733 1.55e-148

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 1.


Pssm-ID: 350405 [Multi-domain]  Cd Length: 201  Bit Score: 442.34  E-value: 1.55e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  533 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFKDIVVTINDH 612
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  613 KRCPDYIIQKLNVAHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 692
Cdd:cd14557    81 KICPDYIIRKLNINNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIGI 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 392871558  693 DAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 733
Cdd:cd14557   161 DAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 843-1048 3.23e-116

PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 2.


Pssm-ID: 350406 [Multi-domain]  Cd Length: 203  Bit Score: 357.86  E-value: 3.23e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  843 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYWGEGKQTYGDMEVEMKDTNRA 922
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIEVELKDTEKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  923 SAYTLRTFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVSMIQDLKQKLPKASpegMKYHKHASILVHCRDGSQQTG 1002
Cdd:cd14558    81 PTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKN---SKHGRSVPIVVHCSDGSSRTG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 392871558 1003 LFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYD 1048
Cdd:cd14558   158 IFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
478-737 1.64e-112

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 350.04  E-value: 1.64e-112
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558    478 LFLAEFQSIPRVFS-KFPIKDARKPHNQNKNRYVDILPYDYNRVELSEINGDaGSTYINASYIDGFKEPRKYIAAQGPRD 556
Cdd:smart00194    1 GLEEEFEKLDRLKPdDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE-GSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558    557 ETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFKDIVVTINDHKRCPDYIIQKLNVAHKKEKATgRE 636
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSET-RT 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558    637 VTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLRR 716
Cdd:smart00194  159 VTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRS 238

                           250       260
                    ....*....|....*....|.
gi 392871558    717 QRCLMVQVEAQYILIHQALVE 737
Cdd:smart00194  239 QRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
503-737 7.72e-107

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 334.21  E-value: 7.72e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558   503 NQNKNRYVDILPYDYNRVELSEINGDagSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEE 582
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP--SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558   583 GNRNKCAEYWPSMEEGTRAFKDIVVTI-NDHKRCPDYIIQKLNVAHKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLR 661
Cdd:pfam00102   79 KGREKCAQYWPEEEGESLEYGDFTVTLkKEKEDEKDYTVRTLEVSNGGSEET-RTVKHFHYTGWPDHGVPESPNSLLDLL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392871558   662 RRVNAFSN-FFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 737
Cdd:pfam00102  158 RKVRKSSLdGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
770-1051 1.01e-88

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 286.48  E-value: 1.01e-88
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558    770 LEAEYQRLPSYRSW-RTQHIGNQEENKKKNRNSNVVPYDFNRVPLKHELEmskesepesdessdddsdseETSKYINASF 848
Cdd:smart00194    2 LEEEFEKLDRLKPDdESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPG--------------------EGSDYINASY 61

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558    849 VMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYW---GEGKQTYGDMEVEMKDTNRASAY 925
Cdd:smart00194   62 IDGPNGPKAYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWpdeEGEPLTYGDITVTLKSVEKVDDY 141

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558    926 TLRTFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVSMIQDLKQKLPkaspegmkyHKHASILVHCRDGSQQTGLFC 1005
Cdd:smart00194  142 TIRTLEVTNTGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQS---------TSTGPIVVHCSAGVGRTGTFI 212

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*.
gi 392871558   1006 ALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYDIIA 1051
Cdd:smart00194  213 AIDILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAIL 258
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
794-1051 5.65e-86

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 277.97  E-value: 5.65e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558   794 NKKKNRNSNVVPYDFNRVPLKHElemskesepesdessdddsdsEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFW 873
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGD---------------------PGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFW 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558   874 QMIFQRKVKVIVMLTELVNGDQEVCAQYW---GEGKQTYGDMEVEMKDTNR-ASAYTLRTFELRHSKRKEPRTVYQYQCT 949
Cdd:pfam00102   60 RMVWEEKVTIIVMLTELEEKGREKCAQYWpeeEGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYT 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558   950 TWKGEELPAEPKDLVSMIQDLKQKLPKaspegmkyHKHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSL 1029
Cdd:pfam00102  140 GWPDHGVPESPNSLLDLLRKVRKSSLD--------GRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKEL 211

                          250       260
                   ....*....|....*....|..
gi 392871558  1030 RKARPGVVCSYEQYQFLYDIIA 1051
Cdd:pfam00102  212 RSQRPGMVQTLEQYIFLYDAIL 233
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 461-735 7.25e-50

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 179.84  E-value: 7.25e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  461 SDILLETYKRKIADEGRLFLAEFQSIPrvfSKFPIKDARKPHNQNKNRYVDILPYDYNRVELSE---------------- 524
Cdd:PHA02746   12 FDFFDKTNHAKFCEFVLLEHAEVMDIP---IRGTTNHFLKKENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkk 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  525 ---INGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRnKCAEYWPSMEEGTRA 601
Cdd:PHA02746   89 ievTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDDDE-KCFELWTKEEDSELA 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  602 FKDIVVTINDHKRCPDYIIQKLNVAHKKEKaTGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA----------FSNFF 671
Cdd:PHA02746  168 FGRFVAKILDIIEELSFTKTRLMITDKISD-TSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEeqaelikqadNDPQT 246

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392871558  672 SGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQAL 735
Cdd:PHA02746  247 LGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
496-731 6.84e-40

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 149.47  E-value: 6.84e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  496 KDARKPHNQN---KNRYVDILPYDYNRVElseINGdagsTYINASYIDGfKEPRKYIAAQGPRDETVDDFWRMIWEQKAT 572
Cdd:COG5599    32 NDPQYLQNINgspLNRFRDIQPYKETALR---ANL----GYLNANYIQV-IGNHRYIATQYPLEEQLEDFFQMLFDNNTP 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  573 VIVMVTRCEEG--NRNKCAEYWPsmEEGTRAFKDIVVTINDHKRCPDYI---IQKLNVAHKKEKatGREVTHIQFTSWPD 647
Cdd:COG5599   104 VLVVLASDDEIskPKVKMPVYFR--QDGEYGKYEVSSELTESIQLRDGIearTYVLTIKGTGQK--KIEIPVLHVKNWPD 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  648 HGVP--EDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEG--KVDVYGYVVKLRRQR-CLMV 722
Cdd:COG5599   180 HGAIsaEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMV 259


                  ....*....
gi 392871558  723 QVEAQYILI 731
Cdd:COG5599   260 QTSEQLDVL 268
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 793-1046 9.46e-31

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 123.96  E-value: 9.46e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  793 ENKKKNRNSNVVPYDFNRVPLKhelemskesepesdessdddSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDF 872
Cdd:PHA02747   50 ENQPKNRYWDIPCWDHNRVILD--------------------SGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  873 WQMIFQRKVKVIVML--TELVNGdQEVCAQYWGEGKQTYGDME---VEMKDTNRASAYTLRTFELRHSKRKEPRTVYQYQ 947
Cdd:PHA02747  110 WKAVWQEHCSIIVMLtpTKGTNG-EEKCYQYWCLNEDGNIDMEdfrIETLKTSVRAKYILTLIEITDKILKDSRKISHFQ 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  948 CTTWKGEELPAEPKDLV---SMIQDLKQKlpKASPEGMKYHKHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQ 1024
Cdd:PHA02747  189 CSEWFEDETPSDHPDFIkfiKIIDINRKK--SGKLFNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAK 266

                         250       260
                  ....*....|....*....|..
gi 392871558 1025 VVKSLRKARPGVVCSYEQYQFL 1046
Cdd:PHA02747  267 TAEKIREQRHAGIMNFDDYLFI 288
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
785-1053 6.33e-23

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 100.17  E-value: 6.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  785 TQHIGNQEeNKKKNRNSNVVPYDFNRVplkhelemskesepesdessdddsdsEETSKYINASFVMSYwKPEMMIAAQGP 864
Cdd:COG5599    34 PQYLQNIN-GSPLNRFRDIQPYKETAL--------------------------RANLGYLNANYIQVI-GNHRYIATQYP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  865 LKETIGDFWQMIFQRKVKVIVMLTELVNGD--QEVCAQYWGEgKQTYGDMEVEMKDT---NRASAYTLRTFEL-RHSKRK 938
Cdd:COG5599    86 LEEQLEDFFQMLFDNNTPVLVVLASDDEISkpKVKMPVYFRQ-DGEYGKYEVSSELTesiQLRDGIEARTYVLtIKGTGQ 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  939 EPRTVYQYQCTTWK-GEELPAEP-KDLVSMIqDLKQKLpKASPEGmkyhkhaSILVHCRDGSQQTGLFCALFNLLES--A 1014
Cdd:COG5599   165 KKIEIPVLHVKNWPdHGAISAEAlKNLADLI-DKKEKI-KDPDKL-------LPVVHCRAGVGRTGTLIACLALSKSinA 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 392871558 1015 ETEDVVDVFQVVKSLRKAR-PGVVCSYEQYQFLYDIIASI 1053
Cdd:COG5599   236 LVQITLSVEEIVIDMRTSRnGGMVQTSEQLDVLVKLAEQQ 275
CD45 pfam12567
Leukocyte receptor CD45; This family of proteins is found in eukaryotes. Proteins in this ...
 49-102 1.30e-16

Leukocyte receptor CD45; This family of proteins is found in eukaryotes. Proteins in this family are typically between 77 and 1130 amino acids in length. The family is found in association with pfam00041. CD45 plays a critical role in T-cell receptor (TCR)-mediated signaling. CD45 interacts with SKAP55 which is a transcriptional activator of IL-2.


Pssm-ID: 432641  Cd Length: 59  Bit Score: 74.71  E-value: 1.30e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 392871558    49 VNYTYESSNQTFKADLKDVQNAKCGNEDCE-NVLNNLEECSQIkNISVSNDSCAP 102
Cdd:pfam12567    1 VEYTYNSENKSFTAKLNVNDNVECENNDCEnNELHNLQECEQI-NVSISHNSCTS 54
PTP_N pfam12453
Protein tyrosine phosphatase N terminal; This domain family is found in eukaryotes, and is ...
 7-31 4.41e-08

Protein tyrosine phosphatase N terminal; This domain family is found in eukaryotes, and is approximately 30 amino acids in length. The family is found in association with pfam00041. There is a single completely conserved residue L that may be functionally important. This family consists of various protein tyrosine phosphatase haematopoietic receptors, e.g. CD45, which dephosphorylate growth stimulating proteins. This limits growth signalling in haematopoietic cells.


Pssm-ID: 403599  Cd Length: 26  Bit Score: 49.85  E-value: 4.41e-08
                           10        20
                   ....*....|....*....|....*
gi 392871558     7 LKLLAFGFALLDTEVFVTGQTPTPS 31
Cdd:pfam12453    1 LKLLAFGFAFLDTEVFVTGESLTSS 25
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 311-390 1.97e-06

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 47.11  E-value: 1.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  311 PDKVNGMKTSRPTDNSINVTCGPPYETNGPKTFYILVVRSGGS----FVTKYNKTNCQFYVDNLYYSTDYEFLVSFHNGV 386
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSgdwkEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80


                  ....
gi 392871558  387 YEGD 390
Cdd:cd00063    81 GESP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 230-288 7.38e-05

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 42.48  E-value: 7.38e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392871558  230 LVSWPEPvskPESASKPHGYVLCYK----NNSEKCKSLPNNVTSFEVESLKPYKYYEVSLLAY 288
Cdd:cd00063    18 TLSWTPP---EDDGGPITGYVVEYRekgsGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAV 77
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 311-381 9.09e-03

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 36.44  E-value: 9.09e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392871558    311 PDKVNGMKTSRPTDNSINVTCGPPYETN--GPKTFYILVVRSGGSFVTKYNKTN--CQFYVDNLYYSTDYEFLVS 381
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGitGYIVGYRVEYREEGSEWKEVNVTPssTSYTLTGLKPGTEYEFRVR 75
 
Name Accession Description Interval E-value
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 533-733 1.55e-148

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 1.


Pssm-ID: 350405 [Multi-domain]  Cd Length: 201  Bit Score: 442.34  E-value: 1.55e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  533 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFKDIVVTINDH 612
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  613 KRCPDYIIQKLNVAHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 692
Cdd:cd14557    81 KICPDYIIRKLNINNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIGI 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 392871558  693 DAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 733
Cdd:cd14557   161 DAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 843-1048 3.23e-116

PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 2.


Pssm-ID: 350406 [Multi-domain]  Cd Length: 203  Bit Score: 357.86  E-value: 3.23e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  843 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYWGEGKQTYGDMEVEMKDTNRA 922
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIEVELKDTEKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  923 SAYTLRTFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVSMIQDLKQKLPKASpegMKYHKHASILVHCRDGSQQTG 1002
Cdd:cd14558    81 PTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKN---SKHGRSVPIVVHCSDGSSRTG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 392871558 1003 LFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYD 1048
Cdd:cd14558   158 IFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
478-737 1.64e-112

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 350.04  E-value: 1.64e-112
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558    478 LFLAEFQSIPRVFS-KFPIKDARKPHNQNKNRYVDILPYDYNRVELSEINGDaGSTYINASYIDGFKEPRKYIAAQGPRD 556
Cdd:smart00194    1 GLEEEFEKLDRLKPdDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE-GSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558    557 ETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFKDIVVTINDHKRCPDYIIQKLNVAHKKEKATgRE 636
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSET-RT 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558    637 VTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLRR 716
Cdd:smart00194  159 VTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRS 238

                           250       260
                    ....*....|....*....|.
gi 392871558    717 QRCLMVQVEAQYILIHQALVE 737
Cdd:smart00194  239 QRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
503-737 7.72e-107

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 334.21  E-value: 7.72e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558   503 NQNKNRYVDILPYDYNRVELSEINGDagSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEE 582
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP--SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558   583 GNRNKCAEYWPSMEEGTRAFKDIVVTI-NDHKRCPDYIIQKLNVAHKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLR 661
Cdd:pfam00102   79 KGREKCAQYWPEEEGESLEYGDFTVTLkKEKEDEKDYTVRTLEVSNGGSEET-RTVKHFHYTGWPDHGVPESPNSLLDLL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392871558   662 RRVNAFSN-FFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 737
Cdd:pfam00102  158 RKVRKSSLdGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 501-737 2.15e-98

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350401 [Multi-domain]  Cd Length: 238  Bit Score: 311.64  E-value: 2.15e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  501 PHNQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRC 580
Cdd:cd14553     1 EVNKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  581 EEGNRNKCAEYWPSmeEGTRAFKDIVVTINDHKRCPDYIIQKLNVaHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKL 660
Cdd:cd14553    81 EERSRVKCDQYWPT--RGTETYGLIQVTLLDTVELATYTVRTFAL-HKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAF 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392871558  661 RRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 737
Cdd:cd14553   158 LRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 533-733 4.44e-95

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr (pTyr) residues, instead of pSer or pThr. This family has a distinctive active site signature motif, HCSAGxGRxG, and are characterized as either transmembrane, receptor-like or non-transmembrane (soluble) PTPs. Receptor-like PTP domains tend to occur in two copies in the cytoplasmic region of the transmembrane proteins, only one copy may be active.


Pssm-ID: 350343 [Multi-domain]  Cd Length: 200  Bit Score: 301.13  E-value: 4.44e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  533 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFKDIVVTINDH 612
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  613 KRCPDYIIQKLNVAHKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 692
Cdd:cd00047    81 EELSDYTIRTLELSPKGCSES-REVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAI 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 392871558  693 DAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 733
Cdd:cd00047   160 DILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 508-733 1.67e-93

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar proteins; R3 subfamily receptor-type phosphotyrosine phosphatases (RPTP) are characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. Vertebrate members include receptor-type tyrosine-protein phosphatase-like O (PTPRO), J (PTPRJ), Q (PTPRQ), B (PTPRB), V (PTPRV) and H (PTPRH). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Most members are PTPs, except for PTPRQ, which dephosphorylates phosphatidylinositide substrates. PTPRV is characterized only in rodents; its function has been lost in humans. Both vertebrate and invertebrate R3 subfamily RPTPs are involved in the control of a variety of cellular processes, including cell growth, differentiation, mitotic cycle and oncogenic transformation.


Pssm-ID: 350396 [Multi-domain]  Cd Length: 222  Bit Score: 297.73  E-value: 1.67e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  508 RYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNK 587
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  588 CAEYWPSMEEGTrAFKDIVVTINDHKRCPDYIIQKLNVAHKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAF 667
Cdd:cd14548    81 CDHYWPFDQDPV-YYGDITVTMLSESVLPDWTIREFKLERGDEV---RSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDY 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392871558  668 SNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 733
Cdd:cd14548   157 IKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
770-1051 1.01e-88

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 286.48  E-value: 1.01e-88
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558    770 LEAEYQRLPSYRSW-RTQHIGNQEENKKKNRNSNVVPYDFNRVPLKHELEmskesepesdessdddsdseETSKYINASF 848
Cdd:smart00194    2 LEEEFEKLDRLKPDdESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPG--------------------EGSDYINASY 61

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558    849 VMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYW---GEGKQTYGDMEVEMKDTNRASAY 925
Cdd:smart00194   62 IDGPNGPKAYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWpdeEGEPLTYGDITVTLKSVEKVDDY 141

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558    926 TLRTFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVSMIQDLKQKLPkaspegmkyHKHASILVHCRDGSQQTGLFC 1005
Cdd:smart00194  142 TIRTLEVTNTGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQS---------TSTGPIVVHCSAGVGRTGTFI 212

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*.
gi 392871558   1006 ALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYDIIA 1051
Cdd:smart00194  213 AIDILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAIL 258
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 458-746 1.01e-88

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350469 [Multi-domain]  Cd Length: 296  Bit Score: 287.69  E-value: 1.01e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  458 PIHSDILLETYKRKIADEGRLFLAEFQSIPRVFSKFPIKDARKPHNQNKNRYVDILPYDYNRVELSEINGDAGSTYINAS 537
Cdd:cd14621     7 PLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINAS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  538 YIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmEEGTRAFKDIVVTINDHKRCPD 617
Cdd:cd14621    87 FINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWP--DQGCWTYGNIRVSVEDVTVLVD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  618 YIIQKL---NVAHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDA 694
Cdd:cd14621   165 YTVRKFciqQVGDVTNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDA 244

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392871558  695 MLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVEYNQFGETEV 746
Cdd:cd14621   245 MLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
794-1051 5.65e-86

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 277.97  E-value: 5.65e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558   794 NKKKNRNSNVVPYDFNRVPLKHElemskesepesdessdddsdsEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFW 873
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGD---------------------PGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFW 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558   874 QMIFQRKVKVIVMLTELVNGDQEVCAQYW---GEGKQTYGDMEVEMKDTNR-ASAYTLRTFELRHSKRKEPRTVYQYQCT 949
Cdd:pfam00102   60 RMVWEEKVTIIVMLTELEEKGREKCAQYWpeeEGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYT 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558   950 TWKGEELPAEPKDLVSMIQDLKQKLPKaspegmkyHKHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSL 1029
Cdd:pfam00102  140 GWPDHGVPESPNSLLDLLRKVRKSSLD--------GRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKEL 211

                          250       260
                   ....*....|....*....|..
gi 392871558  1030 RKARPGVVCSYEQYQFLYDIIA 1051
Cdd:pfam00102  212 RSQRPGMVQTLEQYIFLYDAIL 233
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 533-732 8.58e-85

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 273.46  E-value: 8.58e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  533 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSmeEGTRAFKDIVVTINDH 612
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPK--EGTETYGNIQVTLLST 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  613 KRCPDYIIQKLNVAHKKEK-----ATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTG 687
Cdd:cd14549    79 EVLATYTVRTFSLKNLKLKkvkgrSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 392871558  688 TYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIH 732
Cdd:cd14549   159 TYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 464-737 3.36e-82

catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350474 [Multi-domain]  Cd Length: 276  Bit Score: 269.21  E-value: 3.36e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  464 LLETYKRKIADEGRLFLAEFQSI-PRvfSKFPIKDARKPHNQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGF 542
Cdd:cd14626     3 LADNIERLKANDGLKFSQEYESIdPG--QQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  543 KEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSmeEGTRAFKDIVVTINDHKRCPDYIIQK 622
Cdd:cd14626    81 RKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPI--RGTETYGMIQVTLLDTVELATYSVRT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  623 LNVaHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAE 702
Cdd:cd14626   159 FAL-YKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHE 237

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 392871558  703 GKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 737
Cdd:cd14626   238 KTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 509-737 1.79e-81

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the first PTP domain (repeat 1).


Pssm-ID: 350468 [Multi-domain]  Cd Length: 229  Bit Score: 265.27  E-value: 1.79e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  509 YVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKC 588
Cdd:cd14620     1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  589 AEYWPsmEEGTRAFKDIVVTINDHKRCPDYIIQKLNVA---HKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVN 665
Cdd:cd14620    81 YQYWP--DQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQpqlPDGCKAP-RLVTQLHFTSWPDFGVPFTPIGMLKFLKKVK 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392871558  666 AFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 737
Cdd:cd14620   158 SVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 498-732 8.19e-81

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein phosphatase non-receptor type 9 (PTPN9), also called protein-tyrosine phosphatase MEG2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN9 plays an important role in promoting intracellular secretary vesicle fusion in hematopoietic cells and promotes the dephosphorylation of ErbB2 and EGFR in breast cancer cells, leading to impaired activation of STAT5 and STAT3. It also directly dephosphorylates STAT3 at the Tyr705 residue, resulting in its inactivation. PTPN9 has been found to be dysregulated in various human cancers, including breast, colorectal, and gastric cancer.


Pssm-ID: 350391 [Multi-domain]  Cd Length: 271  Bit Score: 265.00  E-value: 8.19e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  498 ARKPHNQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMV 577
Cdd:cd14543    24 SLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMT 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  578 TRCEEGNRNKCAEYWPSMEEGTRAFKDIVVT---INDHKrcpDYIIQKLNVaHKKEKATGREVTHIQFTSWPDHGVPEDP 654
Cdd:cd14543   104 TRVVERGRVKCGQYWPLEEGSSLRYGDLTVTnlsVENKE---HYKKTTLEI-HNTETDESRQVTHFQFTSWPDFGVPSSA 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  655 HLLL--------KLRRRVNAFSNFFSG-----PIVVHCSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLM 721
Cdd:cd14543   180 AALLdflgevrqQQALAVKAMGDRWKGhppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQRAFS 259

                         250
                  ....*....|.
gi 392871558  722 VQVEAQYILIH 732
Cdd:cd14543   260 IQTPDQYYFCY 270
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 507-738 5.12e-79

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type tyrosine-protein phosphatase H (PTPRH or R-PTP-H), also known as stomach cancer-associated protein tyrosine phosphatase 1 (SAP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRH is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is localized specifically at microvilli of the brush border in gastrointestinal epithelial cells. It plays a role in intestinal immunity by regulating CEACAM20 through tyrosine dephosphorylation. It is also a negative regulator of integrin-mediated signaling and may contribute to contact inhibition of cell growth and motility.


