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Conserved domains on  [gi|1720392689|ref|XP_030106224|]
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tyrosine-protein phosphatase non-receptor type 2 isoform X2 [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 ...
 1-173 5.25e-127

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 cd14607:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 257  Bit Score: 361.59  E-value: 5.25e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDD-REMVFKETGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYT 79
Cdd:cd14607    82 MVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEeEVLSFKETGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYT 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  80 TWPDFGVPESPASFLNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEK--GEDVNVKQLLLNMRKYRM 157
Cdd:cd14607   162 TWPDFGVPESPASFLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKkdPDSVDIKQVLLDMRKYRM 241

                         170
                  ....*....|....*.
gi 1720392689 158 GLIQTPDQLRFSYMAI 173
Cdd:cd14607   242 GLIQTPDQLRFSYMAV 257
 
Name Accession Description Interval E-value
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 1-173 5.25e-127

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: 361.59  E-value: 5.25e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDD-REMVFKETGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYT 79
Cdd:cd14607    82 MVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEeEVLSFKETGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYT 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  80 TWPDFGVPESPASFLNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEK--GEDVNVKQLLLNMRKYRM 157
Cdd:cd14607   162 TWPDFGVPESPASFLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKkdPDSVDIKQVLLDMRKYRM 241

                         170
                  ....*....|....*.
gi 1720392689 158 GLIQTPDQLRFSYMAI 173
Cdd:cd14607   242 GLIQTPDQLRFSYMAV 257
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1-175 5.36e-76

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 231.36  E-value: 5.36e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPT-DDREMVFKetGFSVKLLSE-DVKSYYTVHLLQLENINTGETRTISHFHY 78
Cdd:pfam00102  61 MVWEEKVTIIVMLTELEEKGREKCAQYWPEeEGESLEYG--DFTVTLKKEkEDEKDYTVRTLEVSNGGSEETRTVKHFHY 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  79 TTWPDFGVPESPASFLNFLFKVRESgCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMG 158
Cdd:pfam00102 139 TGWPDHGVPESPNSLLDLLRKVRKS-SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPG 217

                         170
                  ....*....|....*..
gi 1720392689 159 LIQTPDQLRFSYMAIIE 175
Cdd:pfam00102 218 MVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1-175 9.87e-71

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 218.68  E-value: 9.87e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689    1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTD-DREMVFKetGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYT 79
Cdd:smart00194  88 MVWEQKVTVIVMLTELVEKGREKCAQYWPDEeGEPLTYG--DITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVTHYHYT 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   80 TWPDFGVPESPASFLNFLFKVRESGclTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGL 159
Cdd:smart00194 166 NWPDHGVPESPESILDLIRAVRKSQ--STSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQRPGM 243

                          170
                   ....*....|....*.
gi 1720392689  160 IQTPDQLRFSYMAIIE 175
Cdd:smart00194 244 VQTEEQYIFLYRAILE 259
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1-178 1.86e-32

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 121.26  E-value: 1.86e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREMVfkeTGFSVKLLSEDVKS--YYTVHLLQLENINTGETRTISHFHY 78
Cdd:PHA02742  112 AIFQDQVRVIVMITKIMEDGKEACYPYWMPHERGKA---THGEFKIKTKKIKSfrNYAVTNLCLTDTNTGASLDIKHFAY 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  79 TTWPDFGVPESPASFLNFLFKVRESGCLT--PDHG-------PAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLL 149
Cdd:PHA02742  189 EDWPHGGLPRDPNKFLDFVLAVREADLKAdvDIKGenivkepPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIV 268

                         170       180
                  ....*....|....*....|....*....
gi 1720392689 150 LNMRKYRMGLIQTPDQLRFSYMAIIEGAK 178
Cdd:PHA02742  269 RDLRKQRHNCLSLPQQYIFCYFIVLIFAK 297
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
1-166 2.38e-23

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 96.31  E-value: 2.38e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVE--KESVKCAQYWPTDDREMVFKetgFSVKLL-SEDVKSYYTVHLLQLENINTG-ETRTISHF 76
Cdd:COG5599    96 MLFDNNTPVLVVLASDDEisKPKVKMPVYFRQDGEYGKYE---VSSELTeSIQLRDGIEARTYVLTIKGTGqKKIEIPVL 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  77 HYTTWPDFGVPESPAsFLNFLFKVRES-GCLTPDHGPAVIHCSAGIGRSGTFSLvdtCLVLM-----EKGEDVNVKQLLL 150
Cdd:COG5599   173 HVKNWPDHGAISAEA-LKNLADLIDKKeKIKDPDKLLPVVHCRAGVGRTGTLIA---CLALSksinaLVQITLSVEEIVI 248

                         170
                  ....*....|....*..
gi 1720392689 151 NMRKYR-MGLIQTPDQL 166
Cdd:COG5599   249 DMRTSRnGGMVQTSEQL 265
 
Name Accession Description Interval E-value
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 1-173 5.25e-127

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: 361.59  E-value: 5.25e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDD-REMVFKETGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYT 79
Cdd:cd14607    82 MVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEeEVLSFKETGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYT 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  80 TWPDFGVPESPASFLNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEK--GEDVNVKQLLLNMRKYRM 157
Cdd:cd14607   162 TWPDFGVPESPASFLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKkdPDSVDIKQVLLDMRKYRM 241

                         170
                  ....*....|....*.
gi 1720392689 158 GLIQTPDQLRFSYMAI 173
Cdd:cd14607   242 GLIQTPDQLRFSYMAV 257
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 1-191 1.07e-118

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: 341.23  E-value: 1.07e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPT-DDREMVFKETGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYT 79
Cdd:cd14608    83 MVWEQKSRGVVMLNRVMEKGSLKCAQYWPQkEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYT 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  80 TWPDFGVPESPASFLNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGED---VNVKQLLLNMRKYR 156
Cdd:cd14608   163 TWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDpssVDIKKVLLEMRKFR 242

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1720392689 157 MGLIQTPDQLRFSYMAIIEGAKYTKGDSNIQKRWK 191
Cdd:cd14608   243 MGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQWK 277
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 1-171 9.75e-117

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: 334.75  E-value: 9.75e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDRE-MVFKETGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYT 79
Cdd:cd14545    58 MVWEQNSKAVIMLNKLMEKGQIKCAQYWPQGEGNaMIFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYT 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  80 TWPDFGVPESPASFLNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGE--DVNVKQLLLNMRKYRM 157
Cdd:cd14545   138 TWPDFGVPESPAAFLNFLQKVRESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKYRM 217

                         170
                  ....*....|....
gi 1720392689 158 GLIQTPDQLRFSYM 171
Cdd:cd14545   218 GLIQTPDQLRFSYL 231
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1-175 5.36e-76

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 231.36  E-value: 5.36e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPT-DDREMVFKetGFSVKLLSE-DVKSYYTVHLLQLENINTGETRTISHFHY 78
Cdd:pfam00102  61 MVWEEKVTIIVMLTELEEKGREKCAQYWPEeEGESLEYG--DFTVTLKKEkEDEKDYTVRTLEVSNGGSEETRTVKHFHY 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  79 TTWPDFGVPESPASFLNFLFKVRESgCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMG 158
Cdd:pfam00102 139 TGWPDHGVPESPNSLLDLLRKVRKS-SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPG 217

                         170
                  ....*....|....*..
gi 1720392689 159 LIQTPDQLRFSYMAIIE 175
Cdd:pfam00102 218 MVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1-175 9.87e-71

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 218.68  E-value: 9.87e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689    1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTD-DREMVFKetGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYT 79
Cdd:smart00194  88 MVWEQKVTVIVMLTELVEKGREKCAQYWPDEeGEPLTYG--DITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVTHYHYT 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   80 TWPDFGVPESPASFLNFLFKVRESGclTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGL 159
Cdd:smart00194 166 NWPDHGVPESPESILDLIRAVRKSQ--STSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQRPGM 243

                          170
                   ....*....|....*.
gi 1720392689  160 IQTPDQLRFSYMAIIE 175
Cdd:smart00194 244 VQTEEQYIFLYRAILE 259
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1-171 3.12e-67

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: 207.91  E-value: 3.12e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDdrEMVFKETG-FSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYT 79
Cdd:cd00047    33 MVWEQKVSVIVMLTNLVEKGREKCERYWPEE--GGKPLEYGdITVTLVSEEELSDYTIRTLELSPKGCSESREVTHLHYT 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  80 TWPDFGVPESPASFLNFLFKVRESgcLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGL 159
Cdd:cd00047   111 GWPDHGVPSSPEDLLALVRRVRKE--ARKPNGPIVVHCSAGVGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGM 188

                         170
                  ....*....|..
gi 1720392689 160 IQTPDQLRFSYM 171
Cdd:cd00047   189 VQTLEQYEFIYE 200
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 1-171 1.81e-54

