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Conserved domains on  [gi|193202549|ref|NP_001122448|]
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Tyrosine-protein phosphatase non-receptor type eak-6 [Caenorhabditis elegans]

Protein Classification

protein tyrosine phosphatase family protein( domain architecture ID 12193126)

cys-based protein tyrosine phosphatase (PTP) family protein, such as tyrosine-protein phosphatase that catalyzes the dephosphorylation of phosphotyrosine groups in phosphoproteins

CATH:  3.90.190.10
EC:  3.1.3.-
Gene Ontology:  GO:0004721|GO:0006470
PubMed:  27514797|17057753

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
36-308 8.11e-60

Protein tyrosine phosphatase, catalytic domain;


:

Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 194.41  E-value: 8.11e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549    36 IIADFDRYQRAR----TISEGQRTENIHRNIYGAV-PYDYNLVNLTSTQRNPLGYINASVAEFPEIGRHYIITGAAQDTQ 110
Cdd:smart00194   2 LEEEFEKLDRLKpddeSCTVAAFPENRDKNRYKDVlPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPST 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549   111 IPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKYFPNNTREELKFGIYDITCKEFVKRNILEYRLLEVSVGN--ETHQVHH 188
Cdd:smart00194  82 VEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGcsETRTVTH 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549   189 YKFHGWTEFNLPKY-EDFMAFYNTMKEVgvpllavmknncmssffkKYHHTPPTnapIIQCSTGGARCGVFiiIDILINL 267
Cdd:smart00194 162 YHYTNWPDHGVPESpESILDLIRAVRKS------------------QSTSTGPI---VVHCSAGVGRTGTF--IAIDILL 218

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 193202549   268 IDNRIKNSYSIEWWMLKVRSKRNHSALTNQQHSFIYDIIIK 308
Cdd:smart00194 219 QQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
36-308 8.11e-60

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 194.41  E-value: 8.11e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549    36 IIADFDRYQRAR----TISEGQRTENIHRNIYGAV-PYDYNLVNLTSTQRNPLGYINASVAEFPEIGRHYIITGAAQDTQ 110
Cdd:smart00194   2 LEEEFEKLDRLKpddeSCTVAAFPENRDKNRYKDVlPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPST 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549   111 IPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKYFPNNTREELKFGIYDITCKEFVKRNILEYRLLEVSVGN--ETHQVHH 188
Cdd:smart00194  82 VEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGcsETRTVTH 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549   189 YKFHGWTEFNLPKY-EDFMAFYNTMKEVgvpllavmknncmssffkKYHHTPPTnapIIQCSTGGARCGVFiiIDILINL 267
Cdd:smart00194 162 YHYTNWPDHGVPESpESILDLIRAVRKS------------------QSTSTGPI---VVHCSAGVGRTGTF--IAIDILL 218

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 193202549   268 IDNRIKNSYSIEWWMLKVRSKRNHSALTNQQHSFIYDIIIK 308
Cdd:smart00194 219 QQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 85-304 1.54e-43

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: 150.13  E-value: 1.54e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  85 YINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKYFPNNTREELKFGIYDITCKEF 164
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLVSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 165 VKRNILEYRLLEVSVGN--ETHQVHHYKFHGWTEFNLP-KYEDFMAFYNTMKEvgvpllavmknncmssffkkyHHTPPT 241
Cdd:cd00047   81 EELSDYTIRTLELSPKGcsESREVTHLHYTGWPDHGVPsSPEDLLALVRRVRK---------------------EARKPN 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193202549 242 NAPIIQCSTGGARCGVFiiIDILINLIDNRIKNSYSIEWWMLKVRSKRNHSALTNQQHSFIYD 304
Cdd:cd00047  140 GPIVVHCSAGVGRTGTF--IAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
57-308 1.50e-36

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 132.75  E-value: 1.50e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549   57 NIHRNIYGAV-PYDYNLVNLTSTQrNPLGYINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVEL 135
Cdd:pfam00102   1 NLEKNRYKDVlPYDHTRVKLTGDP-GPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  136 GIEKSDKYFPNNTREELKFGIYDITCKEFVKRNI-LEYRLLEVSVG--NETHQVHHYKFHGWTEFNLPkyEDFMAFYNTM 212
Cdd:pfam00102  80 GREKCAQYWPEEEGESLEYGDFTVTLKKEKEDEKdYTVRTLEVSNGgsEETRTVKHFHYTGWPDHGVP--ESPNSLLDLL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  213 KEVgvpllavmknncmssffKKYHHTPPTNAPIIQCSTGGARCGVF----IIIDILINLIDNRIKNSysiewwMLKVRSK 288
Cdd:pfam00102 158 RKV-----------------RKSSLDGRSGPIVVHCSAGIGRTGTFiaidIALQQLEAEGEVDIFQI------VKELRSQ 214

                         250       260
                  ....*....|....*....|
gi 193202549  289 RNHSALTNQQHSFIYDIIIK 308
Cdd:pfam00102 215 RPGMVQTLEQYIFLYDAILE 234
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 48-313 2.62e-13

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 70.06  E-value: 2.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  48 TISEGQRTENIHRNIYGAVP-YDYNLVNLTS--------------------TQRNPLGYINAS-VAEFPEIGRHYIITGA 105
Cdd:PHA02746  42 TTNHFLKKENLKKNRFHDIPcWDHSRVVINAheslkmfdvgdsdgkkievtSEDNAENYIHANfVDGFKEANKFICAQGP 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 106 AQDTQiPFFWQMVFEQKSPAIVMLlEDVELGIEKSDKYFPNNTREELKFGIYDITCKEFVKR-NILEYRLLEVSVGNET- 183
Cdd:PHA02746 122 KEDTS-EDFFKLISEHESQVIVSL-TDIDDDDEKCFELWTKEEDSELAFGRFVAKILDIIEElSFTKTRLMITDKISDTs 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 184 HQVHHYKFHGWTEFNLPK-YEDFMAFYNTMKEVGVPLLAVMKNNcmssffkkyhhtPPTNAPII-QCSTGGARCGVFIII 261
Cdd:PHA02746 200 REIHHFWFPDWPDNGIPTgMAEFLELINKVNEEQAELIKQADND------------PQTLGPIVvHCSAGIGRAGTFCAI 267

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 193202549 262 DILINLIdnRIKNSYSIEWWMLKVRSKRNHSALTNQQHSFIYdIIIKYIRTR 313
Cdd:PHA02746 268 DNALEQL--EKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCY-KALKYAIIE 316
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
36-308 8.11e-60

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 194.41  E-value: 8.11e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549    36 IIADFDRYQRAR----TISEGQRTENIHRNIYGAV-PYDYNLVNLTSTQRNPLGYINASVAEFPEIGRHYIITGAAQDTQ 110
Cdd:smart00194   2 LEEEFEKLDRLKpddeSCTVAAFPENRDKNRYKDVlPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPST 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549   111 IPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKYFPNNTREELKFGIYDITCKEFVKRNILEYRLLEVSVGN--ETHQVHH 188
Cdd:smart00194  82 VEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGcsETRTVTH 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549   189 YKFHGWTEFNLPKY-EDFMAFYNTMKEVgvpllavmknncmssffkKYHHTPPTnapIIQCSTGGARCGVFiiIDILINL 267
Cdd:smart00194 162 YHYTNWPDHGVPESpESILDLIRAVRKS------------------QSTSTGPI---VVHCSAGVGRTGTF--IAIDILL 218

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 193202549   268 IDNRIKNSYSIEWWMLKVRSKRNHSALTNQQHSFIYDIIIK 308
Cdd:smart00194 219 QQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 85-304 1.54e-43

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: 150.13  E-value: 1.54e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  85 YINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKYFPNNTREELKFGIYDITCKEF 164
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLVSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 165 VKRNILEYRLLEVSVGN--ETHQVHHYKFHGWTEFNLP-KYEDFMAFYNTMKEvgvpllavmknncmssffkkyHHTPPT 241
Cdd:cd00047   81 EELSDYTIRTLELSPKGcsESREVTHLHYTGWPDHGVPsSPEDLLALVRRVRK---------------------EARKPN 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193202549 242 NAPIIQCSTGGARCGVFiiIDILINLIDNRIKNSYSIEWWMLKVRSKRNHSALTNQQHSFIYD 304
Cdd:cd00047  140 GPIVVHCSAGVGRTGTF--IAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
57-308 1.50e-36

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 132.75  E-value: 1.50e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549   57 NIHRNIYGAV-PYDYNLVNLTSTQrNPLGYINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVEL 135
Cdd:pfam00102   1 NLEKNRYKDVlPYDHTRVKLTGDP-GPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  136 GIEKSDKYFPNNTREELKFGIYDITCKEFVKRNI-LEYRLLEVSVG--NETHQVHHYKFHGWTEFNLPkyEDFMAFYNTM 212
Cdd:pfam00102  80 GREKCAQYWPEEEGESLEYGDFTVTLKKEKEDEKdYTVRTLEVSNGgsEETRTVKHFHYTGWPDHGVP--ESPNSLLDLL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  213 KEVgvpllavmknncmssffKKYHHTPPTNAPIIQCSTGGARCGVF----IIIDILINLIDNRIKNSysiewwMLKVRSK 288
Cdd:pfam00102 158 RKV-----------------RKSSLDGRSGPIVVHCSAGIGRTGTFiaidIALQQLEAEGEVDIFQI------VKELRSQ 214

                         250       260
                  ....*....|....*....|
gi 193202549  289 RNHSALTNQQHSFIYDIIIK 308
Cdd:pfam00102 215 RPGMVQTLEQYIFLYDAILE 234
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 60-258 2.61e-26

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: 105.17  E-value: 2.61e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  60 RNIYGAV-PYDYNLVNLTStQRNPLGYINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVELGIE 138
Cdd:cd14545    1 LNRYRDRdPYDHDRSRVKL-KQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 139 KSDKYFPNNTREE--LKFGIYDITCKEFVKRNILEYRLLEVS--VGNETHQVHHYKFHGWTEFNLPKYED-FMAFyntmk 213
Cdd:cd14545   80 KCAQYWPQGEGNAmiFEDTGLKVTLLSEEDKSYYTVRTLELEnlKTQETREVLHFHYTTWPDFGVPESPAaFLNF----- 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 193202549 214 evgvpLLAVMKNNCMSSffkkyHHTPptnaPIIQCSTGGARCGVF 258
Cdd:cd14545  155 -----LQKVRESGSLSS-----DVGP----PVVHCSAGIGRSGTF 185
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 56-258 7.31e-21

