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Conserved domains on  [gi|1958801472|ref|XP_038939139|]
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tyrosine-protein phosphatase non-receptor type 18 isoform X9 [Rattus norvegicus]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 17-176 2.56e-94

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


The actual alignment was detected with superfamily member cd14603:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 266  Bit Score: 281.33  E-value: 2.56e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  17 RKCERYWAQEREPLQAGPFCITLTKETALTADITLRTLQVTFQKvpkgqkESRPVHQLQYMSWPDHGVPSSSDHILTMVE 96
Cdd:cd14603   113 KKCERYWAQEQEPLQTGPFTITLVKEKRLNEEVILRTLKVTFQK------ESRSVSHFQYMAWPDHGIPDSPDCMLAMIE 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  97 EARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQLF 176
Cdd:cd14603   187 LARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQMF 266
 
Name Accession Description Interval E-value
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 17-176 2.56e-94

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: 281.33  E-value: 2.56e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  17 RKCERYWAQEREPLQAGPFCITLTKETALTADITLRTLQVTFQKvpkgqkESRPVHQLQYMSWPDHGVPSSSDHILTMVE 96
Cdd:cd14603   113 KKCERYWAQEQEPLQTGPFTITLVKEKRLNEEVILRTLKVTFQK------ESRSVSHFQYMAWPDHGIPDSPDCMLAMIE 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  97 EARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQLF 176
Cdd:cd14603   187 LARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQMF 266
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
17-174 6.57e-58

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 187.06  E-value: 6.57e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  17 RKCERYWAQERE-PLQAGPFCITLTKETALTADITLRTLQVTFqkvpKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMV 95
Cdd:pfam00102  82 EKCAQYWPEEEGeSLEYGDFTVTLKKEKEDEKDYTVRTLEVSN----GGSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  96 EEARCLQGLGP-GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 174
Cdd:pfam00102 158 RKVRKSSLDGRsGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGE---VDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
17-174 7.76e-56

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 182.47  E-value: 7.76e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472   17 RKCERYWAQE-REPLQAGPFCITLTKETAlTADITLRTLQVTfqkvPKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMV 95
Cdd:smart00194 109 EKCAQYWPDEeGEPLTYGDITVTLKSVEK-VDDYTIRTLEVT----NTGCSETRTVTHYHYTNWPDHGVPESPESILDLI 183

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958801472   96 EEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQtipPNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 174
Cdd:smart00194 184 RAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAG---KEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
12-168 4.14e-23

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 96.70  E-value: 4.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  12 GMPDTRKCERYWAQEReplQAGPFCI--TLTKETALTADITLRTLQVTFQKvpKGQKeSRPVHQLQYMSWPDHGVPSSS- 88
Cdd:COG5599   114 ISKPKVKMPVYFRQDG---EYGKYEVssELTESIQLRDGIEARTYVLTIKG--TGQK-KIEIPVLHVKNWPDHGAISAEa 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  89 --DHILTMVEEARCLQGLGpGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIpPNFSLFEVVLEMRKQR-PAAVQTEEQY 165
Cdd:COG5599   188 lkNLADLIDKKEKIKDPDK-LLPVVHCRAGVGRTGTLIACLALSKSINALVQ-ITLSVEEIVIDMRTSRnGGMVQTSEQL 265


                  ...
gi 1958801472 166 RFL 168
Cdd:COG5599   266 DVL 268
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 15-184 5.63e-19

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 86.24  E-value: 5.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  15 DTRKCERYWAQERE-PLQAGPFcITLTKETALTADITLRTLQVTfqkvPKGQKESRPVHQLQYMSWPDHGVPSSSDHILT 93
Cdd:PHA02746  150 DDEKCFELWTKEEDsELAFGRF-VAKILDIIEELSFTKTRLMIT----DKISDTSREIHHFWFPDWPDNGIPTGMAEFLE 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  94 MV-----EEARCL-----QGLGPGPLCVHCSAGCGRTGVLCAVD-YVRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTE 162
Cdd:PHA02746  225 LInkvneEQAELIkqadnDPQTLGPIVVHCSAGIGRAGTFCAIDnALEQLEKEKEV----CLGEIVLKIRKQRHSSVFLP 300

                         170       180
                  ....*....|....*....|..
gi 1958801472 163 EQYRFLYHTVAQLFSRTLQNNS 184
Cdd:PHA02746  301 EQYAFCYKALKYAIIEEAKKKF 322
 
Name Accession Description Interval E-value
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 17-176 2.56e-94

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: 281.33  E-value: 2.56e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  17 RKCERYWAQEREPLQAGPFCITLTKETALTADITLRTLQVTFQKvpkgqkESRPVHQLQYMSWPDHGVPSSSDHILTMVE 96
Cdd:cd14603   113 KKCERYWAQEQEPLQTGPFTITLVKEKRLNEEVILRTLKVTFQK------ESRSVSHFQYMAWPDHGIPDSPDCMLAMIE 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  97 EARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQLF 176
Cdd:cd14603   187 LARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQMF 266
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 18-170 9.20e-82

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: 246.95  E-value: 9.20e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWAQEREP-LQAGPFCITLTKETALTADITLRTLQVTFQKvpkgqkESRPVHQLQYMSWPDHGVPSSSDHILTMVE 96
Cdd:cd14542    55 KCERYWPEEGEEqLQFGPFKISLEKEKRVGPDFLIRTLKVTFQK------ESRTVYQFHYTAWPDHGVPSSVDPILDLVR 128

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958801472  97 EARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFEVVLEMRKQRPAAVQTEEQYRFLYH 170
Cdd:cd14542   129 LVRDYQGSEDVPICVHCSAGCGRTGTICAIDYVWNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 17-176 2.69e-63

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: 200.84  E-value: 2.69e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  17 RKCERYWAQE-REPLQAGPFCITLTKETALTaDITLRTLQVTFQKvpkgqkESRPVHQLQYMSWPDHGVPSSSDHILTMV 95
Cdd:cd14602    81 KKCERYWAEPgEMQLEFGPFSVTCEAEKRKS-DYIIRTLKVKFNS------ETRTIYQFHYKNWPDHDVPSSIDPILELI 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  96 EEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQL 175
Cdd:cd14602   154 WDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIEL 233


                  .
gi 1958801472 176 F 176
Cdd:cd14602   234 F 234
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
17-174 6.57e-58

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 187.06  E-value: 6.57e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  17 RKCERYWAQERE-PLQAGPFCITLTKETALTADITLRTLQVTFqkvpKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMV 95
Cdd:pfam00102  82 EKCAQYWPEEEGeSLEYGDFTVTLKKEKEDEKDYTVRTLEVSN----GGSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  96 EEARCLQGLGP-GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 174
Cdd:pfam00102 158 RKVRKSSLDGRsGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGE---VDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 15-170 1.11e-56

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: 182.49  E-value: 1.11e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  15 DTRKCERYWAQERE-PLQAGPFCITLTKETALtADITLRTLQVTfqkvPKGQKESRPVHQLQYMSWPDHGVPSSSDHILT 93
Cdd:cd00047    52 GREKCERYWPEEGGkPLEYGDITVTLVSEEEL-SDYTIRTLELS----PKGCSESREVTHLHYTGWPDHGVPSSPEDLLA 126

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801472  94 MVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPpnfSLFEVVLEMRKQRPAAVQTEEQYRFLYH 170
Cdd:cd00047   127 LVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAIDILLERLEAEGEV---DVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
17-174 7.76e-56

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 182.47  E-value: 7.76e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472   17 RKCERYWAQE-REPLQAGPFCITLTKETAlTADITLRTLQVTfqkvPKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMV 95
Cdd:smart00194 109 EKCAQYWPDEeGEPLTYGDITVTLKSVEK-VDDYTIRTLEVT----NTGCSETRTVTHYHYTNWPDHGVPESPESILDLI 183

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958801472   96 EEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQtipPNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 174
Cdd:smart00194 184 RAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAG---KEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 17-180 6.95e-53