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: 177.56  E-value: 1.81e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTD-DREMVFKEtgFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYT 79
Cdd:cd14543    91 MVWEQKVLVIVMTTRVVERGRVKCGQYWPLEeGSSLRYGD--LTVTNLSVENKEHYKKTTLEIHNTETDESRQVTHFQFT 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  80 TWPDFGVPESPASFLNFLFKVRE---SGCLT--------PDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQL 148
Cdd:cd14543   169 SWPDFGVPSSAAALLDFLGEVRQqqaLAVKAmgdrwkghPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQT 248

                         170       180
                  ....*....|....*....|...
gi 1720392689 149 LLNMRKYRMGLIQTPDQLRFSYM 171
Cdd:cd14543   249 VRRMRTQRAFSIQTPDQYYFCYK 271
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1-175 4.90e-53

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: 171.79  E-value: 4.90e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREMVFKETGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTT 80
Cdd:cd14538    35 MVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPLICGGRLEVSLEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTT 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  81 WPDFGVPESPASFLNFLFKVRESGcltpDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLI 160
Cdd:cd14538   115 WPDHGTPQSADPLLRFIRYMRRIH----NSGPIVVHCSAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMI 190

                         170
                  ....*....|....*
gi 1720392689 161 QTPDQLRFSYMAIIE 175
Cdd:cd14538   191 QTKDQYIFCYKACLE 205
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1-174 4.98e-50

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: 164.04  E-value: 4.98e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREMVFKetGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTT 80
Cdd:cd14541    38 MVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFG--NLQITCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLA 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  81 WPDFGVPESPASFLNFLFKVR--ESGCLTPdhgpAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMG 158
Cdd:cd14541   116 WPDHGVPDDSSDFLDFVKRVRqnRVGMVEP----TVVHCSAGIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAM 191

                         170
                  ....*....|....*.
gi 1720392689 159 LIQTPDQLRFSYMAII 174
Cdd:cd14541   192 LIQTPSQYRFVCEAIL 207
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 1-177 7.30e-50

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: 164.49  E-value: 7.30e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREmvfKETGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTT 80
Cdd:cd14553    65 MVWEQRSATIVMMTKLEERSRVKCDQYWPTRGTE---TYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTA 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  81 WPDFGVPESPASFLNFLFKVResGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLI 160
Cdd:cd14553   142 WPDHGVPEHPTPFLAFLRRVK--ACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMV 219

                         170
                  ....*....|....*..
gi 1720392689 161 QTPDQLRFSYMAIIEGA 177
Cdd:cd14553   220 QTEDQYIFIHDALLEAV 236
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1-168 9.66e-50

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


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 163.29  E-value: 9.66e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREmvfkETG-FSVKLLSEDVKSYYTVHLLQLENIN------TGETRTI 73
Cdd:cd14549    33 MVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTE----TYGnIQVTLLSTEVLATYTVRTFSLKNLKlkkvkgRSSERVV 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  74 SHFHYTTWPDFGVPESPASFLNFLFKVreSGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMR 153
Cdd:cd14549   109 YQYHYTQWPDHGVPDYTLPVLSFVRKS--SAANPPGAGPIVVHCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIR 186

                         170
                  ....*....|....*
gi 1720392689 154 KYRMGLIQTPDQLRF 168
Cdd:cd14549   187 TQRNYLVQTEEQYIF 201
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1-168 1.89e-49

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: 162.91  E-value: 1.89e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREMVFKEtgFSVKLLSEDVKSYYTVHLLQLENIntGETRTISHFHYTT 80
Cdd:cd14548    58 MVWEQNSHTIVMLTQCMEKGRVKCDHYWPFDQDPVYYGD--ITVTMLSESVLPDWTIREFKLERG--DEVRSVRQFHFTA 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  81 WPDFGVPESPASFLNFLFKVRESgcLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLI 160
Cdd:cd14548   134 WPDHGVPEAPDSLLRFVRLVRDY--IKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMV 211


                  ....*...
gi 1720392689 161 QTPDQLRF 168
Cdd:cd14548   212 QTEAQYIF 219
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1-175 9.58e-44

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: 147.97  E-value: 9.58e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPtDDREMVFKETGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTT 80
Cdd:cd14596    35 MVWENRSDVIAMMTREVERGKVKCHRYWP-ETLQEPMELENYQLRLENYQALQYFIIRIIKLVEKETGENRLIKHLQFTT 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  81 WPDFGVPESPASFLNFLFKVRESGCLtpdhGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLI 160
Cdd:cd14596   114 WPDHGTPQSSDQLVKFICYMRKVHNT----GPIVVHCSAGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMI 189

                         170
                  ....*....|....*
gi 1720392689 161 QTPDQLRFSYMAIIE 175
Cdd:cd14596   190 QTKDQYLFCYKVVLE 204
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 1-173 9.93e-44

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: 149.15  E-value: 9.93e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPtdDREMVFKETGFSVKLLSEDVKSYYTVHLLQLENINTGE-TRTISHFHYT 79
Cdd:cd14544    71 MVWQENSRVIVMTTKEVERGKNKCVRYWP--DEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDpIREIWHYQYL 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  80 TWPDFGVPESPASFLNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCL-VLMEKGED--VNVKQLLLNMRKYR 156
Cdd:cd14544   149 SWPDHGVPSDPGGVLNFLEDVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLdQIKRKGLDcdIDIQKTIQMVRSQR 228

                         170
                  ....*....|....*..
gi 1720392689 157 MGLIQTPDQLRFSYMAI 173
Cdd:cd14544   229 SGMVQTEAQYKFIYVAV 245
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 1-168 2.09e-43

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: 147.66  E-value: 2.09e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREMVfkeTGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTT 80
Cdd:cd14615    58 MVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQKKDY---GDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTS 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  81 WPDFGVPESPASFLNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLI 160
Cdd:cd14615   135 WPDHGVPETTDLLINFRHLVREYMKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMV 214


                  ....*...
gi 1720392689 161 QTPDQLRF 168
Cdd:cd14615   215 QTEDQYVF 222
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 1-173 4.24e-42

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: 145.16  E-value: 4.24e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTddrEMVFKETG-FSVKLLSEDVKSYYTVHLLQLENINTGET-RTISHFHY 78
Cdd:cd14605    73 MVFQENSRVIVMTTKEVERGKSKCVKYWPD---EYALKEYGvMRVRNVKESAAHDYILRELKLSKVGQGNTeRTVWQYHF 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  79 TTWPDFGVPESPASFLNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCL-VLMEKGE--DVNVKQLLLNMRKY 155
Cdd:cd14605   150 RTWPDHGVPSDPGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIdIIREKGVdcDIDVPKTIQMVRSQ 229

                         170
                  ....*....|....*...
gi 1720392689 156 RMGLIQTPDQLRFSYMAI 173
Cdd:cd14605   230 RSGMVQTEAQYRFIYMAV 247
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 1-175 6.48e-42

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: 142.97  E-value: 6.48e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREMVFKetgFSVKLLSEDVKS-YYTVHLLQLENINTGETRTISHFHYT 79
Cdd:cd14546    34 MIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHI---YEVHLVSEHIWCdDYLVRSFYLKNLQTSETRTVTQFHFL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  80 TWPDFGVPESPASFLNFLFKVRES----GCltpdhgPAVIHCSAGIGRSGTFSLVDTCLVLMEKG-EDVNVKQLLLNMRK 154
Cdd:cd14546   111 SWPDEGIPASAKPLLEFRRKVNKSyrgrSC------PIVVHCSDGAGRTGTYILIDMVLNRMAKGaKEIDIAATLEHLRD 184

                         170       180
                  ....*....|....*....|.
gi 1720392689 155 YRMGLIQTPDQLRFSYMAIIE 175
Cdd:cd14546   185 QRPGMVKTKDQFEFVLTAVAE 205
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1-175 1.01e-41

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: 142.78  E-value: 1.01e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREMVFKetGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTT 80
Cdd:cd14601    38 MTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYG--GFQVTCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIA 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  81 WPDFGVPESPASFLNFLFKVRESGCLTPDhgPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLI 160
Cdd:cd14601   116 WPDHGVPDDSSDFLDFVCLVRNKRAGKDE--PVVVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMI 193

                         170
                  ....*....|....*
gi 1720392689 161 QTPDQLRFSYMAIIE 175
Cdd:cd14601   194 QTPSQYRFVCEAILK 208
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1-170 1.39e-40