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: 90.80  E-value: 7.31e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  56 ENIHRNIYGAV-PYDYNLVNLTSTQRNplgYINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVE 134
Cdd:cd14607   23 ENRNRNRYRDVsPYDHSRVKLQNTEND---YINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVE 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 135 LGIEKSDKYFPNNTREELKFGIYDItCKEFVKRNILEY---RLLEVSVGN--ETHQVHHYKFHGWTEFNLPkyEDFMAFY 209
Cdd:cd14607  100 KDSVKCAQYWPTDEEEVLSFKETGF-SVKLLSEDVKSYytvHLLQLENINsgETRTISHFHYTTWPDFGVP--ESPASFL 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 193202549 210 NTmkevgvpLLAVMKNNCMSsffkkyhhtpPTNAP-IIQCSTGGARCGVF 258
Cdd:cd14607  177 NF-------LFKVRESGSLS----------PEHGPaVVHCSAGIGRSGTF 209
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 35-306 9.84e-20

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: 88.45  E-value: 9.84e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  35 NIIADFDRYQRART---------ISEGQRTENIHRNIYGAV-PYDYNLVNLT-STQRNPLGYINASVAEFPEIGRHYIIT 103
Cdd:cd14604   26 NFASDFMRLRRLSTkyrtekiypTATGEKEENVKKNRYKDIlPFDHSRVKLTlKTSSQDSDYINANFIKGVYGPKAYIAT 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 104 GAAQDTQIPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKYFPNNTREELKFGIYDITCKEFVKRNILEYRLLEVSVGNET 183
Cdd:cd14604  106 QGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNET 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 184 HQVHHYKFHGWTEFNLPKYEDFMafyntmkevgVPLLAVMKnncmssffkkyHHTPPTNAPI-IQCSTGGARCG-VFIII 261
Cdd:cd14604  186 RRLYQFHYVNWPDHDVPSSFDSI----------LDMISLMR-----------KYQEHEDVPIcIHCSAGCGRTGaICAID 244

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 193202549 262 DILINLIDNRIKNSYSIEWWMLKVRSKRNHSALTNQQHSFIYDII 306
Cdd:cd14604  245 YTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 289
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 85-310 1.33e-19

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: 86.36  E-value: 1.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  85 YINASVAEFPEIG--RHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKYFPNNTREE--LKFGIYDIT 160
Cdd:cd14540    1 YINASHITATVGGkqRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHdaLTFGEYKVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 161 CKEFVKRNILEYRLLEVS--VGNETHQVHHYKFHGWTEFNLPKYED-FMAFYNTMKEVGVPLLAVMKNNcmssffkkyHH 237
Cdd:cd14540   81 TKFSVSSGCYTTTGLRVKhtLSGQSRTVWHLQYTDWPDHGCPEDVSgFLDFLEEINSVRRHTNQDVAGH---------NR 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193202549 238 TPPTnapIIQCSTGGARCGVfiiiDILINLIDNRIKNSYSIEWWML--KVRSKRNHSALTNQQHSFIYDIIIKYI 310
Cdd:cd14540  152 NPPT---LVHCSAGVGRTGV----VILADLMLYCLDHNEELDIPRVlaLLRHQRMLLVQTLAQYKFVYNVLIQYL 219
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 85-258 1.84e-19

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: 85.76  E-value: 1.84e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  85 YINASVAEFPEI-GRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKYFPNNTrEELKFGIYDITC-- 161
Cdd:cd18533    1 YINASYITLPGTsSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGE-YEGEYGDLTVELvs 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 162 KEFVKRNILEYRLLEVSVGN-ETHQVHHYKFHGWTEFNLPkyedfmafyntmkEVGVPLLAVMKnncmssfFKKY--HHT 238
Cdd:cd18533   80 EEENDDGGFIVREFELSKEDgKVKKVYHIQYKSWPDFGVP-------------DSPEDLLTLIK-------LKRElnDSA 139

                        170       180
                 ....*....|....*....|
gi 193202549 239 PPTNAPIIQCSTGGARCGVF 258
Cdd:cd18533  140 SLDPPIIVHCSAGVGRTGTF 159
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 52-303 5.94e-19

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: 85.65  E-value: 5.94e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  52 GQRTENIHRNIYGAV-PYDYNLVNLTSTQRN-PLGYINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVML 129
Cdd:cd14603   25 GGRKENVKKNRYKDIlPYDQTRVILSLLQEEgHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMA 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 130 LEDVELGIEKSDKYFPnNTREELKFGIYDITC--KEFVKRNILeYRLLEVSVGNETHQVHHYKFHGWTEFNLP-KYEDFM 206
Cdd:cd14603  105 CREIEMGKKKCERYWA-QEQEPLQTGPFTITLvkEKRLNEEVI-LRTLKVTFQKESRSVSHFQYMAWPDHGIPdSPDCML 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 207 AFYNTMKEvgvpllavmknncmssffKKYHHTPPTnapIIQCSTGGARCGVF-IIIDILINLIDNRIKNSYSIEWWMLKV 285
Cdd:cd14603  183 AMIELARR------------------LQGSGPEPL---CVHCSAGCGRTGVIcTVDYVRQLLLTQRIPPDFSIFDVVLEM 241

                        250
                 ....*....|....*...
gi 193202549 286 RSKRNHSALTNQQHSFIY 303
Cdd:cd14603  242 RKQRPAAVQTEEQYEFLY 259
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 56-310 6.72e-19

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: 85.85  E-value: 6.72e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  56 ENIHRNIYGAV-PYDYNLVNLtstQRNPLGYINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVE 134
Cdd:cd14608   24 KNKNRNRYRDVsPFDHSRIKL---HQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVME 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 135 LGIEKSDKYFPNNTREELKFGIYDITCKeFVKRNILEY---RLLEVS--VGNETHQVHHYKFHGWTEFNLPkyEDFMAFY 209
Cdd:cd14608  101 KGSLKCAQYWPQKEEKEMIFEDTNLKLT-LISEDIKSYytvRQLELEnlTTQETREILHFHYTTWPDFGVP--ESPASFL 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 210 NTmkevgvpLLAVMKNNCMSsffkkyhhtpPTNAPI-IQCSTGGARCGVFIIIDILINLIDNRIK-NSYSIEWWMLKVRS 287
Cdd:cd14608  178 NF-------LFKVRESGSLS----------PEHGPVvVHCSAGIGRSGTFCLADTCLLLMDKRKDpSSVDIKKVLLEMRK 240

                        250       260
                 ....*....|....*....|....*.
gi 193202549 288 KRNHSALTNQQHSFIYDIII---KYI 310
Cdd:cd14608  241 FRMGLIQTADQLRFSYLAVIegaKFI 266
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 56-311 2.83e-17

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: 81.20  E-value: 2.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  56 ENIHRN-IYGAVPYDYNLVNLTSTQRNPLGYINASVAEFPEIGR--HYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLED 132
Cdd:cd14599   37 ENAERNrIREVVPYEENRVELVPTKENNTGYINASHIKVTVGGEewHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAE 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 133 VELGIEKSDKYFPN--NTREELKFGIYDITCKEFVKRNILEYRLLEVS--VGNETHQVHHYKFHGWTEFNLPkyEDFMAF 208
Cdd:cd14599  117 EEGGRSKSHRYWPKlgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKhlLSGQERTVWHLQYTDWPDHGCP--EEVQGF 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 209 YNTMKEVGvpllAVMKN-NCMSSFFKKYHhtPPTnapIIQCSTGGARCGVFIIIDILINLidnrIKNSYSIEWWML--KV 285
Cdd:cd14599  195 LSYLEEIQ----SVRRHtNSMLDSTKNCN--PPI---VVHCSAGVGRTGVVILTELMIGC----LEHNEKVEVPVMlrHL 261

                        250       260
                 ....*....|....*....|....*.
gi 193202549 286 RSKRNHSALTNQQHSFIYDIIIKYIR 311
Cdd:cd14599  262 REQRMFMIQTIAQYKFVYQVLIQFLK 287
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 54-312 3.30e-17

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: 80.58  E-value: 3.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  54 RTENIHRNIygaVPYDYNLVNLTSTQRNPLG--YINASVAEFP-------EIGRHYIITGAAQDTQIPFFWQMVFEQKSP 124
Cdd:cd14544    2 KGKNRYKNI---LPFDHTRVILKDRDPNVPGsdYINANYIRNEnegpttdENAKTYIATQGCLENTVSDFWSMVWQENSR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 125 AIVMLLEDVELGIEKSDKYFPNNTREElKFGIYDIT-CKEFVKRnilEYRLLEVSV-----GNETHQVHHYKFHGWTEFn 198
Cdd:cd14544   79 VIVMTTKEVERGKNKCVRYWPDEGMQK-QYGPYRVQnVSEHDTT---DYTLRELQVskldqGDPIREIWHYQYLSWPDH- 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 199 lpkyedfmafyntmkevGVPLlavmKNNCMSSFFKKYHHTP---PTNAPII-QCSTGGARCGVFIIIDILINLIDNR-IK 273
Cdd:cd14544  154 -----------------GVPS----DPGGVLNFLEDVNQRQeslPHAGPIVvHCSAGIGRTGTFIVIDMLLDQIKRKgLD 212

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 193202549 274 NSYSIEWWMLKVRSKRNHSALTNQQHSFIYDIIIKYIRT 312
Cdd:cd14544  213 CDIDIQKTIQMVRSQRSGMVQTEAQYKFIYVAVAQYIET 251
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 51-312 3.75e-17