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: 176.28  E-value: 6.95e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  17 RKCERYWAQE-REPLQAGPFCITLTKETALTaDITLRTLQVTFQKvpkgqkESRPVHQLQYMSWPDHGVPSSSDHILTMV 95
Cdd:cd14604   140 KKCERYWPLYgEEPMTFGPFRISCEAEQART-DYFIRTLLLEFQN------ETRRLYQFHYVNWPDHDVPSSFDSILDMI 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  96 EEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQL 175
Cdd:cd14604   213 SLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQL 292


                  ....*
gi 1958801472 176 FSRTL 180
Cdd:cd14604   293 FEKQL 297
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 17-170 5.60e-46

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: 155.48  E-value: 5.60e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  17 RKCERYWAQEREPLQAGPFCITLTKETALT-ADITLRTLQVTfqkvpKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMV 95
Cdd:cd18533    55 EKCDQYWPSGEYEGEYGDLTVELVSEEENDdGGFIVREFELS-----KEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLI 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  96 EEARCLQGLGP--GPLCVHCSAGCGRTGVLCAVDYVRQLL---LTQTIPPNFSL---FEVVLEMRKQRPAAVQTEEQYRF 167
Cdd:cd18533   130 KLKRELNDSASldPPIIVHCSAGVGRTGTFIALDSLLDELkrgLSDSQDLEDSEdpvYEIVNQLRKQRMSMVQTLRQYIF 209


                  ...
gi 1958801472 168 LYH 170
Cdd:cd18533   210 LYD 212
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
70-174 2.05e-40

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 137.49  E-value: 2.05e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472   70 PVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGP--GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFslFEV 147
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDI--FDT 78

                           90       100
                   ....*....|....*....|....*..
gi 1958801472  148 VLEMRKQRPAAVQTEEQYRFLYHTVAQ 174
Cdd:smart00404  79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 70-174 2.05e-40

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


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 137.49  E-value: 2.05e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472   70 PVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGP--GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFslFEV 147
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDI--FDT 78

                           90       100
                   ....*....|....*....|....*..
gi 1958801472  148 VLEMRKQRPAAVQTEEQYRFLYHTVAQ 174
Cdd:smart00012  79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 18-174 8.05e-35

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: 127.58  E-value: 8.05e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWAQEREPLQAGPFCITLTKETAlTADITLRTLQVTfqkvPKGQKES-RPVHQLQYMSWPDHGVPSSSDHILTMVE 96
Cdd:cd14544    93 KCVRYWPDEGMQKQYGPYRVQNVSEHD-TTDYTLRELQVS----KLDQGDPiREIWHYQYLSWPDHGVPSDPGGVLNFLE 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  97 EARCLQG--LGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 174
Cdd:cd14544   168 DVNQRQEslPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDCDIDIQKTIQMVRSQRSGMVQTEAQYKFIYVAVAQ 247
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 18-174 4.29e-34

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: 124.41  E-value: 4.29e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWA-QEREPL-QAGPFCITLTKETALtADITLRTLQVTfqkvPKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMV 95
Cdd:cd14538    57 KCHRYWPdSLNKPLiCGGRLEVSLEKYQSL-QDFVIRRISLR----DKETGEVHHITHLNFTTWPDHGTPQSADPLLRFI 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958801472  96 EEARCLQglGPGPLCVHCSAGCGRTGVLCAVDYVrQLLLTQTIPpnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 174
Cdd:cd14538   132 RYMRRIH--NSGPIVVHCSAGIGRTGVLITIDVA-LGLIERDLP--FDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 17-169 8.32e-34

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


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 123.62  E-value: 8.32e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  17 RKCERYWAQEREPlQAGPFCITLTKETALtADITLRTLQVTFQKV--PKGQKESRPVHQLQYMSWPDHGVPSSSDHILTM 94
Cdd:cd14549    54 RKCDQYWPKEGTE-TYGNIQVTLLSTEVL-ATYTVRTFSLKNLKLkkVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSF 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801472  95 VEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVD-YVRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTEEQYRFLY 169
Cdd:cd14549   132 VRKSSAANPPGAGPIVVHCSAGVGRTGTYIVIDsMLQQIQDKGTV----NVFGFLKHIRTQRNYLVQTEEQYIFIH 203
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 18-169 1.00e-33

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: 123.62  E-value: 1.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWAQEREPLQAGPFCITLTKETALTaDITLRTLQVTfqkvpkGQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEE 97
Cdd:cd14548    80 KCDHYWPFDQDPVYYGDITVTMLSESVLP-DWTIREFKLE------RGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRL 152

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958801472  98 ARCLQGLGPGPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIPPnfslFEVVLEMRKQRPAAVQTEEQYRFLY 169
Cdd:cd14548   153 VRDYIKQEKGPTIVHCSAGVGRTGTFIALDRlLQQIESEDYVDI----FGIVYDLRKHRPLMVQTEAQYIFLH 221
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 18-174 4.14e-31

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: 118.06  E-value: 4.14e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWAQEREPLQAGPFCITLTKETAlTADITLRTLQVTfqkVPKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEE 97
Cdd:cd14606   108 KCVPYWPEVGMQRAYGPYSVTNCGEHD-TTEYKLRTLQVS---PLDNGELIREIWHYQYLSWPDHGVPSEPGGVLSFLDQ 183

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958801472  98 ARCLQGLGP--GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 174
Cdd:cd14606   184 INQRQESLPhaGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLDCDIDIQKTIQMVRAQRSGMVQTEAQYKFIYVAIAQ 262
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 18-167 5.13e-31

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


Pssm-ID: 350389 [Multi-domain]  Cd Length: 212  Bit Score: 116.27  E-value: 5.13e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWAQEREPLQAGPFCITLTKETAlTADITLRTLQVTFQKvpkgQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEE 97
Cdd:cd14541    60 KCHQYWPDLGETMQFGNLQITCVSEEV-TPSFAFREFILTNTN----TGEERHITQMQYLAWPDHGVPDDSSDFLDFVKR 134

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958801472  98 AR-CLQGLGPgPLCVHCSAGCGRTGVLCAVDYVrqLLLTQTIPPNFSLfEVVLEMRKQRPAAVQTEEQYRF 167
Cdd:cd14541   135 VRqNRVGMVE-PTVVHCSAGIGRTGVLITMETA--MCLIEANEPVYPL-DIVRTMRDQRAMLIQTPSQYRF 201
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 17-169 2.38e-29

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: 113.61  E-value: 2.38e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  17 RKCERYWAQEREPLQAGPFCITLTKETALTADITLRTLQVTFQKvpkgQKESRPVHQLQYMSWPDHGVPSSSDHILTMVE 96
Cdd:cd14543   112 VKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTE----TDESRQVTHFQFTSWPDFGVPSSAAALLDFLG 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  97 E-----ARCLQGLGPG--------PLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTE 162
Cdd:cd14543   188 EvrqqqALAVKAMGDRwkghppgpPIVVHCSAGIGRTGTFCTLDIcLSQLEDVGTL----NVMQTVRRMRTQRAFSIQTP 263


                  ....*..
gi 1958801472 163 EQYRFLY 169
Cdd:cd14543   264 DQYYFCY 270
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 18-172 3.13e-29

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: 111.38  E-value: 3.13e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWA-QEREPLQAGPFCITLTKETALtADITLRTLQVtfqkVPKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMVE 96
Cdd:cd14596    57 KCHRYWPeTLQEPMELENYQLRLENYQAL-QYFIIRIIKL----VEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFIC 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801472  97 EARCLQGLgpGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTV 172
Cdd:cd14596   132 YMRKVHNT--GPIVVHCSAGIGRAGVLICVDVLLSLIEKDL---SFNIKDIVREMRQQRYGMIQTKDQYLFCYKVV 202
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 16-174 2.95e-28