Pssm-ID: 350467 [Multi-domain]  Cd Length: 233  Bit Score: 258.67  E-value: 5.12e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  507 NRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRN 586
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  587 KCAEYWPsMEEGTRAFKDIVVTINDHKRCPDYIIQKLNVAHKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA 666
Cdd:cd14619    81 KCEHYWP-LDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKT-LSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQ 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392871558  667 F--SNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVEY 738
Cdd:cd14619   159 WldQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDF 232
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 533-733 1.11e-75

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350399 [Multi-domain]  Cd Length: 202  Bit Score: 248.29  E-value: 1.11e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  533 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmEEGTRAFKDIVVTINDH 612
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWP--DQGCWTYGNLRVRVEDT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  613 KRCPDYIIQKLNVaHKKEKATG----REVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGT 688
Cdd:cd14551    79 VVLVDYTTRKFCI-QKVNRGIGekrvRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 392871558  689 YIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 733
Cdd:cd14551   158 FIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 843-1048 5.58e-75

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr (pTyr) residues, instead of pSer or pThr. This family has a distinctive active site signature motif, HCSAGxGRxG, and are characterized as either transmembrane, receptor-like or non-transmembrane (soluble) PTPs. Receptor-like PTP domains tend to occur in two copies in the cytoplasmic region of the transmembrane proteins, only one copy may be active.


Pssm-ID: 350343 [Multi-domain]  Cd Length: 200  Bit Score: 246.04  E-value: 5.58e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  843 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYW---GEGKQTYGDMEVEMKDT 919
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWpeeGGKPLEYGDITVTLVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  920 NRASAYTLRTFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVSMIQDLKQKLPKASPegmkyhkhaSILVHCRDGSQ 999
Cdd:cd00047    81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNG---------PIVVHCSAGVG 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 392871558 1000 QTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYD 1048
Cdd:cd00047   152 RTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 507-733 1.31e-74

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type tyrosine-protein phosphatase J (PTPRJ or R-PTP-J), also known as receptor-type tyrosine-protein phosphatase eta (R-PTP-eta) or density-enhanced phosphatase 1 (DEP-1) OR CD148, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRJ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (eight in PTPRJ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed in various cell types including epithelial, hematopoietic, and endothelial cells. It plays a role in cell adhesion, migration, proliferation and differentiation. It dephosphorylates or contributes to the dephosphorylation of various substrates including protein kinases such as FLT3, PDGFRB, MET, RET (variant MEN2A), VEGFR-2, LYN, SRC, MAPK1, MAPK3, and EGFR, as well as PIK3R1 and PIK3R2.


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 246.27  E-value: 1.31e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  507 NRYVDILPYDYNRVELSeINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRN 586
Cdd:cd14615     1 NRYNNVLPYDISRVKLS-VQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  587 KCAEYWPSmeEGTRAFKDIVVTINDHKRCPDYIIQKLNVAHKKEkATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA 666
Cdd:cd14615    80 KCEEYWPS--KQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQT-NESRTVRHFHFTSWPDHGVPETTDLLINFRHLVRE 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392871558  667 FS--NFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 733
Cdd:cd14615   157 YMkqNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 225
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 458-737 3.12e-74

catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350473 [Multi-domain]  Cd Length: 282  Bit Score: 247.31  E-value: 3.12e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  458 PIHSDILLETYKRKIADEGRLFLAEFQSIPRvFSKFPIKDARKPHNQNKNRYVDILPYDYNRVELSEINGDAGSTYINAS 537
Cdd:cd14625     3 PIPISELAEHTERLKANDNLKLSQEYESIDP-GQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINAN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  538 YIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSmeEGTRAFKDIVVTINDHKRCPD 617
Cdd:cd14625    82 YIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPS--RGTETYGMIQVTLLDTIELAT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  618 YIIQKLNVaHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLE 697
Cdd:cd14625   160 FCVRTFSL-HKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLE 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 392871558  698 GLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 737
Cdd:cd14625   239 RIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 507-733 1.31e-73

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; The kinase interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes tyrosine-protein phosphatases non-receptor type 7 (PTPN7) and non-receptor type 5 (PTPN5), and protein-tyrosine phosphatase receptor type R (PTPRR). PTPN7 is also called hematopoietic protein-tyrosine phosphatase (HePTP) while PTPN5 is also called striatal-enriched protein-tyrosine phosphatase (STEP). They belong to the family of classical tyrosine-specific PTPs (EC 3.1.3.48) that catalyze the dephosphorylation of phosphotyrosine peptides. KIM-PTPs are characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. They are highly specific to the MAPKs ERK1/2 (extracellular-signal-regulated kinase 1/2) and p38, over JNK (c-Jun N-terminal kinase); they dephosphorylate these kinases and thereby critically modulate cell proliferation and differentiation.


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 243.46  E-value: 1.31e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  507 NRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFK-EPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNR 585
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  586 nKCAEYWPsMEEGTRaFKDIVVTINDHKRCPDYIIQKLNVAHKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVN 665
Cdd:cd14547    81 -KCAQYWP-EEENET-YGDFEVTVQSVKETDGYTVRKLTLKYGGEK---RYLKHYWYTSWPDHKTPEAAQPLLSLVQEVE 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  666 --AFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 733
Cdd:cd14547   155 eaRQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 458-737 4.90e-73

catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type tyrosine-protein phosphatase D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 244.26  E-value: 4.90e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  458 PIHSDILLETYKRKIADEGRLFLAEFQSIPRvFSKFPIKDARKPHNQNKNRYVDILPYDYNRVELSEINGDAGSTYINAS 537
Cdd:cd14624     3 PIPILELADHIERLKANDNLKFSQEYESIDP-GQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINAN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  538 YIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSmeEGTRAFKDIVVTINDHKRCPD 617
Cdd:cd14624    82 YIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPS--RGTETYGLIQVTLLDTVELAT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  618 YIIQKLNVaHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLE 697
Cdd:cd14624   160 YCVRTFAL-YKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLE 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 392871558  698 GLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 737
Cdd:cd14624   239 RIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 507-733 3.49e-72

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type tyrosine-protein phosphatase B (PTPRB), also known as receptor-type tyrosine-protein phosphatase beta (R-PTP-beta) or vascular endothelial protein tyrosine phosphatase(VE-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRB/VE-PTP is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed specifically in vascular endothelial cells and it plays an important role in blood vessel remodeling and angiogenesis.


Pssm-ID: 350465 [Multi-domain]  Cd Length: 228  Bit Score: 239.44  E-value: 3.49e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  507 NRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRN 586
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  587 KCAEYWPsMEEGTRAFKDIVVTINDHKRCPDYIIQKLNVAHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA 666
Cdd:cd14617    81 KCDHYWP-ADQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRD 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392871558  667 FSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 733
Cdd:cd14617   160 YINRTpgSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 498-733 8.45e-72

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type tyrosine-protein phosphatase O (PTPRO or R-PTP-O), also known as glomerular epithelial protein 1 or protein tyrosine phosphatase U2 (PTP-U2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRO is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is essential for sustaining the structure and function of foot processes by regulating tyrosine phosphorylation of podocyte proteins. It has been identified as a synaptic cell adhesion molecule (CAM) that serves as a potent initiator of synapse formation. It is also a tumor suppressor in several types of cancer, such as hepatocellular carcinoma, lung cancer, and breast cancer.


Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 239.02  E-value: 8.45e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  498 ARKPHNQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMV 577
Cdd:cd14614     7 ADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVML 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  578 TRCEEGNRNKCAEYWPSMEEGTrAFKDIVVTINDHKRCPDYIIQKLNVAHKKEKatgREVTHIQFTSWPDHGVP--EDPH 655
Cdd:cd14614    87 TQCNEKRRVKCDHYWPFTEEPV-AYGDITVEMLSEEEQPDWAIREFRVSYADEV---QDVMHFNYTAWPDHGVPtaNAAE 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392871558  656 LLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 733
Cdd:cd14614   163 SILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 479-737 7.10e-71

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG has four splicing isoforms: three transmembrane isoforms, PTPRG-A, B, and C, and one secretory isoform, PTPRG-S, which are expressed in many tissues including the brain. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 237.63  E-value: 7.10e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  479 FLAEFQSIPRVFSKFPI--KDARKPHNQNKNRYVDILPYDYNRVELSEINGDAG--STYINASYIDGFKEPRKYIAAQGP 554
Cdd:cd17667     1 FSEDFEEVQRCTADMNItaEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIATQGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  555 RDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSmeEGTRAFKDIVVTINDHKRCPDYIIQKLNVAHKKEK--- 631
Cdd:cd17667    81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPT--ENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKkgq 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  632 ---ATGRE----VTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGK 704
Cdd:cd17667   159 kgnPKGRQnertVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKST 238

                         250       260       270
                  ....*....|....*....|....*....|...
gi 392871558  705 VDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 737
Cdd:cd17667   239 VNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 271
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 503-737 7.96e-71

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350478 [Multi-domain]  Cd Length: 237  Bit Score: 236.08  E-value: 7.96e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  503 NQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEE 582
Cdd:cd14630     3 NRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  583 GNRNKCAEYWPsmeEGTRAFKDIVVTINDHKRCPDYIIQKLNVaHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRR 662
Cdd:cd14630    83 VGRVKCVRYWP---DDTEVYGDIKVTLIETEPLAEYVIRTFTV-QKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392871558  663 RVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 737
Cdd:cd14630   159 QVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 462-737 8.77e-69

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 231.86  E-value: 8.77e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  462 DILLETYKRKIAdEGRLFLAEFQSIPRVFSKfPIKDARKPHNQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDG 541
Cdd:cd14633     1 DLLQHITQMKCA-EGYGFKEEYESFFEGQSA-PWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  542 FKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmeEGTRAFKDIVVTINDHKRCPDYIIQ 621
Cdd:cd14633    79 YHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWP---DDTEIYKDIKVTLIETELLAEYVIR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  622 KLNVaHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEA 701
Cdd:cd14633   156 TFAV-EKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAER 234

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 392871558  702 EGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 737
Cdd:cd14633   235 EGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 498-734 1.18e-68

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2).


Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 230.10  E-value: 1.18e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  498 ARKPHNQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMV 577
Cdd:cd14554     1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  578 TRCEEGNRNKCAEYWPSmEEGTRAFKDIVVTINDHKRcPDYIIQKLNVAHKKEKaTGREVTHIQFTSWPDHGVPEDPHLL 657
Cdd:cd14554    81 TKLREMGREKCHQYWPA-ERSARYQYFVVDPMAEYNM-PQYILREFKVTDARDG-QSRTVRQFQFTDWPEQGVPKSGEGF 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392871558  658 LKLRRRV-NAFSNF-FSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQA 734
Cdd:cd14554   158 IDFIGQVhKTKEQFgQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 503-738 5.04e-68

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) and type 6 (PTPN6) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 and PTPN6, are also called SH2 domain-containing tyrosine phosphatase 2 (SHP2) and 1 (SHP1), respectively. They contain two tandem SH2 domains: a catalytic PTP domain, and a C-terminal tail with regulatory properties. Although structurally similar, they have different localization and different roles in signal transduction. PTPN11/SHP2 is expressed ubiquitously and plays a positive role in cell signaling, leading to cell activation, while PTPN6/SHP1 expression is restricted mainly to hematopoietic and epithelial cells and functions as a negative regulator of signaling events.


Pssm-ID: 350392 [Multi-domain]  Cd Length: 251  Bit Score: 228.89  E-value: 5.04e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  503 NQNKNRYVDILPYDYNRVELSEINGD-AGSTYINASYI-------DGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVI 574
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRDPNvPGSDYINANYIrnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  575 VMVTRCEEGNRNKCAEYWPSmEEGTRAFKDIVVTINDHKRCPDYIIQKLNVAHKKEKATGREVTHIQFTSWPDHGVPEDP 654
Cdd:cd14544    81 VMTTKEVERGKNKCVRYWPD-EGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPIREIWHYQYLSWPDHGVPSDP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  655 HLLLKLRRRVNAFSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEG---KVDVYGYVVKLRRQRCLMVQVEAQYI 729
Cdd:cd14544   160 GGVLNFLEDVNQRQESLphAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMVQTEAQYK 239


                  ....*....
gi 392871558  730 LIHQALVEY 738
Cdd:cd14544   240 FIYVAVAQY 248
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 533-733 5.67e-68

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae protein-tyrosine phosphatases 1 (PTP1) and 2 (PTP2), Schizosaccharomyces pombe PTP1, PTP2, and PTP3, and similar fungal proteins. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. PTP2, together with PTP3, is the major phosphatase that dephosphorylates and inactivates the MAP kinase HOG1 and also modulates its subcellular localization.


Pssm-ID: 350509 [Multi-domain]  Cd Length: 212  Bit Score: 227.13  E-value: 5.67e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  533 YINASYID-GFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSmEEGTRAFKDIVVTIND 611
Cdd:cd18533     1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPS-GEYEGEYGDLTVELVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  612 HKRCPD--YIIQKLNVAHKKEKAtgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA--FSNFFSGPIVVHCSAGVGRTG 687
Cdd:cd18533    80 EEENDDggFIVREFELSKEDGKV--KKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRElnDSASLDPPIIVHCSAGVGRTG 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392871558  688 TYIGIDAMLEGLEA--------EGKVD-VYGYVVKLRRQRCLMVQVEAQYILIHQ 733
Cdd:cd18533   158 TFIALDSLLDELKRglsdsqdlEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 507-736 1.93e-66

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type tyrosine-protein phosphatase V (PTPRV or R-PTP-V), also known as embryonic stem cell protein-tyrosine phosphatase (ES cell phosphatase) or osteotesticular protein-tyrosine phosphatase (OST-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRV is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. In rodents, it may play a role in the maintenance of pluripotency and may function in signaling pathways during bone remodeling. It is the only PTP whose function has been lost between rodent and human. The human OST-PTP gene is a pseudogene.


Pssm-ID: 350466 [Multi-domain]  Cd Length: 230  Bit Score: 223.67  E-value: 1.93e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  507 NRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRN 586
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  587 KCAEYWPSmEEGTRAFKDIVVTINDHKRCPDYIIQKLNVAHKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA 666
Cdd:cd14618    81 LCDHYWPS-ESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKE-RRVKHLHYTAWPDHGIPESTSSLMAFRELVRE 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392871558  667 F--SNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALV 736
Cdd:cd14618   159 HvqATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 533-737 2.03e-64

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The type II (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350403 [Multi-domain]  Cd Length: 204  Bit Score: 216.71  E-value: 2.03e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  533 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmeEGTRAFKDIVVTINDH 612
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP---DDTEVYGDIKVTLVET 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  613 KRCPDYIIQKLNVAHKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 692
Cdd:cd14555    78 EPLAEYVVRTFALERRGYHEI-REVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVI 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 392871558  693 DAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 737
Cdd:cd14555   157 DIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 533-736 3.04e-64

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350506 [Multi-domain]  Cd Length: 209  Bit Score: 216.38  E-value: 3.04e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  533 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSmeEGTRAFKDIVVTINDH 612
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPA--DGSEEYGNFLVTQKSV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  613 KRCPDYIIQ-------KLNVAHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGR 685
Cdd:cd17668    79 QVLAYYTVRnftlrntKIKKGSQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGR 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 392871558  686 TGTYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALV 736
Cdd:cd17668   159 TGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 507-733 1.31e-63

catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type tyrosine-protein phosphatase Q (PTPRQ or R-PTP-Q), also called phosphatidylinositol phosphatase PTPRQ, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRQ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (18 in PTPRQ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It displays low tyrosine-protein phosphatase activity; rather, it functions as a phosphatidylinositol phosphatase required for auditory processes. It regulates the levels of phosphatidylinositol 4,5-bisphosphate (PIP2) in the basal region of hair bundles. It can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates.


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 215.16  E-value: 1.31e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  507 NRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRN 586
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  587 KCAEYWPSMEEGTRAFKDIVVTINDHKRCPDYIIQKLNVAHKKEKATgreVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA 666
Cdd:cd14616    81 RCHQYWPEDNKPVTVFGDIVITKLMEDVQIDWTIRDLKIERHGDYMM---VRQCNFTSWPEHGVPESSAPLIHFVKLVRA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392871558  667 FSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 733
Cdd:cd14616   158 SRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 498-738 1.36e-61

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 212.29  E-value: 1.36e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  498 ARKPHNQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMV 577
Cdd:cd14627    48 ANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVML 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  578 TRCEEGNRNKCAEYWPSmeEGTRAFKDIVVTINDHKRCPDYIIQKLNVAHKKEkATGREVTHIQFTSWPDHGVPEDPHLL 657
Cdd:cd14627   128 TKLREMGREKCHQYWPA--ERSARYQYFVVDPMAEYNMPQYILREFKVTDARD-GQSRTVRQFQFTDWPEQGVPKSGEGF 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  658 LKLRRRVNAFSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQAL 735
Cdd:cd14627   205 IDFIGQVHKTKEQFgqDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAA 284


                  ...
gi 392871558  736 VEY 738
Cdd:cd14627   285 LEY 287
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 498-738 1.89e-61

PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type tyrosine-protein phosphatase-like D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 211.90  E-value: 1.89e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  498 ARKPHNQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMV 577
Cdd:cd14628    47 ANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  578 TRCEEGNRNKCAEYWPSmeEGTRAFKDIVVTINDHKRCPDYIIQKLNVAHKKEkATGREVTHIQFTSWPDHGVPEDPHLL 657
Cdd:cd14628   127 TKLREMGREKCHQYWPA--ERSARYQYFVVDPMAEYNMPQYILREFKVTDARD-GQSRTVRQFQFTDWPEQGVPKSGEGF 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  658 LKLRRRVNAFSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQAL 735
Cdd:cd14628   204 IDFIGQVHKTKEQFgqDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAA 283


                  ...
gi 392871558  736 VEY 738
Cdd:cd14628   284 LEY 286
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 498-738 2.17e-61

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350477 [Multi-domain]  Cd Length: 291  Bit Score: 211.51  E-value: 2.17e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  498 ARKPHNQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMV 577
Cdd:cd14629    48 ANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  578 TRCEEGNRNKCAEYWPSmeEGTRAFKDIVVTINDHKRCPDYIIQKLNVAHKKEkATGREVTHIQFTSWPDHGVPEDPHLL 657
Cdd:cd14629   128 TKLREMGREKCHQYWPA--ERSARYQYFVVDPMAEYNMPQYILREFKVTDARD-GQSRTIRQFQFTDWPEQGVPKTGEGF 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  658 LKLRRRVNAFSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQAL 735
Cdd:cd14629   205 IDFIGQVHKTKEQFgqDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAA 284


                  ...
gi 392871558  736 VEY 738
Cdd:cd14629   285 LEY 287
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 496-738 3.12e-61

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein phosphatase non-receptor type 6 (PTPN6), also called SH2 domain-containing protein-tyrosine phosphatase 1 (SHP1 or SHP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN6 expression is restricted mainly to hematopoietic and epithelial cells. It is an important regulator of hematopoietic cells, downregulating pathways that promote cell growth, survival, adhesion, and activation. It regulates glucose homeostasis by modulating insulin signalling in the liver and muscle, and it also negatively regulates bone resorption, affecting both the formation and the function of osteoclasts. PTPN6 contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350454 [Multi-domain]  Cd Length: 266  Bit Score: 210.12  E-value: 3.12e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  496 KDARKPHNQNKNRYVDILPYDYNRVELSeiNGDA---GSTYINASYID----GFKEPRK-YIAAQGPRDETVDDFWRMIW 567
Cdd:cd14606    11 LEGQRPENKSKNRYKNILPFDHSRVILQ--GRDSnipGSDYINANYVKnqllGPDENAKtYIASQGCLEATVNDFWQMAW 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  568 EQKATVIVMVTRCEEGNRNKCAEYWPSMeEGTRAFKDIVVTINDHKRCPDYIIQKLNVAHKKEKATGREVTHIQFTSWPD 647
Cdd:cd14606    89 QENSRVIVMTTREVEKGRNKCVPYWPEV-GMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGELIREIWHYQYLSWPD 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  648 HGVPEDPHLLLKLRRRVNAFSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEG---KVDVYGYVVKLRRQRCLMV 722
Cdd:cd14606   168 HGVPSEPGGVLSFLDQINQRQESLphAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGldcDIDIQKTIQMVRAQRSGMV 247

                         250
                  ....*....|....*.
gi 392871558  723 QVEAQYILIHQALVEY 738
Cdd:cd14606   248 QTEAQYKFIYVAIAQF 263
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 533-737 6.68e-61

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) and type 13 (PTPN13, also known as PTPL1) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization. Human PTPN13 is an important regulator of tumor aggressiveness.


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 206.84  E-value: 6.68e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  533 YINASYI--DGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWP-SMEEGTRAFKDIVVTI 609
Cdd:cd14538     1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdSLNKPLICGGRLEVSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  610 NDHKRCPDYIIQKLNVAHkKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNffSGPIVVHCSAGVGRTGTY 689
Cdd:cd14538    81 EKYQSLQDFVIRRISLRD-KETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHN--SGPIVVHCSAGIGRTGVL 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 392871558  690 IGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 737
Cdd:cd14538   158 ITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 519-737 1.21e-60

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350479 [Multi-domain]  Cd Length: 218  Bit Score: 206.80  E-value: 1.21e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  519 RVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmeEG 598
Cdd:cd14631     1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP---DD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  599 TRAFKDIVVTINDHKRCPDYIIQKLNVAHKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVH 678
Cdd:cd14631    78 TEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEI-REVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVH 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 392871558  679 CSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 737
Cdd:cd14631   157 CSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 501-738 1.57e-60

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein phosphatase non-receptor type 7 (PTPN7), also called hematopoietic protein-tyrosine phosphatase (HePTP) or LC-PTP. belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN7/HePTP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. PTPN7/HePTP is found exclusively in the white blood cells in bone marrow, thymus, spleen, lymph nodes and all myeloid and lymphoid cell lines. It negatively regulates T-cell activation and proliferation, and is often dysregulated in the preleukemic disorder myelodysplastic syndrome, as well as in acute myelogenous leukemia.


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 207.38  E-value: 1.57e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  501 PHNQNKNRYVDILPYDYNRVEL-SEINGDAGSTYINASYIDGFK-EPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVT 578
Cdd:cd14612    13 PGHASKDRYKTILPNPQSRVCLrRAGSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMIT 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  579 RCEEGNRnKCAEYWPSmEEGTraFKDIVVTINDHKRCPDYIIQKLNVAHKKEKatgREVTHIQFTSWPDHGVPEDPHLLL 658
Cdd:cd14612    93 KLKEKKE-KCVHYWPE-KEGT--YGRFEIRVQDMKECDGYTIRDLTIQLEEES---RSVKHYWFSSWPDHQTPESAGPLL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  659 KL-----RRRVNAFSnffSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 733
Cdd:cd14612   166 RLvaeveESRQTAAS---PGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLHH 242


                  ....*
gi 392871558  734 ALVEY 738
Cdd:cd14612   243 TLALY 247
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 533-737 1.41e-58

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350480 [Multi-domain]  Cd Length: 205  Bit Score: 200.28  E-value: 1.41e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  533 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmeEGTRAFKDIVVTINDH 612
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP---DDSDTYGDIKITLLKT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  613 KRCPDYIIQKLNVAHKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 692
Cdd:cd14632    78 ETLAEYSVRTFALERRGYSAR-HEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVL 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 392871558  693 DAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 737
Cdd:cd14632   157 DVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 503-736 1.06e-57

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein phosphatase non-receptor type 13 (PTPN13, also known as PTPL1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN13 is an important regulator of tumor aggressiveness. It regulates breast cancer cell aggressiveness through direct inactivation of Src kinase. In hepatocellular carcinoma, PTPN13 is a tumor suppressor. PTPN13 contains a FERM domain, five PDZ domains, and a C-terminal catalytic PTP domain. With its PDZ domains, PTPN13 has numerous interacting partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated substrates. Its FERM domain is necessary for localization to the membrane.