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: 80.69  E-value: 3.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  51 EGQRTENIHRNIYGAV-PYDYNLVNLTSTQRNPLG--YINASVAEFPEIG-----RHYIITGAAQDTQIPFFWQMVFEQK 122
Cdd:cd14606   12 EGQRPENKSKNRYKNIlPFDHSRVILQGRDSNIPGsdYINANYVKNQLLGpdenaKTYIASQGCLEATVNDFWQMAWQEN 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 123 SPAIVMLLEDVELGIEKSDKYFPnNTREELKFGIYDIT-CKEfvkRNILEY--RLLEVSVGNET---HQVHHYKFHGWTE 196
Cdd:cd14606   92 SRVIVMTTREVEKGRNKCVPYWP-EVGMQRAYGPYSVTnCGE---HDTTEYklRTLQVSPLDNGeliREIWHYQYLSWPD 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 197 FNLPkyedfmafyntmKEVGVPLLAVMKNNCMssffkkyHHTPPTNAPI-IQCSTGGARCGVFIIIDILINLIDNR-IKN 274
Cdd:cd14606  168 HGVP------------SEPGGVLSFLDQINQR-------QESLPHAGPIiVHCSAGIGRTGTIIVIDMLMENISTKgLDC 228

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 193202549 275 SYSIEWWMLKVRSKRNHSALTNQQHSFIYDIIIKYIRT 312
Cdd:cd14606  229 DIDIQKTIQMVRAQRSGMVQTEAQYKFIYVAIAQFIET 266
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 66-308 1.28e-16

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: 78.34  E-value: 1.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  66 VPYDYNLVNLT-STQRNPLGYINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKYF 144
Cdd:cd14602    8 LPYDHSRVELSlITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGKKKCERYW 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 145 PNNTREELKFGIYDITCKEFVKRNILEYRLLEVSVGNETHQVHHYKFHGWTEFNLPKYEDfmafyntmkevgvPLLAvmk 224
Cdd:cd14602   88 AEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSID-------------PILE--- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 225 nncMSSFFKKYHHTppTNAPI-IQCSTGGARCGVFIIIDILINLIDNRI-KNSYSIEWWMLKVRSKRNHSALTNQQHSFI 302
Cdd:cd14602  152 ---LIWDVRCYQED--DSVPIcIHCSAGCGRTGVICAIDYTWMLLKDGIiPENFSVFSLIQEMRTQRPSLVQTKEQYELV 226


                 ....*.
gi 193202549 303 YDIIIK 308
Cdd:cd14602  227 YNAVIE 232
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 57-310 3.46e-16

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: 77.05  E-value: 3.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  57 NIHRNIYGAV-PYDYNLVNLTSTQRNPLG-YINASVAEFPEIGRHYIIT-GAAQDTqIPFFWQMVFEQKSPAIVMLLEDV 133
Cdd:cd14553    3 NKPKNRYANViAYDHSRVILQPIEGVPGSdYINANYCDGYRKQNAYIATqGPLPET-FGDFWRMVWEQRSATIVMMTKLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 134 ELGIEKSDKYFPNNTREelKFGIYDITCKEFVKRNILEYRLLEVSVG--NETHQVHHYKFHGWTEFNLPKYEdfmafynt 211
Cdd:cd14553   82 ERSRVKCDQYWPTRGTE--TYGLIQVTLLDTVELATYTVRTFALHKNgsSEKREVRQFQFTAWPDHGVPEHP-------- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 212 mkevgVPLLAVMKnnCMSSffkkyhHTPPTNAPII-QCSTGGARCGVFiiidILINLIDNRIKNSYSIEWW--MLKVRSK 288
Cdd:cd14553  152 -----TPFLAFLR--RVKA------CNPPDAGPIVvHCSAGVGRTGCF----IVIDSMLERIKHEKTVDIYghVTCLRAQ 214

                        250       260
                 ....*....|....*....|..
gi 193202549 289 RNHSALTNQQHSFIYDIIIKYI 310
Cdd:cd14553  215 RNYMVQTEDQYIFIHDALLEAV 236
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 54-258 4.43e-16

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: 76.62  E-value: 4.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  54 RTENIhrniygaVPYDYNLVNLTSTQRNPLG-YINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLED 132
Cdd:cd14548    1 RYTNI-------LPYDHSRVKLIPINEEEGSdYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQC 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 133 VELGIEKSDKYFPNNTrEELKFGiyDIT--------CKEFVKRNileyrlLEVSVGNETHQVHHYKFHGWTEFNLPKYED 204
Cdd:cd14548   74 MEKGRVKCDHYWPFDQ-DPVYYG--DITvtmlsesvLPDWTIRE------FKLERGDEVRSVRQFHFTAWPDHGVPEAPD 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 193202549 205 fmafyntmkevgvPLLAVMKnncmssFFKKYHHtPPTNAPIIQCSTGGARCGVF 258
Cdd:cd14548  145 -------------SLLRFVR------LVRDYIK-QEKGPTIVHCSAGVGRTGTF 178
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 57-258 1.45e-15

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: 76.25  E-value: 1.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  57 NIHRNIYGAVP-YDYNLVNLTSTQRNPLG-YINASVAEFPEIGRHYIIT-GAAQDTqIPFFWQMVFEQKSPAIVMLLEDV 133
Cdd:cd14543   29 NQEKNRYGDVLcLDQSRVKLPKRNGDERTdYINANFMDGYKQKNAYIATqGPLPKT-YSDFWRMVWEQKVLVIVMTTRVV 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 134 ELGIEKSDKYFPNNTREELKFGIY-----DITCKEFVKRNILEYRLLEvsvGNETHQVHHYKFHGWTEFNLPKYE----D 204
Cdd:cd14543  108 ERGRVKCGQYWPLEEGSSLRYGDLtvtnlSVENKEHYKKTTLEIHNTE---TDESRQVTHFQFTSWPDFGVPSSAaallD 184

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 193202549 205 FMAFYNTMKEVGVpllavmknNCMSSFFKKYHHTPPTnapIIQCSTGGARCGVF 258
Cdd:cd14543  185 FLGEVRQQQALAV--------KAMGDRWKGHPPGPPI---VVHCSAGIGRTGTF 227
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 56-312 1.83e-15

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: 75.44  E-value: 1.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  56 ENIHRNIYGAV-PYDYNLVNLTSTQRNPLG--YINASV--AEF------PEIGRHYIIT-GAAQDTqIPFFWQMVFEQKS 123
Cdd:cd14605    1 ENKNKNRYKNIlPFDHTRVVLHDGDPNEPVsdYINANIimPEFetkcnnSKPKKSYIATqGCLQNT-VNDFWRMVFQENS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 124 PAIVMLLEDVELGIEKSDKYFPnntrEELKFGIYDITCKEFVKRN------ILEYRLLEVSVGNETHQVHHYKFHGWTEF 197
Cdd:cd14605   80 RVIVMTTKEVERGKSKCVKYWP----DEYALKEYGVMRVRNVKESaahdyiLRELKLSKVGQGNTERTVWQYHFRTWPDH 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 198 NLPKyeDFMAFYNTMKEVGVPLLAVMKnncmssffkkyhhtppTNAPIIQCSTGGARCGVFIIIDILINLIDNR-IKNSY 276
Cdd:cd14605  156 GVPS--DPGGVLDFLEEVHHKQESIMD----------------AGPVVVHCSAGIGRTGTFIVIDILIDIIREKgVDCDI 217

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 193202549 277 SIEWWMLKVRSKRNHSALTNQQHSFIYDIIIKYIRT 312
Cdd:cd14605  218 DVPKTIQMVRSQRSGMVQTEAQYRFIYMAVQHYIET 253
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 85-306 1.91e-15

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: 74.23  E-value: 1.91e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  85 YINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKYFPNN---TREELKFGIYDIT- 160
Cdd:cd14552    1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDgsvSSGDITVELKDQTd 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 161 CKEFVKRNIleyrLLEVSVGNETHQVHHYKFHGWtefnlpkyedfmafyntmKEVGVPLLAVMKNNCMSSFFKKYHHTpp 240
Cdd:cd14552   81 YEDYTLRDF----LVTKGKGGSTRTVRQFHFHGW------------------PEVGIPDNGKGMIDLIAAVQKQQQQS-- 136

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193202549 241 TNAPI-IQCSTGGARCGVFiiidILINLIDNRIKNSYSIEWWML--KVRSKRNHSALTNQQHSFIYDII 306
Cdd:cd14552  137 GNHPItVHCSAGAGRTGTF----CALSTVLERVKAEGVLDVFQVvkSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 38-310 2.17e-15

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: 75.46  E-value: 2.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  38 ADFDRYQRAR-----TISEGQRTENIHRNIY-GAVPYDYNLVNLtstqrNPLG--------YINASVAEFPEIGRHYIIT 103
Cdd:cd17667    3 EDFEEVQRCTadmniTAEHSNHPDNKHKNRYiNILAYDHSRVKL-----RPLPgkdskhsdYINANYVDGYNKAKAYIAT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 104 GAAQDTQIPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKYFPNNTREElkFGIYDITCKE-------FVKR-NILEYRLL 175
Cdd:cd17667   78 QGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEE--YGNIIVTLKStkihacyTVRRfSIRNTKVK 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 176 EVSVGN-----ETHQVHHYKFHGWTEFNLPKYedfmafyntmkevGVPLLAVMKNNCMSsffkkyhHTPPTNAPIIQCST 250
Cdd:cd17667  156 KGQKGNpkgrqNERTVIQYHYTQWPDMGVPEY-------------ALPVLTFVRRSSAA-------RTPEMGPVLVHCSA 215

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 251 GGARCGVFiiIDILINLIDNRIKNSYSIEWWMLKVRSKRNHSALTNQQHSFIYDIIIKYI 310
Cdd:cd17667  216 GVGRTGTY--IVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 273
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 85-258 9.96e-15

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: 72.50  E-value: 9.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  85 YINASVAEFPEIGRH--YIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVE-LGIEKSDKYFPNNTREELKFGIYDITC 161
Cdd:cd17658    1 YINASLVETPASESLpkFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDnYSTAKCADYFPAEENESREFGRISVTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 162 KEF-VKRNILEYRLLEVSvGNETHQ----VHHYKFHGWTEFNLPKYEDFmafyntMKEVgvpllavmknncmssfFKKYH 236
Cdd:cd17658   81 KKLkHSQHSITLRVLEVQ-YIESEEpplsVLHIQYPEWPDHGVPKDTRS------VREL----------------LKRLY 137

                        170       180
                 ....*....|....*....|...
gi 193202549 237 HTPPTNAPII-QCSTGGARCGVF 258
Cdd:cd17658  138 GIPPSAGPIVvHCSAGIGRTGAY 160
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 51-308 1.09e-14

