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Conserved domains on  [gi|1907067822|ref|XP_036018687|]
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tyrosine-protein phosphatase non-receptor type 18 isoform X3 [Mus musculus]

Protein Classification

protein-tyrosine phosphatase family protein( domain architecture ID 1000023)

cys-based protein-tyrosine phosphatase (PTP) family protein may be a PTP or a dual-specificity phosphatase (DUSP or DSP), and may catalyze the dephosphorylation of target phosphoproteins at tyrosine or tyrosine and serine/threonine residues, respectively

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 27-260 6.67e-139

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.


The actual alignment was detected with superfamily member cd14603:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 266  Bit Score: 397.66  E-value: 6.67e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  27 AREFSDIKARSVAWKSEGVCSTKAGSRLGNTNKNRYKDVVAYDETRVILSLLQEEGHGDYINANFIR------------- 93
Cdd:cd14603     1 AGEFSEIRACSAAFKADYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKgvdgsrayiatqg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  94 -------------------VILMACQETENGRRKCERYWAREQEPLKAGPFCITLTKETTLNADITLRTLQVTFQKEFRS 154
Cdd:cd14603    81 plshtvldfwrmiwqygvkVILMACREIEMGKKKCERYWAQEQEPLQTGPFTITLVKEKRLNEEVILRTLKVTFQKESRS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 155 VHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFQVVLE 234
Cdd:cd14603   161 VSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIFDVVLE 240

                         250       260
                  ....*....|....*....|....*.
gi 1907067822 235 MRKQRPAAVQTEEQYRFLYHTVAQLF 260
Cdd:cd14603   241 MRKQRPAAVQTEEQYEFLYHTVAQMF 266
PRK12323 super family cl46901
DNA polymerase III subunit gamma/tau;
299-420 1.73e-03

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK14951:

Pssm-ID: 481241 [Multi-domain]  Cd Length: 618  Bit Score: 40.47  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 299 RPPGGVLRSI-SVPAPPTLPMADTYAVVQKRGASAGTGPGPRAPTSTDTPIYSQVA---PRAQRPVAHTEDAQGTTALRR 374
Cdd:PRK14951  365 KPAAAAEAAApAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAappAPVAAPAAAAPAAAPAAAPAA 444

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907067822 375 VPADQNSSGPDAYEEVTDGAQTGGLGFNLRIGRPKGPRDPPAEWTR 420
Cdd:PRK14951  445 VALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTP 490
 
Name Accession Description Interval E-value
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 27-260 6.67e-139

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: 397.66  E-value: 6.67e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  27 AREFSDIKARSVAWKSEGVCSTKAGSRLGNTNKNRYKDVVAYDETRVILSLLQEEGHGDYINANFIR------------- 93
Cdd:cd14603     1 AGEFSEIRACSAAFKADYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKgvdgsrayiatqg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  94 -------------------VILMACQETENGRRKCERYWAREQEPLKAGPFCITLTKETTLNADITLRTLQVTFQKEFRS 154
Cdd:cd14603    81 plshtvldfwrmiwqygvkVILMACREIEMGKKKCERYWAQEQEPLQTGPFTITLVKEKRLNEEVILRTLKVTFQKESRS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 155 VHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFQVVLE 234
Cdd:cd14603   161 VSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIFDVVLE 240

                         250       260
                  ....*....|....*....|....*.
gi 1907067822 235 MRKQRPAAVQTEEQYRFLYHTVAQLF 260
Cdd:cd14603   241 MRKQRPAAVQTEEQYEFLYHTVAQMF 266
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
56-258 1.62e-80

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 247.93  E-value: 1.62e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  56 NTNKNRYKDVVAYDETRVILSllQEEGHGDYINANFI--------------------------------RVILMACQETE 103
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIdgykkpkkyiatqgplpntvedfwrmvweekvTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 104 NGRRKCERYWAREQE-PLKAGPFCITLTKETTLNADITLRTLQVTF--QKEFRSVHQLQYMSWPDHGVPSSSDHILTMVE 180
Cdd:pfam00102  79 KGREKCAQYWPEEEGeSLEYGDFTVTLKKEKEDEKDYTVRTLEVSNggSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907067822 181 EARCLQGLGP-GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 258
Cdd:pfam00102 159 KVRKSSLDGRsGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGE---VDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
26-258 2.09e-80

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 248.34  E-value: 2.09e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822   26 LAREFSDIKARSVawkseGVCSTKAGSRLGNTNKNRYKDVVAYDETRVILSLLQEEGHgDYINANFIR------------ 93
Cdd:smart00194   2 LEEEFEKLDRLKP-----DDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGS-DYINASYIDgpngpkayiatq 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822   94 --------------------VILMACQETENGRRKCERYWAREQ-EPLKAGPFCITLTKETTLnADITLRTLQVTFQKEF 152
Cdd:smart00194  76 gplpstvedfwrmvweqkvtVIVMLTELVEKGREKCAQYWPDEEgEPLTYGDITVTLKSVEKV-DDYTIRTLEVTNTGCS 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  153 --RSVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQtipPNFSLFQ 230
Cdd:smart00194 155 etRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAG---KEVDIFE 231

                          250       260
                   ....*....|....*....|....*...
gi 1907067822  231 VVLEMRKQRPAAVQTEEQYRFLYHTVAQ 258
Cdd:smart00194 232 IVKELRSQRPGMVQTEEQYIFLYRAILE 259
PHA02738 PHA02738
hypothetical protein; Provisional
 11-256 2.32e-32

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 124.65  E-value: 2.32e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  11 FLEQLEARDYREgaILAREFSDIkarsVAWKSEGVCStkagSRLGNTNKNRYKDVVAYDETRVILSllQEEGHGDYINAN 90
Cdd:PHA02738   14 FLALMEKSDCEE--VITREHQKV----ISEKVDGTFN----AEKKNRKLNRYLDAVCFDHSRVILP--AERNRGDYINAN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  91 FI--------------------------------RVILMACQETENGRRKCERYWAR-EQEPLKAGPFCITLTKETTLNA 137
Cdd:PHA02738   82 YVdgfeykkkficgqaptrqtcydfyrmlwmehvQIIVMLCKKKENGREKCFPYWSDvEQGSIRFGKFKITTTQVETHPH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 138 DITlRTLQVTFQKE-FRSVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQ-------------GLGPGPLCVHCSAGCGR 203
Cdd:PHA02738  162 YVK-STLLLTDGTSaTQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCQkelaqeslqighnRLQPPPIVVHCNAGLGR 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907067822 204 TGVLCAVDY-VRQLLLTQTIppnfSLFQVVLEMRKQRPAAVQTEEQYRFLYHTV 256
Cdd:PHA02738  241 TPCYCVVDIsISRFDACATV----SIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
54-252 1.94e-29

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 115.57  E-value: 1.94e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  54 LGNTNKNRYKDVVAYDETRVilsllQEEGhgDYINANFIRVI---------------------------------LMACQ 100
Cdd:COG5599    40 INGSPLNRFRDIQPYKETAL-----RANL--GYLNANYIQVIgnhryiatqypleeqledffqmlfdnntpvlvvLASDD 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 101 ETENGRRKCERYWaREQEplKAGPFCI--TLTKETTLNADITLRTLQVTFQ---KEFRSVHQLQYMSWPDHGVPSSS--- 172
Cdd:COG5599   113 EISKPKVKMPVYF-RQDG--EYGKYEVssELTESIQLRDGIEARTYVLTIKgtgQKKIEIPVLHVKNWPDHGAISAEalk 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 173 DHILTMVEEARCLQGLGpGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIpPNFSLFQVVLEMRKQR-PAAVQTEEQYRF 251
Cdd:COG5599   190 NLADLIDKKEKIKDPDK-LLPVVHCRAGVGRTGTLIACLALSKSINALVQ-ITLSVEEIVIDMRTSRnGGMVQTSEQLDV 267


                  .
gi 1907067822 252 L 252
Cdd:COG5599   268 L 268
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 299-420 1.73e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 40.47  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 299 RPPGGVLRSI-SVPAPPTLPMADTYAVVQKRGASAGTGPGPRAPTSTDTPIYSQVA---PRAQRPVAHTEDAQGTTALRR 374
Cdd:PRK14951  365 KPAAAAEAAApAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAappAPVAAPAAAAPAAAPAAAPAA 444

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907067822 375 VPADQNSSGPDAYEEVTDGAQTGGLGFNLRIGRPKGPRDPPAEWTR 420
Cdd:PRK14951  445 VALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTP 490
 
Name Accession Description Interval E-value
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 27-260 6.67e-139

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: 397.66  E-value: 6.67e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  27 AREFSDIKARSVAWKSEGVCSTKAGSRLGNTNKNRYKDVVAYDETRVILSLLQEEGHGDYINANFIR------------- 93
Cdd:cd14603     1 AGEFSEIRACSAAFKADYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKgvdgsrayiatqg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  94 -------------------VILMACQETENGRRKCERYWAREQEPLKAGPFCITLTKETTLNADITLRTLQVTFQKEFRS 154
Cdd:cd14603    81 plshtvldfwrmiwqygvkVILMACREIEMGKKKCERYWAQEQEPLQTGPFTITLVKEKRLNEEVILRTLKVTFQKESRS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 155 VHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFQVVLE 234
Cdd:cd14603   161 VSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIFDVVLE 240

                         250       260
                  ....*....|....*....|....*.
gi 1907067822 235 MRKQRPAAVQTEEQYRFLYHTVAQLF 260
Cdd:cd14603   241 MRKQRPAAVQTEEQYEFLYHTVAQMF 266
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 86-254 1.23e-91

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: 275.07  E-value: 1.23e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  86 YINANFIR--------------------------------VILMACQETENGRRKCERYWAREQEP-LKAGPFCITLTKE 132
Cdd:cd14542     1 YINANFIKgvsgskayiatqgplpntvldfwrmiweynvqVIVMACREFEMGKKKCERYWPEEGEEqLQFGPFKISLEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 133 TTLNADITLRTLQVTFQKEFRSVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDY 212
Cdd:cd14542    81 KRVGPDFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICAIDY 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1907067822 213 VRQLLLTQTIPPNFSLFQVVLEMRKQRPAAVQTEEQYRFLYH 254
Cdd:cd14542   161 VWNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 59-260 6.78e-84

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: 256.31  E-value: 6.78e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  59 KNRYKDVVAYDETRVILSLLQEEGHGDYINANFIR--------------------------------VILMACQETENGR 106
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKgvygprayiatqgplsttlldfwrmiweysvlIIVMACMEFEMGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 107 RKCERYWARE-QEPLKAGPFCITLTKETTLNaDITLRTLQVTFQKEFRSVHQLQYMSWPDHGVPSSSDHILTMVEEARCL 185
Cdd:cd14602    81 KKCERYWAEPgEMQLEFGPFSVTCEAEKRKS-DYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCY 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907067822 186 QGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTVAQLF 260
Cdd:cd14602   160 QEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIELF 234
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
56-258 1.62e-80

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 247.93  E-value: 1.62e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  56 NTNKNRYKDVVAYDETRVILSllQEEGHGDYINANFI--------------------------------RVILMACQETE 103
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIdgykkpkkyiatqgplpntvedfwrmvweekvTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 104 NGRRKCERYWAREQE-PLKAGPFCITLTKETTLNADITLRTLQVTF--QKEFRSVHQLQYMSWPDHGVPSSSDHILTMVE 180
Cdd:pfam00102  79 KGREKCAQYWPEEEGeSLEYGDFTVTLKKEKEDEKDYTVRTLEVSNggSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907067822 181 EARCLQGLGP-GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 258
Cdd:pfam00102 159 KVRKSSLDGRsGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGE---VDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
26-258 2.09e-80