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: 109.08  E-value: 2.95e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  16 TRKCERYWAQ---EREPLQAGPFCITLTKETAlTADITLRTLQVtfQKVPKGQkeSRPVHQLQYMSWPDHGVPSSSDHIL 92
Cdd:cd14540    55 REKCFRYWPTlggEHDALTFGEYKVSTKFSVS-SGCYTTTGLRV--KHTLSGQ--SRTVWHLQYTDWPDHGCPEDVSGFL 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  93 TMVEEA-----RCLQGLG----PGPLCVHCSAGCGRTGVLCAVDYVrQLLLTQTIPPNfsLFEVVLEMRKQRPAAVQTEE 163
Cdd:cd14540   130 DFLEEInsvrrHTNQDVAghnrNPPTLVHCSAGVGRTGVVILADLM-LYCLDHNEELD--IPRVLALLRHQRMLLVQTLA 206

                         170
                  ....*....|.
gi 1958801472 164 QYRFLYHTVAQ 174
Cdd:cd14540   207 QYKFVYNVLIQ 217
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 18-172 5.21e-28

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: 109.34  E-value: 5.21e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWAQEREPLQAGPFCITLTKETAlTADITLRTLQVTfqKVPKGQKEsRPVHQLQYMSWPDHGVPSSSDHILTMVEE 97
Cdd:cd14605    95 KCVKYWPDEYALKEYGVMRVRNVKESA-AHDYILRELKLS--KVGQGNTE-RTVWQYHFRTWPDHGVPSDPGGVLDFLEE 170

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801472  98 ARCLQG--LGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTV 172
Cdd:cd14605   171 VHHKQEsiMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIQMVRSQRSGMVQTEAQYRFIYMAV 247
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 18-172 1.24e-27

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: 108.05  E-value: 1.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWAQEREPLQAGPFCITLTKETALtADITLRTLQVTFQKvpkgQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEE 97
Cdd:cd14619    81 KCEHYWPLDYTPCTYGHLRVTVVSEEVM-ENWTVREFLLKQVE----EQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRL 155

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801472  98 AR--CLQGLGPGPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIPPnfslFEVVLEMRKQRPAAVQTEEQYRFLYHTV 172
Cdd:cd14619   156 LRqwLDQTMSGGPTVVHCSAGVGRTGTLIALDVlLQQLQSEGLLGP----FSFVQKMRENRPLMVQTESQYVFLHQCI 229
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 18-172 1.25e-27

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: 106.97  E-value: 1.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWAQEREpLQAGPFCITLTKETaLTADITLRTLQVTFQKvpkgQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEE 97
Cdd:cd14552    55 KCAQYWPEDGS-VSSGDITVELKDQT-DYEDYTLRDFLVTKGK----GGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAA 128

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801472  98 A-RCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTV 172
Cdd:cd14552   129 VqKQQQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGV---LDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 18-176 1.94e-27

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: 106.95  E-value: 1.94e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWAQEREPLQAGPFCITLTKETALTADItLRTLQVTFQKvpkgQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEE 97
Cdd:cd14601    60 KCHQYWPEPSGSSSYGGFQVTCHSEEGNPAYV-FREMTLTNLE----KNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCL 134

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958801472  98 ARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVrqLLLTQTIPPNFSLfEVVLEMRKQRPAAVQTEEQYRFLYHTVAQLF 176
Cdd:cd14601   135 VRNKRAGKDEPVVVHCSAGIGRTGVLITMETA--MCLIECNQPVYPL-DIVRTMRDQRAMMIQTPSQYRFVCEAILKVY 210
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 18-169 6.01e-27

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: 106.33  E-value: 6.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWAQeREPLQAGPFCITLTKETALtADITLRTLQVTFQkvpkGQKESRPVHQLQYMSWPDHGVPsssDHILTMVEE 97
Cdd:cd14553    87 KCDQYWPT-RGTETYGLIQVTLLDTVEL-ATYTVRTFALHKN----GSSEKREVRQFQFTAWPDHGVP---EHPTPFLAF 157

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801472  98 ARCLQGLGP---GPLCVHCSAGCGRTGVLCAVD-YVRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTEEQYRFLY 169
Cdd:cd14553   158 LRRVKACNPpdaGPIVVHCSAGVGRTGCFIVIDsMLERIKHEKTV----DIYGHVTCLRAQRNYMVQTEDQYIFIH 229
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 16-169 8.10e-27

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: 105.55  E-value: 8.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  16 TRKCERYWAQErePLQAGPFCITLTKETALTADI----TLRTLQVTFQKVPkgqkESRPVHQLQYMSWPDHGVPSSSD-- 89
Cdd:cd14545    78 QIKCAQYWPQG--EGNAMIFEDTGLKVTLLSEEDksyyTVRTLELENLKTQ----ETREVLHFHYTTWPDFGVPESPAaf 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  90 -HILTMVEEARCLQGlGPGPLCVHCSAGCGRTGVLCAVDYVrQLLLTQTIPPNFSLFEVVLEMRKQRPAAVQTEEQYRFL 168
Cdd:cd14545   152 lNFLQKVRESGSLSS-DVGPPVVHCSAGIGRSGTFCLVDTC-LVLIEKGNPSSVDVKKVLLEMRKYRMGLIQTPDQLRFS 229


                  .
gi 1958801472 169 Y 169
Cdd:cd14545   230 Y 230
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 18-170 8.10e-27

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: 105.56  E-value: 8.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWAQErEPLQAGPFCITLTKeTALTADITLRTLQVTFQKvpkgqkESRPVHQLQYMSWPDHGVPSSSDHILTM--- 94
Cdd:cd14547    81 KCAQYWPEE-ENETYGDFEVTVQS-VKETDGYTVRKLTLKYGG------EKRYLKHYWYTSWPDHKTPEAAQPLLSLvqe 152

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801472  95 VEEARcLQGLGPGPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTEEQYRFLYH 170
Cdd:cd14547   153 VEEAR-QTEPHRGPIVVHCSAGIGRTGCFIATSIgCQQLREEGVV----DVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 18-174 1.31e-26

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: 105.49  E-value: 1.31e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWAQEREPLqaGPFCITLTkETALTADITLRTLqvTFQKvpKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEE 97
Cdd:cd14630    87 KCVRYWPDDTEVY--GDIKVTLI-ETEPLAEYVIRTF--TVQK--KGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQ 159

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801472  98 ARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 174
Cdd:cd14630   160 VKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGV---VDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 17-172 1.98e-26

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


Pssm-ID: 350506 [Multi-domain]  Cd Length: 209  Bit Score: 103.90  E-value: 1.98e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  17 RKCERYWAQEREPlQAGPFCITLtKETALTADITLRTLQVTFQKVPKGQKESRP----VHQLQYMSWPDHGVPSSSDHIL 92
Cdd:cd17668    54 RKCDQYWPADGSE-EYGNFLVTQ-KSVQVLAYYTVRNFTLRNTKIKKGSQKGRPsgrvVTQYHYTQWPDMGVPEYTLPVL 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  93 TMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVD-YVRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTEEQYRFLYHT 171
Cdd:cd17668   132 TFVRKASYAKRHAVGPVVVHCSAGVGRTGTYIVLDsMLQQIQHEGTV----NIFGFLKHIRSQRNYLVQTEEQYVFIHDA 207


                  .
gi 1958801472 172 V 172
Cdd:cd17668   208 L 208
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 16-169 2.21e-26

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: 103.70  E-value: 2.21e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  16 TRKCERYW-AQEREPLQAGPFCITLTKETALTADITLRTLQVTFQKVPKgqkESRPVHQLQYMSWPDHGVPSSSDHILTM 94
Cdd:cd17658    56 TAKCADYFpAEENESREFGRISVTNKKLKHSQHSITLRVLEVQYIESEE---PPLSVLHIQYPEWPDHGVPKDTRSVREL 132

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801472  95 VeeaRCLQGLGP--GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPnFSLFEVVLEMRKQRPAAVQTEEQYRFLY 169
Cdd:cd17658   133 L---KRLYGIPPsaGPIVVHCSAGIGRTGAYCTIHNTIRRILEGDMSA-VDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 18-168 4.62e-26