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: 73.53  E-value: 1.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  51 EGQRTENIHRNIygaVPYDYNLVNLTSTQRNP-LGYINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVML 129
Cdd:cd14626   39 EVNKPKNRYANV---IAYDHSRVILTSVDGVPgSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMM 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 130 LEDVELGIEKSDKYFPNNTREelKFGIYDITCKEFVKRNILEYRLLEV--SVGNETHQVHHYKFHGWTEFNLPKYEdfma 207
Cdd:cd14626  116 TRLEEKSRVKCDQYWPIRGTE--TYGMIQVTLLDTVELATYSVRTFALykNGSSEKREVRQFQFMAWPDHGVPEYP---- 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 208 fyntmkevgVPLLAVMK--NNCmssffkkyhhTPPTNAP-IIQCSTGGARCGVFiiidILINLIDNRIKNSYSIEWW--M 282
Cdd:cd14626  190 ---------TPILAFLRrvKAC----------NPPDAGPmVVHCSAGVGRTGCF----IVIDAMLERMKHEKTVDIYghV 246

                        250       260
                 ....*....|....*....|....*.
gi 193202549 283 LKVRSKRNHSALTNQQHSFIYDIIIK 308
Cdd:cd14626  247 TCMRSQRNYMVQTEDQYIFIHEALLE 272
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 44-310 1.98e-14

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: 72.82  E-value: 1.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  44 QRARTISEGQRTENIHRNI---------YGAVPYDYNLVNLTSTQrNPLG--YINASVAEFPEIGRHYIITGAAQDTQIP 112
Cdd:cd14625   26 QEYESIDPGQQFTWEHSNLevnkpknryANVIAYDHSRVILQPIE-GIMGsdYINANYIDGYRKQNAYIATQGPLPETFG 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 113 FFWQMVFEQKSPAIVMLLEDVELGIEKSDKYFPNNTREelKFGIYDITCKEFVKRNILEYRL--LEVSVGNETHQVHHYK 190
Cdd:cd14625  105 DFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTE--TYGMIQVTLLDTIELATFCVRTfsLHKNGSSEKREVRQFQ 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 191 FHGWTEFNLPKYED-FMAFYNTMKevgvpllavmknNCmssffkkyhhTPPTNAPI-IQCSTGGARCGVFiiidILINLI 268
Cdd:cd14625  183 FTAWPDHGVPEYPTpFLAFLRRVK------------TC----------NPPDAGPIvVHCSAGVGRTGCF----IVIDAM 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 193202549 269 DNRIKNSYSIEWW--MLKVRSKRNHSALTNQQHSFIYDIIIKYI 310
Cdd:cd14625  237 LERIKHEKTVDIYghVTLMRSQRNYMVQTEDQYSFIHDALLEAV 280
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 66-306 3.89e-14

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: 71.23  E-value: 3.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  66 VPYDYN--LVNLTSTQRNPlGYINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKY 143
Cdd:cd14623    6 IPYEFNrvIIPVKRGEENT-DYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEKCAQY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 144 FPNNTreELKFGiyDIT--------CKEFVKRNILEYRLLEvsvgNETHQVHHYKFHGWTEFNLPkyEDFMAFYNTMKev 215
Cdd:cd14623   85 WPSDG--SVSYG--DITielkkeeeCESYTVRDLLVTNTRE----NKSRQIRQFHFHGWPEVGIP--SDGKGMINIIA-- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 216 gvpllAVMKNNCMSSffkkyhhtpptNAPI-IQCSTGGARCGVFiiidILINLIDNRIKNSYSIEWWML--KVRSKRNHS 292
Cdd:cd14623  153 -----AVQKQQQQSG-----------NHPItVHCSAGAGRTGTF----CALSTVLERVKAEGILDVFQTvkSLRLQRPHM 212

                        250
                 ....*....|....
gi 193202549 293 ALTNQQHSFIYDII 306
Cdd:cd14623  213 VQTLEQYEFCYKVV 226
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 85-311 4.93e-14

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: 70.55  E-value: 4.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  85 YINASVAEFP--EIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKYFPNNTREELKFGIYDItck 162
Cdd:cd14596    1 YINASYITMPvgEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQL--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 163 EFVKRNILEY------RLLEVSVGnETHQVHHYKFHGWTEFNLPKYEDFMAFYntmkevgvpllavmknncmSSFFKKYH 236
Cdd:cd14596   78 RLENYQALQYfiiriiKLVEKETG-ENRLIKHLQFTTWPDHGTPQSSDQLVKF-------------------ICYMRKVH 137

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193202549 237 HTPPTnapIIQCSTGGARCGVFIIIDILINLIDNRIknSYSIEWWMLKVRSKRNHSALTNQQHSFIYDIIIKYIR 311
Cdd:cd14596  138 NTGPI---VVHCSAGIGRAGVLICVDVLLSLIEKDL--SFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 85-308 5.86e-14

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: 70.43  E-value: 5.86e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  85 YINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKYFPNNTreELkFGIYDITCKEF 164
Cdd:cd14631   15 YINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDT--EV-YGDFKVTCVEM 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 165 vkRNILEYRLLEVSVG----NETHQVHHYKFHGWTEFNLPkyedfmafYNtmkevGVPLLAVMKNNCMSSffkkyhhtPP 240
Cdd:cd14631   92 --EPLAEYVVRTFTLErrgyNEIREVKQFHFTGWPDHGVP--------YH-----ATGLLSFIRRVKLSN--------PP 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193202549 241 TNAPI-IQCSTGGARCGVFIIIDILINLIDNriKNSYSIEWWMLKVRSKRNHSALTNQQHSFIYDIIIK 308
Cdd:cd14631  149 SAGPIvVHCSAGAGRTGCYIVIDIMLDMAER--EGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 85-308 2.10e-13

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: 68.40  E-value: 2.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  85 YINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKYFPNNTReelKFGIYDITC--K 162
Cdd:cd14555    1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTE---VYGDIKVTLveT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 163 EFVKRNILEYRLLEVSVGNETHQVHHYKFHGWTEFNLPKYED-FMAFYNTMKEVgvpllavmknncmssffkkyhhTPPT 241
Cdd:cd14555   78 EPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATgLLGFIRRVKAS----------------------NPPS 135

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193202549 242 NAPI-IQCSTGGARCGVFIIIDILINLIDNriKNSYSIEWWMLKVRSKRNHSALTNQQHSFIYDIIIK 308
Cdd:cd14555  136 AGPIvVHCSAGAGRTGCYIVIDIMLDMAER--EGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 85-304 2.51e-13

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: 68.15  E-value: 2.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  85 YINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKYFPNNTREElkFGIYDITCKEF 164
Cdd:cd14549    1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTET--YGNIQVTLLST 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 165 VKRNILEYRLLEV--------SVGNETHQVHHYKFHGWTEFNLPKYEdfmafyntmkevgVPLLAVMKnncmssffKKYH 236
Cdd:cd14549   79 EVLATYTVRTFSLknlklkkvKGRSSERVVYQYHYTQWPDHGVPDYT-------------LPVLSFVR--------KSSA 137

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193202549 237 HTPPTNAPII-QCSTGGARCGVFIIIDILINLIDNriKNSYSIEWWMLKVRSKRNHSALTNQQHSFIYD 304
Cdd:cd14549  138 ANPPGAGPIVvHCSAGVGRTGTYIVIDSMLQQIQD--KGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 48-313 2.62e-13

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 70.06  E-value: 2.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  48 TISEGQRTENIHRNIYGAVP-YDYNLVNLTS--------------------TQRNPLGYINAS-VAEFPEIGRHYIITGA 105
Cdd:PHA02746  42 TTNHFLKKENLKKNRFHDIPcWDHSRVVINAheslkmfdvgdsdgkkievtSEDNAENYIHANfVDGFKEANKFICAQGP 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 106 AQDTQiPFFWQMVFEQKSPAIVMLlEDVELGIEKSDKYFPNNTREELKFGIYDITCKEFVKR-NILEYRLLEVSVGNET- 183
Cdd:PHA02746 122 KEDTS-EDFFKLISEHESQVIVSL-TDIDDDDEKCFELWTKEEDSELAFGRFVAKILDIIEElSFTKTRLMITDKISDTs 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 184 HQVHHYKFHGWTEFNLPK-YEDFMAFYNTMKEVGVPLLAVMKNNcmssffkkyhhtPPTNAPII-QCSTGGARCGVFIII 261
Cdd:PHA02746 200 REIHHFWFPDWPDNGIPTgMAEFLELINKVNEEQAELIKQADND------------PQTLGPIVvHCSAGIGRAGTFCAI 267

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 193202549 262 DILINLIdnRIKNSYSIEWWMLKVRSKRNHSALTNQQHSFIYdIIIKYIRTR 313
Cdd:PHA02746 268 DNALEQL--EKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCY-KALKYAIIE 316
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 44-310 2.85e-13

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: 69.76  E-value: 2.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  44 QRARTISEGQRTENIHRNI---------YGAVPYDYNLVNLTSTQRNP-LGYINASVAEFPEIGRHYIITGAAQDTQIPF 113
Cdd:cd14624   26 QEYESIDPGQQFTWEHSNLevnkpknryANVIAYDHSRVLLSAIEGIPgSDYINANYIDGYRKQNAYIATQGALPETFGD 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 114 FWQMVFEQKSPAIVMLLEDVELGIEKSDKYFPNNTREelKFGIYDITCKEFVKRNILEYRLLEV--SVGNETHQVHHYKF 191
Cdd:cd14624  106 FWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTE--TYGLIQVTLLDTVELATYCVRTFALykNGSSEKREVRQFQF 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 192 HGWTEFNLPKYED-FMAFYNTMKEVgvpllavmknncmssffkkyhhTPPTNAP-IIQCSTGGARCGVFiiidILINLID 269
Cdd:cd14624  184 TAWPDHGVPEHPTpFLAFLRRVKTC----------------------NPPDAGPmVVHCSAGVGRTGCF----IVIDAML 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 193202549 270 NRIKNSYSIEWW--MLKVRSKRNHSALTNQQHSFIYDIIIKYI 310
Cdd:cd14624  238 ERIKHEKTVDIYghVTLMRAQRNYMVQTEDQYIFIHDALLEAV 280
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 73-258 2.96e-13