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 248.34  E-value: 2.09e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822   26 LAREFSDIKARSVawkseGVCSTKAGSRLGNTNKNRYKDVVAYDETRVILSLLQEEGHgDYINANFIR------------ 93
Cdd:smart00194   2 LEEEFEKLDRLKP-----DDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGS-DYINASYIDgpngpkayiatq 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822   94 --------------------VILMACQETENGRRKCERYWAREQ-EPLKAGPFCITLTKETTLnADITLRTLQVTFQKEF 152
Cdd:smart00194  76 gplpstvedfwrmvweqkvtVIVMLTELVEKGREKCAQYWPDEEgEPLTYGDITVTLKSVEKV-DDYTIRTLEVTNTGCS 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  153 --RSVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQtipPNFSLFQ 230
Cdd:smart00194 155 etRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAG---KEVDIFE 231

                          250       260
                   ....*....|....*....|....*...
gi 1907067822  231 VVLEMRKQRPAAVQTEEQYRFLYHTVAQ 258
Cdd:smart00194 232 IVKELRSQRPGMVQTEEQYIFLYRAILE 259
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 6-264 1.79e-79

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: 247.54  E-value: 1.79e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822   6 DLVRSFLEQLEA---RDYREGAILAREFSDIKARSVAWKSEGVCSTKAGSRLGNTNKNRYKDVVAYDETRVILSLLQEEG 82
Cdd:cd14604     4 EILKKFIERVQAmksTDHNGEDNFASDFMRLRRLSTKYRTEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  83 HGDYINANFIR--------------------------------VILMACQETENGRRKCERYWARE-QEPLKAGPFCITL 129
Cdd:cd14604    84 DSDYINANFIKgvygpkayiatqgplantvidfwrmiweynvaIIVMACREFEMGRKKCERYWPLYgEEPMTFGPFRISC 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 130 TKETTLNaDITLRTLQVTFQKEFRSVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCA 209
Cdd:cd14604   164 EAEQART-DYFIRTLLLEFQNETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICA 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907067822 210 VDYVRQLLLTQTIPPNFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTVAQLFSRTL 264
Cdd:cd14604   243 IDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEKQL 297
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 86-254 1.53e-63

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: 202.90  E-value: 1.53e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  86 YINANFI--------------------------------RVILMACQETENGRRKCERYWAREQE-PLKAGPFCITLTKE 132
Cdd:cd00047     1 YINASYIdgyrgpkeyiatqgplpntvedfwrmvweqkvSVIVMLTNLVEKGREKCERYWPEEGGkPLEYGDITVTLVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 133 TTLNaDITLRTLQVTFQK--EFRSVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAV 210
Cdd:cd00047    81 EELS-DYTIRTLELSPKGcsESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAI 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907067822 211 DYVRQLLLTQTIPpnfSLFQVVLEMRKQRPAAVQTEEQYRFLYH 254
Cdd:cd00047   160 DILLERLEAEGEV---DVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 86-254 1.43e-51

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: 172.43  E-value: 1.43e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  86 YINANFI---------------------------------RVILMACQETENGRRKCERYWAREQEPLKAGPFCITLTKE 132
Cdd:cd18533     1 YINASYItlpgtsskryiatqgplpatigdfwkmiwqnnvGVIVMLTPLVENGREKCDQYWPSGEYEGEYGDLTVELVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 133 TTLN-ADITLRTLQVTF-QKEFRSVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGP--GPLCVHCSAGCGRTGVLC 208
Cdd:cd18533    81 EENDdGGFIVREFELSKeDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASldPPIIVHCSAGVGRTGTFI 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907067822 209 AVDYVRQLL---LTQTIPPNFSL---FQVVLEMRKQRPAAVQTEEQYRFLYH 254
Cdd:cd18533   161 ALDSLLDELkrgLSDSQDLEDSEdpvYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 61-253 1.40e-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: 170.23  E-value: 1.40e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  61 RYKDVVAYDETRVILSLLQEEGHGDYINANFI--------------------------------RVILMACQETENGRRK 108
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIpgynsprefiatqgplpgtkddfwrmvweqnsHTIVMLTQCMEKGRVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 109 CERYWAREQEPLKAGPFCITLTKETTLnADITLRTLQVTFQKEFRSVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGL 188
Cdd:cd14548    81 CDHYWPFDQDPVYYGDITVTMLSESVL-PDWTIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIKQ 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907067822 189 GPGPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIPPnfslFQVVLEMRKQRPAAVQTEEQYRFLY 253
Cdd:cd14548   160 EKGPTIVHCSAGVGRTGTFIALDRlLQQIESEDYVDI----FGIVYDLRKHRPLMVQTEAQYIFLH 221
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 56-258 2.45e-49

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: 168.02  E-value: 2.45e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  56 NTNKNRYKDVVAYDETRVILSLLQEEGHG-DYINANFI---------------------------------------RVI 95
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRDPNVPGsDYINANYIrnenegpttdenaktyiatqgclentvsdfwsmvwqensRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  96 LMACQETENGRRKCERYWAREQEPLKAGPFCITLTKETTlNADITLRTLQVTFQKEF---RSVHQLQYMSWPDHGVPSSS 172
Cdd:cd14544    81 VMTTKEVERGKNKCVRYWPDEGMQKQYGPYRVQNVSEHD-TTDYTLRELQVSKLDQGdpiREIWHYQYLSWPDHGVPSDP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 173 DHILTMVEEARCLQG--LGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFQVVLEMRKQRPAAVQTEEQYR 250
Cdd:cd14544   160 GGVLNFLEDVNQRQEslPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDCDIDIQKTIQMVRSQRSGMVQTEAQYK 239


                  ....*...
gi 1907067822 251 FLYHTVAQ 258
Cdd:cd14544   240 FIYVAVAQ 247
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 28-253 4.21e-48

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: 165.23  E-value: 4.21e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  28 REFSDIKARSVAWKSEgvCSTKAGsrlgNTNKNRYKDVVAYDETRVILSLLQEEGHGDYINANF---------------- 91
Cdd:cd14543     7 EEYEDIRREPPAGTFL--CSLAPA----NQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFmdgykqknayiatqgp 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  92 ----------------IRVILMACQETENGRRKCERYWAREQEP-LKAGPFCITlTKETTLNADITLRTLQV----TFQK 150
Cdd:cd14543    81 lpktysdfwrmvweqkVLVIVMTTRVVERGRVKCGQYWPLEEGSsLRYGDLTVT-NLSVENKEHYKKTTLEIhnteTDES 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 151 efRSVHQLQYMSWPDHGVPSSSDHILTMVEE-----ARCLQGLGPG--------PLCVHCSAGCGRTGVLCAVDY-VRQL 216
Cdd:cd14543   160 --RQVTHFQFTSWPDFGVPSSAAALLDFLGEvrqqqALAVKAMGDRwkghppgpPIVVHCSAGIGRTGTFCTLDIcLSQL 237

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1907067822 217 LLTQTIppnfSLFQVVLEMRKQRPAAVQTEEQYRFLY 253
Cdd:cd14543   238 EDVGTL----NVMQTVRRMRTQRAFSIQTPDQYYFCY 270
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 47-258 3.44e-46

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: 160.05  E-value: 3.44e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  47 STKAGSRLGNTNKNRYKDVVAYDETRVILSLLQEEGHG-DYINANFI--------------------------------- 92
Cdd:cd14606     9 QRLEGQRPENKSKNRYKNILPFDHSRVILQGRDSNIPGsDYINANYVknqllgpdenaktyiasqgcleatvndfwqmaw 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  93 ----RVILMACQETENGRRKCERYWAREQEPLKAGPFCITLTKETTlNADITLRTLQVTF---QKEFRSVHQLQYMSWPD 165
Cdd:cd14606    89 qensRVIVMTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHD-TTEYKLRTLQVSPldnGELIREIWHYQYLSWPD 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 166 HGVPSSSDHILTMVEEARCLQGLGP--GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFQVVLEMRKQRPAAV 243
Cdd:cd14606   168 HGVPSEPGGVLSFLDQINQRQESLPhaGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLDCDIDIQKTIQMVRAQRSGMV 247

                         250
                  ....*....|....*
gi 1907067822 244 QTEEQYRFLYHTVAQ 258
Cdd:cd14606   248 QTEAQYKFIYVAIAQ 262
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 60-256 1.95e-40

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: 143.88  E-value: 1.95e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  60 NRYKDVVAYDETRVILSLLQEEGHGDYINANFI--------------------------------RVILMACQETENGRR 107
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMpgywssqefiatqgplpqtvgdfwrmiweqqsSTIVMLTNCMEAGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 108 KCERYWAREQEPLKAGPFCITLTKETTLNaDITLR--TLQVTFQKEFRSVHQLQYMSWPDHGVPSSSDHILTMVEEAR-- 183
Cdd:cd14619    81 KCEHYWPLDYTPCTYGHLRVTVVSEEVME-NWTVRefLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRqw 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907067822 184 CLQGLGPGPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIPPnfslFQVVLEMRKQRPAAVQTEEQYRFLYHTV 256
Cdd:cd14619   160 LDQTMSGGPTVVHCSAGVGRTGTLIALDVlLQQLQSEGLLGP----FSFVQKMRENRPLMVQTESQYVFLHQCI 229
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 154-258 3.78e-40

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: 138.65  E-value: 3.78e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  154 SVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGP--GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFslFQV 231
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDI--FDT 78

                           90       100
                   ....*....|....*....|....*..
gi 1907067822  232 VLEMRKQRPAAVQTEEQYRFLYHTVAQ 258
Cdd:smart00012  79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
154-258 3.78e-40

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 138.65  E-value: 3.78e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  154 SVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGP--GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFslFQV 231
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDI--FDT 78

                           90       100
                   ....*....|....*....|....*..
gi 1907067822  232 VLEMRKQRPAAVQTEEQYRFLYHTVAQ 258
Cdd:smart00404  79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 56-253 1.46e-39

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: 141.77  E-value: 1.46e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  56 NTNKNRYKDVVAYDETRVILSLLQEEGHGDYINANFI--------------------------------RVILMACQETE 103
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCdgyrkqnayiatqgplpetfgdfwrmvweqrsATIVMMTKLEE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 104 NGRRKCERYW-AREQEplKAGPFCITLTKETTLnADITLRTLQV--TFQKEFRSVHQLQYMSWPDHGVPsssDHILTMVE 180
Cdd:cd14553    83 RSRVKCDQYWpTRGTE--TYGLIQVTLLDTVEL-ATYTVRTFALhkNGSSEKREVRQFQFTAWPDHGVP---EHPTPFLA 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907067822 181 EARCLQGLGP---GPLCVHCSAGCGRTGVLCAVD-YVRQLLLTQTIppnfSLFQVVLEMRKQRPAAVQTEEQYRFLY 253
Cdd:cd14553   157 FLRRVKACNPpdaGPIVVHCSAGVGRTGCFIVIDsMLERIKHEKTV----DIYGHVTCLRAQRNYMVQTEDQYIFIH 229
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 60-253 1.82e-39