Pssm-ID: 350445 [Multi-domain]  Cd Length: 234  Bit Score: 198.90  E-value: 1.06e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  503 NQNKNRYVDILPYDYNRVELSEINGdagstYINASYID---GfKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTR 579
Cdd:cd14597     3 NRKKNRYKNILPYDTTRVPLGDEGG-----YINASFIKmpvG-DEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  580 CEEGNRNKCAEYWPSMEEGTRAFKD-IVVTINDHKRCPDYIIQKLNVaHKKEKATGREVTHIQFTSWPDHGVPEDPHLLL 658
Cdd:cd14597    77 EVEGGKIKCQRYWPEILGKTTMVDNrLQLTLVRMQQLKNFVIRVLEL-EDIQTREVRHITHLNFTAWPDHDTPSQPEQLL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  659 KL---RRRVNAfsnffSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQAL 735
Cdd:cd14597   156 TFisyMRHIHK-----SGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVI 230


                  .
gi 392871558  736 V 736
Cdd:cd14597   231 L 231
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 533-738 1.09e-57

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21) and type 14 (PTPN14) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Both PTPN21 and PTPN14 contain an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350388 [Multi-domain]  Cd Length: 219  Bit Score: 198.45  E-value: 1.09e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  533 YINASYID---GFKEpRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSM--EEGTRAFKDIVV 607
Cdd:cd14540     1 YINASHITatvGGKQ-RFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLggEHDALTFGEYKV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  608 TINDHKRCPDYIIQKLNVAHKKEKaTGREVTHIQFTSWPDHGVPEDPHLLL-------KLRRRVNAFS--NFFSGPIVVH 678
Cdd:cd14540    80 STKFSVSSGCYTTTGLRVKHTLSG-QSRTVWHLQYTDWPDHGCPEDVSGFLdfleeinSVRRHTNQDVagHNRNPPTLVH 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  679 CSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVEY 738
Cdd:cd14540   159 CSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQY 218
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 503-738 8.28e-57

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11), also called SH2 domain-containing tyrosine phosphatase 2 (SHP-2 or SHP2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 promotes the activation of the RAS/Mitogen-Activated Protein Kinases (MAPK) Extracellular-Regulated Kinases 1/2 (ERK1/2) pathway, a canonical signaling cascade that plays key roles in various cellular processes, including proliferation, survival, differentiation, migration, or metabolism. It also regulates the phosphoinositide 3-kinase (PI3K)/AKT pathway, a fundamental cascade that functions in cell survival, proliferation, migration, morphogenesis, and metabolism. PTPN11 dysregulation is associated with several developmental diseases and malignancies, such as Noonan syndrome and juvenile myelomonocytic leukemia. It contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 197.16  E-value: 8.28e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  503 NQNKNRYVDILPYDYNRVELSEinGDA---GSTYINASYI--------DGFKEPRKYIAAQGPRDETVDDFWRMIWEQKA 571
Cdd:cd14605     2 NKNKNRYKNILPFDHTRVVLHD--GDPnepVSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  572 TVIVMVTRCEEGNRNKCAEYWPSmeegTRAFKDI-VVTINDHKRCP--DYIIQKLNVAHKKEKATGREVTHIQFTSWPDH 648
Cdd:cd14605    80 RVIVMTTKEVERGKSKCVKYWPD----EYALKEYgVMRVRNVKESAahDYILRELKLSKVGQGNTERTVWQYHFRTWPDH 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  649 GVPEDPHLLLKLRRRVNAFSNFFS--GPIVVHCSAGVGRTGTYIGIDAMLEGLEAEG---KVDVYGYVVKLRRQRCLMVQ 723
Cdd:cd14605   156 GVPSDPGGVLDFLEEVHHKQESIMdaGPVVVHCSAGIGRTGTFIVIDILIDIIREKGvdcDIDVPKTIQMVRSQRSGMVQ 235

                         250
                  ....*....|....*
gi 392871558  724 VEAQYILIHQALVEY 738
Cdd:cd14605   236 TEAQYRFIYMAVQHY 250
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 501-737 1.29e-56

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein phosphatase non-receptor type 18 (PTPN18), also called brain-derived phosphatase, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. The N-terminal catalytic PTP domain of PTPN18 blocks lysosomal routing and delays the degradation of HER2 by dephosphorylation, and its C-terminal PEST domain promotes K48-linked HER2 ubiquitination and its destruction via the proteasome pathway.


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 196.97  E-value: 1.29e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  501 PHNQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRC 580
Cdd:cd14603    28 KENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACRE 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  581 EEGNRNKCAEYWPSMEEgTRAFKDIVVTINDHKRC-PDYIIQKLNVAHKKEKatgREVTHIQFTSWPDHGVPEDPHLLLK 659
Cdd:cd14603   108 IEMGKKKCERYWAQEQE-PLQTGPFTITLVKEKRLnEEVILRTLKVTFQKES---RSVSHFQYMAWPDHGIPDSPDCMLA 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  660 LRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAE---GKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALV 736
Cdd:cd14603   184 MIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQripPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVA 263


                  .
gi 392871558  737 E 737
Cdd:cd14603   264 Q 264
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 533-736 2.59e-56

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 193.64  E-value: 2.59e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  533 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmEEGTRAFKDIVVTINDH 612
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWP--EDGSVSSGDITVELKDQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  613 KRCPDYIIQKLNVAHKKEKATgREVTHIQFTSWPDHGVPEDP----HLLLKLRRRVNAFSNffsGPIVVHCSAGVGRTGT 688
Cdd:cd14552    79 TDYEDYTLRDFLVTKGKGGST-RTVRQFHFHGWPEVGIPDNGkgmiDLIAAVQKQQQQSGN---HPITVHCSAGAGRTGT 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 392871558  689 YIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALV 736
Cdd:cd14552   155 FCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVVQ 202
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 533-733 2.96e-56

catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), type 18 (PTPN18) and type 12 (PTPN12) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. TPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling.


Pssm-ID: 350390 [Multi-domain]  Cd Length: 202  Bit Score: 193.41  E-value: 2.96e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  533 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFKDIVVTINDH 612
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKISLEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  613 KR-CPDYIIQKLNVAHKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIG 691
Cdd:cd14542    81 KRvGPDFLIRTLKVTFQKES---RTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICA 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 392871558  692 IDAMLEGLEAEGKVD---VYGYVVKLRRQRCLMVQVEAQYILIHQ 733
Cdd:cd14542   158 IDYVWNLLKTGKIPEefsLFDLVREMRKQRPAMVQTKEQYELVYR 202
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 508-737 5.30e-56

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 193.72  E-value: 5.30e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  508 RYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNK 587
Cdd:cd14623     1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  588 CAEYWPSmeEGTRAFKDIVVTINDHKRCPDYIIQKLNVAHKKEKATgREVTHIQFTSWPDHGVPEDP----HLLLKLRRR 663
Cdd:cd14623    81 CAQYWPS--DGSVSYGDITIELKKEEECESYTVRDLLVTNTRENKS-RQIRQFHFHGWPEVGIPSDGkgmiNIIAAVQKQ 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392871558  664 VNAFSNFfsgPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 737
Cdd:cd14623   158 QQQSGNH---PITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 466-738 9.59e-56

catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein phosphatase non-receptor type 14 (PTPN14), also called protein-tyrosine phosphatase pez, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN14 is a potential tumor suppressor and plays a regulatory role in the Hippo and Wnt/beta-catenin signaling pathways. It contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350447 [Multi-domain]  Cd Length: 287  Bit Score: 195.22  E-value: 9.59e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  466 ETYKRKIaDEGRLFlAEFQSIPRVFSKFPIKDARKPHNQNKNRYVDILPYDYNRVELSEiNGDAGSTYINASYIDGF--K 543
Cdd:cd14599     3 KTLERKL-EEGMVF-TEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVP-TKENNTGYINASHIKVTvgG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  544 EPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSM--EEGTRAFKDIVVTINDHKRCPDYIIQ 621
Cdd:cd14599    80 EEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLgsKHSSATYGKFKVTTKFRTDSGCYATT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  622 KLNVAHKkekATGREVT--HIQFTSWPDHGVPEDPHLLLK-------LRRRVNAF---SNFFSGPIVVHCSAGVGRTGTY 689
Cdd:cd14599   160 GLKVKHL---LSGQERTvwHLQYTDWPDHGCPEEVQGFLSyleeiqsVRRHTNSMldsTKNCNPPIVVHCSAGVGRTGVV 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 392871558  690 IGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVEY 738
Cdd:cd14599   237 ILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQF 285
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 506-727 1.14e-54

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1) type 2 (PTPN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases, (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1 (or PTP-1B) is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor. PTPN2 (or TCPTP), a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner.


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 190.30  E-value: 1.14e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  506 KNRYVDILPYDYNRVELSEINGDagSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNR 585
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQGD--NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  586 NKCAEYWPSMEEGTRAFKD--IVVTINDHKRCPDYIIQKLNVAHKKEKATgREVTHIQFTSWPDHGVPEDP----HLLLK 659
Cdd:cd14545    79 IKCAQYWPQGEGNAMIFEDtgLKVTLLSEEDKSYYTVRTLELENLKTQET-REVLHFHYTTWPDFGVPESPaaflNFLQK 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  660 LRRRVNAFSNFfsGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEG--KVDVYGYVVKLRRQRCLMVQVEAQ 727
Cdd:cd14545   158 VRESGSLSSDV--GPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKYRMGLIQTPDQ 225
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 533-728 1.54e-54

PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 2.


Pssm-ID: 350406 [Multi-domain]  Cd Length: 203  Bit Score: 188.76  E-value: 1.54e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  533 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmeEGTRAFKDIVVTINDH 612
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWG---DEKKTYGDIEVELKDT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  613 KRCPDYIIQKLNVAHKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRV------NAFSNFFSGPIVVHCSAGVGRT 686
Cdd:cd14558    78 EKSPTYTVRVFEITHLKRKDS-RTVYQYQYHKWKGEELPEKPKDLVDMIKSIkqklpyKNSKHGRSVPIVVHCSDGSSRT 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 392871558  687 GTYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQY 728
Cdd:cd14558   157 GIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQY 198
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 479-737 2.92e-54

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein phosphatase non-receptor type 12 (PTPN12), also called PTP-PEST or protein-tyrosine phosphatase G1 (PTPG1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling. It regulates various physiological processes, including cell migration, immune response, and neuronal activity, by dephosphorylating multiple substrates including HER2, FAK, PYK2, PSTPIP, WASP, p130Cas, paxillin, Shc, catenin, c-Abl, ArgBP2, p190RhoGAP, RhoGDI, cell adhesion kinase beta, and Rho GTPase.


Pssm-ID: 350452 [Multi-domain]  Cd Length: 297  Bit Score: 191.30  E-value: 2.92e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  479 FLAEFQSIPRVFSKF------PIKDARKPHNQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQ 552
Cdd:cd14604    27 FASDFMRLRRLSTKYrtekiyPTATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQ 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  553 GPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFKDIVVTINDHKRCPDYIIQKLNVAHKKEKa 632
Cdd:cd14604   107 GPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNET- 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  633 tgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAeGKV----DVY 708
Cdd:cd14604   186 --RRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKA-GKIpeefNVF 262

                         250       260
                  ....*....|....*....|....*....
gi 392871558  709 GYVVKLRRQRCLMVQVEAQYILIHQALVE 737
Cdd:cd14604   263 NLIQEMRTQRHSAVQTKEQYELVHRAIAQ 291
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 506-737 7.13e-54

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), also called lymphoid phosphatase (LyP), PEST-domain phosphatase (PEP), or hematopoietic cell protein-tyrosine phosphatase 70Z-PEP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. Mutations in the PTPN22 gene are associated with multiple connective tissue and autoimmune diseases including type 1 diabetes mellitus, rheumatoid arthritis, and systemic lupus erythematosus. PTPN22 contains an N-terminal catalytic PTP domain and four proline-rich regions at the C-terminus.


Pssm-ID: 350450 [Multi-domain]  Cd Length: 234  Bit Score: 188.13  E-value: 7.13e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  506 KNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNR 585
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  586 NKCAEYWPSMEEGTRAFKDIVVTINDHKRCPDYIIQKLNVAHKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVN 665
Cdd:cd14602    81 KKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSET---RTIYQFHYKNWPDHDVPSSIDPILELIWDVR 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392871558  666 AFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEaEGKV----DVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 737
Cdd:cd14602   158 CYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 843-1050 3.14e-53

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 184.78  E-value: 3.14e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  843 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYW-GEGKQTYGDMEVEMKDTNR 921
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWpEDGSVSSGDITVELKDQTD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  922 ASAYTLRTFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVSMIQDLkQKLPKASPEGmkyhkhaSILVHCRDGSQQT 1001
Cdd:cd14552    81 YEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAV-QKQQQQSGNH-------PITVHCSAGAGRT 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 392871558 1002 GLFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYDII 1050
Cdd:cd14552   153 GTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 481-738 3.64e-53

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein phosphatase non-receptor type 5 (PTPN5), also called striatum-enriched protein-tyrosine phosphatase (STEP) or neural-specific PTP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN5/STEP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. It is a CNS-enriched protein that regulates key signaling proteins required for synaptic strengthening, as well as NMDA and AMPA receptor trafficking. PTPN5 is implicated in multiple neurologic and neuropsychiatric disorders, such as Alzheimer's disease, Parkinson's disease, schizophrenia, and fragile X syndrome.


Pssm-ID: 350461 [Multi-domain]  Cd Length: 258  Bit Score: 186.99  E-value: 3.64e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  481 AEFQSIPRVFSKfPiKDARKPHNQNKNRYVDILPYDYNRVEL-SEINGDAGSTYINASYIDGF-KEPRKYIAAQGPRDET 558
Cdd:cd14613     5 AEFFEIPMNFVD-P-KEYDIPGLVRKNRYKTILPNPHSRVCLtSPDQDDPLSSYINANYIRGYgGEEKVYIATQGPTVNT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  559 VDDFWRMIWEQKATVIVMVTRCEEGNRnKCAEYWPsmeEGTRAFKDIVVTINDHKRCPDYIIQKLNVAHKKEKatgREVT 638
Cdd:cd14613    83 VGDFWRMVWQERSPIIVMITNIEEMNE-KCTEYWP---EEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEE---RGLK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  639 HIQFTSWPDHGVPEDPHLLLKLRRRVNAF---SNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLR 715
Cdd:cd14613   156 HYWYTSWPDQKTPDNAPPLLQLVQEVEEArqqAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLR 235

                         250       260
                  ....*....|....*....|...
gi 392871558  716 RQRCLMVQVEAQYILIHQALVEY 738
Cdd:cd14613   236 LDRGGMIQTCEQYQFVHHVLSLY 258
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 483-746 5.88e-53

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1), also called protein-tyrosine phosphatase 1B (PTP-1B), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1/PTP-1B is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It contains an N-terminal catalytic PTP domain, followed by two tandem proline-rich motifs that mediate interaction with SH3-domain-containing proteins, and a small hydrophobic stretch that localizes the enzyme to the endoplasmic reticulum (ER). It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor.


Pssm-ID: 350456 [Multi-domain]  Cd Length: 277  Bit Score: 187.15  E-value: 5.88e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  483 FQSIPRVFSKFPIKDARKPHNQNKNRYVDILPYDYNRVELSEINGDagstYINASYIDGFKEPRKYIAAQGPRDETVDDF 562
Cdd:cd14608     5 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDND----YINASLIKMEEAQRSYILTQGPLPNTCGHF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  563 WRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFKD--IVVTINDHKRCPDYIIQKLNVAHKKEKATgREVTHI 640
Cdd:cd14608    81 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDtnLKLTLISEDIKSYYTVRQLELENLTTQET-REILHF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  641 QFTSWPDHGVPEDP----HLLLKLRRrvNAFSNFFSGPIVVHCSAGVGRTGTYIGIDA---MLEGLEAEGKVDVYGYVVK 713
Cdd:cd14608   160 HYTTWPDFGVPESPasflNFLFKVRE--SGSLSPEHGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLE 237

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 392871558  714 LRRQRCLMVQVEAQYILIHQALVEYNQF--GETEV 746
Cdd:cd14608   238 MRKFRMGLIQTADQLRFSYLAVIEGAKFimGDSSV 272
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 533-728 1.17e-52

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3) and type 4 (PTPN4) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 and PTPN4 are large modular proteins containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses.


Pssm-ID: 350389 [Multi-domain]  Cd Length: 212  Bit Score: 183.68  E-value: 1.17e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  533 YINASYID----GFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEgTRAFKDIVVT 608
Cdd:cd14541     2 YINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGE-TMQFGNLQIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  609 INDHKRCPDYIIQKLNVAHKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGT 688
Cdd:cd14541    81 CVSEEVTPSFAFREFILTNTNTGEE-RHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTGV 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 392871558  689 YIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQY 728
Cdd:cd14541   160 LITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQY 199
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 506-733 2.51e-52

catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type tyrosine-protein phosphatase-like R (PTPRR or R-PTP-R), also called protein-tyrosine phosphatase PCPTP1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRR is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. The human and mouse PTPRR gene produces multiple neuronal protein isoforms of varying sizes (in human, PTPPBS-alpha, beta, gamma and delta). All isoforms contain the KIM motif and the catalytic PTP domain. PTPRR-deficient mice show significant defects in fine motor coordination and balance skills that are reminiscent of a mild ataxia.


Pssm-ID: 350459 [Multi-domain]  Cd Length: 226  Bit Score: 183.20  E-value: 2.51e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  506 KNRYVDILPYDYNRVELSEIN-GDAGSTYINASYIDGFK-EPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEG 583
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKNsNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  584 NRnKCAEYWPsmeEGTRAFKDIVVTINDHKRCPDYIIQKLNVahkKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRR 663
Cdd:cd14611    82 NE-KCVLYWP---EKRGIYGKVEVLVNSVKECDNYTIRNLTL---KQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLD 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392871558  664 V--NAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 733
Cdd:cd14611   155 VeeDRLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 480-736 2.22e-51

catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3), also called protein-tyrosine phosphatase H1 (PTP-H1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN3 and p38gamma cooperate to promote Ras-induced oncogenesis. PTPN3 is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. Its PDZ domain binds with the PDZ-binding motif of p38gamma and enables efficient tyrosine dephosphorylation.


Pssm-ID: 350448 [Multi-domain]  Cd Length: 274  Bit Score: 182.36  E-value: 2.22e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  480 LAEFQSIPRVFSKFPIKDARKPHNQNKNRYVDILPYDYNRVELSEingdaGSTYINASYID----GFKEPRKYIAAQGPR 555
Cdd:cd14600    17 LIQFEQLYRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVLQG-----NEDYINASYVNmeipSANIVNKYIATQGPL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  556 DETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEgTRAFKDIVVTINDHKRCPDYIIQKLNVAhKKEKATGR 635
Cdd:cd14600    92 PHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPD-VMEYGGFRVQCHSEDCTIAYVFREMLLT-NTQTGEER 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  636 EVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAfSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLR 715
Cdd:cd14600   170 TVTHLQYVAWPDHGVPDDSSDFLEFVNYVRS-KRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMR 248

                         250       260
                  ....*....|....*....|.
gi 392871558  716 RQRCLMVQVEAQYILIHQALV 736
Cdd:cd14600   249 DQRAMMVQTSSQYKFVCEAIL 269
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 498-737 1.56e-50

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type tyrosine-protein phosphatase N2 (PTPRN2 or R-PTP-N2), also called islet cell autoantigen-related protein (IAR), ICAAR, phogrin, or IA-2beta, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. It is mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells. It may function as a phosphatidylinositol phosphatase to regulate insulin secretion. It is also required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain.


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 180.25  E-value: 1.56e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  498 ARKPHNQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGfKEPRK--YIAAQGPRDETVDDFWRMIWEQKATVIV 575
Cdd:cd14610    39 AQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMD-HDPRNpaYIATQGPLPATVADFWQMVWESGCVVIV 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  576 MVTRCEEGNRNKCAEYWPsmEEGTRAFKDIVVT-INDHKRCPDYIIQKLNVAHKKEKATgREVTHIQFTSWPDHGVPEDP 654
Cdd:cd14610   118 MLTPLAENGVKQCYHYWP--DEGSNLYHIYEVNlVSEHIWCEDFLVRSFYLKNLQTNET-RTVTQFHFLSWNDQGVPAST 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  655 HLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGK-VDVYGYVVKLRRQRCLMVQVEAQYILIHQ 733
Cdd:cd14610   195 RSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKGAKeIDIAATLEHLRDQRPGMVQTKEQFEFALT 274


                  ....
gi 392871558  734 ALVE 737
Cdd:cd14610   275 AVAE 278
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 533-747 2.26e-50

PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type tyrosine-protein phosphatase-like N (PTPRN) and N2 (PTPRN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). They consist of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. They are mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells, and are involved in involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. They also are major autoantigens in type 1 diabetes and are involved in the regulation of insulin secretion.


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 176.87  E-value: 2.26e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  533 YINASYIDGfKEPRK--YIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmEEGTRAFKDIVVT-I 609
Cdd:cd14546     1 YINASTIYD-HDPRNpaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWP--EEGSEVYHIYEVHlV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  610 NDHKRCPDYIIQKLNVAHKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTY 689
Cdd:cd14546    78 SEHIWCDDYLVRSFYLKNLQTSET-RTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGTY 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 392871558  690 IGIDAMLEGLEAEGK-VDVYGYVVKLRRQRCLMVQVEAQYILIHQALVEynqfgetEVN 747
Cdd:cd14546   157 ILIDMVLNRMAKGAKeIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE-------EVN 208
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 799-1047 2.88e-50

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar proteins; R3 subfamily receptor-type phosphotyrosine phosphatases (RPTP) are characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. Vertebrate members include receptor-type tyrosine-protein phosphatase-like O (PTPRO), J (PTPRJ), Q (PTPRQ), B (PTPRB), V (PTPRV) and H (PTPRH). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Most members are PTPs, except for PTPRQ, which dephosphorylates phosphatidylinositide substrates. PTPRV is characterized only in rodents; its function has been lost in humans. Both vertebrate and invertebrate R3 subfamily RPTPs are involved in the control of a variety of cellular processes, including cell growth, differentiation, mitotic cycle and oncogenic transformation.