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: 68.58  E-value: 2.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  73 VNLTSTQRNPLG-YINAS-VAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVElGIEKSDKYFPnnTRE 150
Cdd:cd14547   14 VCLPSVDDDPLSsYINANyIRGYDGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTE-AKEKCAQYWP--EEE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 151 ELKFGIYDITCKEFVKRNILEYRLLEVSVGNETHQVHHYKFHGWTEFNLPkyedfmafyntmkEVGVPLLAVMK--NNCM 228
Cdd:cd14547   91 NETYGDFEVTVQSVKETDGYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTP-------------EAAQPLLSLVQevEEAR 157

                        170       180       190
                 ....*....|....*....|....*....|
gi 193202549 229 ssffKKYHHTPPtnaPIIQCSTGGARCGVF 258
Cdd:cd14547  158 ----QTEPHRGP---IVVHCSAGIGRTGCF 180
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 56-308 3.05e-13

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: 68.90  E-value: 3.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  56 ENIHRNIYG-AVPYDYNLVNLTSTQRNPLG-YINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDV 133
Cdd:cd14630    2 ENRNKNRYGnIISYDHSRVRLQLLDGDPHSdYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 134 ELGIEKSDKYFPNNTReelkfgIY-DITCKEFVKRNILEYRLLEVSV----GNETHQVHHYKFHGWTEFNLPKYED-FMA 207
Cdd:cd14630   82 EVGRVKCVRYWPDDTE------VYgDIKVTLIETEPLAEYVIRTFTVqkkgYHEIREIRQFHFTSWPDHGVPCYATgLLG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 208 FYNTMKEVgvpllavmknncmssffkkyhhTPPTNAPI-IQCSTGGARCGVFIIIDILINLIDNriKNSYSIEWWMLKVR 286
Cdd:cd14630  156 FVRQVKFL----------------------NPPDAGPIvVHCSAGAGRTGCFIAIDIMLDMAEN--EGVVDIFNCVRELR 211

                        250       260
                 ....*....|....*....|..
gi 193202549 287 SKRNHSALTNQQHSFIYDIIIK 308
Cdd:cd14630  212 AQRVNMVQTEEQYVFVHDAILE 233
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 85-258 4.04e-13

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: 67.78  E-value: 4.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  85 YINASVAEFPEIGR--HYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKYFPNNTREELKF-GIYDITc 161
Cdd:cd14538    1 YINASHIRIPVGGDtyHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPLICgGRLEVS- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 162 keFVKRNILEY------RLLEVSVGnETHQVHHYKFHGWTEFNLPKYedfmafyntmkevGVPLLAVMknncmsSFFKKY 235
Cdd:cd14538   80 --LEKYQSLQDfvirriSLRDKETG-EVHHITHLNFTTWPDHGTPQS-------------ADPLLRFI------RYMRRI 137

                        170       180
                 ....*....|....*....|...
gi 193202549 236 HHTPPTnapIIQCSTGGARCGVF 258
Cdd:cd14538  138 HNSGPI---VVHCSAGIGRTGVL 157
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 54-307 4.19e-13

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: 68.32  E-value: 4.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  54 RTENIHRNIygaVPYDYNLVNLTSTQrnplGYINASVAEFPEIGRH--YIITGAAQDTQIPFFWQMVFEQKSPAIVMLLE 131
Cdd:cd14597    4 RKKNRYKNI---LPYDTTRVPLGDEG----GYINASFIKMPVGDEEfvYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 132 DVELGIEKSDKYFPNNTR------EELKFGIY-DITCKEFVKRnILEYRLLEVsvgNETHQVHHYKFHGWTEFNLPKY-E 203
Cdd:cd14597   77 EVEGGKIKCQRYWPEILGkttmvdNRLQLTLVrMQQLKNFVIR-VLELEDIQT---REVRHITHLNFTAWPDHDTPSQpE 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 204 DFMAFYNTMKEVgvpllavmknncmssffkkyHHTPPTnapIIQCSTGGARCGVFIIIDILINLIDNRIknSYSIEWWML 283
Cdd:cd14597  153 QLLTFISYMRHI--------------------HKSGPI---ITHCSAGIGRSGTLICIDVVLGLISKDL--DFDISDIVR 207

                        250       260
                 ....*....|....*....|....
gi 193202549 284 KVRSKRNHSALTNQQHSFIYDIII 307
Cdd:cd14597  208 TMRLQRHGMVQTEDQYIFCYQVIL 231
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 85-258 5.09e-13

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: 67.74  E-value: 5.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  85 YINASVA--EFP--EIGRHYIITgaaqdtQIPF------FWQMVFEQKSPAIVMLLEDVELGIEKSDKYFPnNTREELKF 154
Cdd:cd14541    2 YINANYVnmEIPgsGIVNRYIAA------QGPLpntcadFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWP-DLGETMQF 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 155 GIYDITC-KE-----FVKRNIleyrLLEVSVGNETHQVHHYKFHGWTEFNLPkyEDFMAFYNTMKEVGVpllavmknncm 228
Cdd:cd14541   75 GNLQITCvSEevtpsFAFREF----ILTNTNTGEERHITQMQYLAWPDHGVP--DDSSDFLDFVKRVRQ----------- 137

                        170       180       190
                 ....*....|....*....|....*....|
gi 193202549 229 ssffKKYHHTPPTnapIIQCSTGGARCGVF 258
Cdd:cd14541  138 ----NRVGMVEPT---VVHCSAGIGRTGVL 160
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 85-258 5.58e-13

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: 67.42  E-value: 5.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  85 YINASVAEFPEIGRHYIIT-GAAQDTqIPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKYFPNntrEELKFGIYDITCKE 163
Cdd:cd14558    1 YINASFIDGYWGPKSLIATqGPLPDT-IADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGD---EKKTYGDIEVELKD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 164 FVKRNILEYRLLEV--SVGNETHQVHHYKFHGWTEFNLPkyEDFMAFYNTMKEVgvpllavmKNNCMSSFFKKYHHTPpt 241
Cdd:cd14558   77 TEKSPTYTVRVFEIthLKRKDSRTVYQYQYHKWKGEELP--EKPKDLVDMIKSI--------KQKLPYKNSKHGRSVP-- 144

                        170
                 ....*....|....*..
gi 193202549 242 naPIIQCSTGGARCGVF 258
Cdd:cd14558  145 --IVVHCSDGSSRTGIF 159
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 85-258 7.74e-13

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: 67.02  E-value: 7.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  85 YINAS-VAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKYFPNNTREELKFGIYDITCKE 163
Cdd:cd14539    1 YINASlIEDLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAITVSLQS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 164 FVKRNILEYRLLEVSVgNETHQ---VHHYKFHGWTEFNLP-KYEDFMAFyntMKEVgvpllavmknncmSSFFKkyhHTP 239
Cdd:cd14539   81 VRTTPTHVERIISIQH-KDTRLsrsVVHLQFTTWPELGLPdSPNPLLRF---IEEV-------------HSHYL---QQR 140

                        170       180
                 ....*....|....*....|
gi 193202549 240 PTNAPII-QCSTGGARCGVF 258
Cdd:cd14539  141 SLQTPIVvHCSSGVGRTGAF 160
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 36-257 1.05e-12

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: 67.57  E-value: 1.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  36 IIADFDRYQRAR---TISEGQRTENIHRNIYGAV-PYDYNLVNLTSTQrnplGYINASVA--EFP--EIGRHYIITGAAQ 107
Cdd:cd14600   16 VLIQFEQLYRKKpglAITCAKLPQNMDKNRYKDVlPYDATRVVLQGNE----DYINASYVnmEIPsaNIVNKYIATQGPL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 108 DTQIPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKYFPnNTREELKFGIYDITCKE------FVKRNILeyrLLEVSVGN 181
Cdd:cd14600   92 PHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWP-DPPDVMEYGGFRVQCHSedctiaYVFREML---LTNTQTGE 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193202549 182 EtHQVHHYKFHGWTEFNLPK-YEDFMAFYNTMKEVGVpllavmknncmssffkkyhhtppTNAP-IIQCSTGGARCGV 257
Cdd:cd14600  168 E-RTVTHLQYVAWPDHGVPDdSSDFLEFVNYVRSKRV-----------------------ENEPvLVHCSAGIGRTGV 221
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 57-303 1.87e-12

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: 66.10  E-value: 1.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  57 NIHRNIygaVPYDYNLVNLTSTQRNPLG-YINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVEL 135
Cdd:cd14617    1 NRYNNI---LPYDSTRVKLSNVDDDPCSdYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 136 GIEKSDKYFPNNtREELKFGiyDITCKEFVKRNILEYRLLEVSVGNETH-----QVHHYKFHGWTEFNLPK-YEDFMAFY 209
Cdd:cd14617   78 GRVKCDHYWPAD-QDSLYYG--DLIVQMLSESVLPEWTIREFKICSEEQldaprLVRHFHYTVWPDHGVPEtTQSLIQFV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 210 NTMKEVgvpllavmknncmssffkkYHHTPPTNAPIIQCSTGGARCGVFIIIDILINLIDNriKNSYSIEWWMLKVRSKR 289
Cdd:cd14617  155 RTVRDY-------------------INRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDS--KDSVDIYGAVHDLRLHR 213

                        250
                 ....*....|....
gi 193202549 290 NHSALTNQQHSFIY 303
Cdd:cd14617  214 VHMVQTECQYVYLH 227
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 66-258 2.49e-12

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: 65.99  E-value: 2.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  66 VPYDYNLVNLTSTQRNPLGYINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKYFP 145
Cdd:cd14615    7 LPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 146 nnTREELKFG-----------IYDITCKEFVKRNILEyrllevsvgNETHQVHHYKFHGWTEFNLPKYEDFM-AFYNTMK 213
Cdd:cd14615   87 --SKQKKDYGditvtmtseivLPEWTIRDFTVKNAQT---------NESRTVRHFHFTSWPDHGVPETTDLLiNFRHLVR 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 193202549 214 EvgvpllaVMKNNcmssffkkyhhtpPTNAPI-IQCSTGGARCGVF 258
Cdd:cd14615  156 E-------YMKQN-------------PPNSPIlVHCSAGVGRTGTF 181
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 85-309 3.59e-12