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: 141.23  E-value: 1.82e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  60 NRYKDVVAYDETRVILSLLQEEGHGDYINANFI--------------------------------RVILMACQETENGRR 107
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIpgytspqefiatqgplkktiedfwrlvweqqvCNIIMLTVGMENGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 108 KCERYWAREQEPLKAGPFCITLTKETTLNaDITLRTLQV---TFQKEfRSVHQLQYMSWPDHGVPSSSDHILTMVEEAR- 183
Cdd:cd14618    81 LCDHYWPSESTPVSYGHITVHLLAQSSED-EWTRREFKLwheDLRKE-RRVKHLHYTAWPDHGIPESTSSLMAFRELVRe 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907067822 184 -CLQGLGPGPLCVHCSAGCGRTGVLCAVD-YVRQLLLTQTIppnfSLFQVVLEMRKQRPAAVQTEEQYRFLY 253
Cdd:cd14618   159 hVQATKGKGPTLVHCSAGVGRSGTFIALDrLLRQLKEEKVV----DVFNTVYILRMHRYLMIQTLSQYIFLH 226
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 86-258 1.86e-39

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: 140.59  E-value: 1.86e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  86 YINANFIR----------------------------------VILMACQETENGRRKCERYWARE-QEPL-KAGPFCITL 129
Cdd:cd14538     1 YINASHIRipvggdtyhyiacqgplpnttgdfwqmvweqkseVIAMVTQDVEGGKVKCHRYWPDSlNKPLiCGGRLEVSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 130 TKETTLNaDITLRTLQVTFQK--EFRSVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQglGPGPLCVHCSAGCGRTGVL 207
Cdd:cd14538    81 EKYQSLQ-DFVIRRISLRDKEtgEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIH--NSGPIVVHCSAGIGRTGVL 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907067822 208 CAVDYVrQLLLTQTIPpnFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 258
Cdd:cd14538   158 ITIDVA-LGLIERDLP--FDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 56-256 3.30e-39

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: 141.31  E-value: 3.30e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  56 NTNKNRYKDVVAYDETRVILSL--LQEEGhGDYINANFI----------------------------------------R 93
Cdd:cd14605     2 NKNKNRYKNILPFDHTRVVLHDgdPNEPV-SDYINANIImpefetkcnnskpkksyiatqgclqntvndfwrmvfqensR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  94 VILMACQETENGRRKCERYWAREQEPLKAGPFCITLTKETTLNaDITLRTL---QVTFQKEFRSVHQLQYMSWPDHGVPS 170
Cdd:cd14605    81 VIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAH-DYILRELklsKVGQGNTERTVWQYHFRTWPDHGVPS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 171 SSDHILTMVEEARCLQG--LGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFQVVLEMRKQRPAAVQTEEQ 248
Cdd:cd14605   160 DPGGVLDFLEEVHHKQEsiMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIQMVRSQRSGMVQTEAQ 239


                  ....*...
gi 1907067822 249 YRFLYHTV 256
Cdd:cd14605   240 YRFIYMAV 247
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 41-252 4.96e-39

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: 141.53  E-value: 4.96e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  41 KSEGVCSTKAgsRLG-NTNKNRYKDVVAYDETRVILsllqeEGHGDYINANFIR-------------------------- 93
Cdd:cd14600    26 KKPGLAITCA--KLPqNMDKNRYKDVLPYDATRVVL-----QGNEDYINASYVNmeipsanivnkyiatqgplphtcaqf 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  94 ----------VILMACQETENGRRKCERYWAREQEPLKAGPFCITLTKETTLNADITlRTLQVTFQK--EFRSVHQLQYM 161
Cdd:cd14600    99 wqvvweqklsLIVMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVF-REMLLTNTQtgEERTVTHLQYV 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 162 SWPDHGVPSSSDHILTMVEEARCLQgLGPGPLCVHCSAGCGRTGVLCAVDYVrqLLLTQTIPPNFSLfQVVLEMRKQRPA 241
Cdd:cd14600   178 AWPDHGVPDDSSDFLEFVNYVRSKR-VENEPVLVHCSAGIGRTGVLVTMETA--MCLTERNQPVYPL-DIVRKMRDQRAM 253

                         250
                  ....*....|.
gi 1907067822 242 AVQTEEQYRFL 252
Cdd:cd14600   254 MVQTSSQYKFV 264
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 56-256 6.95e-39

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: 140.02  E-value: 6.95e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  56 NTNKNRYKDVVAYDETRVILSLLQEEGHGDYINANFI--------------------------------RVILMACQETE 103
Cdd:cd14614    12 NRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIpgynspqeyiatqgplpetrndfwkmvlqqksQIIVMLTQCNE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 104 NGRRKCERYWAREQEPLKAGPFCITLTKETTLNaDITLRTLQVTFQKEFRSVHQLQYMSWPDHGVPS--SSDHILTMVEE 181
Cdd:cd14614    92 KRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQP-DWAIREFRVSYADEVQDVMHFNYTAWPDHGVPTanAAESILQFVQM 170

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907067822 182 ARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTV 256
Cdd:cd14614   171 VRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEF---VDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 242
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 56-258 1.01e-38

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: 139.39  E-value: 1.01e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  56 NTNKNRYKDVVAYDETRVILSLLQEEGHGDYINANFIR--------------------------------VILMACQETE 103
Cdd:cd14630     3 NRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDgyhrprhyiatqgpmqetvkdfwrmiwqensaSVVMVTNLVE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 104 NGRRKCERYWAREQEPLkaGPFCITLTkETTLNADITLRTLqvTFQK----EFRSVHQLQYMSWPDHGVPSSSDHILTMV 179
Cdd:cd14630    83 VGRVKCVRYWPDDTEVY--GDIKVTLI-ETEPLAEYVIRTF--TVQKkgyhEIREIRQFHFTSWPDHGVPCYATGLLGFV 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907067822 180 EEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 258
Cdd:cd14630   158 RQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGV---VDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 60-254 4.95e-38

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: 137.14  E-value: 4.95e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  60 NRYKDVVAYDETRVILSLLQEEGHGDYINANFIR---------------------------------VILMACQETENgR 106
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRgydgeekayiatqgplpntvadfwrmvwqektpIIVMITNLTEA-K 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 107 RKCERYWArEQEPLKAGPFCITL--TKETTlnaDITLRTLQVTFQKEFRSVHQLQYMSWPDHGVPSSSDHILTM---VEE 181
Cdd:cd14547    80 EKCAQYWP-EEENETYGDFEVTVqsVKETD---GYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLvqeVEE 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907067822 182 ARcLQGLGPGPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIppnfSLFQVVLEMRKQRPAAVQTEEQYRFLYH 254
Cdd:cd14547   156 AR-QTEPHRGPIVVHCSAGIGRTGCFIATSIgCQQLREEGVV----DVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 56-256 1.69e-37

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: 136.11  E-value: 1.69e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  56 NTNKNRYKDVVAYDETRVilsLLQEEghGDYINANFIR----------------------------------VILMACQE 101
Cdd:cd14597     3 NRKKNRYKNILPYDTTRV---PLGDE--GGYINASFIKmpvgdeefvyiacqgplpttvadfwqmvweqkstVIAMMTQE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 102 TENGRRKCERYWARE-------QEPLKagpfcITLTKETTL-NADITLRTLQVTFQKEFRSVHQLQYMSWPDHGVPSSSD 173
Cdd:cd14597    78 VEGGKIKCQRYWPEIlgkttmvDNRLQ-----LTLVRMQQLkNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPE 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 174 HILTMVEEARCLQGLgpGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFQVVLEMRKQRPAAVQTEEQYRFLY 253
Cdd:cd14597   153 QLLTFISYMRHIHKS--GPIITHCSAGIGRSGTLICIDVVLGLISKDL---DFDISDIVRTMRLQRHGMVQTEDQYIFCY 227


                  ...
gi 1907067822 254 HTV 256
Cdd:cd14597   228 QVI 230
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 60-253 1.73e-36

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: 133.12  E-value: 1.73e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  60 NRYKDVVAYDETRVILSLLQEEGHGDYINANFI--------------------------------RVILMACQETENGRR 107
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIpgnnfrreyiatqgplpgtkddfwkmvweqnvHNIVMVTQCVEKGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 108 KCERYWAREQEPLKAGPFCITLTKETTLnADITLRTLQVTFQKEFRS---VHQLQYMSWPDHGVPSSSDHILTMVEEARC 184
Cdd:cd14617    81 KCDHYWPADQDSLYYGDLIVQMLSESVL-PEWTIREFKICSEEQLDAprlVRHFHYTVWPDHGVPETTQSLIQFVRTVRD 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907067822 185 L--QGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFQVVLEMRKQRPAAVQTEEQYRFLY 253
Cdd:cd14617   160 YinRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKD---SVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 59-253 2.77e-36

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: 132.90  E-value: 2.77e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  59 KNRYKDVVAYDETRVILSLLQEEGhgDYINANFIRV--------------------------------ILMACQETENGR 106
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQGDN--DYINASLVEVeeakrsyiltqgplpntsghfwqmvweqnskaVIMLNKLMEKGQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 107 RKCERYWAREQEP---LKAGPFCITLTKETTlNADITLRTLQVTFQK--EFRSVHQLQYMSWPDHGVPSSSD---HILTM 178
Cdd:cd14545    79 IKCAQYWPQGEGNamiFEDTGLKVTLLSEED-KSYYTVRTLELENLKtqETREVLHFHYTTWPDFGVPESPAaflNFLQK 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907067822 179 VEEARCLQGlGPGPLCVHCSAGCGRTGVLCAVDYVrQLLLTQTIPPNFSLFQVVLEMRKQRPAAVQTEEQYRFLY 253
Cdd:cd14545   158 VRESGSLSS-DVGPPVVHCSAGIGRSGTFCLVDTC-LVLIEKGNPSSVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 60-252 4.42e-36

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: 132.25  E-value: 4.42e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  60 NRYKDVVAYDETRVILSLlQEEGHGDYINANF--------------------------------IRVILMACQETENGRR 107
Cdd:cd14615     1 NRYNNVLPYDISRVKLSV-QSHSTDDYINANYmpgynskkefiaaqgplpntvkdfwrmvweknVYAIVMLTKCVEQGRT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 108 KCERYWAREQePLKAGPFCITLTKETTLnADITLRTLQVTFQK--EFRSVHQLQYMSWPDHGVPSSSDHILTMVEEAR-- 183
Cdd:cd14615    80 KCEEYWPSKQ-KKDYGDITVTMTSEIVL-PEWTIRDFTVKNAQtnESRTVRHFHFTSWPDHGVPETTDLLINFRHLVRey 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 184 CLQGLGPGPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIppnfSLFQVVLEMRKQRPAAVQTEEQYRFL 252
Cdd:cd14615   158 MKQNPPNSPILVHCSAGVGRTGTFIAIDRlIYQIENENVV----DVYGIVYDLRMHRPLMVQTEDQYVFL 223
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 56-272 2.02e-34