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: 103.74  E-value: 4.62e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWAQErEPLQAGPFCITLTKETALTaDITLRTLQVTFQKvpkgQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEE 97
Cdd:cd14615    80 KCEEYWPSK-QKKDYGDITVTMTSEIVLP-EWTIRDFTVKNAQ----TNESRTVRHFHFTSWPDHGVPETTDLLINFRHL 153

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958801472  98 AR--CLQGLGPGPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTEEQYRFL 168
Cdd:cd14615   154 VReyMKQNPPNSPILVHCSAGVGRTGTFIAIDRlIYQIENENVV----DVYGIVYDLRMHRPLMVQTEDQYVFL 223
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 18-172 1.31e-25

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: 102.66  E-value: 1.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWAQEREPLQAGPFCITLTKETALTaDITLRTLQVTFQKvpkgqkESRPVHQLQYMSWPDHGVPS--SSDHILTMV 95
Cdd:cd14614    96 KCDHYWPFTEEPVAYGDITVEMLSEEEQP-DWAIREFRVSYAD------EVQDVMHFNYTAWPDHGVPTanAAESILQFV 168

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801472  96 EEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTV 172
Cdd:cd14614   169 QMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEF---VDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 242
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 17-174 2.68e-25

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: 102.81  E-value: 2.68e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  17 RKCERYWAQEREPlQAGPFCITLtKETALTADITLRTLQVTFQKV-------PKGQKESRPVHQLQYMSWPDHGVPSSSD 89
Cdd:cd17667   112 RKCDQYWPTENSE-EYGNIIVTL-KSTKIHACYTVRRFSIRNTKVkkgqkgnPKGRQNERTVIQYHYTQWPDMGVPEYAL 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  90 HILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTEEQYRFLY 169
Cdd:cd17667   190 PVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKS---TVNVLGFLKHIRTQRNYLVQTEEQYIFIH 266


                  ....*
gi 1958801472 170 HTVAQ 174
Cdd:cd17667   267 DALLE 271
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 12-169 3.99e-25

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: 101.17  E-value: 3.99e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  12 GMPDTRK-CERYWAQEREPLQAGPFCITLTKETAlTADITLRTlqvtFQKVPKGQKESRPVHQLQYMSWPDHGVPSSSDH 90
Cdd:cd14618    74 GMENGRVlCDHYWPSESTPVSYGHITVHLLAQSS-EDEWTRRE----FKLWHEDLRKERRVKHLHYTAWPDHGIPESTSS 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  91 ILTMVEEAR--CLQGLGPGPLCVHCSAGCGRTGVLCAVD-YVRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTEEQYRF 167
Cdd:cd14618   149 LMAFRELVRehVQATKGKGPTLVHCSAGVGRSGTFIALDrLLRQLKEEKVV----DVFNTVYILRMHRYLMIQTLSQYIF 224


                  ..
gi 1958801472 168 LY 169
Cdd:cd14618   225 LH 226
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 18-172 5.53e-25

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: 99.99  E-value: 5.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWAQEREPLqaGPFCITLTkETALTADITLRTLqvTFQKvpKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEE 97
Cdd:cd14555    55 KCSRYWPDDTEVY--GDIKVTLV-ETEPLAEYVVRTF--ALER--RGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRR 127

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958801472  98 ARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTV 172
Cdd:cd14555   128 VKASNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGV---VDIYNCVKELRSRRVNMVQTEEQYIFIHDAI 199
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 18-168 5.78e-25

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: 101.85  E-value: 5.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWAQEREPLQAGPFCITLTKETALTADITlRTLQVTfqKVPKGQKesRPVHQLQYMSWPDHGVPSSSDHILTMVEE 97
Cdd:cd14600   123 KCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVF-REMLLT--NTQTGEE--RTVTHLQYVAWPDHGVPDDSSDFLEFVNY 197

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958801472  98 ARCLQgLGPGPLCVHCSAGCGRTGVLCAVDYVrqLLLTQTIPPNFSLfEVVLEMRKQRPAAVQTEEQYRFL 168
Cdd:cd14600   198 VRSKR-VENEPVLVHCSAGIGRTGVLVTMETA--MCLTERNQPVYPL-DIVRKMRDQRAMMVQTSSQYKFV 264
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 18-174 1.08e-24

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: 101.26  E-value: 1.08e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWAQEREplQAGPFCITLTKETALTADI----TLRTLQVTFQKVpkgqKESRPVHQLQYMSWPDHGVPSSSDHILT 93
Cdd:cd14608   105 KCAQYWPQKEE--KEMIFEDTNLKLTLISEDIksyyTVRQLELENLTT----QETREILHFHYTTWPDFGVPESPASFLN 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  94 MVEEARCLQGLGP--GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHT 171
Cdd:cd14608   179 FLFKVRESGSLSPehGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLA 258


                  ...
gi 1958801472 172 VAQ 174
Cdd:cd14608   259 VIE 261
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 14-169 1.66e-24

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: 98.63  E-value: 1.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  14 PDTRKCERYWAQErEPLQAGPFCITLTKETaLTADITLRTLQVtfQKVPKGQKESRPVHQLQYMSWPDHG-VPSSSDHIL 92
Cdd:cd14556    50 PKDQSCPQYWPDE-GSGTYGPIQVEFVSTT-IDEDVISRIFRL--QNTTRPQEGYRMVQQFQFLGWPRDRdTPPSKRALL 125

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801472  93 TMVEEA-RCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLY 169
Cdd:cd14556   126 KLLSEVeKWQEQSGEGPIVVHCLNGVGRSGVFCAISSVCERIKVENV---VDVFQAVKTLRNHRPNMVETEEQYKFCY 200
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 18-171 2.41e-24

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: 99.14  E-value: 2.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWAQEREpLQAGPFCITLTKETALTADItLRTLQVTFQKvpkgQKESRPVHQLQYMSWPDHGVPSSSDHIL---TM 94
Cdd:cd14554    90 KCHQYWPAERS-ARYQYFVVDPMAEYNMPQYI-LREFKVTDAR----DGQSRTVRQFQFTDWPEQGVPKSGEGFIdfiGQ 163

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801472  95 VEEARCLQGlGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHT 171
Cdd:cd14554   164 VHKTKEQFG-QEGPITVHCSAGVGRTGVFITLSIVLERMRYEGV---VDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 18-169 2.34e-23

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: 95.66  E-value: 2.34e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYW-AQEREPLQAGPFCITLTKETaLTADITLRTLQVTFQKVPKGQKEsrpVHQLQYMSWPDHGVPSSSDHILTMVE 96
Cdd:cd14557    55 KCAQYWpSMEEGSRAFGDVVVKINEEK-ICPDYIIRKLNINNKKEKGSGRE---VTHIQFTSWPDHGVPEDPHLLLKLRR 130

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958801472  97 EARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTEEQYRFLY 169
Cdd:cd14557   131 RVNAFNNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEG---RVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 18-172 2.50e-23

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: 96.44  E-value: 2.50e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWAQE-------REPLQagpfcITLTKETALTADItLRTLQVtfQKVPKGqkESRPVHQLQYMSWPDHGVPSSSDH 90
Cdd:cd14597    84 KCQRYWPEIlgkttmvDNRLQ-----LTLVRMQQLKNFV-IRVLEL--EDIQTR--EVRHITHLNFTAWPDHDTPSQPEQ 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  91 ILTMVEEARCLQGLgpGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTEEQYRFLYH 170
Cdd:cd14597   154 LLTFISYMRHIHKS--GPIITHCSAGIGRSGTLICIDVVLGLISKDL---DFDISDIVRTMRLQRHGMVQTEDQYIFCYQ 228


                  ..
gi 1958801472 171 TV 172
Cdd:cd14597   229 VI 230
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 18-174 2.79e-23

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: 97.41  E-value: 2.79e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWAQeREPLQAGPFCITLTKETALtADITLRTlqvtFQKVPKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEE 97
Cdd:cd14626   125 KCDQYWPI-RGTETYGMIQVTLLDTVEL-ATYSVRT----FALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRR 198