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: 65.03  E-value: 3.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  85 YINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKYFPnnTREELKFGIYDITCKEF 164
Cdd:cd14622    2 YINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWP--SEGSVTHGEITIEIKND 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 165 VKRNILEYR--LLEVSVGNETHQVHHYKFHGWTEFNLPKYEDFMafyntmkevgVPLLAVMKnncmssffKKYHHTppTN 242
Cdd:cd14622   80 TLLETISIRdfLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGM----------IDLIAAVQ--------KQQQQT--GN 139

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 243 API-IQCSTGGARCGVFiiidILINLIDNRIKNSYSIEWW--MLKVRSKRNHSALTNQQHSFIYDIIIKY 309
Cdd:cd14622  140 HPIvVHCSAGAGRTGTF----IALSNILERVKAEGLLDVFqtVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 52-308 4.03e-12

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: 65.83  E-value: 4.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  52 GQRTENIHRNIYG-AVPYDYNLVNLTSTQ-RNPLGYINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVML 129
Cdd:cd14633   35 AKKDENRMKNRYGnIIAYDHSRVRLQPIEgETSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMV 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 130 LEDVELGIEKSDKYFPNNTR--EELKFGIYDitcKEFVKRNILEYRLLEVSVGNETHQVHHYKFHGWTEFNLPKYED-FM 206
Cdd:cd14633  115 TNLVEVGRVKCCKYWPDDTEiyKDIKVTLIE---TELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATgLL 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 207 AFYNTMKEvgvpllavmknncmssffkkyhHTPPTNAP-IIQCSTGGARCGVFIIIDILINLIDNriKNSYSIEWWMLKV 285
Cdd:cd14633  192 GFVRQVKS----------------------KSPPNAGPlVVHCSAGAGRTGCFIVIDIMLDMAER--EGVVDIYNCVREL 247

                        250       260
                 ....*....|....*....|...
gi 193202549 286 RSKRNHSALTNQQHSFIYDIIIK 308
Cdd:cd14633  248 RSRRVNMVQTEEQYVFIHDAILE 270
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
185-308 9.32e-12

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 61.22  E-value: 9.32e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549   185 QVHHYKFHGWTEFNLPKY-EDFMAFYNTMKevgvpllavmknncmssffKKYHHTPPTNAPIIQCSTGGARCGVFIIIDI 263
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESpDSILELLRAVK-------------------KNLNQSESSGPVVVHCSAGVGRTGTFVAIDI 61

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 193202549   264 LINLIDNRiKNSYSIEWWMLKVRSKRNHSALTNQQHSFIYDIIIK 308
Cdd:smart00404  62 LLQQLEAE-AGEVDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 185-308 9.32e-12

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: 61.22  E-value: 9.32e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549   185 QVHHYKFHGWTEFNLPKY-EDFMAFYNTMKevgvpllavmknncmssffKKYHHTPPTNAPIIQCSTGGARCGVFIIIDI 263
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESpDSILELLRAVK-------------------KNLNQSESSGPVVVHCSAGVGRTGTFVAIDI 61

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 193202549   264 LINLIDNRiKNSYSIEWWMLKVRSKRNHSALTNQQHSFIYDIIIK 308
Cdd:smart00012  62 LLQQLEAE-AGEVDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 85-307 1.06e-11

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: 63.84  E-value: 1.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  85 YINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKYFPNNTREElkFGIYDITCKE- 163
Cdd:cd17668    1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEE--YGNFLVTQKSv 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 164 -----FVKRNiLEYRLLEVSVGNETHQ-----VHHYKFHGWTEFNLPKYEdfmafyntmkevgVPLLAVMKnncmSSFFK 233
Cdd:cd17668   79 qvlayYTVRN-FTLRNTKIKKGSQKGRpsgrvVTQYHYTQWPDMGVPEYT-------------LPVLTFVR----KASYA 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193202549 234 KYHHTPPTnapIIQCSTGGARCGVFiiIDILINLIDNRIKNSYSIEWWMLKVRSKRNHSALTNQQHSFIYDIII 307
Cdd:cd17668  141 KRHAVGPV---VVHCSAGVGRTGTY--IVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 43-258 1.38e-11

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: 64.67  E-value: 1.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  43 YQ-RARTISEGQRTENIHRNIY-GAVPYDYNLVNLTStQRNP--LGYINAS-VAEFPEIGRHYIITGAAQDTQIPFFWQM 117
Cdd:cd14609   27 YQaEPNTCSTAQGEANVKKNRNpDFVPYDHARIKLKA-ESNPsrSDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQM 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 118 VFEQKSPAIVMLLEDVELGIEKSDKYFPNNTREelKFGIYDIT-------CKEFVKRNileYRLLEVSVgNETHQVHHYK 190
Cdd:cd14609  106 VWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSS--LYHIYEVNlvsehiwCEDFLVRS---FYLKNVQT-QETRTLTQFH 179

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193202549 191 FHGWTEFNLPKYEDfmafyntmkevgvPLLAVMK--NNCMSSffkkyhhtppTNAPII-QCSTGGARCGVF 258
Cdd:cd14609  180 FLSWPAEGIPSSTR-------------PLLDFRRkvNKCYRG----------RSCPIIvHCSDGAGRTGTY 227
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 85-308 1.69e-11

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: 63.15  E-value: 1.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  85 YINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKYFPN--NTREELKFGIYDI-TC 161
Cdd:cd14632    1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDdsDTYGDIKITLLKTeTL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 162 KEFVKRNI-LEYRLLEVSvgnetHQVHHYKFHGWTEFNLPKYED-FMAFYNTMKEvgvpllavmknncmssffkkyhHTP 239
Cdd:cd14632   81 AEYSVRTFaLERRGYSAR-----HEVKQFHFTSWPEHGVPYHATgLLAFIRRVKA----------------------STP 133

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 240 PTNAPI-IQCSTGGARCGVFiiIDILINLIDNRIKNSYSIEWWMLKVRSKRNHSALTNQQHSFIYDIIIK 308
Cdd:cd14632  134 PDAGPVvVHCSAGAGRTGCY--IVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 52-258 2.22e-11

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: 63.92  E-value: 2.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  52 GQRTENIHRN-IYGAVPYDYNLVNLT-STQRNPLGYINAS-VAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVM 128
Cdd:cd14610   39 AQREENVQKNrSLAVLPYDHSRIILKaENSHSHSDYINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVM 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 129 LLEDVELGIEKSDKYFPNNTREelKFGIYDIT-------CKEFVKRNileYRLLEVSVgNETHQVHHYKFHGWTEFNLPk 201
Cdd:cd14610  119 LTPLAENGVKQCYHYWPDEGSN--LYHIYEVNlvsehiwCEDFLVRS---FYLKNLQT-NETRTVTQFHFLSWNDQGVP- 191

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 193202549 202 yEDFMAFYNTMKEVgvpllavmkNNCMSSffkkyhhtppTNAPII-QCSTGGARCGVF 258
Cdd:cd14610  192 -ASTRSLLDFRRKV---------NKCYRG----------RSCPIIvHCSDGAGRSGTY 229
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 66-308 2.43e-11

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: 63.04  E-value: 2.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  66 VPYDYNLVNLTSTQRNPLG-YINASVAE-FPEIGRHYIITGAAQDTqIPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKY 143
Cdd:cd14620    5 LPYDHSRVILSQLDGIPCSdYINASYIDgYKEKNKFIAAQGPKQET-VNDFWRMVWEQKSATIVMLTNLKERKEEKCYQY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 144 FPNN---TREELKFGIYDITCkefvkrnILEYRLLEVSVGNETHQ-------VHHYKFHGWTEFnlpkyedfmafyntmk 213
Cdd:cd14620   84 WPDQgcwTYGNIRVAVEDCVV-------LVDYTIRKFCIQPQLPDgckaprlVTQLHFTSWPDF---------------- 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 214 evGVPLLAVmknnCMSSFFKKYHHTPPTNA-PII-QCSTGGARCGVFIIIDILINLIDNRIKnsYSIEWWMLKVRSKRNH 291
Cdd:cd14620  141 --GVPFTPI----GMLKFLKKVKSVNPVHAgPIVvHCSAGVGRTGTFIVIDAMIDMMHAEQK--VDVFEFVSRIRNQRPQ 212

                        250
                 ....*....|....*..
gi 193202549 292 SALTNQQHSFIYDIIIK 308
Cdd:cd14620  213 MVQTDMQYSFIYQALLE 229
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 57-258 4.22e-11

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: 62.54  E-value: 4.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  57 NIHRN-IYGAVPYDYNLVNLTSTqRNPLG--YINASVAEFPEIGRHYIIT-GAAQDTqIPFFWQMVFEQKSPAIVMLLED 132
Cdd:cd14554    6 NKFKNrLVNILPYESTRVCLQPI-RGVEGsdYINASFIDGYRQRGAYIATqGPLAET-TEDFWRMLWEHNSTIIVMLTKL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 133 VELGIEKSDKYFPNNTREELKFGIYDITCKEFVKRNIL-EYRLLEVSVGnETHQVHHYKFHGWTEFNLPK----YEDFMA 207
Cdd:cd14554   84 REMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILrEFKVTDARDG-QSRTVRQFQFTDWPEQGVPKsgegFIDFIG 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 193202549 208 -FYNTMKEVGvpllavmknncmssffkkyhhtppTNAPI-IQCSTGGARCGVF 258
Cdd:cd14554  163 qVHKTKEQFG------------------------QEGPItVHCSAGVGRTGVF 191
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 54-200 5.69e-11

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: 62.21  E-value: 5.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  54 RTENIHRNIygaVPYDYNLVNLTSTQRNP-LGYINASVAEFPEIGRHYIIT-GAAQDTQIPFfWQMVFEQKSPAIVMLLE 131
Cdd:cd14614   13 RCKNRYTNI---LPYDFSRVKLVSMHEEEgSDYINANYIPGYNSPQEYIATqGPLPETRNDF-WKMVLQQKSQIIVMLTQ 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193202549 132 DVELGIEKSDKYFPnNTREELKFGiyDITCKEFVKRNILE--YRLLEVSVGNETHQVHHYKFHGWTEFNLP 200
Cdd:cd14614   89 CNEKRRVKCDHYWP-FTEEPVAYG--DITVEMLSEEEQPDwaIREFRVSYADEVQDVMHFNYTAWPDHGVP 156
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 85-258 7.04e-11