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: 128.99  E-value: 2.02e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  56 NTNKNRYKDVVAYDETRVILsllqEEGHGDYINANFIRV--------------------------------ILMACQETE 103
Cdd:cd14608    25 NKNRNRYRDVSPFDHSRIKL----HQEDNDYINASLIKMeeaqrsyiltqgplpntcghfwemvweqksrgVVMLNRVME 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 104 NGRRKCERYWAREQEplKAGPFCITLTKETTLNADI----TLRTLQVT--FQKEFRSVHQLQYMSWPDHGVPSSSDHILT 177
Cdd:cd14608   101 KGSLKCAQYWPQKEE--KEMIFEDTNLKLTLISEDIksyyTVRQLELEnlTTQETREILHFHYTTWPDFGVPESPASFLN 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 178 MVEEARCLQGLGP--GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFQVVLEMRKQRPAAVQTEEQYRFLYHT 255
Cdd:cd14608   179 FLFKVRESGSLSPehGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLA 258

                         250
                  ....*....|....*..
gi 1907067822 256 VAQLFSRTLQDTSPHYQ 272
Cdd:cd14608   259 VIEGAKFIMGDSSVQDQ 275
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 56-255 2.22e-34

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: 128.03  E-value: 2.22e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  56 NTNKNRYKDVVAYDETRVILSLLQEEGHGDYINANFI--------------------------------RVILMACQETE 103
Cdd:cd14554     6 NKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIdgyrqrgayiatqgplaettedfwrmlwehnsTIIVMLTKLRE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 104 NGRRKCERYWAREQEpLKAGPFCITLTKETTLNADItLRTLQVTFQK--EFRSVHQLQYMSWPDHGVPSSSDHIL---TM 178
Cdd:cd14554    86 MGREKCHQYWPAERS-ARYQYFVVDPMAEYNMPQYI-LREFKVTDARdgQSRTVRQFQFTDWPEQGVPKSGEGFIdfiGQ 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907067822 179 VEEARCLQGlGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLYHT 255
Cdd:cd14554   164 VHKTKEQFG-QEGPITVHCSAGVGRTGVFITLSIVLERMRYEGV---VDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 86-253 2.28e-34

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: 126.70  E-value: 2.28e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  86 YINANFI--------------------------------RVILMACQETENGRRKCERYWAREQEPlKAGPFCITLtKET 133
Cdd:cd14549     1 YINANYVdgynkarayiatqgplpstfddfwrmvweqnsAIIVMITNLVERGRRKCDQYWPKEGTE-TYGNIQVTL-LST 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 134 TLNADITLRTLQVTFQK--------EFRSVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTG 205
Cdd:cd14549    79 EVLATYTVRTFSLKNLKlkkvkgrsSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1907067822 206 VLCAVD-YVRQLLLTQTIppnfSLFQVVLEMRKQRPAAVQTEEQYRFLY 253
Cdd:cd14549   159 TYIVIDsMLQQIQDKGTV----NVFGFLKHIRTQRNYLVQTEEQYIFIH 203
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 94-256 7.99e-34

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: 125.63  E-value: 7.99e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  94 VILMACQETENGRRKCERYWARE-QEPLKAGPFCITLTKETTLNaDITLRTLQVTFQK--EFRSVHQLQYMSWPDHGVPS 170
Cdd:cd14596    43 VIAMMTREVERGKVKCHRYWPETlQEPMELENYQLRLENYQALQ-YFIIRIIKLVEKEtgENRLIKHLQFTTWPDHGTPQ 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 171 SSDHILTMVEEARCLQGLgpGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFQVVLEMRKQRPAAVQTEEQYR 250
Cdd:cd14596   122 SSDQLVKFICYMRKVHNT--GPIVVHCSAGIGRAGVLICVDVLLSLIEKDL---SFNIKDIVREMRQQRYGMIQTKDQYL 196


                  ....*.
gi 1907067822 251 FLYHTV 256
Cdd:cd14596   197 FCYKVV 202
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 85-251 1.84e-33

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: 124.75  E-value: 1.84e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  85 DYINANFI------------------------------------RVILMACQETENGRRKCERYWAREQEPLKAGPFCIT 128
Cdd:cd14541     1 DYINANYVnmeipgsgivnryiaaqgplpntcadfwqmvweqksTLIVMLTTLVERGRVKCHQYWPDLGETMQFGNLQIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 129 LTKETTlNADITLRTLQVTFQK--EFRSVHQLQYMSWPDHGVPSSSDHILTMVEEAR-CLQGLGPgPLCVHCSAGCGRTG 205
Cdd:cd14541    81 CVSEEV-TPSFAFREFILTNTNtgEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRqNRVGMVE-PTVVHCSAGIGRTG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907067822 206 VLCAVDYVrqLLLTQTIPPNFSLfQVVLEMRKQRPAAVQTEEQYRF 251
Cdd:cd14541   159 VLITMETA--MCLIEANEPVYPL-DIVRTMRDQRAMLIQTPSQYRF 201
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 56-258 1.98e-33

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: 126.30  E-value: 1.98e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  56 NTNKNRYKDVVAYDETRVILSLL--QEEGHGDYINANFIR--------------------------------VILMACQE 101
Cdd:cd17667    27 NKHKNRYINILAYDHSRVKLRPLpgKDSKHSDYINANYVDgynkakayiatqgplkstfedfwrmiweqntgIIVMITNL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 102 TENGRRKCERYWAREQEPlKAGPFCITLtKETTLNADITLRTLQVTFQK-------------EFRSVHQLQYMSWPDHGV 168
Cdd:cd17667   107 VEKGRRKCDQYWPTENSE-EYGNIIVTL-KSTKIHACYTVRRFSIRNTKvkkgqkgnpkgrqNERTVIQYHYTQWPDMGV 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 169 PSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFQVVLEMRKQRPAAVQTEEQ 248
Cdd:cd17667   185 PEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKS---TVNVLGFLKHIRTQRNYLVQTEEQ 261

                         250
                  ....*....|
gi 1907067822 249 YRFLYHTVAQ 258
Cdd:cd17667   262 YIFIHDALLE 271
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 55-258 2.32e-33

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: 125.33  E-value: 2.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  55 GNTNKNRYKDVVAYDETRVILSLLQ-EEGHGDYINANFIR---------------------------------VILMACQ 100
Cdd:cd14612    14 GHASKDRYKTILPNPQSRVCLRRAGsQEEEGSYINANYIRgydgkekayiatqgpmlntvsdfwemvwqeecpIIVMITK 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 101 ETEnGRRKCERYWAREQEPLkaGPFCITLT--KETtlnADITLRTLQVTFQKEFRSVHQLQYMSWPDHGVPSSSD---HI 175
Cdd:cd14612    94 LKE-KKEKCVHYWPEKEGTY--GRFEIRVQdmKEC---DGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPESAGpllRL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 176 LTMVEEARCLQGlGPGPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIppnfSLFQVVLEMRKQRPAAVQTEEQYRFLYH 254
Cdd:cd14612   168 VAEVEESRQTAA-SPGPIVVHCSAGIGRTGCFIATSIgCQQLKDTGKV----DILGIVCQLRLDRGGMIQTSEQYQFLHH 242


                  ....
gi 1907067822 255 TVAQ 258
Cdd:cd14612   243 TLAL 246
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 5-258 4.40e-33

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: 125.53  E-value: 4.40e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822   5 TDLVRSfLEQLEARDyreGAILAREFSDIK-ARSVAWKSEGVCSTKAgsrlgntnKNRYKDVVAYDETRVILSLLQEEGH 83
Cdd:cd14626     1 SDLADN-IERLKAND---GLKFSQEYESIDpGQQFTWENSNLEVNKP--------KNRYANVIAYDHSRVILTSVDGVPG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  84 GDYINANFI--------------------------------RVILMACQETENGRRKCERYW-AREQEplKAGPFCITLT 130
Cdd:cd14626    69 SDYINANYIdgyrkqnayiatqgplpetlsdfwrmvweqrtATIVMMTRLEEKSRVKCDQYWpIRGTE--TYGMIQVTLL 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 131 KETTLnADITLRTLQV--TFQKEFRSVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLC 208
Cdd:cd14626   147 DTVEL-ATYSVRTFALykNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFI 225

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907067822 209 AVD-YVRQLLLTQTIppnfSLFQVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 258
Cdd:cd14626   226 VIDaMLERMKHEKTV----DIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272
PHA02738 PHA02738
hypothetical protein; Provisional
 11-256 2.32e-32

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 124.65  E-value: 2.32e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  11 FLEQLEARDYREgaILAREFSDIkarsVAWKSEGVCStkagSRLGNTNKNRYKDVVAYDETRVILSllQEEGHGDYINAN 90
Cdd:PHA02738   14 FLALMEKSDCEE--VITREHQKV----ISEKVDGTFN----AEKKNRKLNRYLDAVCFDHSRVILP--AERNRGDYINAN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  91 FI--------------------------------RVILMACQETENGRRKCERYWAR-EQEPLKAGPFCITLTKETTLNA 137
Cdd:PHA02738   82 YVdgfeykkkficgqaptrqtcydfyrmlwmehvQIIVMLCKKKENGREKCFPYWSDvEQGSIRFGKFKITTTQVETHPH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 138 DITlRTLQVTFQKE-FRSVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQ-------------GLGPGPLCVHCSAGCGR 203
Cdd:PHA02738  162 YVK-STLLLTDGTSaTQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCQkelaqeslqighnRLQPPPIVVHCNAGLGR 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907067822 204 TGVLCAVDY-VRQLLLTQTIppnfSLFQVVLEMRKQRPAAVQTEEQYRFLYHTV 256
Cdd:PHA02738  241 TPCYCVVDIsISRFDACATV----SIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 92-258 2.25e-31

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: 119.10  E-value: 2.25e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  92 IRVILMACQETENGRRKCERYWAR---EQEPLKAGPFCITLTKETTlNADITLRTLQV--TFQKEFRSVHQLQYMSWPDH 166
Cdd:cd14540    41 VYLVVMVTAEEEGGREKCFRYWPTlggEHDALTFGEYKVSTKFSVS-SGCYTTTGLRVkhTLSGQSRTVWHLQYTDWPDH 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 167 GVPSSSDHILTMVEEA-----RCLQGLG----PGPLCVHCSAGCGRTGVLCAVDYVrQLLLTQTIPPNfsLFQVVLEMRK 237
Cdd:cd14540   120 GCPEDVSGFLDFLEEInsvrrHTNQDVAghnrNPPTLVHCSAGVGRTGVVILADLM-LYCLDHNEELD--IPRVLALLRH 196

                         170       180
                  ....*....|....*....|.
gi 1907067822 238 QRPAAVQTEEQYRFLYHTVAQ 258
Cdd:cd14540   197 QRMLLVQTLAQYKFVYNVLIQ 217
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 56-256 7.01e-31

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: 118.92  E-value: 7.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  56 NTNKNRYKDVVAYDETRVILsllqEEGHGDYINANFI--------------------------------RVILMACQETE 103
Cdd:cd14607    24 NRNRNRYRDVSPYDHSRVKL----QNTENDYINASLVvieeaqrsyiltqgplpntcchfwlmvwqqktKAVVMLNRIVE 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 104 NGRRKCERYW-AREQEPL--KAGPFCITLTKETtLNADITLRTLQVTFQK--EFRSVHQLQYMSWPDHGVPSSSDHILTM 178
Cdd:cd14607   100 KDSVKCAQYWpTDEEEVLsfKETGFSVKLLSED-VKSYYTVHLLQLENINsgETRTISHFHYTTWPDFGVPESPASFLNF 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 179 ---VEEARCLqGLGPGPLCVHCSAGCGRTGVLCAVDYVrQLLLTQTIPPNFSLFQVVLEMRKQRPAAVQTEEQYRFLYHT 255
Cdd:cd14607   179 lfkVRESGSL-SPEHGPAVVHCSAGIGRSGTFSLVDTC-LVLMEKKDPDSVDIKQVLLDMRKYRMGLIQTPDQLRFSYMA 256