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: 139.69  E-value: 1.39e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREMVFKetGFSVKLLSEDV--KSYYTVHLLQLeNINTGETRTISHFHY 78
Cdd:cd18533    34 MIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYG--DLTVELVSEEEndDGGFIVREFEL-SKEDGKVKKVYHIQY 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  79 TTWPDFGVPESPASFLNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKG----------EDVnVKQL 148
Cdd:cd18533   111 KSWPDFGVPDSPEDLLTLIKLKRELNDSASLDPPIIVHCSAGVGRTGTFIALDSLLDELKRGlsdsqdledsEDP-VYEI 189

                         170       180
                  ....*....|....*....|..
gi 1720392689 149 LLNMRKYRMGLIQTPDQLRFSY 170
Cdd:cd18533   190 VNQLRKQRMSMVQTLRQYIFLY 211
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1-171 2.05e-40

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: 140.05  E-value: 2.05e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREMVFKEtgFSVKLLSEDVKSYYTVHLLQLENINTGET-RTISHFHYT 79
Cdd:cd14617    59 MVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDSLYYGD--LIVQMLSESVLPEWTIREFKICSEEQLDApRLVRHFHYT 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  80 TWPDFGVPESPASFLNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGL 159
Cdd:cd14617   137 VWPDHGVPETTQSLIQFVRTVRDYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHM 216

                         170
                  ....*....|..
gi 1720392689 160 IQTPDQlrFSYM 171
Cdd:cd14617   217 VQTECQ--YVYL 226
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 1-175 3.78e-40

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: 140.40  E-value: 3.78e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREmvfKETG-FSVKLLSEDVKSYYTVHLLQLENINTGET-RTISHFHY 78
Cdd:cd14606    86 MAWQENSRVIVMTTREVEKGRNKCVPYWPEVGMQ---RAYGpYSVTNCGEHDTTEYKLRTLQVSPLDNGELiREIWHYQY 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  79 TTWPDFGVPESPASFLNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLME-KG--EDVNVKQLLLNMRKY 155
Cdd:cd14606   163 LSWPDHGVPSEPGGVLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENIStKGldCDIDIQKTIQMVRAQ 242

                         170       180
                  ....*....|....*....|
gi 1720392689 156 RMGLIQTPDQLRFSYMAIIE 175
Cdd:cd14606   243 RSGMVQTEAQYKFIYVAIAQ 262
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
72-175 6.71e-40

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 134.41  E-value: 6.71e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   72 TISHFHYTTWPDFGVPESPASFLNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGED-VNVKQLLL 150
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 1720392689  151 NMRKYRMGLIQTPDQLRFSYMAIIE 175
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 72-175 6.71e-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: 134.41  E-value: 6.71e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   72 TISHFHYTTWPDFGVPESPASFLNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGED-VNVKQLLL 150
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 1720392689  151 NMRKYRMGLIQTPDQLRFSYMAIIE 175
Cdd:smart00012  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 1-174 1.14e-39

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: 138.04  E-value: 1.14e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREMVFKETGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTT 80
Cdd:cd14597    62 MVWEQKSTVIAMMTQEVEGGKIKCQRYWPEILGKTTMVDNRLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTA 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  81 WPDFGVPESPASFLNFLFKVREsgclTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLI 160
Cdd:cd14597   142 WPDHDTPSQPEQLLTFISYMRH----IHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMV 217

                         170
                  ....*....|....
gi 1720392689 161 QTPDQLRFSYMAII 174
Cdd:cd14597   218 QTEDQYIFCYQVIL 231
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1-175 1.33e-39

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: 137.59  E-value: 1.33e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREMVFKETG-FSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYT 79
Cdd:cd14540    35 MVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHDALTFGeYKVSTKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYT 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  80 TWPDFGVPESPASFLNFLFKVRE-----SGCLTPD--HGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNM 152
Cdd:cd14540   115 DWPDHGCPEDVSGFLDFLEEINSvrrhtNQDVAGHnrNPPTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALL 194

                         170       180
                  ....*....|....*....|...
gi 1720392689 153 RKYRMGLIQTPDQLRFSYMAIIE 175
Cdd:cd14540   195 RHQRMLLVQTLAQYKFVYNVLIQ 217
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 1-174 2.09e-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: 138.83  E-value: 2.09e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPtdDREMVFKETGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTT 80
Cdd:cd14600   101 VVWEQKLSLIVMLTTLTERGRTKCHQYWP--DPPDVMEYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVA 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  81 WPDFGVPESPASFLNFLFKVREsgcLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLI 160
Cdd:cd14600   179 WPDHGVPDDSSDFLEFVNYVRS---KRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMV 255

                         170
                  ....*....|....
gi 1720392689 161 QTPDQLRFSYMAII 174
Cdd:cd14600   256 QTSSQYKFVCEAIL 269
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 1-168 2.80e-39

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: 136.76  E-value: 2.80e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKEsVKCAQYWPTddrEMVFKETGFSVKLLSEDVKSYYTVHLLQLENinTGETRTISHFHYTT 80
Cdd:cd14547    60 MVWQEKTPIIVMITNLTEAK-EKCAQYWPE---EENETYGDFEVTVQSVKETDGYTVRKLTLKY--GGEKRYLKHYWYTS 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  81 WPDFGVPESPASFLNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDT-CLVLMEKGEdVNVKQLLLNMRKYRMGL 159
Cdd:cd14547   134 WPDHKTPEAAQPLLSLVQEVEEARQTEPHRGPIVVHCSAGIGRTGCFIATSIgCQQLREEGV-VDVLGIVCQLRLDRGGM 212


                  ....*....
gi 1720392689 160 IQTPDQLRF 168
Cdd:cd14547   213 VQTAEQYEF 221
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 1-177 3.58e-39

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: 138.24  E-value: 3.58e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREMVfkeTGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTT 80
Cdd:cd14626   103 MVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETY---GMIQVTLLDTVELATYSVRTFALYKNGSSEKREVRQFQFMA 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  81 WPDFGVPESPASFLNFLFKVResGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLI 160
Cdd:cd14626   180 WPDHGVPEYPTPILAFLRRVK--ACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMV 257

                         170
                  ....*....|....*..
gi 1720392689 161 QTPDQLRFSYMAIIEGA 177
Cdd:cd14626   258 QTEDQYIFIHEALLEAA 274
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 1-175 4.07e-38

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: 134.25  E-value: 4.07e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREMVFKEtgFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTT 80
Cdd:cd14619    59 MIWEQQSSTIVMLTNCMEAGRVKCEHYWPLDYTPCTYGH--LRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTA 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  81 WPDFGVPESPASFLNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLI 160
Cdd:cd14619   137 WPDHGVPSSTDTLLAFRRLLRQWLDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMV 216

                         170
                  ....*....|....*
gi 1720392689 161 QTPDQLRFSYMAIIE 175
Cdd:cd14619   217 QTESQYVFLHQCILD 231
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 1-175 1.12e-37

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: 134.01  E-value: 1.12e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREmvfkETG-FSVKLLSEDVKSYYTVHLLQLENINTGE---------- 69
Cdd:cd17667    91 MIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSE----EYGnIIVTLKSTKIHACYTVRRFSIRNTKVKKgqkgnpkgrq 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  70 -TRTISHFHYTTWPDFGVPESPASFLNFLfkVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQL 148
Cdd:cd17667   167 nERTVIQYHYTQWPDMGVPEYALPVLTFV--RRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGF 244

                         170       180
                  ....*....|....*....|....*..
gi 1720392689 149 LLNMRKYRMGLIQTPDQLRFSYMAIIE 175
Cdd:cd17667   245 LKHIRTQRNYLVQTEEQYIFIHDALLE 271
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1-170 1.99e-37

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


Pssm-ID: 350399 [Multi-domain]  Cd Length: 202  Bit Score: 131.57  E-value: 1.99e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPtDDREMVFKETGFSVKLLSEDVKSYYTVHLLQLENINTGE--TRTISHFHY 78
Cdd:cd14551    33 MIWEQGSATIVMVTNLKERKEKKCSQYWP-DQGCWTYGNLRVRVEDTVVLVDYTTRKFCIQKVNRGIGEkrVRLVTQFHF 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  79 TTWPDFGVPESPASFLNFLFKVResGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMG 158
Cdd:cd14551   112 TSWPDFGVPFTPIGMLKFLKKVK--SANPPRAGPIVVHCSAGVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQ 189

                         170
                  ....*....|..
gi 1720392689 159 LIQTPDQLRFSY 170
Cdd:cd14551   190 MVQTDMQYVFIY 201
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1-174 8.05e-37

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: 130.10  E-value: 8.05e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREmvfkETG-FSVKLLSEDVKSYYTVHLLQLEN--INTG------ETR 71
Cdd:cd17668    33 MIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSE----EYGnFLVTQKSVQVLAYYTVRNFTLRNtkIKKGsqkgrpSGR 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  72 TISHFHYTTWPDFGVPESPASFLNFLFKvrESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLN 151
Cdd:cd17668   109 VVTQYHYTQWPDMGVPEYTLPVLTFVRK--ASYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKH 186