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: 61.50  E-value: 7.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  85 YINASVAEFPEIGRHYIITGAAQDTqIPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKYFPNNTREElKFGIYDITCKE- 163
Cdd:cd14601    7 YINMEIPSSSIINRYIACQGPLPNT-CSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSS-SYGGFQVTCHSe 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 164 -----FVKRNILEYRLLEvsvgNETHQVHHYKFHGWTEFNLP-KYEDFMAFYNTMKEvgvpllavmknncmssffKKYHH 237
Cdd:cd14601   85 egnpaYVFREMTLTNLEK----NESRPLTQIQYIAWPDHGVPdDSSDFLDFVCLVRN------------------KRAGK 142

                        170       180
                 ....*....|....*....|.
gi 193202549 238 TPPTnapIIQCSTGGARCGVF 258
Cdd:cd14601  143 DEPV---VVHCSAGIGRTGVL 160
PHA02738 PHA02738
hypothetical protein; Provisional
 48-310 9.54e-11

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 62.25  E-value: 9.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  48 TISEGQRTENIHRNIYgAVPYDYNLVNLtSTQRNPLGYINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIV 127
Cdd:PHA02738  42 TFNAEKKNRKLNRYLD-AVCFDHSRVIL-PAERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIV 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 128 MLLEDVELGIEKSDKYFPNNTREELKFGIYDITCKEFVKRNILEYRLLEVSVGNE-THQVHHYKFHGWTEFNLPKyeDFM 206
Cdd:PHA02738 120 MLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDGTSaTQTVTHFNFTAWPDHDVPK--NTS 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 207 AFYNTMKEVGvpllAVMKNNCMSSFfkKYHHTPPTNAPI-IQCSTGGARCGVFIIIDILINLIDNriKNSYSIEWWMLKV 285
Cdd:PHA02738 198 EFLNFVLEVR----QCQKELAQESL--QIGHNRLQPPPIvVHCNAGLGRTPCYCVVDISISRFDA--CATVSIPSIVSSI 269

                        250       260
                 ....*....|....*....|....*
gi 193202549 286 RSKRNHSALTNQQHSFIYDIIIKYI 310
Cdd:PHA02738 270 RNQRYYSLFIPFQYFFCYRAVKRYV 294
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 85-201 2.21e-10

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: 59.77  E-value: 2.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  85 YINASVaefpeIGRH------YIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKYFPNNTREelKFGIYD 158
Cdd:cd14546    1 YINAST-----IYDHdprnpaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSE--VYHIYE 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 193202549 159 IT-------CKEFVKRNIleyrLLEVSVGNETHQVHHYKFHGWTEFNLPK 201
Cdd:cd14546   74 VHlvsehiwCDDYLVRSF----YLKNLQTSETRTVTQFHFLSWPDEGIPA 119
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 84-258 4.10e-10

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: 59.85  E-value: 4.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  84 GYINAS-VAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVElGIEKSDKYFPNntrEELKFGIYDITCK 162
Cdd:cd14612   45 SYINANyIRGYDGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKE-KKEKCVHYWPE---KEGTYGRFEIRVQ 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 163 EFVKRNILEYRLLEVSVGNETHQVHHYKFHGWTEFNLPkyedfmafyntmkEVGVPLLAVMKNncmssfFKKYHHTPPTN 242
Cdd:cd14612  121 DMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTP-------------ESAGPLLRLVAE------VEESRQTAASP 181

                        170
                 ....*....|....*..
gi 193202549 243 APII-QCSTGGARCGVF 258
Cdd:cd14612  182 GPIVvHCSAGIGRTGCF 198
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 85-303 4.63e-10

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: 58.77  E-value: 4.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  85 YINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKYFPNN---TREELKFGIYDITC 161
Cdd:cd14551    1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQgcwTYGNLRVRVEDTVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 162 K-EFVKRNILEYRLLEVSVGNETHQVHHYKFHGWTEFNLPKyedfmafyntmKEVGvpllavmknncMSSFFKKYHH-TP 239
Cdd:cd14551   81 LvDYTTRKFCIQKVNRGIGEKRVRLVTQFHFTSWPDFGVPF-----------TPIG-----------MLKFLKKVKSaNP 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193202549 240 PTNAPI-IQCSTGGARCGVFiiIDILINLIDNRIKNSYSIEWWMLKVRSKRNHSALTNQQHSFIY 303
Cdd:cd14551  139 PRAGPIvVHCSAGVGRTGTF--IVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 48-309 5.78e-10

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: 59.65  E-value: 5.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  48 TISEGQRTENIHRNIY-GAVPYDYNLVNLTSTQRNP-LGYINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPA 125
Cdd:cd14621   43 TCEAASKEENKEKNRYvNILPYDHSRVHLTPVEGVPdSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTAT 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 126 IVMLLEDVELGIEKSDKYFPNN---TREELKFGIYDITC-KEFVKRNILEYRLLEVSVGNETHQVHHYKFHGWTEFnlpk 201
Cdd:cd14621  123 IVMVTNLKERKECKCAQYWPDQgcwTYGNIRVSVEDVTVlVDYTVRKFCIQQVGDVTNKKPQRLITQFHFTSWPDF---- 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 202 yedfmafyntmkevGVPLLAVmknnCMSSFFKKYHHTPPT--NAPIIQCSTGGARCGVFIIIDILINLIDNRIKnsYSIE 279
Cdd:cd14621  199 --------------GVPFTPI----GMLKFLKKVKNCNPQyaGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERK--VDVY 258

                        250       260       270
                 ....*....|....*....|....*....|
gi 193202549 280 WWMLKVRSKRNHSALTNQQHSFIYDIIIKY 309
Cdd:cd14621  259 GFVSRIRAQRCQMVQTDMQYVFIYQALLEH 288
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 58-258 7.60e-10

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: 59.11  E-value: 7.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  58 IHRNIYGAV-PYDYNLVNLTST-QRNPLG-YINAS-VAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMlLEDV 133
Cdd:cd14613   26 VRKNRYKTIlPNPHSRVCLTSPdQDDPLSsYINANyIRGYGGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVM-ITNI 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 134 ELGIEKSDKYFPnntREELKFGIYDITCKEFVKRNILEYRLLEVSVGNETHQVHHYKFHGWTEFNLPkyedfmafyntmk 213
Cdd:cd14613  105 EEMNEKCTEYWP---EEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEERGLKHYWYTSWPDQKTP------------- 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 193202549 214 EVGVPLLAVMKNncmssFFKKYHHTPPTNAP-IIQCSTGGARCGVF 258
Cdd:cd14613  169 DNAPPLLQLVQE-----VEEARQQAEPNCGPvIVHCSAGIGRTGCF 209
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 85-310 1.21e-09

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: 58.97  E-value: 1.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  85 YINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKYFPNNTREELKFGIYDITCKEF 164
Cdd:cd14628   82 YINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYN 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 165 VKRNIL-EYRLLEVSVGnETHQVHHYKFHGWTEFNLPK----YEDFMAFYNTMKEvgvpllavmknncmssffkKYHHTP 239
Cdd:cd14628  162 MPQYILrEFKVTDARDG-QSRTVRQFQFTDWPEQGVPKsgegFIDFIGQVHKTKE-------------------QFGQDG 221

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193202549 240 PTNapiIQCSTGGARCGVFiiIDILINLIDNRIKNSYSIEWWMLKVRSKRNHSALTNQQHSFIYDIIIKYI 310
Cdd:cd14628  222 PIS---VHCSAGVGRTGVF--ITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYL 287
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 85-310 1.23e-09

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: 58.59  E-value: 1.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  85 YINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKYFPNNTREELKFGIYDITCKEF 164
Cdd:cd14627   83 YINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYN 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 165 VKRNIL-EYRLLEVSVGnETHQVHHYKFHGWTEFNLPK----YEDFMAFYNTMKEvgvpllavmknncmssffkKYHHTP 239
Cdd:cd14627  163 MPQYILrEFKVTDARDG-QSRTVRQFQFTDWPEQGVPKsgegFIDFIGQVHKTKE-------------------QFGQDG 222

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193202549 240 PTNapiIQCSTGGARCGVFiiIDILINLIDNRIKNSYSIEWWMLKVRSKRNHSALTNQQHSFIYDIIIKYI 310
Cdd:cd14627  223 PIS---VHCSAGVGRTGVF--ITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYL 288
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 85-258 1.27e-09

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: 57.53  E-value: 1.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  85 YINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKYFPNNTREELKFGiyDITCKEF 164
Cdd:cd14557    1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFG--DVVVKIN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 165 VKRNILEYRLLEVSVGNETHQ-----VHHYKFHGWTEFNLPkyEDFMAFYNTMKEVgvpllavmknNCMSSFFkkyhhtp 239
Cdd:cd14557   79 EEKICPDYIIRKLNINNKKEKgsgreVTHIQFTSWPDHGVP--EDPHLLLKLRRRV----------NAFNNFF------- 139

                        170
                 ....*....|....*....
gi 193202549 240 pTNAPIIQCSTGGARCGVF 258
Cdd:cd14557  140 -SGPIVVHCSAGVGRTGTY 157
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 57-256 3.15e-09

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: 56.82  E-value: 3.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  57 NIHRNIygaVPYDYNLVNLTSTQRNPLG-YINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVEL 135
Cdd:cd14619    1 NRFRNV---LPYDWSRVPLKPIHEEPGSdYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 136 GIEKSDKYFPNN----TREELKFGIY------DITCKEFVKRNILEyrllevsvgNETHQVHHYKFHGWTEFNLPK-YED 204
Cdd:cd14619   78 GRVKCEHYWPLDytpcTYGHLRVTVVseevmeNWTVREFLLKQVEE---------QKTLSVRHFHFTAWPDHGVPSsTDT 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 193202549 205 FMAFYNTMKEVgvpllavmknncMSSFFKkyhhtppTNAPIIQCSTGGARCG 256
Cdd:cd14619  149 LLAFRRLLRQW------------LDQTMS-------GGPTVVHCSAGVGRTG 181
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 85-257 3.20e-09