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801472  98 ARCLQGLGPGPLCVHCSAGCGRTGVLCAVD-YVRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 174
Cdd:cd14626   199 VKACNPPDAGPMVVHCSAGVGRTGCFIVIDaMLERMKHEKTV----DIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 19-169 4.04e-23

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: 95.15  E-value: 4.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  19 CERYWAQEREPLqaGPFCITLtKETALTADITLRTLQVTFQKvpkgQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEA 98
Cdd:cd14558    56 CAQYWGDEKKTY--GDIEVEL-KDTEKSPTYTVRVFEITHLK----RKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSI 128

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801472  99 RCLQGLGPG------PLCVHCSAGCGRTGVLCAVdyvRQLLLTQTIPPNFSLFEVVLEMRKQRPAAVQTEEQYRFLY 169
Cdd:cd14558   129 KQKLPYKNSkhgrsvPIVVHCSDGSSRTGIFCAL---WNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
12-168 4.14e-23

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 96.70  E-value: 4.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  12 GMPDTRKCERYWAQEReplQAGPFCI--TLTKETALTADITLRTLQVTFQKvpKGQKeSRPVHQLQYMSWPDHGVPSSS- 88
Cdd:COG5599   114 ISKPKVKMPVYFRQDG---EYGKYEVssELTESIQLRDGIEARTYVLTIKG--TGQK-KIEIPVLHVKNWPDHGAISAEa 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  89 --DHILTMVEEARCLQGLGpGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIpPNFSLFEVVLEMRKQR-PAAVQTEEQY 165
Cdd:COG5599   188 lkNLADLIDKKEKIKDPDK-LLPVVHCRAGVGRTGTLIACLALSKSINALVQ-ITLSVEEIVIDMRTSRnGGMVQTSEQL 265


                  ...
gi 1958801472 166 RFL 168
Cdd:COG5599   266 DVL 268
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 15-172 5.82e-23

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: 95.80  E-value: 5.82e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  15 DTRKCERYW-AQEREPL--QAGPFCITLTKETaLTADITLRTLQVtfQKVPKGqkESRPVHQLQYMSWPDHGVPSSSDHI 91
Cdd:cd14607   101 DSVKCAQYWpTDEEEVLsfKETGFSVKLLSED-VKSYYTVHLLQL--ENINSG--ETRTISHFHYTTWPDFGVPESPASF 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  92 LTM---VEEARCLqGLGPGPLCVHCSAGCGRTGVLCAVDYVrQLLLTQTIPPNFSLFEVVLEMRKQRPAAVQTEEQYRFL 168
Cdd:cd14607   176 LNFlfkVRESGSL-SPEHGPAVVHCSAGIGRSGTFSLVDTC-LVLMEKKDPDSVDIKQVLLDMRKYRMGLIQTPDQLRFS 253


                  ....
gi 1958801472 169 YHTV 172
Cdd:cd14607   254 YMAV 257
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 18-174 6.49e-23

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: 95.67  E-value: 6.49e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWAQEREPLqaGPFCITLtKETALTADITLRTLQVtfqkvpKGQKESRPVHQLQYMSWPDHGVPSSSD---HILTM 94
Cdd:cd14612   100 KCVHYWPEKEGTY--GRFEIRV-QDMKECDGYTIRDLTI------QLEEESRSVKHYWFSSWPDHQTPESAGpllRLVAE 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  95 VEEARCLQGlGPGPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVA 173
Cdd:cd14612   171 VEESRQTAA-SPGPIVVHCSAGIGRTGCFIATSIgCQQLKDTGKV----DILGIVCQLRLDRGGMIQTSEQYQFLHHTLA 245


                  .
gi 1958801472 174 Q 174
Cdd:cd14612   246 L 246
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 17-169 6.68e-23

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: 94.37  E-value: 6.68e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  17 RKCERYWAQER-EPLQAGPFCITLTKETALTADITlRTLQVTFqkvpKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMV 95
Cdd:cd14539    55 QKVHRYWPTERgQALVYGAITVSLQSVRTTPTHVE-RIISIQH----KDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFI 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  96 EEA-------RCLQglgpGPLCVHCSAGCGRTGVLCAV-DYVRQLLLTQTIPpnfSLFEVVLEMRKQRPAAVQTEEQYRF 167
Cdd:cd14539   130 EEVhshylqqRSLQ----TPIVVHCSSGVGRTGAFCLLyAAVQEIEAGNGIP---DLPQLVRKMRQQRKYMLQEKEHLKF 202


                  ..
gi 1958801472 168 LY 169
Cdd:cd14539   203 CY 204
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 18-169 2.13e-22

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: 93.83  E-value: 2.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWAQEREPLQAGPFCITLTKETALtADITLRTLQVTFQKvpkgQKES-RPVHQLQYMSWPDHGVPSSSDHILTMVE 96
Cdd:cd14617    81 KCDHYWPADQDSLYYGDLIVQMLSESVL-PEWTIREFKICSEE----QLDApRLVRHFHYTVWPDHGVPETTQSLIQFVR 155

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958801472  97 EARCL--QGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTEEQYRFLY 169
Cdd:cd14617   156 TVRDYinRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKD---SVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 17-169 3.23e-22

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: 92.67  E-value: 3.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  17 RKCERYWAQEREpLQAGPFCITLtKETALTADITLRTLQVTFQKVPKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMVE 96
Cdd:cd14551    54 KKCSQYWPDQGC-WTYGNLRVRV-EDTVVLVDYTTRKFCIQKVNRGIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLK 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958801472  97 EARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTEEQYRFLY 169
Cdd:cd14551   132 KVKSANPPRAGPIVVHCSAGVGRTGTFIVIDAMLDMMHAEG---KVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 18-174 3.79e-22

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: 93.19  E-value: 3.79e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWAQEREpLQAGPFCITLTKETAlTADITLRTLQVTFQKvpkgQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEE 97
Cdd:cd14623    80 KCAQYWPSDGS-VSYGDITIELKKEEE-CESYTVRDLLVTNTR----ENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAA 153

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801472  98 A-RCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 174
Cdd:cd14623   154 VqKQQQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGI---LDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 18-172 5.75e-22

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: 92.70  E-value: 5.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWaqerePLQA----GPFCITLTKETALTaDITLRTLQVTFQkVPKGQKESRPVHQLQYMSWPDHGVPSSSDHILT 93
Cdd:cd14620    79 KCYQYW-----PDQGcwtyGNIRVAVEDCVVLV-DYTIRKFCIQPQ-LPDGCKAPRLVTQLHFTSWPDFGVPFTPIGMLK 151

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958801472  94 MVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTV 172
Cdd:cd14620   152 FLKKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQ---KVDVFEFVSRIRNQRPQMVQTDMQYSFIYQAL 227
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 15-174 8.19e-22

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: 91.74  E-value: 8.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  15 DTRKCERYWAQEREPLQaGPFCITLTKETALTADITLRTLqvtFQKVPKGQkESRPVHQLQYMSWPDHGVPSSSDHILTM 94
Cdd:cd14546    53 GVKQCARYWPEEGSEVY-HIYEVHLVSEHIWCDDYLVRSF---YLKNLQTS-ETRTVTQFHFLSWPDEGIPASAKPLLEF 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  95 VEEA-RCLQGLGpGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTipPNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVA 173
Cdd:cd14546   128 RRKVnKSYRGRS-CPIVVHCSDGAGRTGTYILIDMVLNRMAKGA--KEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVA 204


                  .
gi 1958801472 174 Q 174
Cdd:cd14546   205 E 205
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 18-172 1.91e-21

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: 90.45  E-value: 1.91e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWAQEREpLQAGPFCITLTKETALTAdITLRTLQVTFQKvpkgQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEE 97
Cdd:cd14622    56 KCVQYWPSEGS-VTHGEITIEIKNDTLLET-ISIRDFLVTYNQ----EKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAA 129