                         170       180
                  ....*....|....*....|...
gi 1720392689 152 MRKYRMGLIQTPDQLRFSYMAII 174
Cdd:cd17668   187 IRSQRNYLVQTEEQYVFIHDALV 209
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 1-176 8.87e-37

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: 132.14  E-value: 8.87e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREMVfketGF-SVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYT 79
Cdd:cd14625   109 MVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETY----GMiQVTLLDTIELATFCVRTFSLHKNGSSEKREVRQFQFT 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  80 TWPDFGVPESPASFLNFLFKVREsgCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGL 159
Cdd:cd14625   185 AWPDHGVPEYPTPFLAFLRRVKT--CNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYM 262

                         170
                  ....*....|....*..
gi 1720392689 160 IQTPDQLRFSYMAIIEG 176
Cdd:cd14625   263 VQTEDQYSFIHDALLEA 279
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1-170 1.27e-36

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: 129.43  E-value: 1.27e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDdREMVFKETGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTT 80
Cdd:cd14539    34 MVYEQQVSVIVMLVSEQENEKQKVHRYWPTE-RGQALVYGAITVSLQSVRTTPTHVERIISIQHKDTRLSRSVVHLQFTT 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  81 WPDFGVPESPASFLNFLFKVRESGCLT-PDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKG-EDVNVKQLLLNMRKYRMG 158
Cdd:cd14539   113 WPELGLPDSPNPLLRFIEEVHSHYLQQrSLQTPIVVHCSSGVGRTGAFCLLYAAVQEIEAGnGIPDLPQLVRKMRQQRKY 192

                         170
                  ....*....|..
gi 1720392689 159 LIQTPDQLRFSY 170
Cdd:cd14539   193 MLQEKEHLKFCY 204
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 1-175 1.73e-36

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: 129.68  E-value: 1.73e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPtDDREMVFKetgfSVKLLSED--VKSYYTVHLLQLENINTGET---RTISH 75
Cdd:cd14620    57 MVWEQKSATIVMLTNLKERKEEKCYQYWP-DQGCWTYG----NIRVAVEDcvVLVDYTIRKFCIQPQLPDGCkapRLVTQ 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  76 FHYTTWPDFGVPESPASFLNFLFKVREsgcLTPDH-GPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRK 154
Cdd:cd14620   132 LHFTSWPDFGVPFTPIGMLKFLKKVKS---VNPVHaGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRN 208

                         170       180
                  ....*....|....*....|.
gi 1720392689 155 YRMGLIQTPDQLRFSYMAIIE 175
Cdd:cd14620   209 QRPQMVQTDMQYSFIYQALLE 229
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1-175 3.37e-36

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: 128.11  E-value: 3.37e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPtDDREmVFKEtgFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTT 80
Cdd:cd14555    33 MVWQENSASIVMVTNLVEVGRVKCSRYWP-DDTE-VYGD--IKVTLVETEPLAEYVVRTFALERRGYHEIREVRQFHFTG 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  81 WPDFGVPESPASFLNFLFKVRESGclTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLI 160
Cdd:cd14555   109 WPDHGVPYHATGLLGFIRRVKASN--PPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMV 186

                         170
                  ....*....|....*
gi 1720392689 161 QTPDQLRFSYMAIIE 175
Cdd:cd14555   187 QTEEQYIFIHDAILE 201
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 1-176 3.43e-36

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: 130.62  E-value: 3.43e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREMvfkETGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTT 80
Cdd:cd14624   109 MIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTET---YGLIQVTLLDTVELATYCVRTFALYKNGSSEKREVRQFQFTA 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  81 WPDFGVPESPASFLNFLFKVREsgCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLI 160
Cdd:cd14624   186 WPDHGVPEHPTPFLAFLRRVKT--CNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMV 263

                         170
                  ....*....|....*.
gi 1720392689 161 QTPDQLRFSYMAIIEG 176
Cdd:cd14624   264 QTEDQYIFIHDALLEA 279
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 1-175 7.32e-36

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: 129.79  E-value: 7.32e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREMVFKetgFSVKLLSED-------VKSYYtvhllqLENINTGETRTI 73
Cdd:cd14610   107 MVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHI---YEVNLVSEHiwcedflVRSFY------LKNLQTNETRTV 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  74 SHFHYTTWPDFGVPESPASFLNFLFKVREsgCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKG-EDVNVKQLLLNM 152
Cdd:cd14610   178 TQFHFLSWNDQGVPASTRSLLDFRRKVNK--CYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKGaKEIDIAATLEHL 255

                         170       180
                  ....*....|....*....|...
gi 1720392689 153 RKYRMGLIQTPDQLRFSYMAIIE 175
Cdd:cd14610   256 RDQRPGMVQTKEQFEFALTAVAE 278
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1-174 9.92e-36

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: 127.75  E-value: 9.92e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREMVFKEtgFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTT 80
Cdd:cd14618    59 LVWEQQVCNIIMLTVGMENGRVLCDHYWPSESTPVSYGH--ITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTA 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  81 WPDFGVPESPASFLNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLI 160
Cdd:cd14618   137 WPDHGIPESTSSLMAFRELVREHVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMI 216

                         170
                  ....*....|....
gi 1720392689 161 QTPDQLRFSYMAII 174
Cdd:cd14618   217 QTLSQYIFLHSCIL 230
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 1-168 7.99e-35

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: 125.77  E-value: 7.99e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREMVFKEtgFSVKLLSEDVKSYYTVHLLQLENINtgETRTISHFHYTT 80
Cdd:cd14614    74 MVLQQKSQIIVMLTQCNEKRRVKCDHYWPFTEEPVAYGD--ITVEMLSEEEQPDWAIREFRVSYAD--EVQDVMHFNYTA 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  81 WPDFGVPESPA--SFLNFLFKVRESGCLTPdhGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMG 158
Cdd:cd14614   150 WPDHGVPTANAaeSILQFVQMVRQQAVKSK--GPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMS 227

                         170
                  ....*....|
gi 1720392689 159 LIQTPDQLRF 168
Cdd:cd14614   228 MVQTEEQYIF 237
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 1-176 9.61e-35

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: 124.75  E-value: 9.61e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPtDDREMV--FKETGFSVKLLSEdvksyYTVHLLQLENINTGETRTISHFHY 78
Cdd:cd14631    47 MIWQEQSACIVMVTNLVEVGRVKCYKYWP-DDTEVYgdFKVTCVEMEPLAE-----YVVRTFTLERRGYNEIREVKQFHF 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  79 TTWPDFGVPESPASFLNFLFKVRESGclTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMG 158
Cdd:cd14631   121 TGWPDHGVPYHATGLLSFIRRVKLSN--PPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRIN 198

                         170
                  ....*....|....*...
gi 1720392689 159 LIQTPDQLRFSYMAIIEG 176
Cdd:cd14631   199 MVQTEEQYIFIHDAILEA 216
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1-176 6.78e-34

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: 122.47  E-value: 6.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPtDDREMVfkeTGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTT 80
Cdd:cd14632    33 MVWQEHCSSIVMITKLVEVGRVKCSKYWP-DDSDTY---GDIKITLLKTETLAEYSVRTFALERRGYSARHEVKQFHFTS 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  81 WPDFGVPESPASFLNFLFKVRESgcLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLI 160
Cdd:cd14632   109 WPEHGVPYHATGLLAFIRRVKAS--TPPDAGPVVVHCSAGAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMI 186

                         170
                  ....*....|....*.
gi 1720392689 161 QTPDQLRFSYMAIIEG 176
Cdd:cd14632   187 QTEEQYIFIHDAILEA 202
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 1-172 2.28e-33

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: 121.86  E-value: 2.28e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTddrEMVFKETGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTT 80
Cdd:cd14554    68 MLWEHNSTIIVMLTKLREMGREKCHQYWPA---ERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTD 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  81 WPDFGVPESPASFLNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLI 160
Cdd:cd14554   145 WPEQGVPKSGEGFIDFIGQVHKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMV 224

                         170
                  ....*....|..
gi 1720392689 161 QTPDQLRFSYMA 172
Cdd:cd14554   225 QTEDQYQFCYRA 236
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 1-168 2.76e-33

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


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 121.17  E-value: 2.76e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREM-VFKEtgFSVKLLSEDVKSYYTVHLLQLEniNTGETRTISHFHYT 79
Cdd:cd14616    59 MVWETRAKTIVMLTQCFEKGRIRCHQYWPEDNKPVtVFGD--IVITKLMEDVQIDWTIRDLKIE--RHGDYMMVRQCNFT 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  80 TWPDFGVPESPASFLNFLFKVRESgcLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGL 159
Cdd:cd14616   135 SWPEHGVPESSAPLIHFVKLVRAS--RAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCM 212