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: 56.28  E-value: 3.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  85 YINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKYFPNNTREELKFGIYDITC--K 162
Cdd:cd14542    1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKISLekE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 163 EFVKRNILeYRLLEVSVGNETHQVHHYKFHGWTEFNLPKYEDfmafyntmkevgvPLLAvmknncMSSFFKKYHHTPPTn 242
Cdd:cd14542   81 KRVGPDFL-IRTLKVTFQKESRTVYQFHYTAWPDHGVPSSVD-------------PILD------LVRLVRDYQGSEDV- 139

                        170
                 ....*....|....*.
gi 193202549 243 aPI-IQCSTGGARCGV 257
Cdd:cd14542  140 -PIcVHCSAGCGRTGT 154
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 46-310 4.04e-09

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: 57.04  E-value: 4.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  46 ARTISEGQRTENIHRNIYGAVPYDYNLVNLTSTqRNPLG--YINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKS 123
Cdd:cd14629   43 SRFISANLPCNKFKNRLVNIMPYELTRVCLQPI-RGVEGsdYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNS 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 124 PAIVMLLEDVELGIEKSDKYFPNNTREELKFGIYDITCKEFVKRNIL-EYRLLEVSVGnETHQVHHYKFHGWTEFNLPKY 202
Cdd:cd14629  122 TIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILrEFKVTDARDG-QSRTIRQFQFTDWPEQGVPKT 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 203 -EDFMAF----YNTMKEVGvpllavmknncmssffkkyhhtppTNAPI-IQCSTGGARCGVFiiIDILINLIDNRIKNSY 276
Cdd:cd14629  201 gEGFIDFigqvHKTKEQFG------------------------QDGPItVHCSAGVGRTGVF--ITLSIVLERMRYEGVV 254

                        250       260       270
                 ....*....|....*....|....*....|....
gi 193202549 277 SIEWWMLKVRSKRNHSALTNQQHSFIYDIIIKYI 310
Cdd:cd14629  255 DMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYL 288
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 47-302 6.17e-09

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 56.93  E-value: 6.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  47 RTISEGQRTENIHRNIYGAVP-YDYNLVNLTSTQRNPLGYINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPA 125
Cdd:PHA02747  41 GLIANFEKPENQPKNRYWDIPcWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSI 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 126 IVMLLEDVEL-GIEKSDKYFPNNTREELKFGIYDITCKEFVKRNILEYRLLEVS--VGNETHQVHHYKFHGWTEFNLP-K 201
Cdd:PHA02747 121 IVMLTPTKGTnGEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITdkILKDSRKISHFQCSEWFEDETPsD 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 202 YEDFMAFYNtmkevgvpLLAVMKNNCMSSFFKKYHHTPPTnapIIQCSTGGARCGVFIIIDILINLIDNRikNSYSIEWW 281
Cdd:PHA02747 201 HPDFIKFIK--------IIDINRKKSGKLFNPKDALLCPI---VVHCSDGVGKTGIFCAVDICLNQLVKR--KAICLAKT 267

                        250       260
                 ....*....|....*....|.
gi 193202549 282 MLKVRSKRNHSALTNQQHSFI 302
Cdd:PHA02747 268 AEKIREQRHAGIMNFDDYLFI 288
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 54-311 1.56e-08

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 55.39  E-value: 1.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  54 RTENIHRNIYGAVP-YDYNLVNLtSTQRNPLGYINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLED 132
Cdd:PHA02742  49 ELKNMKKCRYPDAPcFDRNRVIL-KIEDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKI 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 133 VELGIEKSDKYFPNNTREELKFGIYDITCKEFvkRNILEYRLLEVSVGNETH----QVHHYKFHGWTEFNLPK-YEDFMA 207
Cdd:PHA02742 128 MEDGKEACYPYWMPHERGKATHGEFKIKTKKI--KSFRNYAVTNLCLTDTNTgaslDIKHFAYEDWPHGGLPRdPNKFLD 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 208 FyntmkevgvpLLAVMKNNCMSSFFKKYHHTPPTNAPIIQCSTGGARCGVFIIIDILINLIDNRIknSYSIEWWMLKVRS 287
Cdd:PHA02742 206 F----------VLAVREADLKADVDIKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERA--IIPLLSIVRDLRK 273

                        250       260
                 ....*....|....*....|....
gi 193202549 288 KRNHSALTNQQHSFIYDIIIKYIR 311
Cdd:PHA02742 274 QRHNCLSLPQQYIFCYFIVLIFAK 297
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 85-311 2.62e-08

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: 53.83  E-value: 2.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  85 YINASVAEFPEIGRH--YIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKYFP-----NNTreeLKFGIY 157
Cdd:cd14598    1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgsrHNT---VTYGRF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 158 DITCKEFVKRNILEYRLLEVS--VGNETHQVHHYKFHGWTEFNLPkyEDFMAFYNTMKEVGvpllAVMKNNCMSSffkky 235
Cdd:cd14598   78 KITTRFRTDSGCYATTGLKIKhlLTGQERTVWHLQYTDWPEHGCP--EDLKGFLSYLEEIQ----SVRRHTNSTI----- 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193202549 236 hHTPPTNAPI-IQCSTGGARCGVFIIIDILINLIDNriKNSYSIEWWMLKVRSKRNHSALTNQQHSFIYDIIIKYIR 311
Cdd:cd14598  147 -DPKSPNPPVlVHCSAGVGRTGVVILSEIMIACLEH--NEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 67-258 5.47e-08

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: 52.99  E-value: 5.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  67 PYDYNLVNLTSTQRNP-LGYINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKYFP 145
Cdd:cd14616    8 PYNNNRVKLIADAGVPgSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRIRCHQYWP 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 146 NNTREELKFGiyDITCKEFVKRNILEY--RLLEVSVGNETHQVHHYKFHGWTEFNLPkyEDFMAFYNTMKEVGVpllavm 223
Cdd:cd14616   88 EDNKPVTVFG--DIVITKLMEDVQIDWtiRDLKIERHGDYMMVRQCNFTSWPEHGVP--ESSAPLIHFVKLVRA------ 157

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 193202549 224 knncmssffKKYHHTPPTnapIIQCSTGGARCGVF 258
Cdd:cd14616  158 ---------SRAHDNTPM---IVHCSAGVGRTGVF 180
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 66-258 8.95e-06

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: 46.47  E-value: 8.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  66 VPYDYNLVNLTSTQRNPLG-YINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKYF 144
Cdd:cd14618    7 LPYDHSRVRLSQLGGEPHSdYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRVLCDHYW 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 145 PNNTrEELKFGiyDITCKEFVKRNILEYRLLEVSVGNETHQ----VHHYKFHGWTEFNLPKY-EDFMAFYNTMKEvgvpl 219
Cdd:cd14618   87 PSES-TPVSYG--HITVHLLAQSSEDEWTRREFKLWHEDLRkerrVKHLHYTAWPDHGIPEStSSLMAFRELVRE----- 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 193202549 220 lavmknncmssffkKYHHTPPTNAPIIQCSTGGARCGVF 258
Cdd:cd14618  159 --------------HVQATKGKGPTLVHCSAGVGRSGTF 183
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 85-258 9.22e-06

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: 46.45  E-value: 9.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  85 YINAS-VAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVELGiEKSDKYFPNntreelKFGIYDIT--- 160
Cdd:cd14611   30 YINANyIRGYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKN-EKCVLYWPE------KRGIYGKVevl 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 161 ------CKEFVKRNileyrlLEVSVGNETHQVHHYKFHGWTEFNLPkyedfmafyntmkEVGVPLLAVMKNncmssfFKK 234
Cdd:cd14611  103 vnsvkeCDNYTIRN------LTLKQGSQSRSVKHYWYTSWPDHKTP-------------DSAQPLLQLMLD------VEE 157

                        170       180
                 ....*....|....*....|....*
gi 193202549 235 YHHTPPTNAPII-QCSTGGARCGVF 258
Cdd:cd14611  158 DRLASPGRGPVVvHCSAGIGRTGCF 182
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 85-214 1.11e-05

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


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 45.77  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  85 YINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLeDVELGiEKSDKYFPNNTRE------ELKFGIYD 158
Cdd:cd14550    1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLT-DNELN-EDEPIYWPTKEKPlecetfKVTLSGED 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 193202549 159 ITCKEFVKRNILEYRLLEVSVGNETHQVHHYKFHGWTEFNLPKYEDFmAFYNTMKE 214
Cdd:cd14550   79 HSCLSNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTVF-ELINTVQE 133
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 85-258 1.90e-05

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: 45.09  E-value: 1.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  85 YINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMlLEDVELGIEKSDKYFPNNTReeLKFGIYDItckEF 164
Cdd:cd14556    1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVM-LNQLDPKDQSCPQYWPDEGS--GTYGPIQV---EF 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 165 VKRNILE------YRLLEVSVGNETHQ-VHHYKFHGWtefnlPKYEDF----MAFYNTMKEVgvpllavmknncmSSFFK 233
Cdd:cd14556   75 VSTTIDEdvisriFRLQNTTRPQEGYRmVQQFQFLGW-----PRDRDTppskRALLKLLSEV-------------EKWQE 136

                        170       180
                 ....*....|....*....|....*
gi 193202549 234 KYHHTPPTnapiIQCSTGGARCGVF 258
Cdd:cd14556  137 QSGEGPIV----VHCLNGVGRSGVF 157
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 85-308 7.96e-05

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: 43.47  E-value: 7.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549  85 YINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVML--LEDVELGIEksdkYFPNNTReelkfGIYDITCK 162
Cdd:cd14634    1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLneMDAAQLCMQ----YWPEKTS-----CCYGPIQV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193202549 163 EFVKRNILE------YRLLEVSVGNETHQ-VHHYKFHGWtefnlPKYEDFMAFYNTmkevgvpLLAVMKNncMSSFFKKY 235
Cdd:cd14634   72 EFVSADIDEdiisriFRICNMARPQDGYRiVQHLQYIGW-----PAYRDTPPSKRS-------ILKVVRR--LEKWQEQY 137

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193202549 236 HHTppTNAPIIQCSTGGARCGVFIIIDILINLIDNriKNSYSIEWWMLKVRSKRNHSALTNQQHSFIYDIIIK 308
Cdd:cd14634  138 DGR--EGRTVVHCLNGGGRSGTFCAICSVCEMIQQ--QNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
 
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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