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801472  98 A-RCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTV 172
Cdd:cd14622   130 VqKQQQQTGNHPIVVHCSAGAGRTGTFIALSNILERVKAEGL---LDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 18-174 2.77e-21

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: 91.64  E-value: 2.77e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWAQEREPLQagPFCITLTkETALTADITLRTLQVTfqkvPKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEE 97
Cdd:cd14633   124 KCCKYWPDDTEIYK--DIKVTLI-ETELLAEYVIRTFAVE----KRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQ 196

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801472  98 ARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 174
Cdd:cd14633   197 VKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGV---VDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 18-174 6.82e-21

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: 89.31  E-value: 6.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWAQEREPLqaGPFCITLTkETALTADITLRTLqvTFQKvpKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEE 97
Cdd:cd14631    69 KCYKYWPDDTEVY--GDFKVTCV-EMEPLAEYVVRTF--TLER--RGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRR 141

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801472  98 ARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 174
Cdd:cd14631   142 VKLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGV---VDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 18-169 1.39e-20

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: 90.18  E-value: 1.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWAQEREPlQAGPFCITLTKETALTADItLRTLQVTFQKvpKGQkeSRPVHQLQYMSWPDHGVPSSSDHILTMVEE 97
Cdd:cd14628   136 KCHQYWPAERSA-RYQYFVVDPMAEYNMPQYI-LREFKVTDAR--DGQ--SRTVRQFQFTDWPEQGVPKSGEGFIDFIGQ 209

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958801472  98 A-RCLQGLGP-GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLY 169
Cdd:cd14628   210 VhKTKEQFGQdGPISVHCSAGVGRTGVFITLSIVLERMRYEGV---VDIFQTVKMLRTQRPAMVQTEDQYQFCY 280
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 18-174 1.56e-20

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: 88.18  E-value: 1.56e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWAQEREplQAGPFCITLTKETALtADITLRTLqvTFQKvpKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEE 97
Cdd:cd14632    55 KCSKYWPDDSD--TYGDIKITLLKTETL-AEYSVRTF--ALER--RGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRR 127

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801472  98 ARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 174
Cdd:cd14632   128 VKASTPPDAGPVVVHCSAGAGRTGCYIVLDVMLDMAECEGV---VDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 18-174 3.85e-20

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: 89.02  E-value: 3.85e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWAQEREPlQAGPFCITLTKETALTADItLRTLQVTFQKvpkgQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEE 97
Cdd:cd14627   137 KCHQYWPAERSA-RYQYFVVDPMAEYNMPQYI-LREFKVTDAR----DGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQ 210

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958801472  98 A-RCLQGLGP-GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 174
Cdd:cd14627   211 VhKTKEQFGQdGPISVHCSAGVGRTGVFITLSIVLERMRYEGV---VDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALE 286
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 18-169 8.24e-20

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: 86.50  E-value: 8.24e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWAQEREPLQA-GPFCIT-LTKETALtaDITLRTLQVtfqkvpKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMV 95
Cdd:cd14616    81 RCHQYWPEDNKPVTVfGDIVITkLMEDVQI--DWTIRDLKI------ERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFV 152

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801472  96 EEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYvrqllLTQTIPPN--FSLFEVVLEMRKQRPAAVQTEEQYRFLY 169
Cdd:cd14616   153 KLVRASRAHDNTPMIVHCSAGVGRTGVFIALDH-----LTQHINDHdfVDIYGLVAELRSERMCMVQNLAQYIFLH 223
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 15-184 5.63e-19

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 86.24  E-value: 5.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  15 DTRKCERYWAQERE-PLQAGPFcITLTKETALTADITLRTLQVTfqkvPKGQKESRPVHQLQYMSWPDHGVPSSSDHILT 93
Cdd:PHA02746  150 DDEKCFELWTKEEDsELAFGRF-VAKILDIIEELSFTKTRLMIT----DKISDTSREIHHFWFPDWPDNGIPTGMAEFLE 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  94 MV-----EEARCL-----QGLGPGPLCVHCSAGCGRTGVLCAVD-YVRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTE 162
Cdd:PHA02746  225 LInkvneEQAELIkqadnDPQTLGPIVVHCSAGIGRAGTFCAIDnALEQLEKEKEV----CLGEIVLKIRKQRHSSVFLP 300

                         170       180
                  ....*....|....*....|..
gi 1958801472 163 EQYRFLYHTVAQLFSRTLQNNS 184
Cdd:PHA02746  301 EQYAFCYKALKYAIIEEAKKKF 322
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 18-169 5.87e-19

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: 85.55  E-value: 5.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWAQEREPlQAGPFCITLTKETALTADItLRTLQVTFQKvpkgQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEE 97
Cdd:cd14629   137 KCHQYWPAERSA-RYQYFVVDPMAEYNMPQYI-LREFKVTDAR----DGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQ 210

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958801472  98 A-RCLQGLGP-GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLY 169
Cdd:cd14629   211 VhKTKEQFGQdGPITVHCSAGVGRTGVFITLSIVLERMRYEGV---VDMFQTVKTLRTQRPAMVQTEDQYQLCY 281
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 18-174 9.75e-19

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: 84.78  E-value: 9.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWAQeREPLQAGPFCITLTkETALTADITLRTlqvtFQKVPKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEE 97
Cdd:cd14624   131 KCDQYWPS-RGTETYGLIQVTLL-DTVELATYCVRT----FALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRR 204

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801472  98 ARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 174
Cdd:cd14624   205 VKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEK---TVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 18-174 2.52e-18

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: 83.60  E-value: 2.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWAQeREPLQAGPFCITLTkETALTADITLRTlqvtFQKVPKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEE 97
Cdd:cd14625   131 KCDQYWPS-RGTETYGMIQVTLL-DTIELATFCVRT----FSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRR 204

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801472  98 ARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 174
Cdd:cd14625   205 VKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEK---TVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 18-170 8.81e-18

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: 81.12  E-value: 8.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWAQEREPLQAGPFCITLTKETAltaDITLRTLQVtfqkvpKGQKESRPVHQLQYMSWPDHGVPSSSDHILTM--- 94
Cdd:cd14611    84 KCVLYWPEKRGIYGKVEVLVNSVKECD---NYTIRNLTL------KQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLmld 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801472  95 VEEARcLQGLGPGPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTEEQYRFLYH 170
Cdd:cd14611   155 VEEDR-LASPGRGPVVVHCSAGIGRTGCFIATTIgCQQLKEEGVV----DVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1-185 7.84e-17

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 79.66  E-value: 7.84e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472   1 MLHPTiswqqPGMPDTRKCERYWA-QEREPLQAGPFCITlTKETALTADITLRTLQVTfqkvPKGQKESRPVHQLQYMSW 79
Cdd:PHA02747  123 MLTPT-----KGTNGEEKCYQYWClNEDGNIDMEDFRIE-TLKTSVRAKYILTLIEIT----DKILKDSRKISHFQCSEW 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  80 PDHGVPSssDHI-----LTMVEEARCLQG--LGP-----GPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIppnfSLFE 146
Cdd:PHA02747  193 FEDETPS--DHPdfikfIKIIDINRKKSGklFNPkdallCPIVVHCSDGVGKTGIFCAVDIcLNQLVKRKAI----CLAK 266

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958801472 147 VVLEMRKQRPAAVQTEEQYRFL---YHTVAQLFSRTLQNNSP 185
Cdd:PHA02747  267 TAEKIREQRHAGIMNFDDYLFIqpgYEVLHYFLSKIKAIDKI 308
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 18-173 1.35e-16

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: 78.37  E-value: 1.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWAQERepLQAGPFCITLTKETAlTADITLRTLQVtfqkvpKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMV-- 95
Cdd:cd14613   110 KCTEYWPEEQ--VTYEGIEITVKQVIH-ADDYRLRLITL------KSGGEERGLKHYWYTSWPDQKTPDNAPPLLQLVqe 180