                  .
gi 1907067822 256 V 256
Cdd:cd14607   257 V 257
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 56-258 1.33e-30

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: 118.61  E-value: 1.33e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  56 NTNKNRYKDVVAYDETRVILSLLQEEGHGDYINANFI--------------------------------RVILMACQETE 103
Cdd:cd14633    40 NRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIdgyhrpnhyiatqgpmqetiydfwrmvwhentASIIMVTNLVE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 104 NGRRKCERYWAREQEPLKagPFCITLTkETTLNADITLRTLQVTFQ--KEFRSVHQLQYMSWPDHGVPSSSDHILTMVEE 181
Cdd:cd14633   120 VGRVKCCKYWPDDTEIYK--DIKVTLI-ETELLAEYVIRTFAVEKRgvHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQ 196

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907067822 182 ARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 258
Cdd:cd14633   197 VKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGV---VDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 95-256 4.93e-30

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: 115.06  E-value: 4.93e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  95 ILMACQETENGRRKCERYWAREQEpLKAGPFCITLTKETtLNADITLRTLQVTFQKE--FRSVHQLQYMSWPDHGVPSSS 172
Cdd:cd14552    42 IVMLTEIKERSQNKCAQYWPEDGS-VSSGDITVELKDQT-DYEDYTLRDFLVTKGKGgsTRTVRQFHFHGWPEVGIPDNG 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 173 DHILTMVEEA-RCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRF 251
Cdd:cd14552   120 KGMIDLIAAVqKQQQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGV---LDVFQVVKSLRLQRPHMVQTLEQYEF 196


                  ....*
gi 1907067822 252 LYHTV 256
Cdd:cd14552   197 CYKVV 201
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
54-252 1.94e-29

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 115.57  E-value: 1.94e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  54 LGNTNKNRYKDVVAYDETRVilsllQEEGhgDYINANFIRVI---------------------------------LMACQ 100
Cdd:COG5599    40 INGSPLNRFRDIQPYKETAL-----RANL--GYLNANYIQVIgnhryiatqypleeqledffqmlfdnntpvlvvLASDD 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 101 ETENGRRKCERYWaREQEplKAGPFCI--TLTKETTLNADITLRTLQVTFQ---KEFRSVHQLQYMSWPDHGVPSSS--- 172
Cdd:COG5599   113 EISKPKVKMPVYF-RQDG--EYGKYEVssELTESIQLRDGIEARTYVLTIKgtgQKKIEIPVLHVKNWPDHGAISAEalk 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 173 DHILTMVEEARCLQGLGpGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIpPNFSLFQVVLEMRKQR-PAAVQTEEQYRF 251
Cdd:COG5599   190 NLADLIDKKEKIKDPDK-LLPVVHCRAGVGRTGTLIACLALSKSINALVQ-ITLSVEEIVIDMRTSRnGGMVQTSEQLDV 267


                  .
gi 1907067822 252 L 252
Cdd:COG5599   268 L 268
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 85-260 5.21e-28

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: 110.03  E-value: 5.21e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  85 DYINANFIRVIL---------MACQ---------------------------ETENGRRKCERYWAREQEPLKAGPFCIT 128
Cdd:cd14601     1 DYINANYINMEIpsssiinryIACQgplpntcsdfwqmtweqgssmvvmlttQVERGRVKCHQYWPEPSGSSSYGGFQVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 129 LTKETTlNADITLRTLQVTFQ--KEFRSVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGV 206
Cdd:cd14601    81 CHSEEG-NPAYVFREMTLTNLekNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTGV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907067822 207 LCAVDYVrqLLLTQTIPPNFSLfQVVLEMRKQRPAAVQTEEQYRFLYHTVAQLF 260
Cdd:cd14601   160 LITMETA--MCLIECNQPVYPL-DIVRTMRDQRAMMIQTPSQYRFVCEAILKVY 210
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 60-253 6.48e-28

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: 110.00  E-value: 6.48e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  60 NRYKDVVAYDETRVilSLLQEEG--HGDYINANFI--------------------------------RVILMACQETENG 105
Cdd:cd14616     1 NRFPNIKPYNNNRV--KLIADAGvpGSDYINASYIsgylcpnefiatqgplpgtvgdfwrmvwetraKTIVMLTQCFEKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 106 RRKCERYWAREQEPLKA-GPFCITLTKETTlNADITLRTLQVTFQKEFRSVHQLQYMSWPDHGVPSSSDHILTMVEEARC 184
Cdd:cd14616    79 RIRCHQYWPEDNKPVTVfGDIVITKLMEDV-QIDWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRA 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907067822 185 LQGLGPGPLCVHCSAGCGRTGVLCAVDYvrqllLTQTIPPN--FSLFQVVLEMRKQRPAAVQTEEQYRFLY 253
Cdd:cd14616   158 SRAHDNTPMIVHCSAGVGRTGVFIALDH-----LTQHINDHdfVDIYGLVAELRSERMCMVQNLAQYIFLH 223
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 61-258 9.52e-28

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: 109.75  E-value: 9.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  61 RYKDVVAYDETRVILSLLQEEGHGDYINANFIR--------------------------------VILMACQETENGRRK 108
Cdd:cd14623     1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDgyrqkdsyiasqgplqhtiedfwrmiwewkscSIVMLTELEERGQEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 109 CERYWAREQEpLKAGPFCITLTKETTLNAdITLRTLQVTFQKE--FRSVHQLQYMSWPDHGVPSSSDHILTMVEEA-RCL 185
Cdd:cd14623    81 CAQYWPSDGS-VSYGDITIELKKEEECES-YTVRDLLVTNTREnkSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVqKQQ 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907067822 186 QGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 258
Cdd:cd14623   159 QQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGI---LDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 56-253 2.03e-27

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: 110.59  E-value: 2.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  56 NTNKNRYKDVVAYDETRVILSLLQEEGHGDYINANFI--------------------------------RVILMACQETE 103
Cdd:cd14628    52 NKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIdgyrqqkayiatqgplaettedfwrmlwehnsTIVVMLTKLRE 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 104 NGRRKCERYWAREQEPlKAGPFCITLTKETTLNADItLRTLQVTFQK--EFRSVHQLQYMSWPDHGVPSSSDHILTMVEE 181
Cdd:cd14628   132 MGREKCHQYWPAERSA-RYQYFVVDPMAEYNMPQYI-LREFKVTDARdgQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQ 209

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907067822 182 A-RCLQGLGP-GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLY 253
Cdd:cd14628   210 VhKTKEQFGQdGPISVHCSAGVGRTGVFITLSIVLERMRYEGV---VDIFQTVKMLRTQRPAMVQTEDQYQFCY 280
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 56-258 4.09e-27

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: 109.44  E-value: 4.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  56 NTNKNRYKDVVAYDETRVILSLLQEEGHGDYINANFI--------------------------------RVILMACQETE 103
Cdd:cd14627    53 NKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIdgyrqqkayiatqgplaettedfwrmlwennsTIVVMLTKLRE 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 104 NGRRKCERYWAREQEPlKAGPFCITLTKETTLNADItLRTLQVTFQK--EFRSVHQLQYMSWPDHGVPSSSDHILTMVEE 181
Cdd:cd14627   133 MGREKCHQYWPAERSA-RYQYFVVDPMAEYNMPQYI-LREFKVTDARdgQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQ 210

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907067822 182 A-RCLQGLGP-GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 258
Cdd:cd14627   211 VhKTKEQFGQdGPISVHCSAGVGRTGVFITLSIVLERMRYEGV---VDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALE 286
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 56-253 4.58e-27

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: 109.44  E-value: 4.58e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  56 NTNKNRYKDVVAYDETRVILSLLQEEGHGDYINANFI--------------------------------RVILMACQETE 103
Cdd:cd14624    47 NKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIdgyrkqnayiatqgalpetfgdfwrmiweqrsATVVMMTKLEE 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 104 NGRRKCERYW-AREQEplKAGPFCITLTKETTLnADITLRTLQV--TFQKEFRSVHQLQYMSWPDHGVPSSSDHILTMVE 180
Cdd:cd14624   127 RSRVKCDQYWpSRGTE--TYGLIQVTLLDTVEL-ATYCVRTFALykNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLR 203

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907067822 181 EARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFQVVLEMRKQRPAAVQTEEQYRFLY 253
Cdd:cd14624   204 RVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEK---TVDIYGHVTLMRAQRNYMVQTEDQYIFIH 273
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 94-253 5.18e-27

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: 107.17  E-value: 5.18e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  94 VILMACQETENGRR-KCERYWAREQ-EPLKAGPFCITLTKETTLNADITLRTLQVTF---QKEFRSVHQLQYMSWPDHGV 168
Cdd:cd17658    43 VIIMLTRLVDNYSTaKCADYFPAEEnESREFGRISVTNKKLKHSQHSITLRVLEVQYiesEEPPLSVLHIQYPEWPDHGV 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 169 PSSSDHILTMVeeaRCLQGLGP--GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPnFSLFQVVLEMRKQRPAAVQTE 246
Cdd:cd17658   123 PKDTRSVRELL---KRLYGIPPsaGPIVVHCSAGIGRTGAYCTIHNTIRRILEGDMSA-VDLSKTVRKFRSQRIGMVQTQ 198


                  ....*..
gi 1907067822 247 EQYRFLY 253
Cdd:cd17658   199 DQYIFCY 205
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 56-258 9.11e-27

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: 108.26  E-value: 9.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  56 NTNKNRYKDVVAYDETRVILSLLQEEGHGDYINANFI--------------------------------RVILMACQETE 103
Cdd:cd14625    47 NKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANYIdgyrkqnayiatqgplpetfgdfwrmvweqrsATVVMMTKLEE 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 104 NGRRKCERYW-AREQEPLkaGPFCITLTKETTLnADITLRT--LQVTFQKEFRSVHQLQYMSWPDHGVPSSSDHILTMVE 180
Cdd:cd14625   127 KSRIKCDQYWpSRGTETY--GMIQVTLLDTIEL-ATFCVRTfsLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLR 203

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907067822 181 EARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 258
Cdd:cd14625   204 RVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEK---TVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 43-258 1.51e-26

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: 107.84  E-value: 1.51e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  43 EGVCSTKA-------GSRLGNTNKNRYKDVVAYDETRVILSLLQEEGHGDYINANFIR---------------------- 93
Cdd:cd14610    24 EALCAYQAepnatnvAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMdhdprnpayiatqgplpatvad 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  94 -----------VILMACQETENGRRKCERYWAREQEPLKAgPFCITLTKETTLNADITLRT--LQVTFQKEFRSVHQLQY 160
Cdd:cd14610   104 fwqmvwesgcvVIVMLTPLAENGVKQCYHYWPDEGSNLYH-IYEVNLVSEHIWCEDFLVRSfyLKNLQTNETRTVTQFHF 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 161 MSWPDHGVPSSSDHILTMVEEA-RCLQGLGpGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTipPNFSLFQVVLEMRKQR 239
Cdd:cd14610   183 LSWNDQGVPASTRSLLDFRRKVnKCYRGRS-CPIIVHCSDGAGRSGTYILIDMVLNKMAKGA--KEIDIAATLEHLRDQR 259