                  ....*....
gi 1720392689 160 IQTPDQLRF 168
Cdd:cd14616   213 VQNLAQYIF 221
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 1-175 3.45e-33

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: 122.45  E-value: 3.45e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREM--VFKETGFSVKLLSED--VKSYYtvhllqLENINTGETRTISHF 76
Cdd:cd14609   105 MVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLyhIYEVNLVSEHIWCEDflVRSFY------LKNVQTQETRTLTQF 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  77 HYTTWPDFGVPESPASFLNFLFKVREsgCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKG-EDVNVKQLLLNMRKY 155
Cdd:cd14609   179 HFLSWPAEGIPSSTRPLLDFRRKVNK--CYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDIAATLEHVRDQ 256

                         170       180
                  ....*....|....*....|
gi 1720392689 156 RMGLIQTPDQLRFSYMAIIE 175
Cdd:cd14609   257 RPGMVRTKDQFEFALTAVAE 276
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 1-186 5.96e-33

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: 122.44  E-value: 5.96e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPtDDREMVFKETGFSVkllsEDVKSY--YTVHLLQLENI----NTGETRTIS 74
Cdd:cd14621   114 MIWEQNTATIVMVTNLKERKECKCAQYWP-DQGCWTYGNIRVSV----EDVTVLvdYTVRKFCIQQVgdvtNKKPQRLIT 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  75 HFHYTTWPDFGVPESPASFLNFLFKVResGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRK 154
Cdd:cd14621   189 QFHFTSWPDFGVPFTPIGMLKFLKKVK--NCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRA 266

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1720392689 155 YRMGLIQTPDQLRFSYMAIIEgaKYTKGDSNI 186
Cdd:cd14621   267 QRCQMVQTDMQYVFIYQALLE--HYLYGDTEL 296
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1-170 1.04e-32

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: 119.06  E-value: 1.04e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPtDDREMVFKETGFSVKLLSEDVKSY-YTVHLLQLENINtgETRTISHFHYT 79
Cdd:cd14542    33 MIWEYNVQVIVMACREFEMGKKKCERYWP-EEGEEQLQFGPFKISLEKEKRVGPdFLIRTLKVTFQK--ESRTVYQFHYT 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  80 TWPDFGVPESPASFLNFLFKVREsgCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKG---EDVNVKQLLLNMRKYR 156
Cdd:cd14542   110 AWPDHGVPSSVDPILDLVRLVRD--YQGSEDVPICVHCSAGCGRTGTICAIDYVWNLLKTGkipEEFSLFDLVREMRKQR 187

                         170
                  ....*....|....
gi 1720392689 157 MGLIQTPDQLRFSY 170
Cdd:cd14542   188 PAMVQTKEQYELVY 201
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1-178 1.86e-32

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 121.26  E-value: 1.86e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREMVfkeTGFSVKLLSEDVKS--YYTVHLLQLENINTGETRTISHFHY 78
Cdd:PHA02742  112 AIFQDQVRVIVMITKIMEDGKEACYPYWMPHERGKA---THGEFKIKTKKIKSfrNYAVTNLCLTDTNTGASLDIKHFAY 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  79 TTWPDFGVPESPASFLNFLFKVRESGCLT--PDHG-------PAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLL 149
Cdd:PHA02742  189 EDWPHGGLPRDPNKFLDFVLAVREADLKAdvDIKGenivkepPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIV 268

                         170       180
                  ....*....|....*....|....*....
gi 1720392689 150 LNMRKYRMGLIQTPDQLRFSYMAIIEGAK 178
Cdd:PHA02742  269 RDLRKQRHNCLSLPQQYIFCYFIVLIFAK 297
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1-173 4.38e-32

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: 117.37  E-value: 4.38e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDremVFKETGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTT 80
Cdd:cd14552    33 MIWEWKSCSIVMLTEIKERSQNKCAQYWPEDG---SVSSGDITVELKDQTDYEDYTLRDFLVTKGKGGSTRTVRQFHFHG 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  81 WPDFGVPESPASFLNFLFKVRESGCLTPDHgPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLI 160
Cdd:cd14552   110 WPEVGIPDNGKGMIDLIAAVQKQQQQSGNH-PITVHCSAGAGRTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMV 188

                         170
                  ....*....|...
gi 1720392689 161 QTPDQLRFSYMAI 173
Cdd:cd14552   189 QTLEQYEFCYKVV 201
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 1-176 4.97e-32

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: 119.38  E-value: 4.97e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPtDDREmVFKEtgFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTT 80
Cdd:cd14633   102 MVWHENTASIIMVTNLVEVGRVKCCKYWP-DDTE-IYKD--IKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTG 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  81 WPDFGVPESPASFLNFLFKVRESGclTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLI 160
Cdd:cd14633   178 WPDHGVPYHATGLLGFVRQVKSKS--PPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMV 255

                         170
                  ....*....|....*.
gi 1720392689 161 QTPDQLRFSYMAIIEG 176
Cdd:cd14633   256 QTEEQYVFIHDAILEA 271
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 1-175 7.14e-32

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: 118.77  E-value: 7.14e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREMVFKEtgFSVKLLSEDVKSYYTVhLLQLENINTGETRTISHFHYTT 80
Cdd:cd14603    92 MIWQYGVKVILMACREIEMGKKKCERYWAQEQEPLQTGP--FTITLVKEKRLNEEVI-LRTLKVTFQKESRSVSHFQYMA 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  81 WPDFGVPESPASFLNFLFKVRESGCLTPDhgPAVIHCSAGIGRSGTFSLVDTC--LVLMEK-GEDVNVKQLLLNMRKYRM 157
Cdd:cd14603   169 WPDHGIPDSPDCMLAMIELARRLQGSGPE--PLCVHCSAGCGRTGVICTVDYVrqLLLTQRiPPDFSIFDVVLEMRKQRP 246

                         170
                  ....*....|....*...
gi 1720392689 158 GLIQTPDQLRFSYMAIIE 175
Cdd:cd14603   247 AAVQTEEQYEFLYHTVAQ 264
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 1-176 9.52e-32

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: 117.82  E-value: 9.52e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPtDDREmVFKEtgFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTT 80
Cdd:cd14630    65 MIWQENSASVVMVTNLVEVGRVKCVRYWP-DDTE-VYGD--IKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTS 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  81 WPDFGVPESPASFLNFLFKVRESGclTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLI 160
Cdd:cd14630   141 WPDHGVPCYATGLLGFVRQVKFLN--PPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMV 218

                         170
                  ....*....|....*.
gi 1720392689 161 QTPDQLRFSYMAIIEG 176
Cdd:cd14630   219 QTEEQYVFVHDAILEA 234
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1-178 5.23e-31

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 117.82  E-value: 5.23e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTvEKESVKCAQYWPT-DDREMVFKEtgFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYT 79
Cdd:PHA02746  132 LISEHESQVIVSLTDI-DDDDEKCFELWTKeEDSELAFGR--FVAKILDIIEELSFTKTRLMITDKISDTSREIHHFWFP 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  80 TWPDFGVPESPASFLNFLFKVRE--------SGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLN 151
Cdd:PHA02746  209 DWPDNGIPTGMAEFLELINKVNEeqaelikqADNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLK 288

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1720392689 152 MRKYRMGLIQTPDQLRFSYM----AIIEGAK 178
Cdd:PHA02746  289 IRKQRHSSVFLPEQYAFCYKalkyAIIEEAK 319
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 1-170 1.35e-29

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: 112.24  E-value: 1.35e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESvKCAQYWPTddREMVFKETGFSVKLLSEdvKSYYTVHLL--QLEnintGETRTISHFHY 78
Cdd:cd14612    79 MVWQEECPIIVMITKLKEKKE-KCVHYWPE--KEGTYGRFEIRVQDMKE--CDGYTIRDLtiQLE----EESRSVKHYWF 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  79 TTWPDFGVPESPASFLNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDT-CLVLMEKGeDVNVKQLLLNMRKYRM 157
Cdd:cd14612   150 SSWPDHQTPESAGPLLRLVAEVEESRQTAASPGPIVVHCSAGIGRTGCFIATSIgCQQLKDTG-KVDILGIVCQLRLDRG 228

                         170
                  ....*....|...
gi 1720392689 158 GLIQTPDQLRFSY 170
Cdd:cd14612   229 GMIQTSEQYQFLH 241
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1-165 2.55e-29

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: 110.30  E-value: 2.55e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREM-VFKEtgFSVKLLSEDVKSYYTVHLLQLENINTGET-RTISHFHY 78
Cdd:cd14557    33 MIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSrAFGD--VVVKINEEKICPDYIIRKLNINNKKEKGSgREVTHIQF 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  79 TTWPDFGVPESPasflNFLFKVRE-----SGCLTpdhGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMR 153
Cdd:cd14557   111 TSWPDHGVPEDP----HLLLKLRRrvnafNNFFS---GPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLR 183