Pssm-ID: 350396 [Multi-domain]  Cd Length: 222  Bit Score: 177.16  E-value: 2.88e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  799 RNSNVVPYDFNRVPLKhelemskesepesdessddDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQ 878
Cdd:cd14548     1 RYTNILPYDHSRVKLI-------------------PINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWE 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  879 RKVKVIVMLTELVNGDQEVCAQYWGEGKQ--TYGDMEVEMKDTNRASAYTLRTFELRHskRKEPRTVYQYQCTTWKGEEL 956
Cdd:cd14548    62 QNSHTIVMLTQCMEKGRVKCDHYWPFDQDpvYYGDITVTMLSESVLPDWTIREFKLER--GDEVRSVRQFHFTAWPDHGV 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  957 PAEPKDLVSMIQDLKQKLPK-ASPegmkyhkhasILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPG 1035
Cdd:cd14548   140 PEAPDSLLRFVRLVRDYIKQeKGP----------TIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPL 209

                         250
                  ....*....|..
gi 392871558 1036 VVCSYEQYQFLY 1047
Cdd:cd14548   210 MVQTEAQYIFLH 221
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 461-735 7.25e-50

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 179.84  E-value: 7.25e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  461 SDILLETYKRKIADEGRLFLAEFQSIPrvfSKFPIKDARKPHNQNKNRYVDILPYDYNRVELSE---------------- 524
Cdd:PHA02746   12 FDFFDKTNHAKFCEFVLLEHAEVMDIP---IRGTTNHFLKKENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkk 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  525 ---INGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRnKCAEYWPSMEEGTRA 601
Cdd:PHA02746   89 ievTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDDDE-KCFELWTKEEDSELA 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  602 FKDIVVTINDHKRCPDYIIQKLNVAHKKEKaTGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA----------FSNFF 671
Cdd:PHA02746  168 FGRFVAKILDIIEELSFTKTRLMITDKISD-TSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEeqaelikqadNDPQT 246

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392871558  672 SGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQAL 735
Cdd:PHA02746  247 LGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 843-1048 7.41e-50

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 175.23  E-value: 7.41e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  843 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYW-GEGKQTYGDMEVEMKDTNR 921
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWpKEGTETYGNIQVTLLSTEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  922 ASAYTLRTFELRHSK------RKEPRTVYQYQCTTWKGEELPAEPKDLVSMIqdlkQKLPKASPEGMkyhkhASILVHCR 995
Cdd:cd14549    81 LATYTVRTFSLKNLKlkkvkgRSSERVVYQYHYTQWPDHGVPDYTLPVLSFV----RKSSAANPPGA-----GPIVVHCS 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 392871558  996 DGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYD 1048
Cdd:cd14549   152 AGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 533-738 3.11e-49

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 173.65  E-value: 3.11e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  533 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSmeEGTRAFKDIVVTINDH 612
Cdd:cd14622     2 YINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPS--EGSVTHGEITIEIKND 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  613 KRCPDYIIQKLNVAHKKEKATgREVTHIQFTSWPDHGVPEDPH----LLLKLRRRVNAFSNffsGPIVVHCSAGVGRTGT 688
Cdd:cd14622    80 TLLETISIRDFLVTYNQEKQT-RLVRQFHFHGWPEIGIPAEGKgmidLIAAVQKQQQQTGN---HPIVVHCSAGAGRTGT 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 392871558  689 YIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVEY 738
Cdd:cd14622   156 FIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 799-1050 3.43e-49

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 174.46  E-value: 3.43e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  799 RNSNVVPYDFNRV--PLKHELEmskesepesdessdddsdseeTSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMI 876
Cdd:cd14623     1 RVLQIIPYEFNRViiPVKRGEE---------------------NTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMI 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  877 FQRKVKVIVMLTELVNGDQEVCAQYW-GEGKQTYGDMEVEMKDTNRASAYTLRTFELRHSKRKEPRTVYQYQCTTWKGEE 955
Cdd:cd14623    60 WEWKSCSIVMLTELEERGQEKCAQYWpSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVG 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  956 LPAEPKDLVSMIQDLKQKLPKASpegmkyhkHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPG 1035
Cdd:cd14623   140 IPSDGKGMINIIAAVQKQQQQSG--------NHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPH 211

                         250
                  ....*....|....*
gi 392871558 1036 VVCSYEQYQFLYDII 1050
Cdd:cd14623   212 MVQTLEQYEFCYKVV 226
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 843-1048 6.71e-49

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae protein-tyrosine phosphatases 1 (PTP1) and 2 (PTP2), Schizosaccharomyces pombe PTP1, PTP2, and PTP3, and similar fungal proteins. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. PTP2, together with PTP3, is the major phosphatase that dephosphorylates and inactivates the MAP kinase HOG1 and also modulates its subcellular localization.


Pssm-ID: 350509 [Multi-domain]  Cd Length: 212  Bit Score: 172.82  E-value: 6.71e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  843 YINASFV-MSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYW--GEGKQTYGDMEVEM--K 917
Cdd:cd18533     1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWpsGEYEGEYGDLTVELvsE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  918 DTNRASAYTLRTFELRHSKrKEPRTVYQYQCTTWKGEELPAEPKDLVSMIqDLKQKLPKASPEGmkyhkhASILVHCRDG 997
Cdd:cd18533    81 EENDDGGFIVREFELSKED-GKVKKVYHIQYKSWPDFGVPDSPEDLLTLI-KLKRELNDSASLD------PPIIVHCSAG 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  998 SQQTGLFCALFNLL--------ESAETEDVVD-VFQVVKSLRKARPGVVCSYEQYQFLYD 1048
Cdd:cd18533   153 VGRTGTFIALDSLLdelkrglsDSQDLEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 792-1050 9.42e-49

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350401 [Multi-domain]  Cd Length: 238  Bit Score: 173.35  E-value: 9.42e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  792 EENKKKNRNSNVVPYDFNRVPLKhelemskesepesdessddDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGD 871
Cdd:cd14553     1 EVNKPKNRYANVIAYDHSRVILQ-------------------PIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGD 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  872 FWQMIFQRKVKVIVMLTELVNGDQEVCAQYW-GEGKQTYGDMEVEMKDTNRASAYTLRTFELRHSKRKEPRTVYQYQCTT 950
Cdd:cd14553    62 FWRMVWEQRSATIVMMTKLEERSRVKCDQYWpTRGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTA 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  951 WKGEELPAEPKDLVSMIQDLKQ-KLPKASPegmkyhkhasILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSL 1029
Cdd:cd14553   142 WPDHGVPEHPTPFLAFLRRVKAcNPPDAGP----------IVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCL 211

                         250       260
                  ....*....|....*....|.
gi 392871558 1030 RKARPGVVCSYEQYQFLYDII 1050
Cdd:cd14553   212 RAQRNYMVQTEDQYIFIHDAL 232
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 480-737 1.16e-48

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type tyrosine-protein phosphatase-like N (PTPRN or R-PTP-N), also called islet cell antigen 512 (ICA512) or PTP IA-2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. PTPRN is located in secretory granules of neuroendocrine cells and is involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. It is a major autoantigen in type 1 diabetes and is involved in the regulation of insulin secretion.


Pssm-ID: 350457 [Multi-domain]  Cd Length: 281  Bit Score: 174.84  E-value: 1.16e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  480 LAEFQSIPRVFSKfpikdARKPHNQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGfKEPR--KYIAAQGPRDE 557
Cdd:cd14609    24 LCAYQAEPNTCST-----AQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIE-HDPRmpAYIATQGPLSH 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  558 TVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPsmEEGTRAFKDIVVT-INDHKRCPDYIIQKLNVAHKKEKATgRE 636
Cdd:cd14609    98 TIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWP--DEGSSLYHIYEVNlVSEHIWCEDFLVRSFYLKNVQTQET-RT 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  637 VTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLeAEG--KVDVYGYVVKL 714
Cdd:cd14609   175 LTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRM-AKGvkEIDIAATLEHV 253

                         250       260
                  ....*....|....*....|...
gi 392871558  715 RRQRCLMVQVEAQYILIHQALVE 737
Cdd:cd14609   254 RDQRPGMVRTKDQFEFALTAVAE 276
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 533-732 1.31e-48

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis thaliana protein tyrosine phosphatase 1 (AtPTP1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. AtPTP1 dephosphorylates and inhibits MAP kinase 6 (MPK6) in non-oxidative stress conditions. Together with MAP kinase phosphatase 1 (MKP1) it expresses salicylic acid (SA) and camalexin biosynthesis, and therefore, modulating defense response.


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 171.88  E-value: 1.31e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  533 YINASYI--DGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNR-NKCAEYWPSMEEGTRAFKDIVVTI 609
Cdd:cd17658     1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPAEENESREFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  610 NDHKrCPDYIIQK--LNVAHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFsGPIVVHCSAGVGRTG 687
Cdd:cd17658    81 KKLK-HSQHSITLrvLEVQYIESEEPPLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGIPPSA-GPIVVHCSAGIGRTG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 392871558  688 TYIGID----AMLEG-LEAegkVDVYGYVVKLRRQRCLMVQVEAQYILIH 732
Cdd:cd17658   159 AYCTIHntirRILEGdMSA---VDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 843-1050 3.45e-48

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 170.57  E-value: 3.45e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  843 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYW-GEGKQTYGDMEVEMKDTNR 921
Cdd:cd14622     2 YINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWpSEGSVTHGEITIEIKNDTL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  922 ASAYTLRTFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVSMIQDLKQKLPKASpegmkyhkHASILVHCRDGSQQT 1001
Cdd:cd14622    82 LETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTG--------NHPIVVHCSAGAGRT 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 392871558 1002 GLFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYDII 1050
Cdd:cd14622   154 GTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 491-727 4.42e-48

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein phosphatase non-receptor type 2 (PTPN2), also called T-cell protein-tyrosine phosphatase (TCPTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN2, a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner. It is deleted in 6% of all T-cell acute lymphoblastic leukemias and is associated with constitutive JAK1/STAT5 signaling and tumorigenesis.


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 172.07  E-value: 4.42e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  491 SKFPIKDARKPHNQNKNRYVDILPYDYNRVELSEINGDagstYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQK 570
Cdd:cd14607    12 HDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTEND----YINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  571 ATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFKD--IVVTINDHKRCPDYIIQKLNVAHKKEKATgREVTHIQFTSWPDH 648
Cdd:cd14607    88 TKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKEtgFSVKLLSEDVKSYYTVHLLQLENINSGET-RTISHFHYTTWPDF 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  649 GVPEDP----HLLLKLRRrvNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEG--KVDVYGYVVKLRRQRCLMV 722
Cdd:cd14607   167 GVPESPasflNFLFKVRE--SGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGLI 244


                  ....*
gi 392871558  723 QVEAQ 727
Cdd:cd14607   245 QTPDQ 249
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 533-737 8.08e-48

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization.


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 169.54  E-value: 8.08e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  533 YINASYID---GFKEpRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFKDIVVTI 609
Cdd:cd14596     1 YINASYITmpvGEEE-LFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  610 NDHKRCPDYIIQKLNVAhKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNffSGPIVVHCSAGVGRTGTY 689
Cdd:cd14596    80 ENYQALQYFIIRIIKLV-EKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHN--TGPIVVHCSAGIGRAGVL 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 392871558  690 IGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 737
Cdd:cd14596   157 ICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLE 204
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 794-1047 3.97e-47

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2).


Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 168.86  E-value: 3.97e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  794 NKKKNRNSNVVPYDFNRVPLKhelemskesepesdessddDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFW 873
Cdd:cd14554     6 NKFKNRLVNILPYESTRVCLQ-------------------PIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFW 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  874 QMIFQRKVKVIVMLTELVNGDQEVCAQYW-GEGKQTYGDMEVEMKDTNRASAYTLRTFELRHSKRKEPRTVYQYQCTTWK 952
Cdd:cd14554    67 RMLWEHNSTIIVMLTKLREMGREKCHQYWpAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWP 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  953 GEELPAEPK---DLVSMIQDLKQKLPKASPegmkyhkhasILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSL 1029
Cdd:cd14554   147 EQGVPKSGEgfiDFIGQVHKTKEQFGQEGP----------ITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLL 216

                         250
                  ....*....|....*...
gi 392871558 1030 RKARPGVVCSYEQYQFLY 1047
Cdd:cd14554   217 RTQRPAMVQTEDQYQFCY 234
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 798-1046 2.69e-46

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type tyrosine-protein phosphatase J (PTPRJ or R-PTP-J), also known as receptor-type tyrosine-protein phosphatase eta (R-PTP-eta) or density-enhanced phosphatase 1 (DEP-1) OR CD148, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRJ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (eight in PTPRJ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed in various cell types including epithelial, hematopoietic, and endothelial cells. It plays a role in cell adhesion, migration, proliferation and differentiation. It dephosphorylates or contributes to the dephosphorylation of various substrates including protein kinases such as FLT3, PDGFRB, MET, RET (variant MEN2A), VEGFR-2, LYN, SRC, MAPK1, MAPK3, and EGFR, as well as PIK3R1 and PIK3R2.


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 166.15  E-value: 2.69e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  798 NRNSNVVPYDFNRVPLKHElemskesepesdessdddsdSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIF 877
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQ--------------------SHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVW 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  878 QRKVKVIVMLTELVNGDQEVCAQYW-GEGKQTYGDMEVEMKDTNRASAYTLRTFELRHSKRKEPRTVYQYQCTTWKGEEL 956
Cdd:cd14615    61 EKNVYAIVMLTKCVEQGRTKCEEYWpSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGV 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  957 PaEPKDLVSMIQDLKQKLPKASPegmkyhKHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGV 1036
Cdd:cd14615   141 P-ETTDLLINFRHLVREYMKQNP------PNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLM 213

                         250
                  ....*....|
gi 392871558 1037 VCSYEQYQFL 1046
Cdd:cd14615   214 VQTEDQYVFL 223
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 495-732 4.68e-46

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 168.26  E-value: 4.68e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  495 IKDARKPHNQNKNRYVDILPYDYNRVELsEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVI 574
Cdd:PHA02747   43 IANFEKPENQPKNRYWDIPCWDHNRVIL-DSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSII 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  575 VMVTRCEEGN-RNKCAEYWPSMEEGTRAFKDIVV-TINDHKRcPDYIIQKLNVAHKKEKaTGREVTHIQFTSWPDHGVPE 652
Cdd:PHA02747  122 VMLTPTKGTNgEEKCYQYWCLNEDGNIDMEDFRIeTLKTSVR-AKYILTLIEITDKILK-DSRKISHFQCSEWFEDETPS 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  653 DPHLLLKL-----RRRVNAFSNFFS-----GPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMV 722
Cdd:PHA02747  200 DHPDFIKFikiidINRKKSGKLFNPkdallCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGI 279

                         250
                  ....*....|
gi 392871558  723 QVEAQYILIH 732
Cdd:PHA02747  280 MNFDDYLFIQ 289
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 794-1047 2.03e-45

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein phosphatase non-receptor type 9 (PTPN9), also called protein-tyrosine phosphatase MEG2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN9 plays an important role in promoting intracellular secretary vesicle fusion in hematopoietic cells and promotes the dephosphorylation of ErbB2 and EGFR in breast cancer cells, leading to impaired activation of STAT5 and STAT3. It also directly dephosphorylates STAT3 at the Tyr705 residue, resulting in its inactivation. PTPN9 has been found to be dysregulated in various human cancers, including breast, colorectal, and gastric cancer.


Pssm-ID: 350391 [Multi-domain]  Cd Length: 271  Bit Score: 164.84  E-value: 2.03e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  794 NKKKNRNSNVVPYDFNRVPLKHELEmskesepesdessdddsdsEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFW 873
Cdd:cd14543    29 NQEKNRYGDVLCLDQSRVKLPKRNG-------------------DERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFW 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  874 QMIFQRKVKVIVMLTELVNGDQEVCAQYW---GEGKQTYGDMEVEMKDTNRASAYTLRTFELRHSKRKEPRTVYQYQCTT 950
Cdd:cd14543    90 RMVWEQKVLVIVMTTRVVERGRVKCGQYWpleEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESRQVTHFQFTS 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  951 WKGEELPAEPKDLVSMIQDLKQKLPKA-SPEGMKYHKHAS---ILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVV 1026
Cdd:cd14543   170 WPDFGVPSSAAALLDFLGEVRQQQALAvKAMGDRWKGHPPgppIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTV 249

                         250       260
                  ....*....|....*....|.
gi 392871558 1027 KSLRKARPGVVCSYEQYQFLY 1047
Cdd:cd14543   250 RRMRTQRAFSIQTPDQYYFCY 270
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 843-1048 2.29e-45

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The type IIb (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 162.19  E-value: 2.29e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  843 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEvCAQYWGE-GKQTYGDMEVEMKDTNR 921
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQS-CPQYWPDeGSGTYGPIQVEFVSTTI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  922 ASAYTLRTFELRHSKRKEP--RTVYQYQCTTW-KGEELPAEPKDLVSMIQDLkQKLPKASPEGmkyhkhaSILVHCRDGS 998
Cdd:cd14556    80 DEDVISRIFRLQNTTRPQEgyRMVQQFQFLGWpRDRDTPPSKRALLKLLSEV-EKWQEQSGEG-------PIVVHCLNGV 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 392871558  999 QQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYD 1048
Cdd:cd14556   152 GRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 533-733 4.87e-45

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein phosphatase non-receptor type 23 (PTPN23), also called His domain-containing protein tyrosine phosphatase (HD-PTP) or protein tyrosine phosphatase TD14 (PTP-TD14), is a catalytically inactive member of the tyrosine-specific protein tyrosine phosphatase (PTP) family. Human PTPN23 may be involved in the regulation of small nuclear ribonucleoprotein assembly and pre-mRNA splicing by modifying the survival motor neuron (SMN) complex. It plays a role in ciliogenesis and is part of endosomal sorting complex required for transport (ESCRT) pathways. PTPN23 contains five domains: a BRO1-like domain that plays a role in endosomal sorting; a V-domain that interacts with Lys63-linked polyubiquitinated substrates; a central proline-rich region that might recruit SH3-containing proteins; a PTP-like domain; and a proteolytic degradation-targeting motif, also known as a PEST sequence.


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 161.40  E-value: 4.87e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  533 YINASYIDGFKE--PRkYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFKDIVVTIN 610
Cdd:cd14539     1 YINASLIEDLTPycPR-FIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAITVSLQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  611 DHKRCPDYIIQKLNVAHKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSG---PIVVHCSAGVGRTG 687
Cdd:cd14539    80 SVRTTPTHVERIISIQHKDTRLS-RSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSlqtPIVVHCSSGVGRTG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 392871558  688 TY-IGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 733
Cdd:cd14539   159 AFcLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 792-1050 2.30e-44

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350478 [Multi-domain]  Cd Length: 237  Bit Score: 160.96  E-value: 2.30e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  792 EENKKKNRNSNVVPYDFNRVPLKhelemskesepesdessddDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGD 871
Cdd:cd14630     1 DENRNKNRYGNIISYDHSRVRLQ-------------------LLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKD 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  872 FWQMIFQRKVKVIVMLTELVNGDQEVCAQYWGEGKQTYGDMEVEMKDTNRASAYTLRTFELRHSKRKEPRTVYQYQCTTW 951
Cdd:cd14630    62 FWRMIWQENSASVVMVTNLVEVGRVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSW 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  952 KGEELPAEPKDLVSMIQDLK-QKLPKASPegmkyhkhasILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLR 1030
Cdd:cd14630   142 PDHGVPCYATGLLGFVRQVKfLNPPDAGP----------IVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELR 211

                         250       260
                  ....*....|....*....|
gi 392871558 1031 KARPGVVCSYEQYQFLYDII 1050
Cdd:cd14630   212 AQRVNMVQTEEQYVFVHDAI 231
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 798-1050 6.88e-44

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type tyrosine-protein phosphatase H (PTPRH or R-PTP-H), also known as stomach cancer-associated protein tyrosine phosphatase 1 (SAP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRH is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is localized specifically at microvilli of the brush border in gastrointestinal epithelial cells. It plays a role in intestinal immunity by regulating CEACAM20 through tyrosine dephosphorylation. It is also a negative regulator of integrin-mediated signaling and may contribute to contact inhibition of cell growth and motility.


Pssm-ID: 350467 [Multi-domain]  Cd Length: 233  Bit Score: 159.28  E-value: 6.88e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  798 NRNSNVVPYDFNRVPLKhelemskesepesdessddDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIF 877
Cdd:cd14619     1 NRFRNVLPYDWSRVPLK-------------------PIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIW 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  878 QRKVKVIVMLTELVNGDQEVCAQYWGEGKQ--TYGDMEVEMKDTNRASAYTLRTFELRHSKRKEPRTVYQYQCTTWKGEE 955
Cdd:cd14619    62 EQQSSTIVMLTNCMEAGRVKCEHYWPLDYTpcTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHG 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  956 LPAEPKDLVSMIQDLKQKLPKASPEGmkyhkhaSILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPG 1035
Cdd:cd14619   142 VPSSTDTLLAFRRLLRQWLDQTMSGG-------PTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPL 214

                         250
                  ....*....|....*
gi 392871558 1036 VVCSYEQYQFLYDII 1050
Cdd:cd14619   215 MVQTESQYVFLHQCI 229
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 533-738 5.48e-43

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21), also called protein-tyrosine phosphatase D1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN21 is a component of a multivalent scaffold complex nucleated by focal adhesion kinase (FAK) at specific intracellular sites. It promotes cytoskeleton events that induce cell adhesion and migration by modulating Src-FAK signaling. It can also selectively associate with and stimulate Tec family kinases and modulate Stat3 activation. Human PTPN21 may also play a pathologic role in gastrointestinal tract tumorigenesis. PTPN21 contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350446 [Multi-domain]  Cd Length: 220  Bit Score: 156.29  E-value: 5.48e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  533 YINASYID---GFKEpRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMeeGTR-------AF 602
Cdd:cd14598     1 YINASHIKvtvGGKE-WDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRL--GSRhntvtygRF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  603 KdIVVTINDHKRCpdYIIQKLNVAHkkeKATGREVT--HIQFTSWPDHGVPEDPHLLL-------KLRRRVNAFSNFFSG 673
Cdd:cd14598    78 K-ITTRFRTDSGC--YATTGLKIKH---LLTGQERTvwHLQYTDWPEHGCPEDLKGFLsyleeiqSVRRHTNSTIDPKSP 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392871558  674 --PIVVHCSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVEY 738
Cdd:cd14598   152 npPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQF 218
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 841-1047 8.27e-43

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; The kinase interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes tyrosine-protein phosphatases non-receptor type 7 (PTPN7) and non-receptor type 5 (PTPN5), and protein-tyrosine phosphatase receptor type R (PTPRR). PTPN7 is also called hematopoietic protein-tyrosine phosphatase (HePTP) while PTPN5 is also called striatal-enriched protein-tyrosine phosphatase (STEP). They belong to the family of classical tyrosine-specific PTPs (EC 3.1.3.48) that catalyze the dephosphorylation of phosphotyrosine peptides. KIM-PTPs are characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. They are highly specific to the MAPKs ERK1/2 (extracellular-signal-regulated kinase 1/2) and p38, over JNK (c-Jun N-terminal kinase); they dephosphorylate these kinases and thereby critically modulate cell proliferation and differentiation.