                         250
                  ....*....|....*....
gi 1907067822 240 PAAVQTEEQYRFLYHTVAQ 258
Cdd:cd14610   260 PGMVQTKEQFEFALTAVAE 278
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 94-253 1.98e-26

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: 105.29  E-value: 1.98e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  94 VILMACQETENGRRKCERYWAREQEPLKA-GPFCITLTKETTLnADITLRTLQVTFQKEFRS---VHQLQYMSWPDHGVP 169
Cdd:cd14557    41 VIVMVTRCEEGNRNKCAQYWPSMEEGSRAfGDVVVKINEEKIC-PDYIIRKLNINNKKEKGSgreVTHIQFTSWPDHGVP 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 170 SSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFQVVLEMRKQRPAAVQTEEQY 249
Cdd:cd14557   120 EDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEG---RVDVYGYVVKLRRQRCLMVQVEAQY 196


                  ....
gi 1907067822 250 RFLY 253
Cdd:cd14557   197 ILIH 200
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 92-253 2.40e-26

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: 105.16  E-value: 2.40e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  92 IRVILMACQETENGRRKCERYWAREQ-EPLKAGPFCITLTKETTLNADITlRTLQVTF--QKEFRSVHQLQYMSWPDHGV 168
Cdd:cd14539    40 VSVIVMLVSEQENEKQKVHRYWPTERgQALVYGAITVSLQSVRTTPTHVE-RIISIQHkdTRLSRSVVHLQFTTWPELGL 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 169 PSSSDHILTMVEEA-------RCLQglgpGPLCVHCSAGCGRTGVLCAVdY--VRQLLLTQTIPpnfSLFQVVLEMRKQR 239
Cdd:cd14539   119 PDSPNPLLRFIEEVhshylqqRSLQ----TPIVVHCSSGVGRTGAFCLL-YaaVQEIEAGNGIP---DLPQLVRKMRQQR 190

                         170
                  ....*....|....
gi 1907067822 240 PAAVQTEEQYRFLY 253
Cdd:cd14539   191 KYMLQEKEHLKFCY 204
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 92-256 2.91e-26

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: 105.06  E-value: 2.91e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  92 IRVILMACQETENGRRKCERYWAREQEPlKAGPFCITLTKETTLnADITLRTLQVTFQK----------EFRSVHQLQYM 161
Cdd:cd17668    39 VEVIVMITNLVEKGRRKCDQYWPADGSE-EYGNFLVTQKSVQVL-AYYTVRNFTLRNTKikkgsqkgrpSGRVVTQYHYT 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 162 SWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVD-YVRQLLLTQTIppnfSLFQVVLEMRKQRP 240
Cdd:cd17668   117 QWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGRTGTYIVLDsMLQQIQHEGTV----NIFGFLKHIRSQRN 192

                         170
                  ....*....|....*.
gi 1907067822 241 AAVQTEEQYRFLYHTV 256
Cdd:cd17668   193 YLVQTEEQYVFIHDAL 208
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 95-256 4.32e-26

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: 104.61  E-value: 4.32e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  95 ILMACQETENGRRKCERYWAREQEPLkaGPFCITLTKETTLnADITLRTLQVTFQ--KEFRSVHQLQYMSWPDHGVPSSS 172
Cdd:cd14555    42 IVMVTNLVEVGRVKCSRYWPDDTEVY--GDIKVTLVETEPL-AEYVVRTFALERRgyHEIREVRQFHFTGWPDHGVPYHA 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 173 DHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFL 252
Cdd:cd14555   119 TGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGV---VDIYNCVKELRSRRVNMVQTEEQYIFI 195


                  ....
gi 1907067822 253 YHTV 256
Cdd:cd14555   196 HDAI 199
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 94-258 7.23e-26

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: 104.06  E-value: 7.23e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  94 VILMACQETENGRRKCERYWAREQEPLKaGPFCITLTKETTLNADITLRT--LQVTFQKEFRSVHQLQYMSWPDHGVPSS 171
Cdd:cd14546    42 VIVMLTRLQENGVKQCARYWPEEGSEVY-HIYEVHLVSEHIWCDDYLVRSfyLKNLQTSETRTVTQFHFLSWPDEGIPAS 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 172 SDHILTMVEEA-RCLQGLGpGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTipPNFSLFQVVLEMRKQRPAAVQTEEQYR 250
Cdd:cd14546   121 AKPLLEFRRKVnKSYRGRS-CPIVVHCSDGAGRTGTYILIDMVLNRMAKGA--KEIDIAATLEHLRDQRPGMVKTKDQFE 197


                  ....*...
gi 1907067822 251 FLYHTVAQ 258
Cdd:cd14546   198 FVLTAVAE 205
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 62-256 7.24e-26

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: 104.64  E-value: 7.24e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  62 YKDVVAYDETRVILSLLQEEGHGDYINANFI--------------------------------RVILMACQETENGRRKC 109
Cdd:cd14620     1 YPNILPYDHSRVILSQLDGIPCSDYINASYIdgykeknkfiaaqgpkqetvndfwrmvweqksATIVMLTNLKERKEEKC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 110 ERYWArEQEPLKAGPFCITLTKETTLnADITLRTLQVTFQ-----KEFRSVHQLQYMSWPDHGVPSSSDHILTMVEEARC 184
Cdd:cd14620    81 YQYWP-DQGCWTYGNIRVAVEDCVVL-VDYTIRKFCIQPQlpdgcKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKS 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907067822 185 LQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTV 256
Cdd:cd14620   159 VNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQ---KVDVFEFVSRIRNQRPQMVQTDMQYSFIYQAL 227
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 56-253 1.93e-25

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: 104.81  E-value: 1.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  56 NTNKNRYKDVVAYDETRVILSLLQEEGHGDYINANFI--------------------------------RVILMACQETE 103
Cdd:cd14629    53 NKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIdgyrqqkayiatqgplaettedfwrmlwehnsTIVVMLTKLRE 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 104 NGRRKCERYWAREQEPlKAGPFCITLTKETTLNADItLRTLQVTFQK--EFRSVHQLQYMSWPDHGVPSSSDHILTMVEE 181
Cdd:cd14629   133 MGREKCHQYWPAERSA-RYQYFVVDPMAEYNMPQYI-LREFKVTDARdgQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQ 210

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907067822 182 A-RCLQGLGP-GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLY 253
Cdd:cd14629   211 VhKTKEQFGQdGPITVHCSAGVGRTGVFITLSIVLERMRYEGV---VDMFQTVKTLRTQRPAMVQTEDQYQLCY 281
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 43-258 3.06e-25

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: 104.35  E-value: 3.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  43 EGVCSTKA-------GSRLGNTNKNRYKDVVAYDETRVILSLLQEEGHGDYINANFI----------------------- 92
Cdd:cd14609    22 QALCAYQAepntcstAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIiehdprmpayiatqgplshtiad 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  93 ----------RVILMACQETENGRRKCERYWAREQEPLkAGPFCITLTKETTLNADITLRT--LQVTFQKEFRSVHQLQY 160
Cdd:cd14609   102 fwqmvwengcTVIVMLTPLVEDGVKQCDRYWPDEGSSL-YHIYEVNLVSEHIWCEDFLVRSfyLKNVQTQETRTLTQFHF 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 161 MSWPDHGVPSSSDHILTMVEEA-RCLQGLGpGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTipPNFSLFQVVLEMRKQR 239
Cdd:cd14609   181 LSWPAEGIPSSTRPLLDFRRKVnKCYRGRS-CPIIVHCSDGAGRTGTYILIDMVLNRMAKGV--KEIDIAATLEHVRDQR 257

                         250
                  ....*....|....*....
gi 1907067822 240 PAAVQTEEQYRFLYHTVAQ 258
Cdd:cd14609   258 PGMVRTKDQFEFALTAVAE 276
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 92-253 3.69e-25

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: 101.70  E-value: 3.69e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  92 IRVILMACQETENGRRKCERYWarEQEPLKAGPFCITLTKETTLNaDITLRTLQVTF--QKEFRSVHQLQYMSWPDHGVP 169
Cdd:cd14558    39 VKVIVMLTELKEGDQEQCAQYW--GDEKKTYGDIEVELKDTEKSP-TYTVRVFEITHlkRKDSRTVYQYQYHKWKGEELP 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 170 SSSDHILTMVEEARCLQGLGPG------PLCVHCSAGCGRTGVLCAVdyvRQLLLTQTIPPNFSLFQVVLEMRKQRPAAV 243
Cdd:cd14558   116 EKPKDLVDMIKSIKQKLPYKNSkhgrsvPIVVHCSDGSSRTGIFCAL---WNLLESAETEKVVDVFQVVKALRKQRPGMV 192

                         170
                  ....*....|
gi 1907067822 244 QTEEQYRFLY 253
Cdd:cd14558   193 STLEQYQFLY 202
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 109-253 4.44e-25

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: 101.71  E-value: 4.44e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 109 CERYWArEQEPLKAGPFCITLTKeTTLNADITLRTLQVT----FQKEFRSVHQLQYMSWPDHG-VPSSSDHILTMVEEA- 182
Cdd:cd14556    55 CPQYWP-DEGSGTYGPIQVEFVS-TTIDEDVISRIFRLQnttrPQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVe 132

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907067822 183 RCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLY 253
Cdd:cd14556   133 KWQEQSGEGPIVVHCLNGVGRSGVFCAISSVCERIKVENV---VDVFQAVKTLRNHRPNMVETEEQYKFCY 200
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 72-258 1.02e-24

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: 101.25  E-value: 1.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  72 RVILSLLQEEGHGDYINANFI--------------------------------RVILMACQETENGRRKCERYWAREQEP 119
Cdd:cd14631     1 RVILQPVEDDPSSDYINANYIdgyqrpshyiatqgpvhetvydfwrmiwqeqsACIVMVTNLVEVGRVKCYKYWPDDTEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 120 LkaGPFCITLTKETTLnADITLRTLQVTFQ--KEFRSVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHC 197
Cdd:cd14631    81 Y--GDFKVTCVEMEPL-AEYVVRTFTLERRgyNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHC 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907067822 198 SAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 258
Cdd:cd14631   158 SAGAGRTGCYIVIDIMLDMAEREGV---VDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 41-260 1.55e-24

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: 102.38  E-value: 1.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  41 KSEGVCSTKAGSRlgNTNKNRYKDVVAYDETRVILSLLQEEGHGdYINANFIRV-------------------------- 94
Cdd:cd14599    25 KADGVFTTATLPE--NAERNRIREVVPYEENRVELVPTKENNTG-YINASHIKVtvggeewhyiatqgplphtchdfwqm 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  95 --------ILMACQETENGRRKCERYWAR---EQEPLKAGPFCITlTKETTLNADITLRTLQVT--FQKEFRSVHQLQYM 161
Cdd:cd14599   102 vweqgvnvIAMVTAEEEGGRSKSHRYWPKlgsKHSSATYGKFKVT-TKFRTDSGCYATTGLKVKhlLSGQERTVWHLQYT 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 162 SWPDHGVPSSSDHILTMVEEARCLQ-----------GLGPgPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFQ 230
Cdd:cd14599   181 DWPDHGCPEEVQGFLSYLEEIQSVRrhtnsmldstkNCNP-PIVVHCSAGVGRTGVVILTELMIGCLEHNE---KVEVPV 256