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958801472  96 -EEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVA 173
Cdd:cd14613   181 vEEARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGV---VDILRTTCQLRLDRGGMIQTCEQYQFVHHVLS 256
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 17-174 4.97e-16

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: 77.00  E-value: 4.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  17 RKCERYWAQEREPLQaGPFCITLTKETALTADITLRTLqvtFQKVPKGQkESRPVHQLQYMSWPDHGVPSSSDHILTMVE 96
Cdd:cd14609   126 KQCDRYWPDEGSSLY-HIYEVNLVSEHIWCEDFLVRSF---YLKNVQTQ-ETRTLTQFHFLSWPAEGIPSSTRPLLDFRR 200

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958801472  97 EA-RCLQGLGpGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTipPNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 174
Cdd:cd14609   201 KVnKCYRGRS-CPIIVHCSDGAGRTGTYILIDMVLNRMAKGV--KEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAE 276
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 17-174 8.56e-16

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: 76.25  E-value: 8.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  17 RKCERYWAQEREPLQAgPFCITLTKETALTADITLRTLQVTFQKVpkgqKESRPVHQLQYMSWPDHGVPSSSDHILTMVE 96
Cdd:cd14610   128 KQCYHYWPDEGSNLYH-IYEVNLVSEHIWCEDFLVRSFYLKNLQT----NETRTVTQFHFLSWNDQGVPASTRSLLDFRR 202

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958801472  97 EA-RCLQGLGpGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTipPNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 174
Cdd:cd14610   203 KVnKCYRGRS-CPIIVHCSDGAGRSGTYILIDMVLNKMAKGA--KEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 278
PHA02738 PHA02738
hypothetical protein; Provisional
 17-172 1.37e-15

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 76.12  E-value: 1.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  17 RKCERYWAQ-EREPLQAGPFCITLTKETALTADITlRTLQVTfqkvpKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMV 95
Cdd:PHA02738  130 EKCFPYWSDvEQGSIRFGKFKITTTQVETHPHYVK-STLLLT-----DGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFV 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  96 EEARCLQ-------------GLGPGPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQT 161
Cdd:PHA02738  204 LEVRQCQkelaqeslqighnRLQPPPIVVHCNAGLGRTPCYCVVDIsISRFDACATV----SIPSIVSSIRNQRYYSLFI 279

                         170
                  ....*....|.
gi 1958801472 162 EEQYRFLYHTV 172
Cdd:PHA02738  280 PFQYFFCYRAV 290
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 18-174 1.61e-15

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: 75.83  E-value: 1.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYWaqerePLQAgpfCITL------TKETALTADITLRTLQVTFQKVPKGQKESRPVHQLQYMSWPDHGVPSSSDHI 91
Cdd:cd14621   136 KCAQYW-----PDQG---CWTYgnirvsVEDVTVLVDYTVRKFCIQQVGDVTNKKPQRLITQFHFTSWPDFGVPFTPIGM 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  92 LTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHT 171
Cdd:cd14621   208 LKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAER---KVDVYGFVSRIRAQRCQMVQTDMQYVFIYQA 284


                  ...
gi 1958801472 172 VAQ 174
Cdd:cd14621   285 LLE 287
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 89-170 7.52e-15

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


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 69.69  E-value: 7.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  89 DHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLlltqtippNFSLFEVVLEMRKQRPA-AVQTEEQYRF 167
Cdd:cd14494    39 LAMVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLG--------GMSAEEAVRIVRLIRPGgIPQTIEQLDF 110


                  ...
gi 1958801472 168 LYH 170
Cdd:cd14494   111 LIK 113
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 16-169 8.14e-15

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


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 72.37  E-value: 8.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  16 TRKCERYWAQEREpLQAGPF---CITltkeTALTADITLRTLQVTfqKVPKGQKESRPVHQLQYMSWPDH-GVPSSSDHI 91
Cdd:cd14636    51 AQGCPQYWPEEGM-LRYGPIqveCMS----CSMDCDVISRIFRIC--NLTRPQEGYLMVQQFQYLGWASHrEVPGSKRSF 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  92 LTMVEEARCLQ---GLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFL 168
Cdd:cd14636   124 LKLILQVEKWQeecDEGEGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNV---VDVFHAVKTLRNSKPNMVETPEQYRFC 200


                  .
gi 1958801472 169 Y 169
Cdd:cd14636   201 Y 201
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 13-169 4.71e-14

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: 70.05  E-value: 4.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  13 MPDTRKCERYWAqEREPLQAGPFCITLtketaLTADITLRTLQVTFQ--KVPKGQKESRPVHQLQYMSWPDH-GVPSSSD 89
Cdd:cd14634    48 MDAAQLCMQYWP-EKTSCCYGPIQVEF-----VSADIDEDIISRIFRicNMARPQDGYRIVQHLQYIGWPAYrDTPPSKR 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  90 HILTMVEEARCLQGL---GPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYR 166
Cdd:cd14634   122 SILKVVRRLEKWQEQydgREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNI---IDVFHTVKTLRNNKSNMVETLEQYK 198


                  ...
gi 1958801472 167 FLY 169
Cdd:cd14634   199 FVY 201
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 18-176 6.64e-14

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: 70.00  E-value: 6.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  18 KCERYW---AQEREPLQAGPFCITLTKETAltaDITLRTLQVTFQKVPKGQKesRPVHQLQYMSWPDHGVPSSSDHILTM 94
Cdd:cd14598    57 KSFRYWprlGSRHNTVTYGRFKITTRFRTD---SGCYATTGLKIKHLLTGQE--RTVWHLQYTDWPEHGCPEDLKGFLSY 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  95 VEEARCL----------QGLGPgPLCVHCSAGCGRTGVLcavdyVRQLLLTQTIPPNFSL-FEVVLEM-RKQRPAAVQTE 162
Cdd:cd14598   132 LEEIQSVrrhtnstidpKSPNP-PVLVHCSAGVGRTGVV-----ILSEIMIACLEHNEMLdIPRVLDMlRQQRMMMVQTL 205

                         170
                  ....*....|....
gi 1958801472 163 EQYRFLYHTVAQLF 176
Cdd:cd14598   206 SQYTFVYKVLIQFL 219
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 67-176 2.92e-13

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: 69.26  E-value: 2.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  67 ESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQ-----------GLGPgPLCVHCSAGCGRTGVLCAVDYVRQLLLT 135
Cdd:cd14599   170 QERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRrhtnsmldstkNCNP-PIVVHCSAGVGRTGVVILTELMIGCLEH 248

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958801472 136 QTippNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQLF 176
Cdd:cd14599   249 NE---KVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFL 286
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 13-174 3.76e-12

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 66.18  E-value: 3.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  13 MPDTR-KCERYW-AQEREPLQAGPFCITlTKETALTADITLRTLQVTfqkvPKGQKESRPVHQLQYMSWPDHGVPSSSDH 90
Cdd:PHA02742  128 MEDGKeACYPYWmPHERGKATHGEFKIK-TKKIKSFRNYAVTNLCLT----DTNTGASLDIKHFAYEDWPHGGLPRDPNK 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  91 ILTMVEEARCLQG-----------LGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPnfsLFEVVLEMRKQRPAAV 159
Cdd:PHA02742  203 FLDFVLAVREADLkadvdikgeniVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIP---LLSIVRDLRKQRHNCL 279

                         170
                  ....*....|....*
gi 1958801472 160 QTEEQYRFLYHTVAQ 174
Cdd:PHA02742  280 SLPQQYIFCYFIVLI 294
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 19-169 1.47e-11

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


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 63.00  E-value: 1.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  19 CERYWAqerEP--LQAGPFCITLTKETAlTADITLRTLQVtfQKVPKGQKESRPVHQLQYMSW-PDHGVPSSSD---HIL 92
Cdd:cd14637    57 CLQYWP---EPglQQYGPMEVEFVSGSA-DEDIVTRLFRV--QNITRLQEGHLMVRHFQFLRWsAYRDTPDSKKaflHLL 130