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 156.02  E-value: 8.27e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  841 SKYINASFVMSY-WKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEvCAQYWGEGK-QTYGDMEVEMKD 918
Cdd:cd14547    25 SSYINANYIRGYdGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKEK-CAQYWPEEEnETYGDFEVTVQS 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  919 TNRASAYTLRTFELRHskRKEPRTVYQYQCTTWKGEELPAEPKDLVSMIQDLKQkLPKASPEgmkyhkHASILVHCRDGS 998
Cdd:cd14547   104 VKETDGYTVRKLTLKY--GGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEE-ARQTEPH------RGPIVVHCSAGI 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 392871558  999 QQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLY 1047
Cdd:cd14547   175 GRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 744-1047 8.37e-43

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 158.36  E-value: 8.37e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  744 TEVNLSELHSCLHNMKKRDPPSDPSPLEAEYQRLPSYRSWRTQHI-GNQEENKKKNRNSNVVPYDFNRVPLKhelemske 822
Cdd:cd14627     2 TEVPARNLYSYIQKLAQVEVGEHVTGMELEFKRLANSKAHTSRFIsANLPCNKFKNRLVNIMPYETTRVCLQ-------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  823 sepesdessddDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYW 902
Cdd:cd14627    74 -----------PIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYW 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  903 -GEGKQTYGDMEVEMKDTNRASAYTLRTFELRHSKRKEPRTVYQYQCTTWKGEELPAEPK---DLVSMIQDLKQKLPKAS 978
Cdd:cd14627   143 pAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEgfiDFIGQVHKTKEQFGQDG 222

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392871558  979 PegmkyhkhasILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLY 1047
Cdd:cd14627   223 P----------ISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCY 281
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 744-1047 8.92e-43

PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type tyrosine-protein phosphatase-like D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 158.36  E-value: 8.92e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  744 TEVNLSELHSCLHNMKKRDPPSDPSPLEAEYQRLPSYRSWRTQHI-GNQEENKKKNRNSNVVPYDFNRVPLKhelemske 822
Cdd:cd14628     1 TEVPARNLYAYIQKLTQIETGENVTGMELEFKRLASSKAHTSRFIsANLPCNKFKNRLVNIMPYESTRVCLQ-------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  823 sepesdessddDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYW 902
Cdd:cd14628    73 -----------PIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYW 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  903 -GEGKQTYGDMEVEMKDTNRASAYTLRTFELRHSKRKEPRTVYQYQCTTWKGEELPAEPK---DLVSMIQDLKQKLPKAS 978
Cdd:cd14628   142 pAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEgfiDFIGQVHKTKEQFGQDG 221

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392871558  979 PegmkyhkhasILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLY 1047
Cdd:cd14628   222 P----------ISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCY 280
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 533-737 1.07e-42

catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein phosphatase non-receptor type 4 (PTPN4), also called protein-tyrosine phosphatase MEG1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses. It specifically inhibits the TRIF-dependent TLR4 pathway by suppressing tyrosine phosphorylation of TRAM. It is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain; the PDZ domain regulates the catalytic activity of PTPN4.


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 155.10  E-value: 1.07e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  533 YINASYID----GFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMeEGTRAFKDIVVT 608
Cdd:cd14601     2 YINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEP-SGSSSYGGFQVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  609 INDHKRCPDYIIQKLNVAHkKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGT 688
Cdd:cd14601    81 CHSEEGNPAYVFREMTLTN-LEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTGV 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 392871558  689 YIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 737
Cdd:cd14601   160 LITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 798-1050 1.31e-42

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type tyrosine-protein phosphatase V (PTPRV or R-PTP-V), also known as embryonic stem cell protein-tyrosine phosphatase (ES cell phosphatase) or osteotesticular protein-tyrosine phosphatase (OST-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRV is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. In rodents, it may play a role in the maintenance of pluripotency and may function in signaling pathways during bone remodeling. It is the only PTP whose function has been lost between rodent and human. The human OST-PTP gene is a pseudogene.


Pssm-ID: 350466 [Multi-domain]  Cd Length: 230  Bit Score: 155.49  E-value: 1.31e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  798 NRNSNVVPYDFNRVPLKhelEMSKESEpesdessdddsdseetSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIF 877
Cdd:cd14618     1 NRYPHVLPYDHSRVRLS---QLGGEPH----------------SDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVW 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  878 QRKVKVIVMLTELVNGDQEVCAQYWGEGKQ--TYGDMEVEMKDTNRASAYTLRTFELRHSKRKEPRTVYQYQCTTWKGEE 955
Cdd:cd14618    62 EQQVCNIIMLTVGMENGRVLCDHYWPSESTpvSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHG 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  956 LPAEPKDLVSMIQDLKQKLPKASPEGmkyhkhaSILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPG 1035
Cdd:cd14618   142 IPESTSSLMAFRELVREHVQATKGKG-------PTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYL 214

                         250
                  ....*....|....*
gi 392871558 1036 VVCSYEQYQFLYDII 1050
Cdd:cd14618   215 MIQTLSQYIFLHSCI 229
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 843-1050 4.99e-42

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The type II (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350403 [Multi-domain]  Cd Length: 204  Bit Score: 152.76  E-value: 4.99e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  843 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYWGEGKQTYGDMEVEMKDTNRA 922
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEVYGDIKVTLVETEPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  923 SAYTLRTFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVSMIQDLKQKL-PKASPegmkyhkhasILVHCRDGSQQT 1001
Cdd:cd14555    81 AEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNpPSAGP----------IVVHCSAGAGRT 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 392871558 1002 GLFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYDII 1050
Cdd:cd14555   151 GCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAI 199
PHA02738 PHA02738
hypothetical protein; Provisional
 503-746 4.99e-42

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 157.01  E-value: 4.99e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  503 NQNKNRYVDILPYDYNRVEL-SEIN-GDagstYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRC 580
Cdd:PHA02738   49 NRKLNRYLDAVCFDHSRVILpAERNrGD----YINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKK 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  581 EEGNRNKCAEYWPSMEEGTRAFKDIVVTINDHKRCPDYIIQKLNVAHKKEkATgREVTHIQFTSWPDHGVPEDPHLLLKL 660
Cdd:PHA02738  125 KENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDGTS-AT-QTVTHFNFTAWPDHDVPKNTSEFLNF 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  661 RRRV---------NAFSN----FFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQ 727
Cdd:PHA02738  203 VLEVrqcqkelaqESLQIghnrLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQ 282

                         250
                  ....*....|....*....
gi 392871558  728 YILIHQALVEYNQFGETEV 746
Cdd:PHA02738  283 YFFCYRAVKRYVNLTVNKV 301
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 744-1047 1.35e-41

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350477 [Multi-domain]  Cd Length: 291  Bit Score: 154.88  E-value: 1.35e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  744 TEVNLSELHSCLHNMKKRDPPSDPSPLEAEYQRLPSYRSWRTQHI-GNQEENKKKNRNSNVVPYDFNRVPLKhelemske 822
Cdd:cd14629     2 TEVPARNLYAHIQKLTQVPPGESVTAMELEFKLLANSKAHTSRFIsANLPCNKFKNRLVNIMPYELTRVCLQ-------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  823 sepesdessddDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYW 902
Cdd:cd14629    74 -----------PIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYW 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  903 -GEGKQTYGDMEVEMKDTNRASAYTLRTFELRHSKRKEPRTVYQYQCTTWKGEELPAEPK---DLVSMIQDLKQKLPKAS 978
Cdd:cd14629   143 pAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEgfiDFIGQVHKTKEQFGQDG 222

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392871558  979 PegmkyhkhasILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLY 1047
Cdd:cd14629   223 P----------ITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCY 281
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 765-1050 1.36e-41

catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350473 [Multi-domain]  Cd Length: 282  Bit Score: 154.48  E-value: 1.36e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  765 SDPSPLEAEYQRLPSYRSWRTQHiGNQEENKKKNRNSNVVPYDFNRVPLKhelemskesepesdessddDSDSEETSKYI 844
Cdd:cd14625    19 NDNLKLSQEYESIDPGQQFTWEH-SNLEVNKPKNRYANVIAYDHSRVILQ-------------------PIEGIMGSDYI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  845 NASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYW-GEGKQTYGDMEVEMKDTNRAS 923
Cdd:cd14625    79 NANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWpSRGTETYGMIQVTLLDTIELA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  924 AYTLRTFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVSMIQDLKQ-KLPKASPegmkyhkhasILVHCRDGSQQTG 1002
Cdd:cd14625   159 TFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTcNPPDAGP----------IVVHCSAGVGRTG 228

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 392871558 1003 LFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYDII 1050
Cdd:cd14625   229 CFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDAL 276
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 790-1048 1.68e-41

catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350474 [Multi-domain]  Cd Length: 276  Bit Score: 154.04  E-value: 1.68e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  790 NQEENKKKNRNSNVVPYDFNRVPLkhelemskesepesdessdDDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETI 869
Cdd:cd14626    37 NLEVNKPKNRYANVIAYDHSRVIL-------------------TSVDGVPGSDYINANYIDGYRKQNAYIATQGPLPETL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  870 GDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYW-GEGKQTYGDMEVEMKDTNRASAYTLRTFELRHSKRKEPRTVYQYQC 948
Cdd:cd14626    98 SDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWpIRGTETYGMIQVTLLDTVELATYSVRTFALYKNGSSEKREVRQFQF 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  949 TTWKGEELPAEPKDLVSMIQDLKQ-KLPKASPegmkyhkhasILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVK 1027
Cdd:cd14626   178 MAWPDHGVPEYPTPILAFLRRVKAcNPPDAGP----------MVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVT 247

                         250       260
                  ....*....|....*....|.
gi 392871558 1028 SLRKARPGVVCSYEQYQFLYD 1048
Cdd:cd14626   248 CMRSQRNYMVQTEDQYIFIHE 268
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 773-1048 5.48e-41

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG has four splicing isoforms: three transmembrane isoforms, PTPRG-A, B, and C, and one secretory isoform, PTPRG-S, which are expressed in many tissues including the brain. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 152.50  E-value: 5.48e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  773 EYQRLPSYRSWRTQHiGNQEENKKKNRNSNVVPYDFNRVPLKhelemskesepesdessDDDSDSEETSKYINASFVMSY 852
Cdd:cd17667     7 EVQRCTADMNITAEH-SNHPDNKHKNRYINILAYDHSRVKLR-----------------PLPGKDSKHSDYINANYVDGY 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  853 WKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYW-GEGKQTYGDMEVEMKDTNRASAYTLRTFE 931
Cdd:cd17667    69 NKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWpTENSEEYGNIIVTLKSTKIHACYTVRRFS 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  932 LRHSK-----------RKEPRTVYQYQCTTWKGEELPAEPKDLVSMI-QDLKQKLPKASPegmkyhkhasILVHCRDGSQ 999
Cdd:cd17667   149 IRNTKvkkgqkgnpkgRQNERTVIQYHYTQWPDMGVPEYALPVLTFVrRSSAARTPEMGP----------VLVHCSAGVG 218

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 392871558 1000 QTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYD 1048
Cdd:cd17667   219 RTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHD 267
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 791-1050 1.54e-40

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 150.96  E-value: 1.54e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  791 QEENKKKNRNSNVVPYDFNRVPLKhelemskesepesdessddDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIG 870
Cdd:cd14633    37 KDENRMKNRYGNIIAYDHSRVRLQ-------------------PIEGETSSDYINGNYIDGYHRPNHYIATQGPMQETIY 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  871 DFWQMIFQRKVKVIVMLTELVNGDQEVCAQYWGEGKQTYGDMEVEMKDTNRASAYTLRTFELRHSKRKEPRTVYQYQCTT 950
Cdd:cd14633    98 DFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTG 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  951 WKGEELPAEPKDLVSMIQDLKQKLPKASpegmkyhkhASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLR 1030
Cdd:cd14633   178 WPDHGVPYHATGLLGFVRQVKSKSPPNA---------GPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELR 248

                         250       260
                  ....*....|....*....|
gi 392871558 1031 KARPGVVCSYEQYQFLYDII 1050
Cdd:cd14633   249 SRRVNMVQTEEQYVFIHDAI 268
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 503-738 2.59e-40

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 151.31  E-value: 2.59e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  503 NQNKNRYVDILPYDYNRVELSEINGdaGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEE 582
Cdd:PHA02742   52 NMKKCRYPDAPCFDRNRVILKIEDG--GDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  583 GNRNKCAEYWPSMEEGTRAFKDIVVTINDHKRCPDYIIQKLNVAHKKeKATGREVTHIQFTSWPDHGVPEDP-------- 654
Cdd:PHA02742  130 DGKEACYPYWMPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTN-TGASLDIKHFAYEDWPHGGLPRDPnkfldfvl 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  655 ---HLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILI 731
Cdd:PHA02742  209 avrEADLKADVDIKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFC 288


                  ....*..
gi 392871558  732 HQALVEY 738
Cdd:PHA02742  289 YFIVLIF 295
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 840-1050 3.89e-40

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350479 [Multi-domain]  Cd Length: 218  Bit Score: 147.86  E-value: 3.89e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  840 TSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYWGEGKQTYGDMEVEMKDT 919
Cdd:cd14631    12 SSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEVYGDFKVTCVEM 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  920 NRASAYTLRTFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVSMIQDLK-QKLPKASPegmkyhkhasILVHCRDGS 998
Cdd:cd14631    92 EPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKlSNPPSAGP----------IVVHCSAGA 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392871558  999 QQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYDII 1050
Cdd:cd14631   162 GRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 213
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 843-1048 5.33e-40

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350506 [Multi-domain]  Cd Length: 209  Bit Score: 147.43  E-value: 5.33e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  843 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYW-GEGKQTYGDMEVEMKDTNR 921
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWpADGSEEYGNFLVTQKSVQV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  922 ASAYTLRTFELRHSK--------RKEPRTVYQYQCTTWKGEELPAEPKDLVSMIQdlkqklpKASpeGMKYHKHASILVH 993
Cdd:cd17668    81 LAYYTVRNFTLRNTKikkgsqkgRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVR-------KAS--YAKRHAVGPVVVH 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392871558  994 CRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYD 1048
Cdd:cd17668   152 CSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 206
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
496-731 6.84e-40

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 149.47  E-value: 6.84e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  496 KDARKPHNQN---KNRYVDILPYDYNRVElseINGdagsTYINASYIDGfKEPRKYIAAQGPRDETVDDFWRMIWEQKAT 572
Cdd:COG5599    32 NDPQYLQNINgspLNRFRDIQPYKETALR---ANL----GYLNANYIQV-IGNHRYIATQYPLEEQLEDFFQMLFDNNTP 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  573 VIVMVTRCEEG--NRNKCAEYWPsmEEGTRAFKDIVVTINDHKRCPDYI---IQKLNVAHKKEKatGREVTHIQFTSWPD 647
Cdd:COG5599   104 VLVVLASDDEIskPKVKMPVYFR--QDGEYGKYEVSSELTESIQLRDGIearTYVLTIKGTGQK--KIEIPVLHVKNWPD 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  648 HGVP--EDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEG--KVDVYGYVVKLRRQR-CLMV 722
Cdd:COG5599   180 HGAIsaEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMV 259


                  ....*....
gi 392871558  723 QVEAQYILI 731
Cdd:COG5599   260 QTSEQLDVL 268
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 794-1047 1.33e-39

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) and type 6 (PTPN6) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 and PTPN6, are also called SH2 domain-containing tyrosine phosphatase 2 (SHP2) and 1 (SHP1), respectively. They contain two tandem SH2 domains: a catalytic PTP domain, and a C-terminal tail with regulatory properties. Although structurally similar, they have different localization and different roles in signal transduction. PTPN11/SHP2 is expressed ubiquitously and plays a positive role in cell signaling, leading to cell activation, while PTPN6/SHP1 expression is restricted mainly to hematopoietic and epithelial cells and functions as a negative regulator of signaling events.


Pssm-ID: 350392 [Multi-domain]  Cd Length: 251  Bit Score: 147.61  E-value: 1.33e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  794 NKKKNRNSNVVPYDFNRVPLKhelemskesepesdessdDDSDSEETSKYINASFVMSYW--KPEMM-----IAAQGPLK 866
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILK------------------DRDPNVPGSDYINANYIRNENegPTTDEnaktyIATQGCLE 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  867 ETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYW---GEGKQtYGDMEVEMKDTNRASAYTLRTFEL-RHSKRKEPRT 942
Cdd:cd14544    63 NTVSDFWSMVWQENSRVIVMTTKEVERGKNKCVRYWpdeGMQKQ-YGPYRVQNVSEHDTTDYTLRELQVsKLDQGDPIRE 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  943 VYQYQCTTWKGEELPAEPKDLVSMIQDLKQK---LPKASPegmkyhkhasILVHCRDGSQQTGLFCALFNLLESAETEDV 1019
Cdd:cd14544   142 IWHYQYLSWPDHGVPSDPGGVLNFLEDVNQRqesLPHAGP----------IVVHCSAGIGRTGTFIVIDMLLDQIKRKGL 211

                         250       260       270
                  ....*....|....*....|....*....|.
gi 392871558 1020 ---VDVFQVVKSLRKARPGVVCSYEQYQFLY 1047
Cdd:cd14544   212 dcdIDIQKTIQMVRSQRSGMVQTEAQYKFIY 242
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 843-1050 2.87e-39

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350480 [Multi-domain]  Cd Length: 205  Bit Score: 145.19  E-value: 2.87e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  843 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYWGEGKQTYGDMEVEMKDTNRA 922
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDIKITLLKTETL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  923 SAYTLRTFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVSMIQDLKQKLP-KASPegmkyhkhasILVHCRDGSQQT 1001
Cdd:cd14632    81 AEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPpDAGP----------VVVHCSAGAGRT 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 392871558 1002 GLFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYDII 1050
Cdd:cd14632   151 GCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAI 199
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 843-1051 4.96e-39

PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type tyrosine-protein phosphatase-like N (PTPRN) and N2 (PTPRN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). They consist of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. They are mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells, and are involved in involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. They also are major autoantigens in type 1 diabetes and are involved in the regulation of insulin secretion.


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 144.51  E-value: 4.96e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  843 YINASFVMSYwKPE--MMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYW-GEGKQTYGDMEVEM-KD 918
Cdd:cd14546     1 YINASTIYDH-DPRnpAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWpEEGSEVYHIYEVHLvSE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  919 TNRASAYTLRTFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVsmiqDLKQKLPKAspegmkYHKHAS-ILVHCRDG 997
Cdd:cd14546    80 HIWCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLL----EFRRKVNKS------YRGRSCpIVVHCSDG 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392871558  998 SQQTGLFCALFNLLES-AETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYDIIA 1051
Cdd:cd14546   150 AGRTGTYILIDMVLNRmAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVA 204
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 770-1051 6.40e-39

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type tyrosine-protein phosphatase N2 (PTPRN2 or R-PTP-N2), also called islet cell autoantigen-related protein (IAR), ICAAR, phogrin, or IA-2beta, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. It is mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells. It may function as a phosphatidylinositol phosphatase to regulate insulin secretion. It is also required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain.


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 146.74  E-value: 6.40e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  770 LEAEYQRLPSYRSW-RTQHIGNQEENKKKNRNSNVVPYDFNRVPLKHELEMSKesepesdessdddsdseetSKYINASF 848
Cdd:cd14610    19 LEKEWEALCAYQAEpNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSH-------------------SDYINASP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  849 VMSYwKPE--MMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYW-GEGKQTYGDMEVEMKDTN-RASA 924
Cdd:cd14610    80 IMDH-DPRnpAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWpDEGSNLYHIYEVNLVSEHiWCED 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  925 YTLRTFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVsmiqDLKQKLPKAspegmkYH-KHASILVHCRDGSQQTGL 1003
Cdd:cd14610   159 FLVRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLL----DFRRKVNKC------YRgRSCPIIVHCSDGAGRSGT 228

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 392871558 1004 FCALFNLLES-AETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYDIIA 1051
Cdd:cd14610   229 YILIDMVLNKmAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVA 277
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 770-1051 7.82e-39

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type tyrosine-protein phosphatase-like N (PTPRN or R-PTP-N), also called islet cell antigen 512 (ICA512) or PTP IA-2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. PTPRN is located in secretory granules of neuroendocrine cells and is involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. It is a major autoantigen in type 1 diabetes and is involved in the regulation of insulin secretion.


Pssm-ID: 350457 [Multi-domain]  Cd Length: 281  Bit Score: 146.34  E-value: 7.82e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  770 LEAEYQRLPSYRSW-RTQHIGNQEENKKKNRNSNVVPYDFNRVPLKHELEMSKesepesdessdddsdseetSKYINASF 848
Cdd:cd14609    17 LAKEWQALCAYQAEpNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSR-------------------SDYINASP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  849 VMSYwKPEM--MIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYW-GEGKQTYGDMEVEMKDTN-RASA 924
Cdd:cd14609    78 IIEH-DPRMpaYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWpDEGSSLYHIYEVNLVSEHiWCED 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  925 YTLRTFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVsmiqDLKQKLPKAspegmkYH-KHASILVHCRDGSQQTGL 1003
Cdd:cd14609   157 FLVRSFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLL----DFRRKVNKC------YRgRSCPIIVHCSDGAGRTGT 226

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 392871558 1004 FCALFNLLES-AETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYDIIA 1051
Cdd:cd14609   227 YILIDMVLNRmAKGVKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVA 275
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 760-1050 1.63e-38

catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type tyrosine-protein phosphatase D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 145.64  E-value: 1.63e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  760 KRDPPSDPSPLEAEYQRLPSYRSWRTQHiGNQEENKKKNRNSNVVPYDFNRVPLKhelemskesepesdessddDSDSEE 839
Cdd:cd14624    14 ERLKANDNLKFSQEYESIDPGQQFTWEH-SNLEVNKPKNRYANVIAYDHSRVLLS-------------------AIEGIP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  840 TSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYW-GEGKQTYGDMEVEMKD 918
Cdd:cd14624    74 GSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWpSRGTETYGLIQVTLLD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  919 TNRASAYTLRTFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVSMIQDLKQ-KLPKASPegmkyhkhasILVHCRDG 997
Cdd:cd14624   154 TVELATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTcNPPDAGP----------MVVHCSAG 223

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 392871558  998 SQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYDII 1050
Cdd:cd14624   224 VGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDAL 276
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 755-1057 2.46e-38

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein phosphatase non-receptor type 12 (PTPN12), also called PTP-PEST or protein-tyrosine phosphatase G1 (PTPG1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling. It regulates various physiological processes, including cell migration, immune response, and neuronal activity, by dephosphorylating multiple substrates including HER2, FAK, PYK2, PSTPIP, WASP, p130Cas, paxillin, Shc, catenin, c-Abl, ArgBP2, p190RhoGAP, RhoGDI, cell adhesion kinase beta, and Rho GTPase.