                         250       260       270
                  ....*....|....*....|....*....|
gi 1907067822 231 VVLEMRKQRPAAVQTEEQYRFLYHTVAQLF 260
Cdd:cd14599   257 MLRHLREQRMFMIQTIAQYKFVYQVLIQFL 286
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1-258 1.09e-23

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 100.46  E-value: 1.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822   1 MSRHTDLVRSFLEQLEARDYREgaILAREFSDIKARSVAWKSEGVCSTKagsrlgNTNKNRYKDVVAYDETRVILSLlqE 80
Cdd:PHA02742    5 CSKKNSFAKNCEQLIEESNLAE--ILKEEHEHIMQEIVAFSCNESLELK------NMKKCRYPDAPCFDRNRVILKI--E 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  81 EGHGDYINANFI--------------------------------RVILMACQETENGRRKCERYW-AREQEPLKAGPFCI 127
Cdd:PHA02742   75 DGGDDFINASYVdghnakgrfictqapleetaldfwqaifqdqvRVIVMITKIMEDGKEACYPYWmPHERGKATHGEFKI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 128 -TLTKETTLNADITlrTLQVTFQKEFRS--VHQLQYMSWPDHGVPSSSDHILTMVEEARCLQG-----------LGPGPL 193
Cdd:PHA02742  155 kTKKIKSFRNYAVT--NLCLTDTNTGASldIKHFAYEDWPHGGLPRDPNKFLDFVLAVREADLkadvdikgeniVKEPPI 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907067822 194 CVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPnfsLFQVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 258
Cdd:PHA02742  233 LVHCSAGLDRAGAFCAIDICISKYNERAIIP---LLSIVRDLRKQRHNCLSLPQQYIFCYFIVLI 294
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 47-258 1.75e-23

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: 99.71  E-value: 1.75e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  47 STKAGSRLGNTNKNRYKDVVAYDETRVILSLLQEEGHGDYINANFIR--------------------------------V 94
Cdd:cd14621    43 TCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINgyqeknkfiaaqgpkeetvndfwrmiweqntaT 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  95 ILMACQETENGRRKCERYWArEQEPLKAGPFCITLtKETTLNADITLRTL------QVTFQKEFRSVHQLQYMSWPDHGV 168
Cdd:cd14621   123 IVMVTNLKERKECKCAQYWP-DQGCWTYGNIRVSV-EDVTVLVDYTVRKFciqqvgDVTNKKPQRLITQFHFTSWPDFGV 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 169 PSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFQVVLEMRKQRPAAVQTEEQ 248
Cdd:cd14621   201 PFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAER---KVDVYGFVSRIRAQRCQMVQTDMQ 277

                         250
                  ....*....|
gi 1907067822 249 YRFLYHTVAQ 258
Cdd:cd14621   278 YVFIYQALLE 287
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 94-256 2.85e-23

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: 96.61  E-value: 2.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  94 VILMACQETEngRRKCERYWAREQEpLKAGPFCITLTKETTLNAdITLRTLQVTF--QKEFRSVHQLQYMSWPDHGVPSS 171
Cdd:cd14622    44 VMLTELQERE--QEKCVQYWPSEGS-VTHGEITIEIKNDTLLET-ISIRDFLVTYnqEKQTRLVRQFHFHGWPEIGIPAE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 172 SDHILTMVEEA-RCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYR 250
Cdd:cd14622   120 GKGMIDLIAAVqKQQQQTGNHPIVVHCSAGAGRTGTFIALSNILERVKAEGL---LDVFQTVKSLRLQRPHMVQTLEQYE 196


                  ....*.
gi 1907067822 251 FLYHTV 256
Cdd:cd14622   197 FCYRVV 202
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 95-253 3.75e-23

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: 96.13  E-value: 3.75e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  95 ILMACQETENGRRKCERYWAREQEpLKAGPFCITLtKETTLNADITLRTL------QVTFQKEFRSVHQLQYMSWPDHGV 168
Cdd:cd14551    42 IVMVTNLKERKEKKCSQYWPDQGC-WTYGNLRVRV-EDTVVLVDYTTRKFciqkvnRGIGEKRVRLVTQFHFTSWPDFGV 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 169 PSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFQVVLEMRKQRPAAVQTEEQ 248
Cdd:cd14551   120 PFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGTFIVIDAMLDMMHAEG---KVDVFGFVSRIRQQRSQMVQTDMQ 196


                  ....*
gi 1907067822 249 YRFLY 253
Cdd:cd14551   197 YVFIY 201
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 95-258 8.20e-23

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: 95.50  E-value: 8.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  95 ILMACQETENGRRKCERYWAREQEPLkaGPFCITLTKETTLnADITLRTLQVTfQKEFRSVH---QLQYMSWPDHGVPSS 171
Cdd:cd14632    42 IVMITKLVEVGRVKCSKYWPDDSDTY--GDIKITLLKTETL-AEYSVRTFALE-RRGYSARHevkQFHFTSWPEHGVPYH 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 172 SDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRF 251
Cdd:cd14632   118 ATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVLDVMLDMAECEGV---VDIYNCVKTLCSRRINMIQTEEQYIF 194


                  ....*..
gi 1907067822 252 LYHTVAQ 258
Cdd:cd14632   195 IHDAILE 201
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 59-254 2.04e-22

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: 94.98  E-value: 2.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  59 KNRYKDVVAYDETRVILSLLQ-EEGHGDYINANFIR---------------------------------VILMACQETEN 104
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKNsNDSLSTYINANYIRgyggkekafiatqgpmintvndfwqmvwqedspVIVMITKLKEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 105 GRrKCERYWareqePLKAGpfcITLTKETTLNA-----DITLRTLQVTFQKEFRSVHQLQYMSWPDHGVPSSSDHILTM- 178
Cdd:cd14611    82 NE-KCVLYW-----PEKRG---IYGKVEVLVNSvkecdNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLm 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907067822 179 --VEEARcLQGLGPGPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIppnfSLFQVVLEMRKQRPAAVQTEEQYRFLYH 254
Cdd:cd14611   153 ldVEEDR-LASPGRGPVVVHCSAGIGRTGCFIATTIgCQQLKEEGVV----DVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 54-257 2.05e-22

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: 95.70  E-value: 2.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  54 LGNTNKNRYKDVVAYDETRVIL-SLLQEEGHGDYINANFIR--------------------------------VILMACQ 100
Cdd:cd14613    23 PGLVRKNRYKTILPNPHSRVCLtSPDQDDPLSSYINANYIRgyggeekvyiatqgptvntvgdfwrmvwqersPIIVMIT 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 101 ETENGRRKCERYWAREQepLKAGPFCITLTKETTLNaDITLRTLQVTFQKEFRSVHQLQYMSWPDHGVPSSSDHILTMV- 179
Cdd:cd14613   103 NIEEMNEKCTEYWPEEQ--VTYEGIEITVKQVIHAD-DYRLRLITLKSGGEERGLKHYWYTSWPDQKTPDNAPPLLQLVq 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 180 --EEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTVA 257
Cdd:cd14613   180 evEEARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGV---VDILRTTCQLRLDRGGMIQTCEQYQFVHHVLS 256
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 56-256 7.74e-22

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 95.48  E-value: 7.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  56 NTNKNRYKDVVAYDETRVILS-------------------LLQEEGHGDYINANFI------------------------ 92
Cdd:PHA02746   51 NLKKNRFHDIPCWDHSRVVINaheslkmfdvgdsdgkkieVTSEDNAENYIHANFVdgfkeankficaqgpkedtsedff 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  93 -------RVILMACQETENGRRKCERYWAREQE-PLKAGPFcITLTKETTLNADITLRTLQVT--FQKEFRSVHQLQYMS 162
Cdd:PHA02746  131 kliseheSQVIVSLTDIDDDDEKCFELWTKEEDsELAFGRF-VAKILDIIEELSFTKTRLMITdkISDTSREIHHFWFPD 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 163 WPDHGVPSSSDHILTMV-----EEARCL-----QGLGPGPLCVHCSAGCGRTGVLCAVD-YVRQLLLTQTIppnfSLFQV 231
Cdd:PHA02746  210 WPDNGIPTGMAEFLELInkvneEQAELIkqadnDPQTLGPIVVHCSAGIGRAGTFCAIDnALEQLEKEKEV----CLGEI 285

                         250       260
                  ....*....|....*....|....*
gi 1907067822 232 VLEMRKQRPAAVQTEEQYRFLYHTV 256
Cdd:PHA02746  286 VLKIRKQRHSSVFLPEQYAFCYKAL 310
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 56-252 1.05e-21

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 94.68  E-value: 1.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  56 NTNKNRYKDVVAYDETRVILsllqEEGHG---DYINANFIR---------------------------------VILMAC 99
Cdd:PHA02747   51 NQPKNRYWDIPCWDHNRVIL----DSGGGstsDYIHANWIDgfeddkkfiatqgpfaetcadfwkavwqehcsiIVMLTP 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 100 QETENGRRKCERYWA-REQEPLKAGPFCITlTKETTLNADITLRTLQVTFQ--KEFRSVHQLQYMSWPDHGVPSssDHI- 175
Cdd:PHA02747  127 TKGTNGEEKCYQYWClNEDGNIDMEDFRIE-TLKTSVRAKYILTLIEITDKilKDSRKISHFQCSEWFEDETPS--DHPd 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 176 ----LTMVEEARCLQG--LGP-----GPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIppnfSLFQVVLEMRKQRPAAV 243
Cdd:PHA02747  204 fikfIKIIDINRKKSGklFNPkdallCPIVVHCSDGVGKTGIFCAVDIcLNQLVKRKAI----CLAKTAEKIREQRHAGI 279


                  ....*....
gi 1907067822 244 QTEEQYRFL 252
Cdd:PHA02747  280 MNFDDYLFI 288
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 92-260 1.62e-19

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: 86.57  E-value: 1.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  92 IRVILMACQETENGRRKCERYWAR---EQEPLKAGPFCIT--LTKETTLNADITLRTLQVTFQKEfRSVHQLQYMSWPDH 166
Cdd:cd14598    41 VAIIAMVTAEEEGGREKSFRYWPRlgsRHNTVTYGRFKITtrFRTDSGCYATTGLKIKHLLTGQE-RTVWHLQYTDWPEH 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 167 GVPSSSDHILTMVEEARCL----------QGLGPgPLCVHCSAGCGRTGVLcavdyVRQLLLTQTIPPNFSL-FQVVLEM 235
Cdd:cd14598   120 GCPEDLKGFLSYLEEIQSVrrhtnstidpKSPNP-PVLVHCSAGVGRTGVV-----ILSEIMIACLEHNEMLdIPRVLDM 193

                         170       180
                  ....*....|....*....|....*.
gi 1907067822 236 -RKQRPAAVQTEEQYRFLYHTVAQLF 260
Cdd:cd14598   194 lRQQRMMMVQTLSQYTFVYKVLIQFL 219
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 109-253 2.69e-15

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: 74.29  E-value: 2.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 109 CERYWArEQEPLKAGPF---CITltkeTTLNADITLRTLQVTF----QKEFRSVHQLQYMSWPDH-GVPSSSDHILTMVE 180
Cdd:cd14636    54 CPQYWP-EEGMLRYGPIqveCMS----CSMDCDVISRIFRICNltrpQEGYLMVQQFQYLGWASHrEVPGSKRSFLKLIL 128