                         170
                  ....*....|..
gi 1720392689 154 KYRMGLIQTPDQ 165
Cdd:cd14557   184 RQRCLMVQVEAQ 195
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 1-175 4.06e-29

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: 112.13  E-value: 4.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTddrEMVFKETGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTT 80
Cdd:cd14628   114 MLWEHNSTIVVMLTKLREMGREKCHQYWPA---ERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTD 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  81 WPDFGVPESPASFLNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLI 160
Cdd:cd14628   191 WPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMV 270

                         170
                  ....*....|....*
gi 1720392689 161 QTPDQLRFSYMAIIE 175
Cdd:cd14628   271 QTEDQYQFCYRAALE 285
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 1-175 4.35e-29

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: 110.52  E-value: 4.35e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDrEMVFKEtgFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTT 80
Cdd:cd14623    58 MIWEWKSCSIVMLTELEERGQEKCAQYWPSDG-SVSYGD--ITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHG 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  81 WPDFGVPESPASFLNFLFKVRESGCLTPDHgPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLI 160
Cdd:cd14623   135 WPEVGIPSDGKGMINIIAAVQKQQQQSGNH-PITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMV 213

                         170
                  ....*....|....*
gi 1720392689 161 QTPDQLRFSYMAIIE 175
Cdd:cd14623   214 QTLEQYEFCYKVVQE 228
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1-170 6.68e-29

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: 109.02  E-value: 6.68e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDdremvfKET--GFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHY 78
Cdd:cd14558    33 MIFQKKVKVIVMLTELKEGDQEQCAQYWGDE------KKTygDIEVELKDTEKSPTYTVRVFEITHLKRKDSRTVYQYQY 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  79 TTWPDFGVPESPASFLNFLFKVRESG----CLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRK 154
Cdd:cd14558   107 HKWKGEELPEKPKDLVDMIKSIKQKLpyknSKHGRSVPIVVHCSDGSSRTGIFCALWNLLESAETEKVVDVFQVVKALRK 186

                         170
                  ....*....|....*.
gi 1720392689 155 YRMGLIQTPDQLRFSY 170
Cdd:cd14558   187 QRPGMVSTLEQYQFLY 202
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1-170 8.37e-29

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: 109.09  E-value: 8.37e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKES-VKCAQYWPTDDRE-MVFKETGFSVKLLSEDVKSYyTVHLLQLENINTGET-RTISHFH 77
Cdd:cd17658    35 MVIQQRCPVIIMLTRLVDNYStAKCADYFPAEENEsREFGRISVTNKKLKHSQHSI-TLRVLEVQYIESEEPpLSVLHIQ 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  78 YTTWPDFGVPESPASFLNFLfkvRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKG--EDVNVKQLLLNMRKY 155
Cdd:cd17658   114 YPEWPDHGVPKDTRSVRELL---KRLYGIPPSAGPIVVHCSAGIGRTGAYCTIHNTIRRILEGdmSAVDLSKTVRKFRSQ 190

                         170
                  ....*....|....*
gi 1720392689 156 RMGLIQTPDQLRFSY 170
Cdd:cd17658   191 RIGMVQTQDQYIFCY 205
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 1-175 2.26e-28

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: 108.77  E-value: 2.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWpTDDREMVFKETGFSVKLLSEDVKSYYTVHLLQLENINtgETRTISHFHYTT 80
Cdd:cd14602    60 MIWEYSVLIIVMACMEFEMGKKKCERYW-AEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNS--ETRTIYQFHYKN 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  81 WPDFGVPESPASFLNFLFKVResgCLTPDHG-PAVIHCSAGIGRSGTFSLVDTCLVLMEKG---EDVNVKQLLLNMRKYR 156
Cdd:cd14602   137 WPDHDVPSSIDPILELIWDVR---CYQEDDSvPICIHCSAGCGRTGVICAIDYTWMLLKDGiipENFSVFSLIQEMRTQR 213

                         170
                  ....*....|....*....
gi 1720392689 157 MGLIQTPDQLRFSYMAIIE 175
Cdd:cd14602   214 PSLVQTKEQYELVYNAVIE 232
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 1-168 2.68e-28

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: 108.08  E-value: 2.68e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESvKCAQYWPtDDREMVFKetgfsVKLLSEDVKS--YYTVHLLQLENinTGETRTISHFHY 78
Cdd:cd14611    63 MVWQEDSPVIVMITKLKEKNE-KCVLYWP-EKRGIYGK-----VEVLVNSVKEcdNYTIRNLTLKQ--GSQSRSVKHYWY 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  79 TTWPDFGVPESPASFLNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTF-SLVDTCLVLMEKGEdVNVKQLLLNMRKYRM 157
Cdd:cd14611   134 TSWPDHKTPDSAQPLLQLMLDVEEDRLASPGRGPVVVHCSAGIGRTGCFiATTIGCQQLKEEGV-VDVLSIVCQLRVDRG 212

                         170
                  ....*....|.
gi 1720392689 158 GLIQTPDQLRF 168
Cdd:cd14611   213 GMVQTSEQYEF 223
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 1-175 4.25e-28

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: 4.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTddrEMVFKETGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTT 80
Cdd:cd14627   115 MLWENNSTIVVMLTKLREMGREKCHQYWPA---ERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTD 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  81 WPDFGVPESPASFLNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLI 160
Cdd:cd14627   192 WPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMV 271

                         170
                  ....*....|....*
gi 1720392689 161 QTPDQLRFSYMAIIE 175
Cdd:cd14627   272 QTEDEYQFCYQAALE 286
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 1-175 1.44e-27

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: 107.89  E-value: 1.44e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTddrEMVFKETGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTT 80
Cdd:cd14629   115 MLWEHNSTIVVMLTKLREMGREKCHQYWPA---ERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTD 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  81 WPDFGVPESPASFLNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLI 160
Cdd:cd14629   192 WPEQGVPKTGEGFIDFIGQVHKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMV 271

                         170
                  ....*....|....*
gi 1720392689 161 QTPDQLRFSYMAIIE 175
Cdd:cd14629   272 QTEDQYQLCYRAALE 286
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 1-168 3.19e-27

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: 106.10  E-value: 3.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNrTVEKESVKCAQYWPtdDREMVFKETGFSVK--LLSEDvksyYTVHLLQLENinTGETRTISHFHY 78
Cdd:cd14613    89 MVWQERSPIIVMIT-NIEEMNEKCTEYWP--EEQVTYEGIEITVKqvIHADD----YRLRLITLKS--GGEERGLKHYWY 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  79 TTWPDFGVPESPASFLNFLFKVRES-GCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRM 157
Cdd:cd14613   160 TSWPDQKTPDNAPPLLQLVQEVEEArQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRG 239

                         170
                  ....*....|.
gi 1720392689 158 GLIQTPDQLRF 168
Cdd:cd14613   240 GMIQTCEQYQF 250
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 1-173 6.69e-27

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: 106.17  E-value: 6.69e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPT-DDREMVFKEtgFSVKLLSEDVKSYYTVHLLQLENINtgETRTISHFHYT 79
Cdd:cd14604   119 MIWEYNVAIIVMACREFEMGRKKCERYWPLyGEEPMTFGP--FRISCEAEQARTDYFIRTLLLEFQN--ETRRLYQFHYV 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  80 TWPDFGVPESPASFLNFLFKVRESGclTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKG---EDVNVKQLLLNMRKYR 156
Cdd:cd14604   195 NWPDHDVPSSFDSILDMISLMRKYQ--EHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGkipEEFNVFNLIQEMRTQR 272

                         170
                  ....*....|....*..
gi 1720392689 157 MGLIQTPDQLRFSYMAI 173
Cdd:cd14604   273 HSAVQTKEQYELVHRAI 289
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1-175 6.75e-26

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: 101.59  E-value: 6.75e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWP-TDDREMVFKETGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYT 79
Cdd:cd14598    35 MVWEQGVAIIAMVTAEEEGGREKSFRYWPrLGSRHNTVTYGRFKITTRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYT 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  80 TWPDFGVPESPASFLNFLFK---VRESGCLTPD----HGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNM 152
Cdd:cd14598   115 DWPEHGCPEDLKGFLSYLEEiqsVRRHTNSTIDpkspNPPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDML 194

                         170       180
                  ....*....|....*....|...
gi 1720392689 153 RKYRMGLIQTPDQLRFSYMAIIE 175
Cdd:cd14598   195 RQQRMMMVQTLSQYTFVYKVLIQ 217
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 1-175 7.25e-26