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958801472  93 TMVE--EARClqglGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLY 169
Cdd:cd14637   131 ASVEkwQRES----GEGRTVVHCLNGGGRSGTYCASAMILEMIRCHNI---VDVFYAVKTLRNYKPNMVETLEQYRFCY 202
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 19-174 1.14e-10

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


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 60.47  E-value: 1.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  19 CERYWAqEREPLQAGPFCITLTkETALTADITLRTLQVTFQKVPkgQKESRPVHQLQYMSWPDH-GVPSSSDHILTMVEE 97
Cdd:cd14635    54 CPQYWP-ENGVHRHGPIQVEFV-SADLEEDIISRIFRIYNAARP--QDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQ 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  98 ARCLQ---GLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 174
Cdd:cd14635   130 VDKWQeeyNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQR---AVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 78-168 8.49e-10

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


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 57.74  E-value: 8.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  78 SWPDHGVPSSsDHILTMVE-EARCLQGlgPGPLCVHCSAGCGRTGVLCAVdyvrQLLLTQTIPPNfslfEVVLEMRKQRP 156
Cdd:cd14506    83 GWKDYGVPSL-TTILDIVKvMAFALQE--GGKVAVHCHAGLGRTGVLIAC----YLVYALRMSAD----QAIRLVRSKRP 151

                          90
                  ....*....|..
gi 1958801472 157 AAVQTEEQYRFL 168
Cdd:cd14506   152 NSIQTRGQVLCV 163
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
79-170 3.70e-09

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 54.59  E-value: 3.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  79 WPDHGVPSSsDHILTMVEEARCLQGLGpGPLCVHCSAGCGRTGVLCAvdyvrQLLLTQTIPPNfslfEVVLEMRKQRPAA 158
Cdd:COG2453    55 IPDFGAPDD-EQLQEAVDFIDEALREG-KKVLVHCRGGIGRTGTVAA-----AYLVLLGLSAE----EALARVRAARPGA 123

                          90
                  ....*....|..
gi 1958801472 159 VQTEEQYRFLYH 170
Cdd:COG2453   124 VETPAQRAFLER 135
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 79-168 8.11e-08

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


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 52.40  E-value: 8.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  79 WPDHGVPSS------SDHI-------LTMVEEARCLQGLGPGPL--CVHCSAGCGRTGVLCAVDYVRQllltqtiPPN-F 142
Cdd:cd14559   126 WPDHTAISSeglkelADLVnksaeekRNFYKSKGSSAINDKNKLlpVIHCRAGVGRTGQLAAAMELNK-------SPNnL 198

                          90       100
                  ....*....|....*....|....*..
gi 1958801472 143 SLFEVVLEMRKQRPA-AVQTEEQYRFL 168
Cdd:cd14559   199 SVEDIVSDMRTSRNGkMVQKDEQLDTL 225
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 73-169 1.46e-07

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 50.34  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  73 QLQYMSW-----PDHGVPSSSDHILTMVEEAR-CLQGlGPGPLcVHCSAGCGRTGVLCAvdyVRQLLLTQTIPPNfslfE 146
Cdd:cd14505    69 QQAGITWhhlpiPDGGVPSDIAQWQELLEELLsALEN-GKKVL-IHCKGGLGRTGLIAA---CLLLELGDTLDPE----Q 139

                          90       100
                  ....*....|....*....|...
gi 1958801472 147 VVLEMRKQRPAAVQTEEQYRFLY 169
Cdd:cd14505   140 AIAAVRALRPGAIQTPKQENFLH 162
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 71-168 5.97e-07

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


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 48.04  E-value: 5.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  71 VHQLQY--MSWPDHGVPSSS--DHILTMVEEARCLqglgPGPLCVHCSAGCGRTGVLCAVdYvrqLLLTQTIPPNfslfE 146
Cdd:cd14504    47 CPGLRYhhIPIEDYTPPTLEqiDEFLDIVEEANAK----NEAVLVHCLAGKGRTGTMLAC-Y---LVKTGKISAV----D 114

                          90       100
                  ....*....|....*....|..
gi 1958801472 147 VVLEMRKQRPAAVQTEEQYRFL 168
Cdd:cd14504   115 AINEIRRIRPGSIETSEQEKFV 136
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 22-169 1.43e-06

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


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 48.14  E-value: 1.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  22 YWAQEREPLQAGPFCITL---------TKETALTADITLRTLQVTFqkvpkgqkeSRPVHQLQYMSWPDHGVPSSSDHIL 92
Cdd:cd17670    58 YWPSREESMNCEAFTVTLiskdrlclsNEEQIIIHDFILEATQDDY---------VLEVRHFQCPKWPNPDAPISSTFEL 128

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958801472  93 TMV--EEARCLQGlgpgPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLY 169
Cdd:cd17670   129 INVikEEALTRDG----PTIVHDEFGAVSAGTLCALTTLSQQLENENA---VDVYQVAKMINLMRPGVFTDIEQYQFLY 200
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 22-172 3.48e-04

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


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 41.13  E-value: 3.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  22 YWAQEREPLQAGPFCITL---------TKETALTADITLRTLQVTFqkvpkgqkeSRPVHQLQYMSWPDHGVP-SSSDHI 91
Cdd:cd17669    58 YWPNKDEPINCETFKVTLiaeehkclsNEEKLIIQDFILEATQDDY---------VLEVRHFQCPKWPNPDSPiSKTFEL 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  92 LTMVEEARCLQGlgpGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHT 171
Cdd:cd17669   129 ISIIKEEAANRD---GPMIVHDEHGGVTAGTFCALTTLMHQLEKEN---SVDVYQVAKMINLMRPGVFTDIEQYQFLYKA 202


                  .
gi 1958801472 172 V 172
Cdd:cd17669   203 I 203
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 80-123 1.64e-03

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


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 38.59  E-value: 1.64e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958801472  80 PDHGVPSssDHI----LTMVEEArclqglgPGPLCVHCSAGCGRTGVL 123
Cdd:cd14499    88 PDGSTPS--DDIvkkfLDICENE-------KGAIAVHCKAGLGRTGTL 126
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 72-125 4.45e-03

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


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 37.17  E-value: 4.45e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958801472  72 HQLQYMSWPDHGVPSSsDHILTMVEEARCLQGLGPGPLCV-HCSAGCGRTGVLCA 125
Cdd:cd14497    61 GRVLHYGFPDHHPPPL-GLLLEIVDDIDSWLSEDPNNVAVvHCKAGKGRTGTVIC 114
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 17-180 7.90e-03

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 37.64  E-value: 7.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  17 RKC-ERYWA-QEREPLQAGPFCITlTKETALTADITLRTLQVTFQKvpkGQkeSRPVHQLQYMSWPDHGVPSSSD----- 89
Cdd:PHA02740  128 KKCfNQFWSlKEGCVITSDKFQIE-TLEIIIKPHFNLTLLSLTDKF---GQ--AQKISHFQYTAWPADGFSHDPDafidf 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801472  90 --HILTMVEEARCLQGLGP-GPLCVHCSAGCGRTGVLCAVDyvrqLLLTQTIPPN-FSLFEVVLEMRKQRPAAVQTEEQY 165
Cdd:PHA02740  202 fcNIDDLCADLEKHKADGKiAPIIIDCIDGISSSAVFCVFD----ICATEFDKTGmLSIANALKKVRQKKYGCMNCLDDY 277

                         170
                  ....*....|....*
gi 1958801472 166 RFLYHTVAQLFSRTL 180
Cdd:PHA02740  278 VFCYHLIAAYLKEKF 292
Y_phosphatase3 pfam13350
Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 ...
 105-135 8.53e-03

Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 families.


Pssm-ID: 463853 [Multi-domain]  Cd Length: 243  Bit Score: 37.22  E-value: 8.53e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1958801472 105 GPGPLCVHCSAGCGRTGVLCAvdyvrqLLLT 135
Cdd:pfam13350 128 NDGPVLFHCTAGKDRTGVAAA------LLLS 152
 
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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