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907067822 181 EARCLQ---GLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLY 253
Cdd:cd14636   129 QVEKWQeecDEGEGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNV---VDVFHAVKTLRNSKPNMVETPEQYRFCY 201
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 173-254 2.95e-14

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: 68.53  E-value: 2.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 173 DHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLlltqtippNFSLFQVVLEMRKQRPA-AVQTEEQYRF 251
Cdd:cd14494    39 LAMVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLG--------GMSAEEAVRIVRLIRPGgIPQTIEQLDF 110


                  ...
gi 1907067822 252 LYH 254
Cdd:cd14494   111 LIK 113
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 109-253 1.65e-13

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: 69.28  E-value: 1.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 109 CERYWArEQEPLKAGPFCITLTkETTLNADITLRTLQVTF----QKEFRSVHQLQYMSWPDH-GVPSSSDHILTMVEEAR 183
Cdd:cd14634    54 CMQYWP-EKTSCCYGPIQVEFV-SADIDEDIISRIFRICNmarpQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLE 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907067822 184 CLQGL---GPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLY 253
Cdd:cd14634   132 KWQEQydgREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNI---IDVFHTVKTLRNNKSNMVETLEQYKFVY 201
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 109-253 2.41e-11

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: 62.78  E-value: 2.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 109 CERYWArEQEPLKAGPFCITLTkETTLNADITLRTLQVTF----QKEFRSVHQLQYMSWPDH-GVPSSSDHILTMVEEAR 183
Cdd:cd14635    54 CPQYWP-ENGVHRHGPIQVEFV-SADLEEDIISRIFRIYNaarpQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVD 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907067822 184 CLQGL---GPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFQVVLEMRKQRPAAVQTEEQYRFLY 253
Cdd:cd14635   132 KWQEEyngGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQR---AVDVFHAVKTLRNNKPNMVDLLDQYKFCY 201
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 162-252 4.51e-10

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: 58.90  E-value: 4.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 162 SWPDHGVPSSsDHILTMVE-EARCLQGlgPGPLCVHCSAGCGRTGVLCAVdyvrQLLLTQTIPPNfslfQVVLEMRKQRP 240
Cdd:cd14506    83 GWKDYGVPSL-TTILDIVKvMAFALQE--GGKVAVHCHAGLGRTGVLIAC----YLVYALRMSAD----QAIRLVRSKRP 151

                          90
                  ....*....|..
gi 1907067822 241 AAVQTEEQYRFL 252
Cdd:cd14506   152 NSIQTRGQVLCV 163
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 109-256 2.16e-09

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: 57.23  E-value: 2.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 109 CERYWArEQEPLKAGPFCITLTkETTLNADITLRTLQVT----FQKEFRSVHQLQYMSW-PDHGVPSSSD---HILTMVE 180
Cdd:cd14637    57 CLQYWP-EPGLQQYGPMEVEFV-SGSADEDIVTRLFRVQnitrLQEGHLMVRHFQFLRWsAYRDTPDSKKaflHLLASVE 134

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907067822 181 --EARClqglGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTV 256
Cdd:cd14637   135 kwQRES----GEGRTVVHCLNGGGRSGTYCASAMILEMIRCHNI---VDVFYAVKTLRNYKPNMVETLEQYRFCYEIA 205
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 112-253 1.36e-08

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: 54.68  E-value: 1.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 112 YWAREQEPLKAGPFCITL---------TKETTLNADITLRTLQVTFQKEFRsvhQLQYMSWPDHGVPSSSDHILTMV--E 180
Cdd:cd17670    58 YWPSREESMNCEAFTVTLiskdrlclsNEEQIIIHDFILEATQDDYVLEVR---HFQCPKWPNPDAPISSTFELINVikE 134

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907067822 181 EARCLQGlgpgPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLY 253
Cdd:cd17670   135 EALTRDG----PTIVHDEFGAVSAGTLCALTTLSQQLENENA---VDVYQVAKMINLMRPGVFTDIEQYQFLY 200
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
163-254 1.51e-08

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 53.05  E-value: 1.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 163 WPDHGVPSSsDHILTMVEEARCLQGLGpGPLCVHCSAGCGRTGVLCAvdyvrQLLLTQTIPPNfslfQVVLEMRKQRPAA 242
Cdd:COG2453    55 IPDFGAPDD-EQLQEAVDFIDEALREG-KKVLVHCRGGIGRTGTVAA-----AYLVLLGLSAE----EALARVRAARPGA 123

                          90
                  ....*....|..
gi 1907067822 243 VQTEEQYRFLYH 254
Cdd:COG2453   124 VETPAQRAFLER 135
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 157-253 9.51e-08

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: 51.50  E-value: 9.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 157 QLQYMSW-----PDHGVPSSSDHILTMVEEAR-CLQGlGPGPLcVHCSAGCGRTGVLCAvdyVRQLLLTQTIPPNfslfQ 230
Cdd:cd14505    69 QQAGITWhhlpiPDGGVPSDIAQWQELLEELLsALEN-GKKVL-IHCKGGLGRTGLIAA---CLLLELGDTLDPE----Q 139

                          90       100
                  ....*....|....*....|...
gi 1907067822 231 VVLEMRKQRPAAVQTEEQYRFLY 253
Cdd:cd14505   140 AIAAVRALRPGAIQTPKQENFLH 162
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 163-252 1.39e-07

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: 52.02  E-value: 1.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 163 WPDHGVPSS------SDHI-------LTMVEEARCLQGLGPGPL--CVHCSAGCGRTGVLCAVDYVRQllltqtiPPN-F 226
Cdd:cd14559   126 WPDHTAISSeglkelADLVnksaeekRNFYKSKGSSAINDKNKLlpVIHCRAGVGRTGQLAAAMELNK-------SPNnL 198

                          90       100
                  ....*....|....*....|....*..
gi 1907067822 227 SLFQVVLEMRKQRPA-AVQTEEQYRFL 252
Cdd:cd14559   199 SVEDIVSDMRTSRNGkMVQKDEQLDTL 225
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 154-252 1.48e-06

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: 47.27  E-value: 1.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 154 SVHQLQY--MSWPDHGVPSSS--DHILTMVEEARCLqglgPGPLCVHCSAGCGRTGVLCAVdYvrqLLLTQTIPPNfslf 229
Cdd:cd14504    46 TCPGLRYhhIPIEDYTPPTLEqiDEFLDIVEEANAK----NEAVLVHCLAGKGRTGTMLAC-Y---LVKTGKISAV---- 113

                          90       100
                  ....*....|....*....|...
gi 1907067822 230 QVVLEMRKQRPAAVQTEEQYRFL 252
Cdd:cd14504   114 DAINEIRRIRPGSIETSEQEKFV 136
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 112-256 4.08e-06

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: 47.30  E-value: 4.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 112 YWAREQEPLKAGPFCITL---------TKETTLNADITLRTLQVTFQKEFRsvhQLQYMSWPDHGVP-SSSDHILTMVEE 181
Cdd:cd17669    58 YWPNKDEPINCETFKVTLiaeehkclsNEEKLIIQDFILEATQDDYVLEVR---HFQCPKWPNPDSPiSKTFELISIIKE 134

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907067822 182 ARCLQGlgpGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTV 256
Cdd:cd17669   135 EAANRD---GPMIVHDEHGGVTAGTFCALTTLMHQLEKEN---SVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 94-253 6.27e-05

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: 43.85  E-value: 6.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  94 VILMACQETENgrrkCERYWAREQEPLKAGPFCITLTKETT--LNADITLRT----LQVTFQKEFRSVHQLQYMSWPDHG 167
Cdd:cd14550    43 VMLTDNELNED----EPIYWPTKEKPLECETFKVTLSGEDHscLSNEIRLIVrdfiLESTQDDYVLEVRQFQCPSWPNPC 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 168 VP-SSSDHILTMVEEaRCLQglGPGPLCVHCSAGCGRTGVLCAVdyvrQLLLTQTIPPN-FSLFQVVLEMRKQRPAAVQT 245
Cdd:cd14550   119 SPiHTVFELINTVQE-WAQQ--RDGPIVVHDRYGGVQAATFCAL----TTLHQQLEHESsVDVYQVAKLYHLMRPGVFTS 191


                  ....*...
gi 1907067822 246 EEQYRFLY 253
Cdd:cd14550   192 KEDYQFLY 199
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 61-264 3.91e-04

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 42.26  E-value: 3.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822  61 RYKDVVAYDETRVILSLLQEEGHGDYINA---NFIRVILMACQETEngrRKC-ERYWAREQEPLK-AGPFCI-TLTKETT 134
Cdd:PHA02740   82 RFVDGYDFEQKFICIINLCEDACDKFLQAlsdNKVQIIVLISRHAD---KKCfNQFWSLKEGCVItSDKFQIeTLEIIIK 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 135 LNADITLRTLQVTFQKEfRSVHQLQYMSWPDHGVPSSSD-------HILTMVEEARCLQGLGP-GPLCVHCSAGCGRTGV 206
Cdd:PHA02740  159 PHFNLTLLSLTDKFGQA-QKISHFQYTAWPADGFSHDPDafidffcNIDDLCADLEKHKADGKiAPIIIDCIDGISSSAV 237

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907067822 207 LCAVDyvrqLLLTQTIPPN-FSLFQVVLEMRKQRPAAVQTEEQYRFLYHTVAQLFSRTL 264
Cdd:PHA02740  238 FCVFD----ICATEFDKTGmLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYLKEKF 292
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 299-420 1.73e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 40.47  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067822 299 RPPGGVLRSI-SVPAPPTLPMADTYAVVQKRGASAGTGPGPRAPTSTDTPIYSQVA---PRAQRPVAHTEDAQGTTALRR 374
Cdd:PRK14951  365 KPAAAAEAAApAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAappAPVAAPAAAAPAAAPAAAPAA 444

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907067822 375 VPADQNSSGPDAYEEVTDGAQTGGLGFNLRIGRPKGPRDPPAEWTR 420
Cdd:PRK14951  445 VALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTP 490
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 164-207 2.20e-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: 38.59  E-value: 2.20e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1907067822 164 PDHGVPSssDHI----LTMVEEArclqglgPGPLCVHCSAGCGRTGVL 207
Cdd:cd14499    88 PDGSTPS--DDIvkkfLDICENE-------KGAIAVHCKAGLGRTGTL 126
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 156-209 5.91e-03

protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar proteins; Phosphatase and tensin homolog (PTEN) is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It dephosphorylates phosphoinositide trisphosphate. In addition to PTEN, this family includes tensins, voltage-sensitive phosphatases (VSPs), and auxilins. They all contain a protein tyrosine phosphatase-like domain although not all are active phosphatases. Tensins are intracellular proteins that act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility, and they may or may not have phosphatase activity. VSPs are phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. Auxilins are J domain-containing proteins that facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles, and they do not exhibit phosphatase activity.


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 37.17  E-value: 5.91e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907067822 156 HQLQYMSWPDHGVPSSsDHILTMVEEARCLQGLGPGPLCV-HCSAGCGRTGVLCA 209
Cdd:cd14497    61 GRVLHYGFPDHHPPPL-GLLLEIVDDIDSWLSEDPNNVAVvHCKAGKGRTGTVIC 114
 
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.
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