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


Pssm-ID: 350447 [Multi-domain]  Cd Length: 287  Bit Score: 103.15  E-value: 7.25e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREMVFKETG-FSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYT 79
Cdd:cd14599   101 MVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGSKHSSATYGkFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYT 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  80 TWPDFGVPESPASFLNFLFKVRE-----------SGCLTPdhgPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQL 148
Cdd:cd14599   181 DWPDHGCPEEVQGFLSYLEEIQSvrrhtnsmldsTKNCNP---PIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVM 257

                         170       180
                  ....*....|....*....|....*..
gi 1720392689 149 LLNMRKYRMGLIQTPDQLRFSYMAIIE 175
Cdd:cd14599   258 LRHLREQRMFMIQTIAQYKFVYQVLIQ 284
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1-168 1.66e-24

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 100.08  E-value: 1.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRT--VEKESvKCAQYW-PTDDREMVFKetGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFH 77
Cdd:PHA02747  112 AVWQEHCSIIVMLTPTkgTNGEE-KCYQYWcLNEDGNIDME--DFRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQ 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  78 YTTWPDFGVPESPASFLNFLFKV----RESGCLTPDH----GPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLL 149
Cdd:PHA02747  189 CSEWFEDETPSDHPDFIKFIKIIdinrKKSGKLFNPKdallCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTA 268

                         170
                  ....*....|....*....
gi 1720392689 150 LNMRKYRMGLIQTPDQLRF 168
Cdd:PHA02747  269 EKIREQRHAGIMNFDDYLF 287
PHA02738 PHA02738
hypothetical protein; Provisional
 1-173 2.34e-24

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 100.00  E-value: 2.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWP----TDDREMVFKETGFSVKLLSEDVKSyyTVHLLQleniNTGETRTISHF 76
Cdd:PHA02738  109 MLWMEHVQIIVMLCKKKENGREKCFPYWSdveqGSIRFGKFKITTTQVETHPHYVKS--TLLLTD----GTSATQTVTHF 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  77 HYTTWPDFGVPESPASFLNFLFKVRES-----------GCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNV 145
Cdd:PHA02738  183 NFTAWPDHDVPKNTSEFLNFVLEVRQCqkelaqeslqiGHNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSI 262

                         170       180
                  ....*....|....*....|....*...
gi 1720392689 146 KQLLLNMRKYRMGLIQTPDQLRFSYMAI 173
Cdd:PHA02738  263 PSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1-173 3.95e-24

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: 3.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDrEMVFKEtgFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTT 80
Cdd:cd14622    34 MVWEWKCHTIVMLTELQEREQEKCVQYWPSEG-SVTHGE--ITIEIKNDTLLETISIRDFLVTYNQEKQTRLVRQFHFHG 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  81 WPDFGVPESPASFLNFLFKVRESGCLTPDHgPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLI 160
Cdd:cd14622   111 WPEIGIPAEGKGMIDLIAAVQKQQQQTGNH-PIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMV 189

                         170
                  ....*....|...
gi 1720392689 161 QTPDQLRFSYMAI 173
Cdd:cd14622   190 QTLEQYEFCYRVV 202
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
1-166 2.38e-23

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 96.31  E-value: 2.38e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVE--KESVKCAQYWPTDDREMVFKetgFSVKLL-SEDVKSYYTVHLLQLENINTG-ETRTISHF 76
Cdd:COG5599    96 MLFDNNTPVLVVLASDDEisKPKVKMPVYFRQDGEYGKYE---VSSELTeSIQLRDGIEARTYVLTIKGTGqKKIEIPVL 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  77 HYTTWPDFGVPESPAsFLNFLFKVRES-GCLTPDHGPAVIHCSAGIGRSGTFSLvdtCLVLM-----EKGEDVNVKQLLL 150
Cdd:COG5599   173 HVKNWPDHGAISAEA-LKNLADLIDKKeKIKDPDKLLPVVHCRAGVGRTGTLIA---CLALSksinaLVQITLSVEEIVI 248

                         170
                  ....*....|....*..
gi 1720392689 151 NMRKYR-MGLIQTPDQL 166
Cdd:COG5599   249 DMRTSRnGGMVQTSEQL 265
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1-170 7.65e-22

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: 90.54  E-value: 7.65e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNrTVEKESVKCAQYWPTDDRemvfKETG-FSVKLLSEDVKSYYTVHLLQLENINTGE--TRTISHFH 77
Cdd:cd14556    33 LVYDYGCTSIVMLN-QLDPKDQSCPQYWPDEGS----GTYGpIQVEFVSTTIDEDVISRIFRLQNTTRPQegYRMVQQFQ 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  78 YTTWPDFG-VPESPASFLNFLFKV----RESGcltpdHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNM 152
Cdd:cd14556   108 FLGWPRDRdTPPSKRALLKLLSEVekwqEQSG-----EGPIVVHCLNGVGRSGVFCAISSVCERIKVENVVDVFQAVKTL 182

                         170
                  ....*....|....*...
gi 1720392689 153 RKYRMGLIQTPDQLRFSY 170
Cdd:cd14556   183 RNHRPNMVETEEQYKFCY 200
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1-170 1.49e-18

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: 81.60  E-value: 1.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKEsvKCAQYWPTDDREMVFKetGFSVKLLSEDVKSY-----YTVHLLQLENINTGETRTISH 75
Cdd:cd14550    33 MIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKPLECE--TFKVTLSGEDHSCLsneirLIVRDFILESTQDDYVLEVRQ 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  76 FHYTTWPDfgvPESPAS-FLNFLFKVRESgCLTPDhGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQL--LLNM 152
Cdd:cd14550   109 FQCPSWPN---PCSPIHtVFELINTVQEW-AQQRD-GPIVVHDRYGGVQAATFCALTTLHQQLEHESSVDVYQVakLYHL 183

                         170
                  ....*....|....*...
gi 1720392689 153 RkyRMGLIQTPDQLRFSY 170
Cdd:cd14550   184 M--RPGVFTSKEDYQFLY 199
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1-173 3.52e-17

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 79.63  E-value: 3.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKcaQYWPTDDReMVFKETGFSVKLLSEDVKSYYTVHLLQLENiNTGETRTISHFHYTT 80
Cdd:PHA02740  110 ALSDNKVQIIVLISRHADKKCFN--QFWSLKEG-CVITSDKFQIETLEIIIKPHFNLTLLSLTD-KFGQAQKISHFQYTA 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  81 WPDFGVPESPASFLNFLFKVrESGCLTPDH-------GPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMR 153
Cdd:PHA02740  186 WPADGFSHDPDAFIDFFCNI-DDLCADLEKhkadgkiAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVR 264

                         170       180
                  ....*....|....*....|
gi 1720392689 154 KYRMGLIQTPDQLRFSYMAI 173
Cdd:PHA02740  265 QKKYGCMNCLDDYVFCYHLI 284
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1-175 8.47e-15

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: 71.48  E-value: 8.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESV-KCAQYWPTDDREmvfKETGFSVKLLSEDVKSYYTVHLLQLENIN--TGETRTISHFH 77
Cdd:cd14637    33 LVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQ---QYGPMEVEFVSGSADEDIVTRLFRVQNITrlQEGHLMVRHFQ 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  78 YTTWPDF-GVPESPASFLNFLFKV----RESGcltpdHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNM 152
Cdd:cd14637   110 FLRWSAYrDTPDSKKAFLHLLASVekwqRESG-----EGRTVVHCLNGGGRSGTYCASAMILEMIRCHNIVDVFYAVKTL 184

                         170       180
                  ....*....|....*....|...
gi 1720392689 153 RKYRMGLIQTPDQLRFSYMAIIE 175
Cdd:cd14637   185 RNYKPNMVETLEQYRFCYEIALE 207
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1-174 7.80e-12

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: 63.16  E-value: 7.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVML--NRTV-EKESVkcaqYWPTddREMVFKETGFSVKLLSEDV-----KSYYTVHLLQLENINTGETRT 72
Cdd:cd17670    33 MIWDHNAQIIVMLpdNQGLaEDEFV----YWPS--REESMNCEAFTVTLISKDRlclsnEEQIIIHDFILEATQDDYVLE 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  73 ISHFHYTTWPDfgvPESPASFLNFLFKVRESGCLTPDhGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNM 152
Cdd:cd17670   107 VRHFQCPKWPN---PDAPISSTFELINVIKEEALTRD-GPTIVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMI 182

                         170       180
                  ....*....|....*....|..
gi 1720392689 153 RKYRMGLIQTPDQLRFSYMAII 174
Cdd:cd17670   183 NLMRPGVFTDIEQYQFLYKAML 204
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1-175 8.15e-12