Pssm-ID: 350452 [Multi-domain]  Cd Length: 297  Bit Score: 145.46  E-value: 2.46e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  755 LHNMKKRDPPSDPSpLEAEYQRLPSYRS-WRTQHI-----GNQEENKKKNRNSNVVPYDFNRVPLKheLEMSKESepesd 828
Cdd:cd14604    13 VQAMKSTDHNGEDN-FASDFMRLRRLSTkYRTEKIyptatGEKEENVKKNRYKDILPFDHSRVKLT--LKTSSQD----- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  829 essdddsdseetSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYW---GEG 905
Cdd:cd14604    85 ------------SDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWplyGEE 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  906 KQTYGDMEVEMKDTNRASAYTLRTFELRHskRKEPRTVYQYQCTTWKGEELPAEPKDLVSMIQDLKQklpkaspegMKYH 985
Cdd:cd14604   153 PMTFGPFRISCEAEQARTDYFIRTLLLEF--QNETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRK---------YQEH 221

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392871558  986 KHASILVHCRDGSQQTGLFCAL---FNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYDIIASIYPAQ 1057
Cdd:cd14604   222 EDVPICIHCSAGCGRTGAICAIdytWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEKQ 296
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
636-737 6.49e-38

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 137.10  E-value: 6.49e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558    636 EVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNF--FSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAE-GKVDVYGYVV 712
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQseSSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 392871558    713 KLRRQRCLMVQVEAQYILIHQALVE 737
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 636-737 6.49e-38

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine phosphatases. Homologues detected by this profile and not by those of "PTPc" or "DSPc" are predicted to be protein phosphatases with a similar fold to DSPs and PTPs, yet with unpredicted specificities.


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 137.10  E-value: 6.49e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558    636 EVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNF--FSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAE-GKVDVYGYVV 712
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQseSSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 392871558    713 KLRRQRCLMVQVEAQYILIHQALVE 737
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 802-1047 1.55e-37

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the first PTP domain (repeat 1).


Pssm-ID: 350468 [Multi-domain]  Cd Length: 229  Bit Score: 140.85  E-value: 1.55e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  802 NVVPYDFNRVPLKHelemskesepesdessdddSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKV 881
Cdd:cd14620     3 NILPYDHSRVILSQ-------------------LDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKS 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  882 KVIVMLTELVNGDQEVCAQYWGE-GKQTYGDMEVEMKDTNRASAYTLRTFELR---HSKRKEPRTVYQYQCTTWKGEELP 957
Cdd:cd14620    64 ATIVMLTNLKERKEEKCYQYWPDqGCWTYGNIRVAVEDCVVLVDYTIRKFCIQpqlPDGCKAPRLVTQLHFTSWPDFGVP 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  958 AEPkdlVSMIQDLKqKLPKASPegmkyhKHAS-ILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGV 1036
Cdd:cd14620   144 FTP---IGMLKFLK-KVKSVNP------VHAGpIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQM 213

                         250
                  ....*....|.
gi 392871558 1037 VCSYEQYQFLY 1047
Cdd:cd14620   214 VQTDMQYSFIY 224
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 843-1047 2.68e-37

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350399 [Multi-domain]  Cd Length: 202  Bit Score: 139.28  E-value: 2.68e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  843 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYW-GEGKQTYGDMEVEMKDTNR 921
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWpDQGCWTYGNLRVRVEDTVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  922 ASAYTLRTFELRH----SKRKEPRTVYQYQCTTWKGEELPAEPKDLVSMIQDLKQKLP-KASPegmkyhkhasILVHCRD 996
Cdd:cd14551    81 LVDYTTRKFCIQKvnrgIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPpRAGP----------IVVHCSA 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 392871558  997 GSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLY 1047
Cdd:cd14551   151 GVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 773-1054 2.78e-37

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350469 [Multi-domain]  Cd Length: 296  Bit Score: 142.47  E-value: 2.78e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  773 EYQRLPSYRSWRTQHIGNQEENKKKNRNSNVVPYDFNRVPLkhelemskesepesdessdDDSDSEETSKYINASFVMSY 852
Cdd:cd14621    31 EFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHL-------------------TPVEGVPDSDYINASFINGY 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  853 WKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYW-GEGKQTYGDMEVEMKDTNRASAYTLRTFE 931
Cdd:cd14621    92 QEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWpDQGCWTYGNIRVSVEDVTVLVDYTVRKFC 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  932 LRH----SKRKEPRTVYQYQCTTWKGEELPAEPKDLVSMIQDLKQKLPKASpegmkyhkhASILVHCRDGSQQTGLFCAL 1007
Cdd:cd14621   172 IQQvgdvTNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYA---------GAIVVHCSAGVGRTGTFIVI 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 392871558 1008 FNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYDIIASIY 1054
Cdd:cd14621   243 DAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHY 289
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 533-733 1.22e-36

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The type IIb (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 137.15  E-value: 1.22e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  533 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNkCAEYWPsmEEGTRAFKDIVVTINDH 612
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQS-CPQYWP--DEGSGTYGPIQVEFVST 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  613 KRCPDYIIQKL---NVAHKKEKAtgREVTHIQFTSWPDHG-VPEDPHLLLKLRRRVNA-FSNFFSGPIVVHCSAGVGRTG 687
Cdd:cd14556    78 TIDEDVISRIFrlqNTTRPQEGY--RMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKwQEQSGEGPIVVHCLNGVGRSG 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 392871558  688 TYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 733
Cdd:cd14556   156 VFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 843-1047 1.64e-36

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 1.


Pssm-ID: 350405 [Multi-domain]  Cd Length: 201  Bit Score: 136.88  E-value: 1.64e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  843 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYW---GEGKQTYGDMEVEMKDT 919
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWpsmEEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  920 NRASAYTLRTFELRHSKRK-EPRTVYQYQCTTWKGEELPAEPkdlvSMIQDLKQKLPKASPEGmkyhkHASILVHCRDGS 998
Cdd:cd14557    81 KICPDYIIRKLNINNKKEKgSGREVTHIQFTSWPDHGVPEDP----HLLLKLRRRVNAFNNFF-----SGPIVVHCSAGV 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 392871558  999 QQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLY 1047
Cdd:cd14557   152 GRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 793-1047 1.71e-36

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11), also called SH2 domain-containing tyrosine phosphatase 2 (SHP-2 or SHP2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 promotes the activation of the RAS/Mitogen-Activated Protein Kinases (MAPK) Extracellular-Regulated Kinases 1/2 (ERK1/2) pathway, a canonical signaling cascade that plays key roles in various cellular processes, including proliferation, survival, differentiation, migration, or metabolism. It also regulates the phosphoinositide 3-kinase (PI3K)/AKT pathway, a fundamental cascade that functions in cell survival, proliferation, migration, morphogenesis, and metabolism. PTPN11 dysregulation is associated with several developmental diseases and malignancies, such as Noonan syndrome and juvenile myelomonocytic leukemia. It contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 138.61  E-value: 1.71e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  793 ENKKKNRNSNVVPYDFNRVPLkHELEMSKEsepesdessdddsdseeTSKYINASFVMSYW-------KPEM-MIAAQGP 864
Cdd:cd14605     1 ENKNKNRYKNILPFDHTRVVL-HDGDPNEP-----------------VSDYINANIIMPEFetkcnnsKPKKsYIATQGC 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  865 LKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYWGE--GKQTYGDMEVEMKDTNRASAYTLRtfELRHSKRKE--- 939
Cdd:cd14605    63 LQNTVNDFWRMVFQENSRVIVMTTKEVERGKSKCVKYWPDeyALKEYGVMRVRNVKESAAHDYILR--ELKLSKVGQgnt 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  940 PRTVYQYQCTTWKGEELPAEPKDLVSMIQDLKQKLPKASPEGmkyhkhaSILVHCRDGSQQTGLFCALFNLLESAETEDV 1019
Cdd:cd14605   141 ERTVWQYHFRTWPDHGVPSDPGGVLDFLEEVHHKQESIMDAG-------PVVVHCSAGIGRTGTFIVIDILIDIIREKGV 213

                         250       260       270
                  ....*....|....*....|....*....|.
gi 392871558 1020 ---VDVFQVVKSLRKARPGVVCSYEQYQFLY 1047
Cdd:cd14605   214 dcdIDVPKTIQMVRSQRSGMVQTEAQYRFIY 244
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 785-1054 2.26e-36

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein phosphatase non-receptor type 18 (PTPN18), also called brain-derived phosphatase, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. The N-terminal catalytic PTP domain of PTPN18 blocks lysosomal routing and delays the degradation of HER2 by dephosphorylation, and its C-terminal PEST domain promotes K48-linked HER2 ubiquitination and its destruction via the proteasome pathway.


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 138.80  E-value: 2.26e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  785 TQHIGNQEENKKKNRNSNVVPYDFNRV---PLKHELEmskesepesdessdddsdseetSKYINASFVMSYWKPEMMIAA 861
Cdd:cd14603    21 STVAGGRKENVKKNRYKDILPYDQTRVilsLLQEEGH----------------------SDYINANFIKGVDGSRAYIAT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  862 QGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYWGEGKQT--YGDMEVEMKDTNRASAYT-LRTfeLRHSKRK 938
Cdd:cd14603    79 QGPLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEPlqTGPFTITLVKEKRLNEEViLRT--LKVTFQK 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  939 EPRTVYQYQCTTWKGEELPAEPKDLVSMIQDLKQKlPKASPEgmkyhkhaSILVHCRDGSQQTGLFCAL---FNLLESAE 1015
Cdd:cd14603   157 ESRSVSHFQYMAWPDHGIPDSPDCMLAMIELARRL-QGSGPE--------PLCVHCSAGCGRTGVICTVdyvRQLLLTQR 227

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 392871558 1016 TEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYDIIASIY 1054
Cdd:cd14603   228 IPPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQMF 266
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 794-1047 5.02e-36

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type tyrosine-protein phosphatase O (PTPRO or R-PTP-O), also known as glomerular epithelial protein 1 or protein tyrosine phosphatase U2 (PTP-U2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRO is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is essential for sustaining the structure and function of foot processes by regulating tyrosine phosphorylation of podocyte proteins. It has been identified as a synaptic cell adhesion molecule (CAM) that serves as a potent initiator of synapse formation. It is also a tumor suppressor in several types of cancer, such as hepatocellular carcinoma, lung cancer, and breast cancer.


Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 136.94  E-value: 5.02e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  794 NKKKNRNSNVVPYDFNRVPL--KHELEmskesepesdessdddsdseeTSKYINASFVMSYWKPEMMIAAQGPLKETIGD 871
Cdd:cd14614    12 NRCKNRYTNILPYDFSRVKLvsMHEEE---------------------GSDYINANYIPGYNSPQEYIATQGPLPETRND 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  872 FWQMIFQRKVKVIVMLTELVNGDQEVCAQYW--GEGKQTYGDMEVEMKDTNRASAYTLRTFELRHSkrKEPRTVYQYQCT 949
Cdd:cd14614    71 FWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWpfTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYA--DEVQDVMHFNYT 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  950 TWKGEELPA--EPKDLVSMIQDLKQKLPKASpegmkyhkhASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVK 1027
Cdd:cd14614   149 AWPDHGVPTanAAESILQFVQMVRQQAVKSK---------GPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVS 219

                         250       260
                  ....*....|....*....|
gi 392871558 1028 SLRKARPGVVCSYEQYQFLY 1047
Cdd:cd14614   220 EMRSYRMSMVQTEEQYIFIH 239
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 786-1051 5.62e-36

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein phosphatase non-receptor type 6 (PTPN6), also called SH2 domain-containing protein-tyrosine phosphatase 1 (SHP1 or SHP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN6 expression is restricted mainly to hematopoietic and epithelial cells. It is an important regulator of hematopoietic cells, downregulating pathways that promote cell growth, survival, adhesion, and activation. It regulates glucose homeostasis by modulating insulin signalling in the liver and muscle, and it also negatively regulates bone resorption, affecting both the formation and the function of osteoclasts. PTPN6 contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350454 [Multi-domain]  Cd Length: 266  Bit Score: 137.70  E-value: 5.62e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  786 QHIGNQEENKKKNRNSNVVPYDFNRVPLKhelemskesepesdessdDDSDSEETSKYINASFVMSYW-----KPEMMIA 860
Cdd:cd14606    10 RLEGQRPENKSKNRYKNILPFDHSRVILQ------------------GRDSNIPGSDYINANYVKNQLlgpdeNAKTYIA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  861 AQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYWGE--GKQTYGDMEVEMKDTNRASAYTLRTFELRHSKRK 938
Cdd:cd14606    72 SQGCLEATVNDFWQMAWQENSRVIVMTTREVEKGRNKCVPYWPEvgMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNG 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  939 E-PRTVYQYQCTTWKGEELPAEPKDLVSMIQDLKQK---LPKASPegmkyhkhasILVHCRDGSQQTGLFCALFNLLESA 1014
Cdd:cd14606   152 ElIREIWHYQYLSWPDHGVPSEPGGVLSFLDQINQRqesLPHAGP----------IIVHCSAGIGRTGTIIVIDMLMENI 221

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 392871558 1015 ETEDV---VDVFQVVKSLRKARPGVVCSYEQYQFLYDIIA 1051
Cdd:cd14606   222 STKGLdcdIDIQKTIQMVRAQRSGMVQTEAQYKFIYVAIA 261
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 792-1050 1.33e-35

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein phosphatase non-receptor type 13 (PTPN13, also known as PTPL1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN13 is an important regulator of tumor aggressiveness. It regulates breast cancer cell aggressiveness through direct inactivation of Src kinase. In hepatocellular carcinoma, PTPN13 is a tumor suppressor. PTPN13 contains a FERM domain, five PDZ domains, and a C-terminal catalytic PTP domain. With its PDZ domains, PTPN13 has numerous interacting partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated substrates. Its FERM domain is necessary for localization to the membrane.


Pssm-ID: 350445 [Multi-domain]  Cd Length: 234  Bit Score: 135.34  E-value: 1.33e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  792 EENKKKNRNSNVVPYDFNRVPLKHElemskesepesdessdddsdseetSKYINASFV-MSYWKPEMM-IAAQGPLKETI 869
Cdd:cd14597     1 KENRKKNRYKNILPYDTTRVPLGDE------------------------GGYINASFIkMPVGDEEFVyIACQGPLPTTV 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  870 GDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYWGE--GKQTYGD--MEVEMKDTNRASAYTLRTFELRHSKRKEPRTVYQ 945
Cdd:cd14597    57 ADFWQMVWEQKSTVIAMMTQEVEGGKIKCQRYWPEilGKTTMVDnrLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITH 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  946 YQCTTWKGEELPAEPKDLVSMIQDLKQklpkaspegmkYHKHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQV 1025
Cdd:cd14597   137 LNFTAWPDHDTPSQPEQLLTFISYMRH-----------IHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDI 205

                         250       260
                  ....*....|....*....|....*
gi 392871558 1026 VKSLRKARPGVVCSYEQYQFLYDII 1050
Cdd:cd14597   206 VRTMRLQRHGMVQTEDQYIFCYQVI 230
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 843-1047 1.35e-35

catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), type 18 (PTPN18) and type 12 (PTPN12) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. TPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling.


Pssm-ID: 350390 [Multi-domain]  Cd Length: 202  Bit Score: 134.47  E-value: 1.35e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  843 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVML-TELVNGDQEvCAQYW---GEGKQTYGDMEVEM-K 917
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMAcREFEMGKKK-CERYWpeeGEEQLQFGPFKISLeK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  918 DTNRASAYTLRTFELRHSkrKEPRTVYQYQCTTWKGEELPAEPKDLVSMIQDLKqklpkaspegmKYHKHAS--ILVHCR 995
Cdd:cd14542    80 EKRVGPDFLIRTLKVTFQ--KESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVR-----------DYQGSEDvpICVHCS 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392871558  996 DGSQQTGLFCAL---FNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLY 1047
Cdd:cd14542   147 AGCGRTGTICAIdyvWNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 797-1047 7.40e-35

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1) type 2 (PTPN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases, (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1 (or PTP-1B) is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor. PTPN2 (or TCPTP), a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner.


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 133.29  E-value: 7.40e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  797 KNRNSNVVPYDFNRVPLKHELEmskesepesdessdddsdseeTSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMI 876
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQG---------------------DNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMV 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  877 FQRKVKVIVMLTELVNGDQEVCAQYWGEGKQTYGDME-----VEMKDTNRASAYTLRTFELRHSKRKEPRTVYQYQCTTW 951
Cdd:cd14545    60 WEQNSKAVIMLNKLMEKGQIKCAQYWPQGEGNAMIFEdtglkVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTW 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  952 KGEELPAEPKDLVSMIQDLKQklpkaspEGMKYHKHASILVHCRDGSQQTGLFCALFNLLESAETEDV--VDVFQVVKSL 1029
Cdd:cd14545   140 PDFGVPESPAAFLNFLQKVRE-------SGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEM 212

                         250
                  ....*....|....*...
gi 392871558 1030 RKARPGVVCSYEQYQFLY 1047
Cdd:cd14545   213 RKYRMGLIQTPDQLRFSY 230
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 840-1051 9.89e-35

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein phosphatase non-receptor type 7 (PTPN7), also called hematopoietic protein-tyrosine phosphatase (HePTP) or LC-PTP. belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN7/HePTP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. PTPN7/HePTP is found exclusively in the white blood cells in bone marrow, thymus, spleen, lymph nodes and all myeloid and lymphoid cell lines. It negatively regulates T-cell activation and proliferation, and is often dysregulated in the preleukemic disorder myelodysplastic syndrome, as well as in acute myelogenous leukemia.


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 133.42  E-value: 9.89e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  840 TSKYINASFVMSY-WKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGdQEVCAQYWGEGKQTYGDMEVEMKD 918
Cdd:cd14612    43 EGSYINANYIRGYdGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKEK-KEKCVHYWPEKEGTYGRFEIRVQD 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  919 TNRASAYTLRTFELRHSkrKEPRTVYQYQCTTWKGEELPAEPKDLVSMIQDLKQKLPKASPEGmkyhkhaSILVHCRDGS 998
Cdd:cd14612   122 MKECDGYTIRDLTIQLE--EESRSVKHYWFSSWPDHQTPESAGPLLRLVAEVEESRQTAASPG-------PIVVHCSAGI 192

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 392871558  999 QQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYDIIA 1051
Cdd:cd14612   193 GRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLHHTLA 245
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 797-1054 4.36e-34

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), also called lymphoid phosphatase (LyP), PEST-domain phosphatase (PEP), or hematopoietic cell protein-tyrosine phosphatase 70Z-PEP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. Mutations in the PTPN22 gene are associated with multiple connective tissue and autoimmune diseases including type 1 diabetes mellitus, rheumatoid arthritis, and systemic lupus erythematosus. PTPN22 contains an N-terminal catalytic PTP domain and four proline-rich regions at the C-terminus.


Pssm-ID: 350450 [Multi-domain]  Cd Length: 234  Bit Score: 131.12  E-value: 4.36e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  797 KNRNSNVVPYDFNRVPLKhelemskesepesdessddDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMI 876
Cdd:cd14602     1 KNRYKDILPYDHSRVELS-------------------LITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMI 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  877 FQRKVKVIVMLTELVNGDQEVCAQYW---GEGKQTYGDMEVEMKDTNRASAYTLRTfeLRHSKRKEPRTVYQYQCTTWKG 953
Cdd:cd14602    62 WEYSVLIIVMACMEFEMGKKKCERYWaepGEMQLEFGPFSVTCEAEKRKSDYIIRT--LKVKFNSETRTIYQFHYKNWPD 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  954 EELPAEPKDLVSMIQDLKQklpkaspegmkYHKHAS--ILVHCRDGSQQTGLFCAL---FNLLESAETEDVVDVFQVVKS 1028
Cdd:cd14602   140 HDVPSSIDPILELIWDVRC-----------YQEDDSvpICIHCSAGCGRTGVICAIdytWMLLKDGIIPENFSVFSLIQE 208

                         250       260
                  ....*....|....*....|....*.
gi 392871558 1029 LRKARPGVVCSYEQYQFLYDIIASIY 1054
Cdd:cd14602   209 MRTQRPSLVQTKEQYELVYNAVIELF 234
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 841-1054 7.72e-34

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein phosphatase non-receptor type 5 (PTPN5), also called striatum-enriched protein-tyrosine phosphatase (STEP) or neural-specific PTP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN5/STEP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. It is a CNS-enriched protein that regulates key signaling proteins required for synaptic strengthening, as well as NMDA and AMPA receptor trafficking. PTPN5 is implicated in multiple neurologic and neuropsychiatric disorders, such as Alzheimer's disease, Parkinson's disease, schizophrenia, and fragile X syndrome.


Pssm-ID: 350461 [Multi-domain]  Cd Length: 258  Bit Score: 131.14  E-value: 7.72e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  841 SKYINASFVMSYWKPE-MMIAAQGPLKETIGDFWQMIFQRKVKVIVMLT--ELVNgdqEVCAQYWGEGKQTYGDMEVEMK 917
Cdd:cd14613    54 SSYINANYIRGYGGEEkVYIATQGPTVNTVGDFWRMVWQERSPIIVMITniEEMN---EKCTEYWPEEQVTYEGIEITVK 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  918 DTNRASAYTLRTFELRhsKRKEPRTVYQYQCTTWKGEELPAEPKDLVSMIQDLKQKLPKASPegmkyhKHASILVHCRDG 997
Cdd:cd14613   131 QVIHADDYRLRLITLK--SGGEERGLKHYWYTSWPDQKTPDNAPPLLQLVQEVEEARQQAEP------NCGPVIVHCSAG 202

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 392871558  998 SQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYDIIaSIY 1054
Cdd:cd14613   203 IGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVL-SLY 258
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 843-1047 1.95e-33

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21) and type 14 (PTPN14) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Both PTPN21 and PTPN14 contain an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350388 [Multi-domain]  Cd Length: 219  Bit Score: 128.73  E-value: 1.95e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  843 YINASFV-MSYWKPEMM-IAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYW-----GEGKQTYGDMEVE 915
Cdd:cd14540     1 YINASHItATVGGKQRFyIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWptlggEHDALTFGEYKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  916 MKDTNRASAYTLRTFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVSMIQDLKQKLPKASPEGMKYHKHASILVHCR 995
Cdd:cd14540    81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRRHTNQDVAGHNRNPPTLVHCS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392871558  996 DGSQQTG--LFCALfnLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLY 1047
Cdd:cd14540   161 AGVGRTGvvILADL--MLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVY 212
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 798-1047 2.32e-33

catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type tyrosine-protein phosphatase Q (PTPRQ or R-PTP-Q), also called phosphatidylinositol phosphatase PTPRQ, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRQ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (18 in PTPRQ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It displays low tyrosine-protein phosphatase activity; rather, it functions as a phosphatidylinositol phosphatase required for auditory processes. It regulates the levels of phosphatidylinositol 4,5-bisphosphate (PIP2) in the basal region of hair bundles. It can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates.