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: 63.12  E-value: 8.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNrtvEKESVK-CAQYWPTddremvfKETG----FSVKLLSEDVKSYYTVHLLQLENINTGET--RTI 73
Cdd:cd14634    33 LVFDYNCSSVVMLN---EMDAAQlCMQYWPE-------KTSCcygpIQVEFVSADIDEDIISRIFRICNMARPQDgyRIV 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  74 SHFHYTTWPDF-GVPESPASFLNF---LFKVRESgcLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLL 149
Cdd:cd14634   103 QHLQYIGWPAYrDTPPSKRSILKVvrrLEKWQEQ--YDGREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHTV 180

                         170       180
                  ....*....|....*....|....*.
gi 1720392689 150 LNMRKYRMGLIQTPDQLRFSYMAIIE 175
Cdd:cd14634   181 KTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1-174 1.00e-11

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: 62.70  E-value: 1.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVML---NRTVEKESVkcaqYWPTDDREMVFKetGFSVKLLSEDVK--SYYTVHLLQ---LENINTGETRT 72
Cdd:cd17669    33 MIWDHNAQLIVMLpdgQNMAEDEFV----YWPNKDEPINCE--TFKVTLIAEEHKclSNEEKLIIQdfiLEATQDDYVLE 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  73 ISHFHYTTWPDfgvPESPASFLNFLFKVRESGCLTPDhGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNM 152
Cdd:cd17669   107 VRHFQCPKWPN---PDSPISKTFELISIIKEEAANRD-GPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMI 182

                         170       180
                  ....*....|....*....|..
gi 1720392689 153 RKYRMGLIQTPDQLRFSYMAII 174
Cdd:cd17669   183 NLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1-175 6.00e-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: 60.47  E-value: 6.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTveKESVKCAQYWPTDDremVFKETGFSVKLLSEDVKSYYTVHLLQLENINTGET--RTISHFHY 78
Cdd:cd14635    33 LVLDYHCTSIVMLNDV--DPAQLCPQYWPENG---VHRHGPIQVEFVSADLEEDIISRIFRIYNAARPQDgyRMVQQFQF 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  79 TTWPDF-GVPESPASFLNFLFKV-RESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYR 156
Cdd:cd14635   108 LGWPMYrDTPVSKRSFLKLIRQVdKWQEEYNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNK 187

                         170
                  ....*....|....*....
gi 1720392689 157 MGLIQTPDQLRFSYMAIIE 175
Cdd:cd14635   188 PNMVDLLDQYKFCYEVALE 206
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
46-168 8.28e-11

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 58.83  E-value: 8.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  46 LLSEDVKSYYTVHLLQLENINTGETRTISHFHYTtWPDFGVPEsPASFLNFLFKVREsgcLTPDHGPAVIHCSAGIGRSG 125
Cdd:COG2453    21 LKREGIDAVVSLTEEEELLLGLLEEAGLEYLHLP-IPDFGAPD-DEQLQEAVDFIDE---ALREGKKVLVHCRGGIGRTG 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1720392689 126 TFslvdTCLVLMEKGedVNVKQLLLNMRKYRMGLIQTPDQLRF 168
Cdd:COG2453    96 TV----AAAYLVLLG--LSAEEALARVRAARPGAVETPAQRAF 132
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1-175 2.05e-10

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: 59.27  E-value: 2.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESvkCAQYWPtddREMVFKETGFSVKLLSEDVKSYYTVHLLQLENINTGET--RTISHFHY 78
Cdd:cd14636    33 LVYDYGCTSIVMLNEVDLAQG--CPQYWP---EEGMLRYGPIQVECMSCSMDCDVISRIFRICNLTRPQEgyLMVQQFQY 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  79 TTWPDF-GVPESPASFLNFLFKVR--ESGCLTPDhGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKY 155
Cdd:cd14636   108 LGWASHrEVPGSKRSFLKLILQVEkwQEECDEGE-GRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNS 186

                         170       180
                  ....*....|....*....|
gi 1720392689 156 RMGLIQTPDQLRFSYMAIIE 175
Cdd:cd14636   187 KPNMVETPEQYRFCYDVALE 206
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 82-168 2.97e-09

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: 54.96  E-value: 2.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  82 PDFGVPESPASFLNFLFKVREsgCLTpDHGPAVIHCSAGIGRSGtfsLVDTCLvLMEKGEDVNVKQLLLNMRKYRMGLIQ 161
Cdd:cd14505    81 PDGGVPSDIAQWQELLEELLS--ALE-NGKKVLIHCKGGLGRTG---LIAACL-LLELGDTLDPEQAIAAVRALRPGAIQ 153


                  ....*..
gi 1720392689 162 TPDQLRF 168
Cdd:cd14505   154 TPKQENF 160
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 1-166 3.65e-08

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: 52.79  E-value: 3.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689   1 MVWQQKTKAVVMLNRTVEKESVKCAQYWPTDdremvfkETGFSVKLLSEDVKSYY-----TVHLLQLENINTGETRTISH 75
Cdd:cd14559    48 MLADNRTPCLVVLASNKDIQRKGLPPYFRQS-------GTYGSVTVKSKKTGKDElvdglKADMYNLKITDGNKTITIPV 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  76 FHYTTWPDFG-------------VPESPASFLNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSlvdTCLVLMEKGED 142
Cdd:cd14559   121 VHVTNWPDHTaisseglkeladlVNKSAEEKRNFYKSKGSSAINDKNKLLPVIHCRAGVGRTGQLA---AAMELNKSPNN 197

                         170       180
                  ....*....|....*....|....*
gi 1720392689 143 VNVKQLLLNMRKYRMG-LIQTPDQL 166
Cdd:cd14559   198 LSVEDIVSDMRTSRNGkMVQKDEQL 222
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 90-168 1.10e-05

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: 43.49  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  90 PASFLNFLFKVREsgCLTPDHgPAVIHCSAGIGRSGTFslvdTCLVLMEKGeDVNVKQLLLNMRKYR-MGLIQTPDQLRF 168
Cdd:cd14494    39 LAMVDRFLEVLDQ--AEKPGE-PVLVHCKAGVGRTGTL----VACYLVLLG-GMSAEEAVRIVRLIRpGGIPQTIEQLDF 110
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 110-156 4.06e-04

bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa TpbA; This subfamily contains bacterial protein tyrosine phosphatases (PTPs) and dual-specificity phosphatases (DUSPs) related to Pseudomonas aeruginosa TpbA, a DUSP that negatively regulates biofilm formation by converting extracellular quorum sensing signals and to Mycobacterium tuberculosis PtpB, a PTP virulence factor that attenuates host immune defenses by interfering with signal transduction pathways in macrophages. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides, while DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and PTPs.


Pssm-ID: 350378 [Multi-domain]  Cd Length: 158  Bit Score: 40.05  E-value: 4.06e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1720392689 110 HGPAVIHCSAGIGRSGTFSLVdtCLVLMEKGEDVNVKQLLLNMRKYR 156
Cdd:cd14529    89 PGPVLIHCKHGKDRTGLVSAL--YRIVYGGSKEEANEDYRLSNRHLE 133
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 82-168 4.72e-04

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


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 39.57  E-value: 4.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  82 PDFGVP--ESPASFLNFLFKVRESGcltpdhGPAVIHCSAGIGRSGTFSlvdTC-LVLMEK--GEDVnVKQLllnmRKYR 156
Cdd:cd14504    58 EDYTPPtlEQIDEFLDIVEEANAKN------EAVLVHCLAGKGRTGTML---ACyLVKTGKisAVDA-INEI----RRIR 123

                          90
                  ....*....|..
gi 1720392689 157 MGLIQTPDQLRF 168
Cdd:cd14504   124 PGSIETSEQEKF 135
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 73-168 5.36e-04

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: 40.41  E-value: 5.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392689  73 ISHFHYTtWPDFGVPeSPASFLN----FLFKVRESGcltpdhgPAVIHCSAGIGRSGtfsLVDTCLVLMekGEDVNVKQL 148
Cdd:cd14506    77 IYFYNFG-WKDYGVP-SLTTILDivkvMAFALQEGG-------KVAVHCHAGLGRTG---VLIACYLVY--ALRMSADQA 142

                          90       100
                  ....*....|....*....|
gi 1720392689 149 LLNMRKYRMGLIQTPDQLRF 168
Cdd:cd14506   143 IRLVRSKRPNSIQTRGQVLC 162
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 113-170 7.35e-04

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: 39.10  E-value: 7.35e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720392689 113 AVIHCSAGIGRSGTFslvdTCLVLMEKG--EDVNVKQLLLNMRKYRMGL--IQTPDQLRFSY 170
Cdd:cd14497    98 AVVHCKAGKGRTGTV----ICAYLLYYGqySTADEALEYFAKKRFKEGLpgVTIPSQLRYLQ 155
 
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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