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 128.49  E-value: 2.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  798 NRNSNVVPYDFNRVPLKHElemskesepesdessdddsDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIF 877
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIAD-------------------AGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVW 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  878 QRKVKVIVMLTELVNGDQEVCAQYWGEGKQ---TYGDMEVEMKDTNRASAYTLRtfELRHSKRKEPRTVYQYQCTTWKGE 954
Cdd:cd14616    62 ETRAKTIVMLTQCFEKGRIRCHQYWPEDNKpvtVFGDIVITKLMEDVQIDWTIR--DLKIERHGDYMMVRQCNFTSWPEH 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  955 ELPAEPKDLVSMIqdlkqKLPKASpegmKYHKHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARP 1034
Cdd:cd14616   140 GVPESSAPLIHFV-----KLVRAS----RAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERM 210

                         250
                  ....*....|...
gi 392871558 1035 GVVCSYEQYQFLY 1047
Cdd:cd14616   211 CMVQNLAQYIFLH 223
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 843-1050 2.44e-33

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) and type 13 (PTPN13, also known as PTPL1) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization. Human PTPN13 is an important regulator of tumor aggressiveness.


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 127.88  E-value: 2.44e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  843 YINASFV--------MSYwkpemmIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYWGEGKQT----YG 910
Cdd:cd14538     1 YINASHIripvggdtYHY------IACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKplicGG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  911 DMEVEMKDTNRASAYTLRTFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVSMIQDLKqklpkaspegmKYHKHASI 990
Cdd:cd14538    75 RLEVSLEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMR-----------RIHNSGPI 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  991 LVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYDII 1050
Cdd:cd14538   144 VVHCSAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKAC 203
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 797-1047 2.14e-32

catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type tyrosine-protein phosphatase-like R (PTPRR or R-PTP-R), also called protein-tyrosine phosphatase PCPTP1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRR is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. The human and mouse PTPRR gene produces multiple neuronal protein isoforms of varying sizes (in human, PTPPBS-alpha, beta, gamma and delta). All isoforms contain the KIM motif and the catalytic PTP domain. PTPRR-deficient mice show significant defects in fine motor coordination and balance skills that are reminiscent of a mild ataxia.


Pssm-ID: 350459 [Multi-domain]  Cd Length: 226  Bit Score: 125.80  E-value: 2.14e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  797 KNRNSNVVPYDFNRVPLKhelemskesepesdessdDDSDSEETSKYINASFVMSYW-KPEMMIAAQGPLKETIGDFWQM 875
Cdd:cd14611     2 KNRYKTILPNPHSRVCLK------------------PKNSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQM 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  876 IFQRKVKVIVMLTELVNGDqEVCAQYWGEGKQTYGDMEVEMKDTNRASAYTLRTFELRHSKRKepRTVYQYQCTTWKGEE 955
Cdd:cd14611    64 VWQEDSPVIVMITKLKEKN-EKCVLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQS--RSVKHYWYTSWPDHK 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  956 LPAEPKDLVSMIQDLKQKLPKASPEGmkyhkhaSILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPG 1035
Cdd:cd14611   141 TPDSAQPLLQLMLDVEEDRLASPGRG-------PVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGG 213

                         250
                  ....*....|..
gi 392871558 1036 VVCSYEQYQFLY 1047
Cdd:cd14611   214 MVQTSEQYEFVH 225
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 843-1048 8.26e-32

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein phosphatase non-receptor type 23 (PTPN23), also called His domain-containing protein tyrosine phosphatase (HD-PTP) or protein tyrosine phosphatase TD14 (PTP-TD14), is a catalytically inactive member of the tyrosine-specific protein tyrosine phosphatase (PTP) family. Human PTPN23 may be involved in the regulation of small nuclear ribonucleoprotein assembly and pre-mRNA splicing by modifying the survival motor neuron (SMN) complex. It plays a role in ciliogenesis and is part of endosomal sorting complex required for transport (ESCRT) pathways. PTPN23 contains five domains: a BRO1-like domain that plays a role in endosomal sorting; a V-domain that interacts with Lys63-linked polyubiquitinated substrates; a central proline-rich region that might recruit SH3-containing proteins; a PTP-like domain; and a proteolytic degradation-targeting motif, also known as a PEST sequence.


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 123.65  E-value: 8.26e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  843 YINASFV--MSYWKPEMmIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYWGEGK---QTYGDMEVEMK 917
Cdd:cd14539     1 YINASLIedLTPYCPRF-IATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERgqaLVYGAITVSLQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  918 DTNRASAYTLRTFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVSMIQDLKQKLPKASPEgmkyhkHASILVHCRDG 997
Cdd:cd14539    80 SVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSL------QTPIVVHCSSG 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392871558  998 SQQTGLFCALFN-LLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYD 1048
Cdd:cd14539   154 VGRTGAFCLLYAaVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 843-1047 4.51e-31

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis thaliana protein tyrosine phosphatase 1 (AtPTP1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. AtPTP1 dephosphorylates and inhibits MAP kinase 6 (MPK6) in non-oxidative stress conditions. Together with MAP kinase phosphatase 1 (MKP1) it expresses salicylic acid (SA) and camalexin biosynthesis, and therefore, modulating defense response.


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 121.42  E-value: 4.51e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  843 YINASFVM--SYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEV-CAQYW---GEGKQTYGDMEVEM 916
Cdd:cd17658     1 YINASLVEtpASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTAkCADYFpaeENESREFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  917 KDTNRAS-AYTLRTFELRHSKRKE-PRTVYQYQCTTWKGEELPAEPKDLVSMIQDLKQKLPKASPegmkyhkhasILVHC 994
Cdd:cd17658    81 KKLKHSQhSITLRVLEVQYIESEEpPLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGIPPSAGP----------IVVHC 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392871558  995 RDGSQQTGLFCALFNLLESAETEDV--VDVFQVVKSLRKARPGVVCSYEQYQFLY 1047
Cdd:cd17658   151 SAGIGRTGAYCTIHNTIRRILEGDMsaVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 793-1046 9.46e-31

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 123.96  E-value: 9.46e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  793 ENKKKNRNSNVVPYDFNRVPLKhelemskesepesdessdddSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDF 872
Cdd:PHA02747   50 ENQPKNRYWDIPCWDHNRVILD--------------------SGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  873 WQMIFQRKVKVIVML--TELVNGdQEVCAQYWGEGKQTYGDME---VEMKDTNRASAYTLRTFELRHSKRKEPRTVYQYQ 947
Cdd:PHA02747  110 WKAVWQEHCSIIVMLtpTKGTNG-EEKCYQYWCLNEDGNIDMEdfrIETLKTSVRAKYILTLIEITDKILKDSRKISHFQ 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  948 CTTWKGEELPAEPKDLV---SMIQDLKQKlpKASPEGMKYHKHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQ 1024
Cdd:PHA02747  189 CSEWFEDETPSDHPDFIkfiKIIDINRKK--SGKLFNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAK 266

                         250       260
                  ....*....|....*....|..
gi 392871558 1025 VVKSLRKARPGVVCSYEQYQFL 1046
Cdd:PHA02747  267 TAEKIREQRHAGIMNFDDYLFI 288
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 843-1049 1.03e-30

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 120.52  E-value: 1.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  843 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTE--LVNGdqevCAQYWGE-GKQTYGDMEVEMKDT 919
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEvdLAQG----CPQYWPEeGMLRYGPIQVECMSC 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  920 NRASAYTLRTFELRHSKRKEP--RTVYQYQCTTWKGE-ELPAEPKDLVSMIQDLkQKLPKASPEGmkyhkHASILVHCRD 996
Cdd:cd14636    77 SMDCDVISRIFRICNLTRPQEgyLMVQQFQYLGWASHrEVPGSKRSFLKLILQV-EKWQEECDEG-----EGRTIIHCLN 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 392871558  997 GSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYDI 1049
Cdd:cd14636   151 GGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDV 203
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 791-1050 1.16e-30

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 123.99  E-value: 1.16e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  791 QEENKKKNRNSNVVPYDFNRVPLKHELEMSKESEPESDESSDDDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIG 870
Cdd:PHA02746   48 KKENLKKNRFHDIPCWDHSRVVINAHESLKMFDVGDSDGKKIEVTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSE 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  871 DFWQMIFQRKVKVIVMLTElVNGDQEVCAQYWGEGKQ---TYGDMEVEMKDTNRASAYTLRTFELRHSKRKEPRTVYQYQ 947
Cdd:PHA02746  128 DFFKLISEHESQVIVSLTD-IDDDDEKCFELWTKEEDselAFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFW 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  948 CTTWKGEELPAEPKDLVSMIQDLKQKLPKASPEG-MKYHKHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVV 1026
Cdd:PHA02746  207 FPDWPDNGIPTGMAEFLELINKVNEEQAELIKQAdNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIV 286

                         250       260
                  ....*....|....*....|....
gi 392871558 1027 KSLRKARPGVVCSYEQYQFLYDII 1050
Cdd:PHA02746  287 LKIRKQRHSSVFLPEQYAFCYKAL 310
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 843-1047 1.37e-30

PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 119.73  E-value: 1.37e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  843 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTElvNGDQEVCAQYW-GEGKQ--------TYGDmE 913
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTD--NELNEDEPIYWpTKEKPlecetfkvTLSG-E 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  914 VEMKDTNRASaYTLRTFELRHSKRKEPRTVYQYQCTTWKGEELPAEPK-DLVSMIQDLKQKlpkaspegmkyhKHASILV 992
Cdd:cd14550    78 DHSCLSNEIR-LIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTVfELINTVQEWAQQ------------RDGPIVV 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392871558  993 HCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLY 1047
Cdd:cd14550   145 HDRYGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLY 199
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 793-1047 3.84e-30

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein phosphatase non-receptor type 2 (PTPN2), also called T-cell protein-tyrosine phosphatase (TCPTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN2, a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner. It is deleted in 6% of all T-cell acute lymphoblastic leukemias and is associated with constitutive JAK1/STAT5 signaling and tumorigenesis.


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 120.46  E-value: 3.84e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  793 ENKKKNRNSNVVPYDFNRVPLKHelemskesepesdessdddsdseETSKYINASFVMSYWKPEMMIAAQGPLKETIGDF 872
Cdd:cd14607    23 ENRNRNRYRDVSPYDHSRVKLQN-----------------------TENDYINASLVVIEEAQRSYILTQGPLPNTCCHF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  873 WQMIFQRKVKVIVMLTELVNGDQEVCAQYW---GEGKQTYGD--MEVEMKDTNRASAYTLRTFELRHSKRKEPRTVYQYQ 947
Cdd:cd14607    80 WLMVWQQKTKAVVMLNRIVEKDSVKCAQYWptdEEEVLSFKEtgFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFH 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  948 CTTWKGEELPAEPKDLVSMiqdlkqkLPKASPEGMKYHKHASILVHCRDGSQQTGLFCALFNLLESAETED--VVDVFQV 1025
Cdd:cd14607   160 YTTWPDFGVPESPASFLNF-------LFKVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQV 232

                         250       260
                  ....*....|....*....|..
gi 392871558 1026 VKSLRKARPGVVCSYEQYQFLY 1047
Cdd:cd14607   233 LLDMRKYRMGLIQTPDQLRFSY 254
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 843-1050 1.06e-29

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 117.40  E-value: 1.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  843 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAqYWGEGKQ-------TYGDMEVE 915
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEpincetfKVTLIAEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  916 MKDTNRASAYTLRTFELRHSKRKEPRTVYQYQCTTWKGEELP-AEPKDLVSMIQDlkqklpKASpegmkyHKHASILVHC 994
Cdd:cd17669    80 HKCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISIIKE------EAA------NRDGPMIVHD 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392871558  995 RDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYDII 1050
Cdd:cd17669   148 EHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 798-1047 1.20e-29

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type tyrosine-protein phosphatase B (PTPRB), also known as receptor-type tyrosine-protein phosphatase beta (R-PTP-beta) or vascular endothelial protein tyrosine phosphatase(VE-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRB/VE-PTP is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed specifically in vascular endothelial cells and it plays an important role in blood vessel remodeling and angiogenesis.


Pssm-ID: 350465 [Multi-domain]  Cd Length: 228  Bit Score: 118.10  E-value: 1.20e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  798 NRNSNVVPYDFNRVPLKHelemskesepesdessdddSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIF 877
Cdd:cd14617     1 NRYNNILPYDSTRVKLSN-------------------VDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVW 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  878 QRKVKVIVMLTELVNGDQEVCAQYWGEGKQT--YGDMEVEMKDTNRASAYTLRTFEL-RHSKRKEPRTVYQYQCTTWKGE 954
Cdd:cd14617    62 EQNVHNIVMVTQCVEKGRVKCDHYWPADQDSlyYGDLIVQMLSESVLPEWTIREFKIcSEEQLDAPRLVRHFHYTVWPDH 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  955 ELPAEPKDL---VSMIQDLKQKLPKASPEgmkyhkhasiLVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRK 1031
Cdd:cd14617   142 GVPETTQSLiqfVRTVRDYINRTPGSGPT----------VVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRL 211

                         250
                  ....*....|....*.
gi 392871558 1032 ARPGVVCSYEQYQFLY 1047
Cdd:cd14617   212 HRVHMVQTECQYVYLH 227
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 788-1047 1.25e-29

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1), also called protein-tyrosine phosphatase 1B (PTP-1B), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1/PTP-1B is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It contains an N-terminal catalytic PTP domain, followed by two tandem proline-rich motifs that mediate interaction with SH3-domain-containing proteins, and a small hydrophobic stretch that localizes the enzyme to the endoplasmic reticulum (ER). It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor.


Pssm-ID: 350456 [Multi-domain]  Cd Length: 277  Bit Score: 119.75  E-value: 1.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  788 IGNQEENKKKNRNSNVVPYDFNRVPLKHElemskesepesdessdddsdseeTSKYINASFVMSYWKPEMMIAAQGPLKE 867
Cdd:cd14608    19 VAKLPKNKNRNRYRDVSPFDHSRIKLHQE-----------------------DNDYINASLIKMEEAQRSYILTQGPLPN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  868 TIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYWGEGKqtygDMEVEMKDTNR---------ASAYTLRTFELRHSKRK 938
Cdd:cd14608    76 TCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKE----EKEMIFEDTNLkltlisediKSYYTVRQLELENLTTQ 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  939 EPRTVYQYQCTTWKGEELPAEPKDLVSMIQDLKQKlPKASPEgmkyhkHASILVHCRDGSQQTGLFC---ALFNLLESAE 1015
Cdd:cd14608   152 ETREILHFHYTTWPDFGVPESPASFLNFLFKVRES-GSLSPE------HGPVVVHCSAGIGRSGTFCladTCLLLMDKRK 224

                         250       260       270
                  ....*....|....*....|....*....|..
gi 392871558 1016 TEDVVDVFQVVKSLRKARPGVVCSYEQYQFLY 1047
Cdd:cd14608   225 DPSSVDIKKVLLEMRKFRMGLIQTADQLRFSY 256
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 843-1049 2.50e-29

PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 116.55  E-value: 2.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  843 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQE-VCAQYWGE-GKQTYGDMEVEMKDTN 920
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEpGLQQYGPMEVEFVSGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  921 RASAYTLRTFELRHSKR--KEPRTVYQYQCTTWKG-EELPAEPKDLVSMIQDLkQKLPKASPEGmkyhkhaSILVHCRDG 997
Cdd:cd14637    81 ADEDIVTRLFRVQNITRlqEGHLMVRHFQFLRWSAyRDTPDSKKAFLHLLASV-EKWQRESGEG-------RTVVHCLNG 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392871558  998 SQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYDI 1049
Cdd:cd14637   153 GGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEI 204
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 843-1054 3.26e-29

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3) and type 4 (PTPN4) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 and PTPN4 are large modular proteins containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses.


Pssm-ID: 350389 [Multi-domain]  Cd Length: 212  Bit Score: 116.27  E-value: 3.26e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  843 YINASFV-MSYWKPEMM---IAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYW--GEGKQTYGDMEVEM 916
Cdd:cd14541     2 YINANYVnMEIPGSGIVnryIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWpdLGETMQFGNLQITC 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  917 KDTNRASAYTLRTFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVSMIQDLKQklpkaSPEGMKYhkhaSILVHCRD 996
Cdd:cd14541    82 VSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQ-----NRVGMVE----PTVVHCSA 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392871558  997 GSQQTGLFCAL---FNLLESAETedvVDVFQVVKSLRKARPGVVCSYEQYQFLYDIIASIY 1054
Cdd:cd14541   153 GIGRTGVLITMetaMCLIEANEP---VYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRVY 210
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 843-1049 3.75e-29

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 115.89  E-value: 3.75e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  843 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELvnGDQEVCAQYWGEGKQ-TYGDMEVEMKDTNR 921
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM--DAAQLCMQYWPEKTScCYGPIQVEFVSADI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  922 ASAYTLRTFELRHSKRKEP--RTVYQYQCTTWKG-EELPAEPKDLVSMIQDLKQKLPKASpegmkyHKHASILVHCRDGS 998
Cdd:cd14634    79 DEDIISRIFRICNMARPQDgyRIVQHLQYIGWPAyRDTPPSKRSILKVVRRLEKWQEQYD------GREGRTVVHCLNGG 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 392871558  999 QQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYDI 1049
Cdd:cd14634   153 GRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEV 203
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 793-1050 4.68e-29

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 118.57  E-value: 4.68e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  793 ENKKKNRNSNVVPYDFNRVPLKHElemskesepesdessdddsdsEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDF 872
Cdd:PHA02742   51 KNMKKCRYPDAPCFDRNRVILKIE---------------------DGGDDFINASYVDGHNAKGRFICTQAPLEETALDF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  873 WQMIFQRKVKVIVMLTELVNGDQEVCAQYWG---EGKQTYGDMEVEMKDTNRASAYTLRTFELRHSKRKEPRTVYQYQCT 949
Cdd:PHA02742  110 WQAIFQDQVRVIVMITKIMEDGKEACYPYWMpheRGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYE 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  950 TWKGEELPAEPKDLVSMI-----QDLKQKLPKaspEGMKYHKHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQ 1024
Cdd:PHA02742  190 DWPHGGLPRDPNKFLDFVlavreADLKADVDI---KGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLS 266

                         250       260
                  ....*....|....*....|....*.
gi 392871558 1025 VVKSLRKARPGVVCSYEQYQFLYDII 1050
Cdd:PHA02742  267 IVRDLRKQRHNCLSLPQQYIFCYFIV 292
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 533-719 1.66e-28

PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 113.96  E-value: 1.66e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  533 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEgnRNKCAEYWPSMEEGTRA--FK------D 604
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNEL--NEDEPIYWPTKEKPLECetFKvtlsgeD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  605 IVVTIND-HKRCPDYIIQklnvahKKEKATGREVTHIQFTSWPDHGVPedPHLLLKLRRRVNAFSNFFSGPIVVHCSAGV 683
Cdd:cd14550    79 HSCLSNEiRLIVRDFILE------STQDDYVLEVRQFQCPSWPNPCSP--IHTVFELINTVQEWAQQRDGPIVVHDRYGG 150

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 392871558  684 GRTGTYIGIDAMLEGLEAEGKVDVYGYVV--KLRRQRC 719
Cdd:cd14550   151 VQAATFCALTTLHQQLEHESSVDVYQVAKlyHLMRPGV 188
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 791-1054 2.56e-28

catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3), also called protein-tyrosine phosphatase H1 (PTP-H1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN3 and p38gamma cooperate to promote Ras-induced oncogenesis. PTPN3 is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. Its PDZ domain binds with the PDZ-binding motif of p38gamma and enables efficient tyrosine dephosphorylation.


Pssm-ID: 350448 [Multi-domain]  Cd Length: 274  Bit Score: 115.72  E-value: 2.56e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  791 QEENKKKNRNSNVVPYDFNRVPLKHElemskesepesdessdddsdseetSKYINASFV-MSYWKPEMM---IAAQGPLK 866
Cdd:cd14600    37 LPQNMDKNRYKDVLPYDATRVVLQGN------------------------EDYINASYVnMEIPSANIVnkyIATQGPLP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  867 ETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYWGEGKQT--YGDMEVEMKDTNRASAYTLRTFELRHSKRKEPRTVY 944
Cdd:cd14600    93 HTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVmeYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVT 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  945 QYQCTTWKGEELPAEPKDLVSMIQDLKQKLPKASPegmkyhkhasILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQ 1024
Cdd:cd14600   173 HLQYVAWPDHGVPDDSSDFLEFVNYVRSKRVENEP----------VLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLD 242

                         250       260       270
                  ....*....|....*....|....*....|
gi 392871558 1025 VVKSLRKARPGVVCSYEQYQFLYDIIASIY 1054
Cdd:cd14600   243 IVRKMRDQRAMMVQTSSQYKFVCEAILRVY 272
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 843-1050 7.63e-27

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization.


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 109.45  E-value: 7.63e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  843 YINASFVMSYWKPE--MMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYWGEGKQT---YGDMEVEMK 917
Cdd:cd14596     1 YINASYITMPVGEEelFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEpmeLENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  918 DTNRASAYTLRTFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVSMIQDLKqklpkaspegmKYHKHASILVHCRDG 997
Cdd:cd14596    81 NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMR-----------KVHNTGPIVVHCSAG 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 392871558  998 SQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYDII 1050
Cdd:cd14596   150 IGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVV 202
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 942-1052 9.12e-27

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine phosphatases. Homologues detected by this profile and not by those of "PTPc" or "DSPc" are predicted to be protein phosphatases with a similar fold to DSPs and PTPs, yet with unpredicted specificities.


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 105.52  E-value: 9.12e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558    942 TVYQYQCTTWKGEELPAEPKDLVSMIQDLKQKLPKASPegmkyhkHASILVHCRDGSQQTGLFCALFNLLESAETE-DVV 1020
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSES-------SGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEV 73

                            90       100       110
                    ....*....|....*....|....*....|..
gi 392871558   1021 DVFQVVKSLRKARPGVVCSYEQYQFLYDIIAS 1052
Cdd:smart00012   74 DIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
942-1052 9.12e-27

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 105.52  E-value: 9.12e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558    942 TVYQYQCTTWKGEELPAEPKDLVSMIQDLKQKLPKASPegmkyhkHASILVHCRDGSQQTGLFCALFNLLESAETE-DVV 1020
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSES-------SGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEV 73

                            90       100       110
                    ....*....|....*....|....*....|..
gi 392871558   1021 DVFQVVKSLRKARPGVVCSYEQYQFLYDIIAS 1052
Cdd:smart00404   74 DIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 533-737 1.08e-26

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 108.96  E-value: 1.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  533 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTrcEEGNRNKCAEYWPsmEEGTRAFKDIVVTINDH 612
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLN--EMDAAQLCMQYWP--EKTSCCYGPIQVEFVSA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  613 KRCPDYIIQKLNVAHKKEKATG-REVTHIQFTSWPDH-GVPEDPHLLLKLRRRVNAFSNFF---SGPIVVHCSAGVGRTG 687
Cdd:cd14634    77 DIDEDIISRIFRICNMARPQDGyRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQYdgrEGRTVVHCLNGGGRSG 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 392871558  688 TYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 737
Cdd:cd14634   157 TFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 773-1050 7.44e-26

catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein phosphatase non-receptor type 14 (PTPN14), also called protein-tyrosine phosphatase pez, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN14 is a potential tumor suppressor and plays a regulatory role in the Hippo and Wnt/beta-catenin signaling pathways. It contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350447 [Multi-domain]  Cd Length: 287  Bit Score: 108.93  E-value: 7.44e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  773 EYQRLPSYRSWRTQHIGNQEENKKKNRNSNVVPYDFNRVPLKHELEmskesepesdessdddsdseETSKYINASF--VM 850
Cdd:cd14599    17 EYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKE--------------------NNTGYINASHikVT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  851 SYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYWGE-----GKQTYGDMEVEMKDTNRASAY 925
Cdd:cd14599    77 VGGEEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCY 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  926 TLRTFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVSMIQDLK--QKLPKASPEGMKyHKHASILVHCRDGSQQTGL 1003
Cdd:cd14599   157 ATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQsvRRHTNSMLDSTK-NCNPPIVVHCSAGVGRTGV 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 392871558 1004 FCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYDII 1050
Cdd:cd14599   236 VILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVL 282
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 843-1052 1.40e-25

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 105.53  E-value: 1.40e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  843 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTElVNGDQEVCAQYWGEGKQTYG--DMEVEMKDTN 920
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD-NQGLAEDEFVYWPSREESMNceAFTVTLISKD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  921 R-----ASAYTLRTFELRHSKRKEPRTVYQYQCTTWKGEELPAEPK-DLVSMIQDlkQKLPKASPegmkyhkhasILVHC 994
Cdd:cd17670    80 RlclsnEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTfELINVIKE--EALTRDGP----------TIVHD 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 392871558  995 RDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYDIIAS 1052
Cdd:cd17670   148 EFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAMLS 205
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 843-1054 1.72e-25

catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein phosphatase non-receptor type 4 (PTPN4), also called protein-tyrosine phosphatase MEG1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses. It specifically inhibits the TRIF-dependent TLR4 pathway by suppressing tyrosine phosphorylation of TRAM. It is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain; the PDZ domain regulates the catalytic activity of PTPN4.


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 105.41  E-value: 1.72e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  843 YINASFV-MSYWKPEMM---IAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYWGE--GKQTYGDMEVEM 916
Cdd:cd14601     2 YINANYInMEIPSSSIInryIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEpsGSSSYGGFQVTC 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  917 KDTNRASAYTLRTFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVSMIQDLKQKlpkaspegmKYHKHASILVHCRD 996
Cdd:cd14601    82 HSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNK---------RAGKDEPVVVHCSA 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 392871558  997 GSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYDIIASIY 1054
Cdd:cd14601   153 GIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVY 210
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 843-1049 6.16e-25

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 104.00  E-value: 6.16e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  843 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELvnGDQEVCAQYWGE-GKQTYGDMEVEMKDTNR 921
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV--DPAQLCPQYWPEnGVHRHGPIQVEFVSADL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  922 ASAYTLRTFELRHSKRKEP--RTVYQYQCTTWKG-EELPAEPKDLVSMIQDL-KQKLPKASPEGmkyhkhaSILVHCRDG 997
Cdd:cd14635    79 EEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMyRDTPVSKRSFLKLIRQVdKWQEEYNGGEG-------RTVVHCLNG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392871558  998 SQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYDI 1049
Cdd:cd14635   152 GGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEV 203
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 533-737 9.52e-24

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 100.53  E-value: 9.52e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  533 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRnkCAEYWPsmEEGTRAFKDIVVTINDH 612
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQL--CPQYWP--ENGVHRHGPIQVEFVSA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  613 KRCPDYIIQKLNVAHKKEKATG-REVTHIQFTSWPDH-GVPEDPHLLLKLRRRVNAFSNFF---SGPIVVHCSAGVGRTG 687
Cdd:cd14635    77 DLEEDIISRIFRIYNAARPQDGyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYnggEGRTVVHCLNGGGRSG 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 392871558  688 TYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 737
Cdd:cd14635   157 TFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
785-1053 6.33e-23

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 100.17  E-value: 6.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  785 TQHIGNQEeNKKKNRNSNVVPYDFNRVplkhelemskesepesdessdddsdsEETSKYINASFVMSYwKPEMMIAAQGP 864
Cdd:COG5599    34 PQYLQNIN-GSPLNRFRDIQPYKETAL--------------------------RANLGYLNANYIQVI-GNHRYIATQYP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  865 LKETIGDFWQMIFQRKVKVIVMLTELVNGD--QEVCAQYWGEgKQTYGDMEVEMKDT---NRASAYTLRTFEL-RHSKRK 938
Cdd:COG5599    86 LEEQLEDFFQMLFDNNTPVLVVLASDDEISkpKVKMPVYFRQ-DGEYGKYEVSSELTesiQLRDGIEARTYVLtIKGTGQ 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  939 EPRTVYQYQCTTWK-GEELPAEP-KDLVSMIqDLKQKLpKASPEGmkyhkhaSILVHCRDGSQQTGLFCALFNLLES--A 1014
Cdd:COG5599   165 KKIEIPVLHVKNWPdHGAISAEAlKNLADLI-DKKEKI-KDPDKL-------LPVVHCRAGVGRTGTLIACLALSKSinA 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 392871558 1015 ETEDVVDVFQVVKSLRKAR-PGVVCSYEQYQFLYDIIASI 1053
Cdd:COG5599   236 LVQITLSVEEIVIDMRTSRnGGMVQTSEQLDVLVKLAEQQ 275
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 533-736 1.30e-22

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 96.99  E-value: 1.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  533 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAeYWPSMEEGTRAFKDIVVTINDH 612
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEPINCETFKVTLIAEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  613 KRC----PDYIIQKLNVAHKKEKATgREVTHIQFTSWPDhgvPEDP-HLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTG 687
Cdd:cd17669    80 HKClsneEKLIIQDFILEATQDDYV-LEVRHFQCPKWPN---PDSPiSKTFELISIIKEEAANRDGPMIVHDEHGGVTAG 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 392871558  688 TYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALV 736
Cdd:cd17669   156 TFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 843-1050 2.08e-22

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21), also called protein-tyrosine phosphatase D1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN21 is a component of a multivalent scaffold complex nucleated by focal adhesion kinase (FAK) at specific intracellular sites. It promotes cytoskeleton events that induce cell adhesion and migration by modulating Src-FAK signaling. It can also selectively associate with and stimulate Tec family kinases and modulate Stat3 activation. Human PTPN21 may also play a pathologic role in gastrointestinal tract tumorigenesis. PTPN21 contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350446 [Multi-domain]  Cd Length: 220  Bit Score: 96.97  E-value: 2.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  843 YINASFVM-----SYWKpemMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYWG-----EGKQTYGDM 912
Cdd:cd14598     1 YINASHIKvtvggKEWD---YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgsrHNTVTYGRF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  913 EVEMKDTNRASAYTLRTFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVSMIQDLKQKLPKASPEGMKYHKHASILV 992
Cdd:cd14598    78 KITTRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTIDPKSPNPPVLV 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 392871558  993 HCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYDII 1050
Cdd:cd14598   158 HCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVL 215
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 533-736 2.31e-21

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 93.59  E-value: 2.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  533 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRcEEGNRNKCAEYWPSMEEGTRAFKDIVVTINDH 612
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD-NQGLAEDEFVYWPSREESMNCEAFTVTLISKD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  613 KRC---------PDYIIQKLNVAHKkekatgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNffSGPIVVHCSAGV 683
Cdd:cd17670    80 RLClsneeqiiiHDFILEATQDDYV------LEVRHFQCPKWPNPDAPISSTFELINVIKEEALTR--DGPTIVHDEFGA 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 392871558  684 GRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALV 736
Cdd:cd17670   152 VSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 533-737 1.70e-20

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 90.85  E-value: 1.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  533 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGnrNKCAEYWPsmEEGTRAFKDIVVTINDH 612
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLA--QGCPQYWP--EEGMLRYGPIQVECMSC 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  613 KRCPDYIIQKLNVAHKKEKATGR-EVTHIQFTSWPDH-GVPEDPHLLLKLRRRVNAFS---NFFSGPIVVHCSAGVGRTG 687
Cdd:cd14636    77 SMDCDVISRIFRICNLTRPQEGYlMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQeecDEGEGRTIIHCLNGGGRSG 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 392871558  688 TYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 737
Cdd:cd14636   157 MFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
PHA02738 PHA02738
hypothetical protein; Provisional
 770-1050 1.51e-19

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 91.14  E-value: 1.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  770 LEAEYQRLPSYRSWRTqhIGNQEENKKKNRNSNVVPYDFNRVPLKHElemskesepesdessdddsdsEETSKYINASFV 849
Cdd:PHA02738   27 ITREHQKVISEKVDGT--FNAEKKNRKLNRYLDAVCFDHSRVILPAE---------------------RNRGDYINANYV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  850 MSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELVNGDQEVCAQYWGEGKQT---YGDMEVEMKDTNRASAYT 926
Cdd:PHA02738   84 DGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGsirFGKFKITTTQVETHPHYV 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  927 LRTFELRHSKrKEPRTVYQYQCTTWKGEELPAEPKDLVSMIQDLKQKLPKASPEGMKY-HKHAS---ILVHCRDGSQQTG 1002
Cdd:PHA02738  164 KSTLLLTDGT-SATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCQKELAQESLQIgHNRLQpppIVVHCNAGLGRTP 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 392871558 1003 LFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYDII 1050
Cdd:PHA02738  243 CYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 533-737 4.29e-17

PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 81.11  E-value: 4.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  533 YINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRN-KCAEYWPsmEEGTRAFKDIVVTIND 611
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWP--EPGLQQYGPMEVEFVS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  612 HKRCPDYIIQKLNVAHKKEKATGR-EVTHIQFTSW-PDHGVPEDPHLLLKLRRRVNAF-SNFFSGPIVVHCSAGVGRTGT 688
Cdd:cd14637    79 GSADEDIVTRLFRVQNITRLQEGHlMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWqRESGEGRTVVHCLNGGGRSGT 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 392871558  689 YIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVE 737
Cdd:cd14637   159 YCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 497-738 4.69e-17

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 83.09  E-value: 4.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  497 DARKPHNQNKNRYVD-ILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIV 575
Cdd:PHA02740   41 EANKACAQAENKAKDeNLALHITRLLHRRIKLFNDEKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIV 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  576 MVTRCEEgnRNKCAEYWPSMEEGTRAFKDIVVTINDHKRCPDYIIQKLNVAHKKEKAtgREVTHIQFTSWPDHGVPEDPH 655
Cdd:PHA02740  121 LISRHAD--KKCFNQFWSLKEGCVITSDKFQIETLEIIIKPHFNLTLLSLTDKFGQA--QKISHFQYTAWPADGFSHDPD 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  656 -----------LLLKLRRRvNAFSNFfsGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGKVDVYGYVVKLRRQRCLMVQV 724
Cdd:PHA02740  197 afidffcniddLCADLEKH-KADGKI--APIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNC 273

                         250
                  ....*....|....
gi 392871558  725 EAQYILIHQALVEY 738
Cdd:PHA02740  274 LDDYVFCYHLIAAY 287
CD45 pfam12567
Leukocyte receptor CD45; This family of proteins is found in eukaryotes. Proteins in this ...
 49-102 1.30e-16

Leukocyte receptor CD45; This family of proteins is found in eukaryotes. Proteins in this family are typically between 77 and 1130 amino acids in length. The family is found in association with pfam00041. CD45 plays a critical role in T-cell receptor (TCR)-mediated signaling. CD45 interacts with SKAP55 which is a transcriptional activator of IL-2.


Pssm-ID: 432641  Cd Length: 59  Bit Score: 74.71  E-value: 1.30e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 392871558    49 VNYTYESSNQTFKADLKDVQNAKCGNEDCE-NVLNNLEECSQIkNISVSNDSCAP 102
Cdd:pfam12567    1 VEYTYNSENKSFTAKLNVNDNVECENNDCEnNELHNLQECEQI-NVSISHNSCTS 54
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 534-728 5.00e-13

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. YopH is an essential virulence determinant of the pathogenic bacterium by dephosphorylating several focal adhesion proteins including p130Cas in human epithelial cells, resulting in the disruption of focal adhesions and cell detachment from the extracellular matrix. It contains an N-terminal domain that contains signals required for TTSS-mediated delivery of YopH into host cells and a C-terminal catalytic PTP domain.


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 69.74  E-value: 5.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  534 INASYIDgFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRafkdivVTINDHK 613
Cdd:cd14559    18 LNANRVQ-IGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYFRQSGTYGS------VTVKSKK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  614 RCPDYIIQKLNVAHKKEKATGREVTH----IQFTSWPDHGvPEDPHLLLKLRRRVN----------------AFSNFFSG 673
Cdd:cd14559    91 TGKDELVDGLKADMYNLKITDGNKTItipvVHVTNWPDHT-AISSEGLKELADLVNksaeekrnfykskgssAINDKNKL 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392871558  674 PIVVHCSAGVGRTGTYIgidAMLEGLEAEGKVDVYGYVVKLRRQRC-LMVQVEAQY 728
Cdd:cd14559   170 LPVIHCRAGVGRTGQLA---AAMELNKSPNNLSVEDIVSDMRTSRNgKMVQKDEQL 222
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 842-1051 1.22e-10

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 63.83  E-value: 1.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  842 KYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELvnGDQEVCAQYWGEGKQ---TYGDMEVEMKD 918
Cdd:PHA02740   77 KVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRH--ADKKCFNQFWSLKEGcviTSDKFQIETLE 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  919 TNRASAYTLRTFELRHSKRKEpRTVYQYQCTTWKGEELPAEPK---DLVSMIQDLKQKLPKASPEGmkyhKHASILVHCR 995
Cdd:PHA02740  155 IIIKPHFNLTLLSLTDKFGQA-QKISHFQYTAWPADGFSHDPDafiDFFCNIDDLCADLEKHKADG----KIAPIIIDCI 229

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392871558  996 DGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYDIIA 1051
Cdd:PHA02740  230 DGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIA 285
PTP_N pfam12453
Protein tyrosine phosphatase N terminal; This domain family is found in eukaryotes, and is ...
 7-31 4.41e-08

Protein tyrosine phosphatase N terminal; This domain family is found in eukaryotes, and is approximately 30 amino acids in length. The family is found in association with pfam00041. There is a single completely conserved residue L that may be functionally important. This family consists of various protein tyrosine phosphatase haematopoietic receptors, e.g. CD45, which dephosphorylate growth stimulating proteins. This limits growth signalling in haematopoietic cells.


Pssm-ID: 403599  Cd Length: 26  Bit Score: 49.85  E-value: 4.41e-08
                           10        20
                   ....*....|....*....|....*
gi 392871558     7 LKLLAFGFALLDTEVFVTGQTPTPS 31
Cdd:pfam12453    1 LKLLAFGFAFLDTEVFVTGESLTSS 25
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
645-733 7.11e-07

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 49.58  E-value: 7.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  645 WPDHGVPEDPHL---LLKLRRRVNAfsnffSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEgkvDVYGYVvklRRQRCLM 721
Cdd:COG2453    55 IPDFGAPDDEQLqeaVDFIDEALRE-----GKKVLVHCRGGIGRTGTVAAAYLVLLGLSAE---EALARV---RAARPGA 123

                          90
                  ....*....|..
gi 392871558  722 VQVEAQYILIHQ 733
Cdd:COG2453   124 VETPAQRAFLER 135
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 311-390 1.97e-06

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 47.11  E-value: 1.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  311 PDKVNGMKTSRPTDNSINVTCGPPYETNGPKTFYILVVRSGGS----FVTKYNKTNCQFYVDNLYYSTDYEFLVSFHNGV 386
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSgdwkEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80


                  ....
gi 392871558  387 YEGD 390
Cdd:cd00063    81 GESP 84
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 990-1048 3.87e-06

cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of eukaryotic cyclin-dependent kinase inhibitor 3 (CDKN3) and related archaeal and bacterial proteins. CDKN3 is also known as kinase-associated phosphatase (KAP), CDK2-associated dual-specificity phosphatase, cyclin-dependent kinase interactor 1 (CDI1), or cyclin-dependent kinase-interacting protein 2 (CIP2). It has been characterized as dual-specificity phosphatase, which function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and protein-tyrosine-phosphatase (EC 3.1.3.48). It dephosphorylates CDK2 at a threonine residue in a cyclin-dependent manner, resulting in the inhibition of G1/S cell cycle progression. It also interacts with CDK1 and controls progression through mitosis by dephosphorylating CDC2. CDKN3 may also function as a tumor suppressor; its loss of function was found in a variety of cancers including glioblastoma and hepatocellular carcinoma. However, it has also been found over-expressed in many cancers such as breast, cervical, lung and prostate cancers, and may also have an oncogenic function.


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 48.03  E-value: 3.87e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 392871558  990 ILVHCRDGSQQTGLFCALFnLLEsaeTEDVVDVFQVVKSLRKARPGVVCSYEQYQFLYD 1048
Cdd:cd14505   109 VLIHCKGGLGRTGLIAACL-LLE---LGDTLDPEQAIAAVRALRPGAIQTPKQENFLHQ 163
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 230-288 7.38e-05

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 42.48  E-value: 7.38e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392871558  230 LVSWPEPvskPESASKPHGYVLCYK----NNSEKCKSLPNNVTSFEVESLKPYKYYEVSLLAY 288
Cdd:cd00063    18 TLSWTPP---EDDGGPITGYVVEYRekgsGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAV 77
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
984-1049 8.07e-05

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 43.81  E-value: 8.07e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392871558  984 YHKHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVfqvvksLRKARPGVVCSYEQYQFLYDI 1049
Cdd:COG2453    77 LREGKKVLVHCRGGIGRTGTVAAAYLVLLGLSAEEALAR------VRAARPGAVETPAQRAFLERF 136
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 673-718 1.27e-04

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 42.72  E-value: 1.27e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 392871558  673 GPIVVHCSAGVGRTGTYIGIDAMLegleaEGKVDVYGYVVKLRRQR 718
Cdd:cd14494    57 EPVLVHCKAGVGRTGTLVACYLVL-----LGGMSAEEAVRIVRLIR 97
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 990-1048 1.73e-04

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 42.34  E-value: 1.73e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  990 ILVHCRDGSQQTGLFCALFNLLESAETedvvdVFQVVKSLRKARPGVVCSY-EQYQFLYD 1048
Cdd:cd14494    59 VLVHCKAGVGRTGTLVACYLVLLGGMS-----AEEAVRIVRLIRPGGIPQTiEQLDFLIK 113
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 587-733 4.86e-04

cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of eukaryotic cyclin-dependent kinase inhibitor 3 (CDKN3) and related archaeal and bacterial proteins. CDKN3 is also known as kinase-associated phosphatase (KAP), CDK2-associated dual-specificity phosphatase, cyclin-dependent kinase interactor 1 (CDI1), or cyclin-dependent kinase-interacting protein 2 (CIP2). It has been characterized as dual-specificity phosphatase, which function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and protein-tyrosine-phosphatase (EC 3.1.3.48). It dephosphorylates CDK2 at a threonine residue in a cyclin-dependent manner, resulting in the inhibition of G1/S cell cycle progression. It also interacts with CDK1 and controls progression through mitosis by dephosphorylating CDC2. CDKN3 may also function as a tumor suppressor; its loss of function was found in a variety of cancers including glioblastoma and hepatocellular carcinoma. However, it has also been found over-expressed in many cancers such as breast, cervical, lung and prostate cancers, and may also have an oncogenic function.


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 41.87  E-value: 4.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392871558  587 KCAEYWPSMEEGTRAFK----DIVVTIndhkrCPDYIIQKLNVA--HKKEKATGREVTHIQFtswPDHGVPEDP----HL 656
Cdd:cd14505    24 KFKDHRRDLQADLEELKdqgvDDVVTL-----CTDGELEELGVPdlLEQYQQAGITWHHLPI---PDGGVPSDIaqwqEL 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392871558  657 LLKLRRRVNAFSNffsgpIVVHCSAGVGRTGTyigIDAMLEgLEAEGKVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 733
Cdd:cd14505    96 LEELLSALENGKK-----VLIHCKGGLGRTGL---IAACLL-LELGDTLDPEQAIAAVRALRPGAIQTPKQENFLHQ 163
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 673-695 1.07e-03

C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif.


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 41.28  E-value: 1.07e-03
                          10        20
                  ....*....|....*....|...
gi 392871558  673 GPIVVHCSAGVGRTGTYIGIDAM 695
Cdd:cd14499   110 GAIAVHCKAGLGRTGTLIACYLM 132
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 669-727 3.64e-03

dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as VH1-like phosphatase Z (VHZ) or low molecular mass dual specificity phosphatase 3 (LDP-3), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP23 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It is able to enhance activation of JNK and p38 MAPK, and has been shown to dephosphorylate p44-ERK1 (MAPK3) in vitro. It has been associated with cell growth and human primary cancers. It has also been identified as a cell-cell adhesion regulatory protein; it promotes the dephosphorylation of beta-catenin at Tyr 142 and enhances the interaction between alpha- and beta-catenin.


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 39.18  E-value: 3.64e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392871558  669 NFFSGPIVVHCSAGVGRTGT----YIGIDAMLEGLEAegkvdvygyVVKLRRQRCLMVQVEAQ 727
Cdd:cd14504    79 NAKNEAVLVHCLAGKGRTGTmlacYLVKTGKISAVDA---------INEIRRIRPGSIETSEQ 132
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 644-690 4.94e-03

protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine phosphatase domain-containing protein 1 (PTPDC1) is an uncharacterized non-receptor class protein-tyrosine phosphatase (PTP). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Small interfering RNA (siRNA) knockdown of the ptpdc1 gene is associated with elongated cilia.


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 39.64  E-value: 4.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 392871558  644 SWPDHGVPEdPHLLLKLRRrVNAFSNFFSGPIVVHCSAGVGRTGTYI 690
Cdd:cd14506    83 GWKDYGVPS-LTTILDIVK-VMAFALQEGGKVAVHCHAGLGRTGVLI 127
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 311-381 9.09e-03

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 36.44  E-value: 9.09e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392871558    311 PDKVNGMKTSRPTDNSINVTCGPPYETN--GPKTFYILVVRSGGSFVTKYNKTN--CQFYVDNLYYSTDYEFLVS 381
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGitGYIVGYRVEYREEGSEWKEVNVTPssTSYTLTGLKPGTEYEFRVR 75
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH