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Conserved domains on  [gi|41054756|ref|NP_956963|]
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tyrosine-protein phosphatase non-receptor type 12 [Danio rerio]

Protein Classification

PTPc-N12 domain-containing protein( domain architecture ID 12998673)

PTPc-N12 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 2-295 0e+00

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: 644.68  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756   2 EQGNILKKFIEELRSGEQT---GEDNFSSDFMRLRRLSTKYRTEKIYPTDVGEQEENVKKNRYKDILPFDHSRVKVTLKT 78
Cdd:cd14604   1 EQVEILKKFIERVQAMKSTdhnGEDNFASDFMRLRRLSTKYRTEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  79 SNQDTDYINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRKKCERYFPLFGDEPMTFGPFR 158
Cdd:cd14604  81 SSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPMTFGPFR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 159 ISCESEQPRTDYCVRTLTVEFDQECRRLTQFHYVNWPDHDVPSSFDSILDMIELMRKHQQRDTTPICVHCSAGCGRTGAI 238
Cdd:cd14604 161 ISCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAI 240

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41054756 239 CAIDYTWNLLKAGRISEDFNVFQLIQEMRTQRHSAVQTKEQYELVHRAIAQIFQKQL 295
Cdd:cd14604 241 CAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEKQL 297
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 314-566 1.30e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.31  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756   314 DSSPEKHTPNSDEEQWDTPPPKPPRLRSVQGEcavqeeiLQAPEPRPVPPILRPSPASALRTVSSARHSDTYHPKPLLSD 393
Cdd:PHA03247 2606 GDPRGPAPPSPLPPDTHAPDPPPPSPSPAANE-------PDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASS 2678

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756   394 PePSDPEPS---------THFTDPDHHSSDPEPSEPERRVERLAVEIQKVALQEGPR-PLHLLLQSPAHAPALSFT-NPL 462
Cdd:PHA03247 2679 P-PQRPRRRaarptvgslTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPAlPAAPAPPAVPAGPATPGGpARP 2757

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756   463 HTHTHSHTLPDTHPTAAGGTAEqqnQRRATHMSIAGHTLHTESSEEQPAGAADTAPLQAsgdttAAPRENDAEQKSTETP 542
Cdd:PHA03247 2758 ARPPTTAGPPAPAPPAAPAAGP---PRRLTRPAVASLSESRESLPSPWDPADPPAAVLA-----PAAALPPAASPAGPLP 2829

                         250       260
                  ....*....|....*....|....
gi 41054756   543 VSGTKAEIGfgrrCSPPRGPREPP 566
Cdd:PHA03247 2830 PPTSAQPTA----PPPPPGPPPPS 2849
 
Name Accession Description Interval E-value
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 2-295 0e+00

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: 644.68  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756   2 EQGNILKKFIEELRSGEQT---GEDNFSSDFMRLRRLSTKYRTEKIYPTDVGEQEENVKKNRYKDILPFDHSRVKVTLKT 78
Cdd:cd14604   1 EQVEILKKFIERVQAMKSTdhnGEDNFASDFMRLRRLSTKYRTEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  79 SNQDTDYINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRKKCERYFPLFGDEPMTFGPFR 158
Cdd:cd14604  81 SSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPMTFGPFR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 159 ISCESEQPRTDYCVRTLTVEFDQECRRLTQFHYVNWPDHDVPSSFDSILDMIELMRKHQQRDTTPICVHCSAGCGRTGAI 238
Cdd:cd14604 161 ISCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAI 240

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41054756 239 CAIDYTWNLLKAGRISEDFNVFQLIQEMRTQRHSAVQTKEQYELVHRAIAQIFQKQL 295
Cdd:cd14604 241 CAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEKQL 297
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
25-289 3.22e-120

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 355.43  E-value: 3.22e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756     25 FSSDFMRLRRLSTKYRtekiyPTDVGEQEENVKKNRYKDILPFDHSRVKVTLKTSNqDTDYINANFIKGIDGPQAYIATQ 104
Cdd:smart00194   2 LEEEFEKLDRLKPDDE-----SCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE-GSDYINASYIDGPNGPKAYIATQ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756    105 GPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRKKCERYFPLFGDEPMTFGPFRISCESEQPRTDYCVRTLTVEFDQ--E 182
Cdd:smart00194  76 GPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGcsE 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756    183 CRRLTQFHYVNWPDHDVPSSFDSILDMIELMRKHQQRDTTPICVHCSAGCGRTGAICAIDYTWNLLKAGrisEDFNVFQL 262
Cdd:smart00194 156 TRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAG---KEVDIFEI 232

                          250       260
                   ....*....|....*....|....*..
gi 41054756    263 IQEMRTQRHSAVQTKEQYELVHRAIAQ 289
Cdd:smart00194 233 VKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
55-289 3.70e-116

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 343.84  E-value: 3.70e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756    55 NVKKNRYKDILPFDHSRVKvtLKTSNQDTDYINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFE 134
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVK--LTGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756   135 MGRKKCERYFPLFGDEPMTFGPFRISCESEQPRT-DYCVRTLTVEFDQ--ECRRLTQFHYVNWPDHDVPSSFDSILDMIE 211
Cdd:pfam00102  79 KGREKCAQYWPEEEGESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNGGseETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41054756   212 LMRKHQQR-DTTPICVHCSAGCGRTGAICAIDYTWNLLKAGrisEDFNVFQLIQEMRTQRHSAVQTKEQYELVHRAIAQ 289
Cdd:pfam00102 159 KVRKSSLDgRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAE---GEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
41-290 5.96e-49

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 171.04  E-value: 5.96e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  41 TEKIYPTDVGEQEE----NVKKNRYKDILPFDHSRVkvtlktsNQDTDYINANFIKGIDgPQAYIATQGPLPNTVLDFWR 116
Cdd:COG5599  24 TNELAPSHNDPQYLqninGSPLNRFRDIQPYKETAL-------RANLGYLNANYIQVIG-NHRYIATQYPLEEQLEDFFQ 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 117 MIWEYKVAVIVM--ACREFEMGRKKCERYFPLFGDEpmtfgpFRISCESEQPRTDYC-----VRTLTV---EFDQECRRL 186
Cdd:COG5599  96 MLFDNNTPVLVVlaSDDEISKPKVKMPVYFRQDGEY------GKYEVSSELTESIQLrdgieARTYVLtikGTGQKKIEI 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 187 TQFHYVNWPDHDVPSS--FDSILDMIELMRKHQQRDTTPICVHCSAGCGRTGAICAIDYTWNLLKAGrISEDFNVFQLIQ 264
Cdd:COG5599 170 PVLHVKNWPDHGAISAeaLKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINAL-VQITLSVEEIVI 248

                       250       260
                ....*....|....*....|....*...
gi 41054756 265 EMRTQR-HSAVQTKEQY-ELVHRAIAQI 290
Cdd:COG5599 249 DMRTSRnGGMVQTSEQLdVLVKLAEQQI 276
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 51-284 2.42e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 162.48  E-value: 2.42e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756   51 EQEENVKKNRYKDILPFDHSRVkvTLKT-SNQDTDYINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMA 129
Cdd:PHA02747  47 EKPENQPKNRYWDIPCWDHNRV--ILDSgGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVML 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  130 C-REFEMGRKKCERYFPLFGDEPMTFGPFRISCESEQPRTDYcVRTL---TVEFDQECRRLTQFHYVNWPDHDVPSS--- 202
Cdd:PHA02747 125 TpTKGTNGEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKY-ILTLieiTDKILKDSRKISHFQCSEWFEDETPSDhpd 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  203 FDSILDMIELMRK-------HQQRDTTPICVHCSAGCGRTGAICAIDYTWN-LLKAGRISedfnVFQLIQEMRTQRHSAV 274
Cdd:PHA02747 204 FIKFIKIIDINRKksgklfnPKDALLCPIVVHCSDGVGKTGIFCAVDICLNqLVKRKAIC----LAKTAEKIREQRHAGI 279

                        250
                 ....*....|
gi 41054756  275 QTKEQYELVH 284
Cdd:PHA02747 280 MNFDDYLFIQ 289
PHA03247 PHA03247
large tegument protein UL36; Provisional
 314-566 1.30e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.31  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756   314 DSSPEKHTPNSDEEQWDTPPPKPPRLRSVQGEcavqeeiLQAPEPRPVPPILRPSPASALRTVSSARHSDTYHPKPLLSD 393
Cdd:PHA03247 2606 GDPRGPAPPSPLPPDTHAPDPPPPSPSPAANE-------PDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASS 2678

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756   394 PePSDPEPS---------THFTDPDHHSSDPEPSEPERRVERLAVEIQKVALQEGPR-PLHLLLQSPAHAPALSFT-NPL 462
Cdd:PHA03247 2679 P-PQRPRRRaarptvgslTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPAlPAAPAPPAVPAGPATPGGpARP 2757

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756   463 HTHTHSHTLPDTHPTAAGGTAEqqnQRRATHMSIAGHTLHTESSEEQPAGAADTAPLQAsgdttAAPRENDAEQKSTETP 542
Cdd:PHA03247 2758 ARPPTTAGPPAPAPPAAPAAGP---PRRLTRPAVASLSESRESLPSPWDPADPPAAVLA-----PAAALPPAASPAGPLP 2829

                         250       260
                  ....*....|....*....|....
gi 41054756   543 VSGTKAEIGfgrrCSPPRGPREPP 566
Cdd:PHA03247 2830 PPTSAQPTA----PPPPPGPPPPS 2849
 
Name Accession Description Interval E-value
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 2-295 0e+00

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: 644.68  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756   2 EQGNILKKFIEELRSGEQT---GEDNFSSDFMRLRRLSTKYRTEKIYPTDVGEQEENVKKNRYKDILPFDHSRVKVTLKT 78
Cdd:cd14604   1 EQVEILKKFIERVQAMKSTdhnGEDNFASDFMRLRRLSTKYRTEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  79 SNQDTDYINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRKKCERYFPLFGDEPMTFGPFR 158
Cdd:cd14604  81 SSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPMTFGPFR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 159 ISCESEQPRTDYCVRTLTVEFDQECRRLTQFHYVNWPDHDVPSSFDSILDMIELMRKHQQRDTTPICVHCSAGCGRTGAI 238
Cdd:cd14604 161 ISCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAI 240

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41054756 239 CAIDYTWNLLKAGRISEDFNVFQLIQEMRTQRHSAVQTKEQYELVHRAIAQIFQKQL 295
Cdd:cd14604 241 CAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEKQL 297
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 58-291 2.36e-142

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: 410.77  E-value: 2.36e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  58 KNRYKDILPFDHSRVKVTLKTSNQDTDYINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGR 137
Cdd:cd14602   1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 138 KKCERYFPLFGDEPMTFGPFRISCESEQPRTDYCVRTLTVEFDQECRRLTQFHYVNWPDHDVPSSFDSILDMIELMRKHQ 217
Cdd:cd14602  81 KKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQ 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41054756 218 QRDTTPICVHCSAGCGRTGAICAIDYTWNLLKAGRISEDFNVFQLIQEMRTQRHSAVQTKEQYELVHRAIAQIF 291
Cdd:cd14602 161 EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIELF 234
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 85-285 3.79e-134

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: 388.70  E-value: 3.79e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  85 YINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRKKCERYFPLFGDEPMTFGPFRISCESE 164
Cdd:cd14542   1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKISLEKE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 165 QPRT-DYCVRTLTVEFDQECRRLTQFHYVNWPDHDVPSSFDSILDMIELMRKHQQRDTTPICVHCSAGCGRTGAICAIDY 243
Cdd:cd14542  81 KRVGpDFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICAIDY 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 41054756 244 TWNLLKAGRISEDFNVFQLIQEMRTQRHSAVQTKEQYELVHR 285
Cdd:cd14542 161 VWNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 26-291 3.67e-131

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: 383.79  E-value: 3.67e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  26 SSDFMRLRRLSTKYRTEKIYPTDVGEQEENVKKNRYKDILPFDHSRVKVTLKTSNQDTDYINANFIKGIDGPQAYIATQG 105
Cdd:cd14603   1 AGEFSEIRACSAAFKADYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 106 PLPNTVLDFWRMIWEYKVAVIVMACREFEMGRKKCERYFPLfGDEPMTFGPFRIS-CESEQPRTDYCVRTLTVEFDQECR 184
Cdd:cd14603  81 PLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQ-EQEPLQTGPFTITlVKEKRLNEEVILRTLKVTFQKESR 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 185 RLTQFHYVNWPDHDVPSSFDSILDMIELMRKHQQRDTTPICVHCSAGCGRTGAICAIDYTWNLLKAGRISEDFNVFQLIQ 264
Cdd:cd14603 160 SVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIFDVVL 239

                       250       260
                ....*....|....*....|....*..
gi 41054756 265 EMRTQRHSAVQTKEQYELVHRAIAQIF 291
Cdd:cd14603 240 EMRKQRPAAVQTEEQYEFLYHTVAQMF 266
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
25-289 3.22e-120

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 355.43  E-value: 3.22e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756     25 FSSDFMRLRRLSTKYRtekiyPTDVGEQEENVKKNRYKDILPFDHSRVKVTLKTSNqDTDYINANFIKGIDGPQAYIATQ 104
Cdd:smart00194   2 LEEEFEKLDRLKPDDE-----SCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE-GSDYINASYIDGPNGPKAYIATQ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756    105 GPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRKKCERYFPLFGDEPMTFGPFRISCESEQPRTDYCVRTLTVEFDQ--E 182
Cdd:smart00194  76 GPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGcsE 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756    183 CRRLTQFHYVNWPDHDVPSSFDSILDMIELMRKHQQRDTTPICVHCSAGCGRTGAICAIDYTWNLLKAGrisEDFNVFQL 262
Cdd:smart00194 156 TRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAG---KEVDIFEI 232

                          250       260
                   ....*....|....*....|....*..
gi 41054756    263 IQEMRTQRHSAVQTKEQYELVHRAIAQ 289
Cdd:smart00194 233 VKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
55-289 3.70e-116

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 343.84  E-value: 3.70e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756    55 NVKKNRYKDILPFDHSRVKvtLKTSNQDTDYINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFE 134
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVK--LTGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756   135 MGRKKCERYFPLFGDEPMTFGPFRISCESEQPRT-DYCVRTLTVEFDQ--ECRRLTQFHYVNWPDHDVPSSFDSILDMIE 211
Cdd:pfam00102  79 KGREKCAQYWPEEEGESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNGGseETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41054756   212 LMRKHQQR-DTTPICVHCSAGCGRTGAICAIDYTWNLLKAGrisEDFNVFQLIQEMRTQRHSAVQTKEQYELVHRAIAQ 289
Cdd:pfam00102 159 KVRKSSLDgRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAE---GEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 85-285 7.86e-97

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: 293.04  E-value: 7.86e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  85 YINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRKKCERYFPLFGDEPMTFGPFRISCESE 164
Cdd:cd00047   1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLVSE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 165 QPRTDYCVRTLTVEFDQ--ECRRLTQFHYVNWPDHDVPSSFDSILDMIELMRKHQQRDTTPICVHCSAGCGRTGAICAID 242
Cdd:cd00047  81 EELSDYTIRTLELSPKGcsESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAID 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 41054756 243 YTWNLLKAGRIsedFNVFQLIQEMRTQRHSAVQTKEQYELVHR 285
Cdd:cd00047 161 ILLERLEAEGE---VDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 55-284 3.10e-77

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: 245.35  E-value: 3.10e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  55 NVKKNRYKDILPFDHSRVKVTLKTSNQDTDYINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFE 134
Cdd:cd14543  29 NQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMTTRVVE 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 135 MGRKKCERYFPLFGDEPMTFGPFRISCESEQPRTDYCVRTLTVEFDQ--ECRRLTQFHYVNWPDHDVPSSFDSILDMIEL 212
Cdd:cd14543 109 RGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTEtdESRQVTHFQFTSWPDFGVPSSAAALLDFLGE 188

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 213 MRKHQQRDTT-------------PICVHCSAGCGRTGAICAIDYTWNLL-KAGRIsedfNVFQLIQEMRTQRHSAVQTKE 278
Cdd:cd14543 189 VRQQQALAVKamgdrwkghppgpPIVVHCSAGIGRTGTFCTLDICLSQLeDVGTL----NVMQTVRRMRTQRAFSIQTPD 264


                ....*.
gi 41054756 279 QYELVH 284
Cdd:cd14543 265 QYYFCY 270
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 60-284 1.25e-76

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: 241.87  E-value: 1.25e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  60 RYKDILPFDHSRVKVTLKTSNQDTDYINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRKK 139
Cdd:cd14548   1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 140 CERYFPlFGDEPMTFGPFRISCESEQPRTDYCVRTLTVEFDQECRRLTQFHYVNWPDHDVPSSFDSILDMIELMRKHQQR 219
Cdd:cd14548  81 CDHYWP-FDQDPVYYGDITVTMLSESVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIKQ 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41054756 220 DTTPICVHCSAGCGRTGAICAIDYTWNLLKagriSEDF-NVFQLIQEMRTQRHSAVQTKEQYELVH 284
Cdd:cd14548 160 EKGPTIVHCSAGVGRTGTFIALDRLLQQIE----SEDYvDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 59-285 4.39e-74

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: 235.37  E-value: 4.39e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  59 NRYKDILPFDHSRVKVTLKTSNQDTDYINANFIKGIDGPQ-AYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMgR 137
Cdd:cd14547   1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEEkAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA-K 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 138 KKCERYFPLfgDEPMTFGPFRISCESEQPRTDYCVRTLTVEFDQECRRLTQFHYVNWPDHDVPSSFDSILDM---IELMR 214
Cdd:cd14547  80 EKCAQYWPE--EENETYGDFEVTVQSVKETDGYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLvqeVEEAR 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41054756 215 KhQQRDTTPICVHCSAGCGRTGAICAIDYTWNLLKAgRISEDfnVFQLIQEMRTQRHSAVQTKEQYELVHR 285
Cdd:cd14547 158 Q-TEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLRE-EGVVD--VLGIVCQLRLDRGGMVQTAEQYEFVHR 224
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 53-287 7.29e-70

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: 224.97  E-value: 7.29e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  53 EENVKKNRYKDILPFDHSRVKVTLKTSNQDTDYINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACRE 132
Cdd:cd14553   1 EVNKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 133 FEMGRKKCERYFPLFGDEpmTFGPFRISCESEQPRTDYCVRTLTV--EFDQECRRLTQFHYVNWPDHDVPSSFDSILDMI 210
Cdd:cd14553  81 EERSRVKCDQYWPTRGTE--TYGLIQVTLLDTVELATYTVRTFALhkNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFL 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41054756 211 ELMRKHQQRDTTPICVHCSAGCGRTGAICAIDytwNLLKAGRISEDFNVFQLIQEMRTQRHSAVQTKEQYELVHRAI 287
Cdd:cd14553 159 RRVKACNPPDAGPIVVHCSAGVGRTGCFIVID---SMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDAL 232
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 55-289 2.55e-68

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


Pssm-ID: 350392 [Multi-domain]  Cd Length: 251  Bit Score: 221.18  E-value: 2.55e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  55 NVKKNRYKDILPFDHSRVKVTLKTSNQD-TDYINANFIK------GIDGP-QAYIATQGPLPNTVLDFWRMIWEYKVAVI 126
Cdd:cd14544   1 NKGKNRYKNILPFDHTRVILKDRDPNVPgSDYINANYIRnenegpTTDENaKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 127 VMACREFEMGRKKCERYFPlfgDEPMT--FGPFRISCESEQPRTDYCVRTLTV---EFDQECRRLTQFHYVNWPDHDVPS 201
Cdd:cd14544  81 VMTTKEVERGKNKCVRYWP---DEGMQkqYGPYRVQNVSEHDTTDYTLRELQVsklDQGDPIREIWHYQYLSWPDHGVPS 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 202 SFDSILDMIELMRKHQQR--DTTPICVHCSAGCGRTGAICAIDYTWNLLKAGRISEDFNVFQLIQEMRTQRHSAVQTKEQ 279
Cdd:cd14544 158 DPGGVLNFLEDVNQRQESlpHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDCDIDIQKTIQMVRSQRSGMVQTEAQ 237

                       250
                ....*....|
gi 41054756 280 YELVHRAIAQ 289
Cdd:cd14544 238 YKFIYVAVAQ 247
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 85-284 9.74e-68

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


Pssm-ID: 350509 [Multi-domain]  Cd Length: 212  Bit Score: 218.27  E-value: 9.74e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  85 YINANFIKGIDGPQ-AYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRKKCERYFPLfGDEPMTFGPFRISC-- 161
Cdd:cd18533   1 YINASYITLPGTSSkRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPS-GEYEGEYGDLTVELvs 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 162 ESEQPRTDYCVRTLTVEF-DQECRRLTQFHYVNWPDHDVPSSFDSILDMIELMRKHQQ--RDTTPICVHCSAGCGRTGAI 238
Cdd:cd18533  80 EEENDDGGFIVREFELSKeDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDsaSLDPPIIVHCSAGVGRTGTF 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 41054756 239 CAIDYTWNLLKAGRISEDFN------VFQLIQEMRTQRHSAVQTKEQYELVH 284
Cdd:cd18533 160 IALDSLLDELKRGLSDSQDLedsedpVYEIVNQLRKQRMSMVQTLRQYIFLY 211
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 59-287 4.88e-67

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: 217.45  E-value: 4.88e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  59 NRYKDILPFDHSRVKVTLKTSNQDTDYINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRK 138
Cdd:cd14619   1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 139 KCERYFPLfGDEPMTFGPFRISCESEQPRTDYCVRTLTVE--FDQECRRLTQFHYVNWPDHDVPSSFDSILDMIELMRKH 216
Cdd:cd14619  81 KCEHYWPL-DYTPCTYGHLRVTVVSEEVMENWTVREFLLKqvEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQW 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41054756 217 --QQRDTTPICVHCSAGCGRTGAICAIDYtwnLLKAGRISEDFNVFQLIQEMRTQRHSAVQTKEQYELVHRAI 287
Cdd:cd14619 160 ldQTMSGGPTVVHCSAGVGRTGTLIALDV---LLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCI 229
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 46-287 6.30e-65

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: 212.44  E-value: 6.30e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  46 PTDVGEQEENVKKNRYKDILPFDHSRVKVTLKTSNQDTDYINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAV 125
Cdd:cd14614   3 PHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 126 IVMACREFEMGRKKCERYFPlFGDEPMTFGPFRISCESEQPRTDYCVRTLTVEFDQECRRLTQFHYVNWPDHDVPS--SF 203
Cdd:cd14614  83 IVMLTQCNEKRRVKCDHYWP-FTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPTanAA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 204 DSILDMIELMRKHQQRDTTPICVHCSAGCGRTGAICAIDYtwnLLKAGRISEDFNVFQLIQEMRTQRHSAVQTKEQYELV 283
Cdd:cd14614 162 ESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDR---LLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFI 238


                ....
gi 41054756 284 HRAI 287
Cdd:cd14614 239 HQCV 242
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 85-290 3.41e-64

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: 208.77  E-value: 3.41e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  85 YINANFIKGIDG--PQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRKKCERYFPLFGDEPMTF-GPFRISC 161
Cdd:cd14538   1 YINASHIRIPVGgdTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPLICgGRLEVSL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 162 ESEQPRTDYCVRTLTVEFDQ--ECRRLTQFHYVNWPDHDVPSSFDSILDMIELMRK-HQqrdTTPICVHCSAGCGRTGAI 238
Cdd:cd14538  81 EKYQSLQDFVIRRISLRDKEtgEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRiHN---SGPIVVHCSAGIGRTGVL 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 41054756 239 CAIDYTWNLLKAGrisEDFNVFQLIQEMRTQRHSAVQTKEQYELVHRAIAQI 290
Cdd:cd14538 158 ITIDVALGLIERD---LPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEV 206
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 59-280 6.96e-64

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: 208.90  E-value: 6.96e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  59 NRYKDILPFDHSRVKVTLKTSNQDtDYINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRK 138
Cdd:cd14615   1 NRYNNVLPYDISRVKLSVQSHSTD-DYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 139 KCERYFPlfGDEPMTFGPFRISCESEQPRTDYCVRTLTVEFDQ--ECRRLTQFHYVNWPDHDVPSSFDSILDMIELMRKH 216
Cdd:cd14615  80 KCEEYWP--SKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQtnESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREY 157

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41054756 217 --QQRDTTPICVHCSAGCGRTGAICAIDytwNLLKAGRISEDFNVFQLIQEMRTQRHSAVQTKEQY 280
Cdd:cd14615 158 mkQNPPNSPILVHCSAGVGRTGTFIAID---RLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQY 220
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 85-284 1.63e-62

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: 204.51  E-value: 1.63e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  85 YINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRKKCERYFPLFGDEpmTFGPFRISCESE 164
Cdd:cd14549   1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTE--TYGNIQVTLLST 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 165 QPRTDYCVRTLTV--------EFDQECRRLTQFHYVNWPDHDVPSSFDSILDMIELMRKHQQRDTTPICVHCSAGCGRTG 236
Cdd:cd14549  79 EVLATYTVRTFSLknlklkkvKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTG 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 41054756 237 AICAIDytwNLLKAGRISEDFNVFQLIQEMRTQRHSAVQTKEQYELVH 284
Cdd:cd14549 159 TYIVID---SMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 53-289 4.29e-62

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: 204.49  E-value: 4.29e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  53 EENVKKNRYKDILPFDHSRVKVTLKTSNQDTDYINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACRE 132
Cdd:cd14630   1 DENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 133 FEMGRKKCERYFPlfgDEPMTFGPFRISCESEQPRTDYCVRTLTVEFD--QECRRLTQFHYVNWPDHDVPSSFDSILDMI 210
Cdd:cd14630  81 VEVGRVKCVRYWP---DDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKgyHEIREIRQFHFTSWPDHGVPCYATGLLGFV 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41054756 211 ELMRKHQQRDTTPICVHCSAGCGRTGAICAIDYTWNLLKAGRISEDFNVfqlIQEMRTQRHSAVQTKEQYELVHRAIAQ 289
Cdd:cd14630 158 RQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNC---VRELRAQRVNMVQTEEQYVFVHDAILE 233
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 38-289 2.99e-61

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


Pssm-ID: 350454 [Multi-domain]  Cd Length: 266  Bit Score: 203.19  E-value: 2.99e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  38 KYRTEKIYPTDVGEQEENVKKNRYKDILPFDHSRVKVTLKTSN-QDTDYINANFIK----GIDGPQ-AYIATQGPLPNTV 111
Cdd:cd14606   1 KQEVKNLHQRLEGQRPENKSKNRYKNILPFDHSRVILQGRDSNiPGSDYINANYVKnqllGPDENAkTYIASQGCLEATV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 112 LDFWRMIWEYKVAVIVMACREFEMGRKKCERYFPLFGDEPmTFGPFRISCESEQPRTDYCVRTLTV---EFDQECRRLTQ 188
Cdd:cd14606  81 NDFWQMAWQENSRVIVMTTREVEKGRNKCVPYWPEVGMQR-AYGPYSVTNCGEHDTTEYKLRTLQVsplDNGELIREIWH 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 189 FHYVNWPDHDVPSSFDSILDMIELMRKHQQ--RDTTPICVHCSAGCGRTGAICAIDYTWNLLKAGRISEDFNVFQLIQEM 266
Cdd:cd14606 160 YQYLSWPDHGVPSEPGGVLSFLDQINQRQEslPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLDCDIDIQKTIQMV 239

                       250       260
                ....*....|....*....|...
gi 41054756 267 RTQRHSAVQTKEQYELVHRAIAQ 289
Cdd:cd14606 240 RAQRSGMVQTEAQYKFIYVAIAQ 262
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 53-287 4.34e-60

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: 199.29  E-value: 4.34e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  53 EENVKKNRYKDILPFDHSRVKVtlktsNQDTDYINANFIKGIDGPQ--AYIATQGPLPNTVLDFWRMIWEYKVAVIVMAC 130
Cdd:cd14597   1 KENRKKNRYKNILPYDTTRVPL-----GDEGGYINASFIKMPVGDEefVYIACQGPLPTTVADFWQMVWEQKSTVIAMMT 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 131 REFEMGRKKCERYFP-LFGDEPMTFGPFRISCESEQPRTDYCVRTLTVEFDQ--ECRRLTQFHYVNWPDHDVPSSFDSIL 207
Cdd:cd14597  76 QEVEGGKIKCQRYWPeILGKTTMVDNRLQLTLVRMQQLKNFVIRVLELEDIQtrEVRHITHLNFTAWPDHDTPSQPEQLL 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 208 DMIELMRkHQQRdTTPICVHCSAGCGRTGAICAIDYTWNLlkagrISE--DFNVFQLIQEMRTQRHSAVQTKEQYELVHR 285
Cdd:cd14597 156 TFISYMR-HIHK-SGPIITHCSAGIGRSGTLICIDVVLGL-----ISKdlDFDISDIVRTMRLQRHGMVQTEDQYIFCYQ 228


                ..
gi 41054756 286 AI 287
Cdd:cd14597 229 VI 230
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 59-287 3.67e-59

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: 196.70  E-value: 3.67e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  59 NRYKDILPFDHSRVKVTLKTSNQDTDYINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRK 138
Cdd:cd14618   1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 139 KCERYFPLfGDEPMTFGPFRISCESEQPRTDYCVRTLTV--EFDQECRRLTQFHYVNWPDHDVPSSFDSILDMIELMRKH 216
Cdd:cd14618  81 LCDHYWPS-ESTPVSYGHITVHLLAQSSEDEWTRREFKLwhEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVREH 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41054756 217 QQ--RDTTPICVHCSAGCGRTGAICAIDYTWNLLKAGRISEDFNVfqlIQEMRTQRHSAVQTKEQYELVHRAI 287
Cdd:cd14618 160 VQatKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNT---VYILRMHRYLMIQTLSQYIFLHSCI 229
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 54-287 4.93e-58

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: 194.47  E-value: 4.93e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  54 ENVKKNRYKDILPFDHSRVKVTLKTSN-QDTDYINANFI------KGIDGP--QAYIATQGPLPNTVLDFWRMIWEYKVA 124
Cdd:cd14605   1 ENKNKNRYKNILPFDHTRVVLHDGDPNePVSDYINANIImpefetKCNNSKpkKSYIATQGCLQNTVNDFWRMVFQENSR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 125 VIVMACREFEMGRKKCERYFPlfgDEPM--TFGPFRISCESEQPRTDYCVRTLTV----EFDQEcRRLTQFHYVNWPDHD 198
Cdd:cd14605  81 VIVMTTKEVERGKSKCVKYWP---DEYAlkEYGVMRVRNVKESAAHDYILRELKLskvgQGNTE-RTVWQYHFRTWPDHG 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 199 VPSSFDSILDMIELMRKHQQ--RDTTPICVHCSAGCGRTGAICAIDYTWNLLKAGRISEDFNVFQLIQEMRTQRHSAVQT 276
Cdd:cd14605 157 VPSDPGGVLDFLEEVHHKQEsiMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIQMVRSQRSGMVQT 236

                       250
                ....*....|.
gi 41054756 277 KEQYELVHRAI 287
Cdd:cd14605 237 EAQYRFIYMAV 247
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 58-279 8.79e-58

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: 192.99  E-value: 8.79e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  58 KNRYKDILPFDHSRVKVTLKtsNQDTDYINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGR 137
Cdd:cd14545   1 LNRYRDRDPYDHDRSRVKLK--QGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 138 KKCERYFPLFGDEPMTF--GPFRISCESEQPRTDYCVRTLTVE--FDQECRRLTQFHYVNWPDHDVPSSFDSILDMIELM 213
Cdd:cd14545  79 IKCAQYWPQGEGNAMIFedTGLKVTLLSEEDKSYYTVRTLELEnlKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKV 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41054756 214 RKHQ--QRDTTPICVHCSAGCGRTGAICAIDYTWNLLKAGRISeDFNVFQLIQEMRTQRHSAVQTKEQ 279
Cdd:cd14545 159 RESGslSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPS-SVDVKKVLLEMRKYRMGLIQTPDQ 225
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 59-285 9.83e-58

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: 192.43  E-value: 9.83e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  59 NRYKDILPFDHSRVKVTLKTSNQDTDYINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRK 138
Cdd:cd14616   1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 139 KCERYFPLfGDEPMT-FGPFRISCESEQPRTDYCVRTLTVEFDQECRRLTQFHYVNWPDHDVPSSFDSILDMIELMRKHQ 217
Cdd:cd14616  81 RCHQYWPE-DNKPVTvFGDIVITKLMEDVQIDWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRASR 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41054756 218 QRDTTPICVHCSAGCGRTGAICAIDYTWNLLKagriSEDF-NVFQLIQEMRTQRHSAVQTKEQYELVHR 285
Cdd:cd14616 160 AHDNTPMIVHCSAGVGRTGVFIALDHLTQHIN----DHDFvDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 58-289 1.04e-57

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: 193.51  E-value: 1.04e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  58 KNRYKDILPFDHSRVKV-TLKTSNQDTDYINANFIKGIDG-PQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEm 135
Cdd:cd14612  18 KDRYKTILPNPQSRVCLrRAGSQEEEGSYINANYIRGYDGkEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKE- 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 136 GRKKCERYFPlfgDEPMTFGPFRISCESEQPRTDYCVRTLTVEFDQECRRLTQFHYVNWPDHDVPSSFDSILDMIELMRK 215
Cdd:cd14612  97 KKEKCVHYWP---EKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPESAGPLLRLVAEVEE 173

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41054756 216 HQQRDTT--PICVHCSAGCGRTGAICAIDYTWNLLKAgriSEDFNVFQLIQEMRTQRHSAVQTKEQYELVHRAIAQ 289
Cdd:cd14612 174 SRQTAASpgPIVVHCSAGIGRTGCFIATSIGCQQLKD---TGKVDILGIVCQLRLDRGGMIQTSEQYQFLHHTLAL 246
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 53-289 3.40e-56

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: 190.25  E-value: 3.40e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  53 EENVKKNRYKDILPFDHSRVKVTLKTSNQDTDYINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACRE 132
Cdd:cd14626  39 EVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRL 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 133 FEMGRKKCERYFPLFGDEpmTFGPFRISCESEQPRTDYCVRTLTVEFD--QECRRLTQFHYVNWPDHDVPSSFDSILDMI 210
Cdd:cd14626 119 EEKSRVKCDQYWPIRGTE--TYGMIQVTLLDTVELATYSVRTFALYKNgsSEKREVRQFQFMAWPDHGVPEYPTPILAFL 196

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41054756 211 ELMRKHQQRDTTPICVHCSAGCGRTGAICAIDytwNLLKAGRISEDFNVFQLIQEMRTQRHSAVQTKEQYELVHRAIAQ 289
Cdd:cd14626 197 RRVKACNPPDAGPMVVHCSAGVGRTGCFIVID---AMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 47-289 3.55e-56

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: 190.65  E-value: 3.55e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  47 TDVGEQEENVKKNRYKDILPFDHSRVKVTLKTSNQDTDYINANFIKGIDgPQ--AYIATQGPLPNTVLDFWRMIWEYKVA 124
Cdd:cd14610  36 TNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMDHD-PRnpAYIATQGPLPATVADFWQMVWESGCV 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 125 VIVMACREFEMGRKKCERYFPLFGDEpmTFGPFRISCESEQPRT-DYCVRTLTVEFDQ--ECRRLTQFHYVNWPDHDVPS 201
Cdd:cd14610 115 VIVMLTPLAENGVKQCYHYWPDEGSN--LYHIYEVNLVSEHIWCeDFLVRSFYLKNLQtnETRTVTQFHFLSWNDQGVPA 192

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 202 SFDSILDMIELMRKHQQRDTTPICVHCSAGCGRTGAICAIDYTWNLLKAGriSEDFNVFQLIQEMRTQRHSAVQTKEQYE 281
Cdd:cd14610 193 STRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKG--AKEIDIAATLEHLRDQRPGMVQTKEQFE 270


                ....*...
gi 41054756 282 LVHRAIAQ 289
Cdd:cd14610 271 FALTAVAE 278
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 45-289 5.53e-56

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: 189.85  E-value: 5.53e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  45 YPTDVGEQEENVKKNRYKDILPFDHSRVKVtlktSNQDTDYINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVA 124
Cdd:cd14608  15 FPCRVAKLPKNKNRNRYRDVSPFDHSRIKL----HQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSR 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 125 VIVMACREFEMGRKKCERYFPLFGDEPMTF--GPFRISCESEQPRTDYCVRTLTVE--FDQECRRLTQFHYVNWPDHDVP 200
Cdd:cd14608  91 GVVMLNRVMEKGSLKCAQYWPQKEEKEMIFedTNLKLTLISEDIKSYYTVRQLELEnlTTQETREILHFHYTTWPDFGVP 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 201 SSFDSILDMIELMRKHQ--QRDTTPICVHCSAGCGRTGAICAIDYTWNLLKAGRISEDFNVFQLIQEMRTQRHSAVQTKE 278
Cdd:cd14608 171 ESPASFLNFLFKVRESGslSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTAD 250

                       250
                ....*....|.
gi 41054756 279 QYELVHRAIAQ 289
Cdd:cd14608 251 QLRFSYLAVIE 261
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 84-293 1.50e-55

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: 186.38  E-value: 1.50e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  84 DYINANF----IKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRKKCERYFPLFGDEpMTFGPFRI 159
Cdd:cd14541   1 DYINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGET-MQFGNLQI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 160 SCESEQPRTDYCVRTLTVeFDQ---ECRRLTQFHYVNWPDHDVPSSFDSILDMIELMRKHQQRDTTPICVHCSAGCGRTG 236
Cdd:cd14541  80 TCVSEEVTPSFAFREFIL-TNTntgEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTG 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41054756 237 AICAIDYTWNLLKAgriSEDFNVFQLIQEMRTQRHSAVQTKEQYELVHRAIAQIFQK 293
Cdd:cd14541 159 VLITMETAMCLIEA---NEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRVYEE 212
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 25-289 2.00e-55

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: 188.32  E-value: 2.00e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  25 FSSDFMRLRRLSTKYRTEkiypTDVGEQEENVKKNRYKDILPFDHSRVKVT--LKTSNQDTDYINANFIKGIDGPQAYIA 102
Cdd:cd17667   1 FSEDFEEVQRCTADMNIT----AEHSNHPDNKHKNRYINILAYDHSRVKLRplPGKDSKHSDYINANYVDGYNKAKAYIA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 103 TQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRKKCERYFPLFGDEpmTFGPFRISCESEQPRTDYCVRTLTV----- 177
Cdd:cd17667  77 TQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSE--EYGNIIVTLKSTKIHACYTVRRFSIrntkv 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 178 --------EFDQECRRLTQFHYVNWPDHDVPSSFDSILDMIELMRKHQQRDTTPICVHCSAGCGRTGAICAIDytwNLLK 249
Cdd:cd17667 155 kkgqkgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVID---SMLQ 231

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 41054756 250 AGRISEDFNVFQLIQEMRTQRHSAVQTKEQYELVHRAIAQ 289
Cdd:cd17667 232 QIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 271
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 48-289 3.84e-55

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: 187.94  E-value: 3.84e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  48 DVGEQEENVKKNRYKDILPFDHSRVKVTLKTSNQDTDYINANFIKGIDgPQ--AYIATQGPLPNTVLDFWRMIWEYKVAV 125
Cdd:cd14609  35 STAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIEHD-PRmpAYIATQGPLSHTIADFWQMVWENGCTV 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 126 IVMACREFEMGRKKCERYFPlfgDEPMT-FGPFRISCESEQPR-TDYCVRTLTVEF--DQECRRLTQFHYVNWPDHDVPS 201
Cdd:cd14609 114 IVMLTPLVEDGVKQCDRYWP---DEGSSlYHIYEVNLVSEHIWcEDFLVRSFYLKNvqTQETRTLTQFHFLSWPAEGIPS 190

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 202 SFDSILDMIELMRKHQQRDTTPICVHCSAGCGRTGAICAIDYTWNLLKAGriSEDFNVFQLIQEMRTQRHSAVQTKEQYE 281
Cdd:cd14609 191 STRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKG--VKEIDIAATLEHVRDQRPGMVRTKDQFE 268


                ....*...
gi 41054756 282 LVHRAIAQ 289
Cdd:cd14609 269 FALTAVAE 276
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 11-293 4.88e-55

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: 187.36  E-value: 4.88e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  11 IEELRSGEQTGednfssdfMRLRRLSTKYRTEKIYPTDVGEQEENVKKNRYKDILPFDHSRVKVtlktsNQDTDYINANF 90
Cdd:cd14600   4 MAQLKKGLESG--------TVLIQFEQLYRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVL-----QGNEDYINASY 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  91 IK----GIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRKKCERYFPlfgDEP--MTFGPFRISCESE 164
Cdd:cd14600  71 VNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWP---DPPdvMEYGGFRVQCHSE 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 165 QPRTDYCVRTLTVEFDQ--ECRRLTQFHYVNWPDHDVPSSFDSILDMIELMRKHQQrDTTPICVHCSAGCGRTGAICAID 242
Cdd:cd14600 148 DCTIAYVFREMLLTNTQtgEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRV-ENEPVLVHCSAGIGRTGVLVTME 226

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 41054756 243 YTWNLlkagrISEDFNVFQL--IQEMRTQRHSAVQTKEQYELVHRAIAQIFQK 293
Cdd:cd14600 227 TAMCL-----TERNQPVYPLdiVRKMRDQRAMMVQTSSQYKFVCEAILRVYEE 274
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 46-289 5.16e-55

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: 187.17  E-value: 5.16e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  46 PTDVGEQEENVKKNRYKDILPFDHSRVKVTLKTSNQDTDYINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAV 125
Cdd:cd14633  31 PWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTAS 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 126 IVMACREFEMGRKKCERYFPlfgDEPMTFGPFRISCESEQPRTDYCVRTLTVEFD--QECRRLTQFHYVNWPDHDVPSSF 203
Cdd:cd14633 111 IIMVTNLVEVGRVKCCKYWP---DDTEIYKDIKVTLIETELLAEYVIRTFAVEKRgvHEIREIRQFHFTGWPDHGVPYHA 187

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 204 DSILDMIELMRKHQQRDTTPICVHCSAGCGRTGAICAIDYTWNLLKAGRISEDFNVfqlIQEMRTQRHSAVQTKEQYELV 283
Cdd:cd14633 188 TGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNC---VRELRSRRVNMVQTEEQYVFI 264


                ....*.
gi 41054756 284 HRAIAQ 289
Cdd:cd14633 265 HDAILE 270
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 55-286 1.73e-54

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: 184.65  E-value: 1.73e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  55 NVKKNRYKDILPFDHSRVKVTLKTSNQDTDYINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFE 134
Cdd:cd14554   6 NKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLRE 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 135 MGRKKCERYFPLfgDEPMTFGPFRISCESEQPRTDYCVRTLTVE--FDQECRRLTQFHYVNWPDHDVPSSFDSILDMIEL 212
Cdd:cd14554  86 MGREKCHQYWPA--ERSARYQYFVVDPMAEYNMPQYILREFKVTdaRDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQ 163

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41054756 213 MRK--HQQRDTTPICVHCSAGCGRTGAICAIDYtwnLLKAGRISEDFNVFQLIQEMRTQRHSAVQTKEQYELVHRA 286
Cdd:cd14554 164 VHKtkEQFGQEGPITVHCSAGVGRTGVFITLSI---VLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 60-289 1.58e-53

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: 181.78  E-value: 1.58e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  60 RYKDILPFDHSRVKVTLKTSNQDTDYINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRKK 139
Cdd:cd14623   1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 140 CERYFPlfGDEPMTFGPFRISCESEQPRTDYCVRTLTVEFDQE--CRRLTQFHYVNWPDHDVPSSFDSILDMIELMRKHQ 217
Cdd:cd14623  81 CAQYWP--SDGSVSYGDITIELKKEEECESYTVRDLLVTNTREnkSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQ 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41054756 218 QRDTT-PICVHCSAGCGRTGAICAIDYTWNLLKAGRIsedFNVFQLIQEMRTQRHSAVQTKEQYELVHRAIAQ 289
Cdd:cd14623 159 QQSGNhPITVHCSAGAGRTGTFCALSTVLERVKAEGI---LDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 85-287 1.63e-53

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: 180.88  E-value: 1.63e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  85 YINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRKKCERYFPlfgDEPMTFGPFRISCESE 164
Cdd:cd14555   1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP---DDTEVYGDIKVTLVET 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 165 QPRTDYCVRTLTVEFD--QECRRLTQFHYVNWPDHDVPSSFDSILDMIELMRKHQQRDTTPICVHCSAGCGRTGAICAID 242
Cdd:cd14555  78 EPLAEYVVRTFALERRgyHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVID 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 41054756 243 YTWNLLKAGRISEDFNVfqlIQEMRTQRHSAVQTKEQYELVHRAI 287
Cdd:cd14555 158 IMLDMAEREGVVDIYNC---VKELRSRRVNMVQTEEQYIFIHDAI 199
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 85-287 1.65e-53

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


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 180.54  E-value: 1.65e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  85 YINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRKKCERYFPlfGDEPMTFGPFRISCESE 164
Cdd:cd14552   1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWP--EDGSVSSGDITVELKDQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 165 QPRTDYCVRTLTVEFDQE--CRRLTQFHYVNWPDHDVPSSFDSILDMIELMRKHQQRDTT-PICVHCSAGCGRTGAICAI 241
Cdd:cd14552  79 TDYEDYTLRDFLVTKGKGgsTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGNhPITVHCSAGAGRTGTFCAL 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 41054756 242 DYTWNLLKAGRIsedFNVFQLIQEMRTQRHSAVQTKEQYELVHRAI 287
Cdd:cd14552 159 STVLERVKAEGV---LDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 85-287 1.16e-52

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: 178.63  E-value: 1.16e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  85 YINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRKKCERYFPLFGDEpmTFGPFRISCESE 164
Cdd:cd17668   1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSE--EYGNFLVTQKSV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 165 QPRTDYCVRTLTVEFDQ----------ECRRLTQFHYVNWPDHDVPSSFDSILDMIELMRKHQQRDTTPICVHCSAGCGR 234
Cdd:cd17668  79 QVLAYYTVRNFTLRNTKikkgsqkgrpSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGR 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 41054756 235 TGAICAIDytwNLLKAGRISEDFNVFQLIQEMRTQRHSAVQTKEQYELVHRAI 287
Cdd:cd17668 159 TGTYIVLD---SMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDAL 208
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 85-292 3.53e-52

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: 177.25  E-value: 3.53e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  85 YINANFIKGIDGPQA--YIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRKKCERYFPLFGDEPMTFGPFRISCE 162
Cdd:cd14596   1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 163 SEQPRTDYCVRTLTVEFDQ--ECRRLTQFHYVNWPDHDVPSSFDSILDMIELMRKHQQrdTTPICVHCSAGCGRTGAICA 240
Cdd:cd14596  81 NYQALQYFIIRIIKLVEKEtgENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHN--TGPIVVHCSAGIGRAGVLIC 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 41054756 241 IDYTWNLLKAGrISedFNVFQLIQEMRTQRHSAVQTKEQYELVHRAIAQIFQ 292
Cdd:cd14596 159 VDVLLSLIEKD-LS--FNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 85-289 5.06e-52

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


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 176.87  E-value: 5.06e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  85 YINANFIKGIDGPQ-AYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRKKCERYFPLFGDEpmTFGPFRISCES 163
Cdd:cd14546   1 YINASTIYDHDPRNpAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSE--VYHIYEVHLVS 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 164 EQPRT-DYCVRTLTVE--FDQECRRLTQFHYVNWPDHDVPSSFDSILDMIELMRKHQQRDTTPICVHCSAGCGRTGAICA 240
Cdd:cd14546  79 EHIWCdDYLVRSFYLKnlQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGTYIL 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 41054756 241 IDYTWNLLKAGriSEDFNVFQLIQEMRTQRHSAVQTKEQYELVHRAIAQ 289
Cdd:cd14546 159 IDMVLNRMAKG--AKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 59-285 8.37e-52

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: 177.03  E-value: 8.37e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  59 NRYKDILPFDHSRVKVTLKTSNQDTDYINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRK 138
Cdd:cd14617   1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 139 KCERYFPlFGDEPMTFGPFRISCESEQPRTDYCVRTLTV--EFDQECRRLT-QFHYVNWPDHDVPSSFDSILDMIELMRK 215
Cdd:cd14617  81 KCDHYWP-ADQDSLYYGDLIVQMLSESVLPEWTIREFKIcsEEQLDAPRLVrHFHYTVWPDHGVPETTQSLIQFVRTVRD 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41054756 216 HQQR--DTTPICVHCSAGCGRTGAICAIDytwNLLKAGRISEDFNVFQLIQEMRTQRHSAVQTKEQYELVHR 285
Cdd:cd14617 160 YINRtpGSGPTVVHCSAGVGRTGTFIALD---RILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 85-289 2.51e-51

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: 175.34  E-value: 2.51e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  85 YINANFIKGIDGPQA--YIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRKKCERYFPLFGDE--PMTFGPFRIS 160
Cdd:cd14540   1 YINASHITATVGGKQrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEhdALTFGEYKVS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 161 CESEQPRTDYCVRTLTVEFDQECRRLTQFH--YVNWPDHDVPSSFDSILDMIELM---RKHQQRDTT------PICVHCS 229
Cdd:cd14540  81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHlqYTDWPDHGCPEDVSGFLDFLEEInsvRRHTNQDVAghnrnpPTLVHCS 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 230 AGCGRTGAICAIDYTWNLLKAGrisEDFNVFQLIQEMRTQRHSAVQTKEQYELVHRAIAQ 289
Cdd:cd14540 161 AGVGRTGVVILADLMLYCLDHN---EELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 73-289 6.05e-50

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: 171.74  E-value: 6.05e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  73 KVTLKTSNQD--TDYINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRKKCERYFPlfgDE 150
Cdd:cd14631   1 RVILQPVEDDpsSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP---DD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 151 PMTFGPFRISCESEQPRTDYCVRTLTVEFD--QECRRLTQFHYVNWPDHDVPSSFDSILDMIELMRKHQQRDTTPICVHC 228
Cdd:cd14631  78 TEVYGDFKVTCVEMEPLAEYVVRTFTLERRgyNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHC 157

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41054756 229 SAGCGRTGAICAIDYTWNLLKAGRISEDFNVfqlIQEMRTQRHSAVQTKEQYELVHRAIAQ 289
Cdd:cd14631 158 SAGAGRTGCYIVIDIMLDMAEREGVVDIYNC---VKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 85-281 1.46e-49

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: 170.27  E-value: 1.46e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  85 YINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRKKCERYfplFGDEPMTFGPFRISCESE 164
Cdd:cd14558   1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQY---WGDEKKTYGDIEVELKDT 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 165 QPRTDYCVRTLTVEFDQ--ECRRLTQFHYVNWPDHDVPSSFDSILDMIELMRKHQQRD------TTPICVHCSAGCGRTG 236
Cdd:cd14558  78 EKSPTYTVRVFEITHLKrkDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKnskhgrSVPIVVHCSDGSSRTG 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 41054756 237 AICAIdytWNLLKAGRISEDFNVFQLIQEMRTQRHSAVQTKEQYE 281
Cdd:cd14558 158 IFCAL---WNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQ 199
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 45-287 2.08e-49

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: 171.69  E-value: 2.08e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  45 YPTDVGEQEENVKKNRYKDILPFDHSRVKVtlktSNQDTDYINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVA 124
Cdd:cd14607  14 YPHRVAKYPENRNRNRYRDVSPYDHSRVKL----QNTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTK 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 125 VIVMACREFEMGRKKCERYFPLFGDEPMTFGP--FRISCESEQPRTDYCVRTLTVEFDQ--ECRRLTQFHYVNWPDHDVP 200
Cdd:cd14607  90 AVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKEtgFSVKLLSEDVKSYYTVHLLQLENINsgETRTISHFHYTTWPDFGVP 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 201 SSFDSILDMIELMRKHQ--QRDTTPICVHCSAGCGRTGAICAIDyTWNLLKAGRISEDFNVFQLIQEMRTQRHSAVQTKE 278
Cdd:cd14607 170 ESPASFLNFLFKVRESGslSPEHGPAVVHCSAGIGRSGTFSLVD-TCLVLMEKKDPDSVDIKQVLLDMRKYRMGLIQTPD 248


                ....*....
gi 41054756 279 QYELVHRAI 287
Cdd:cd14607 249 QLRFSYMAV 257
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 53-289 2.80e-49

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: 172.20  E-value: 2.80e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  53 EENVKKNRYKDILPFDHSRVKVTLKTSNQDTDYINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACRE 132
Cdd:cd14625  45 EVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKL 124

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 133 FEMGRKKCERYFPLFGDEpmTFGPFRISCESEQPRTDYCVRTLTVEFD--QECRRLTQFHYVNWPDHDVPSSFDSILDMI 210
Cdd:cd14625 125 EEKSRIKCDQYWPSRGTE--TYGMIQVTLLDTIELATFCVRTFSLHKNgsSEKREVRQFQFTAWPDHGVPEYPTPFLAFL 202

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41054756 211 ELMRKHQQRDTTPICVHCSAGCGRTGAICAIDytwNLLKAGRISEDFNVFQLIQEMRTQRHSAVQTKEQYELVHRAIAQ 289
Cdd:cd14625 203 RRVKTCNPPDAGPIVVHCSAGVGRTGCFIVID---AMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 48-289 5.94e-49

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: 171.75  E-value: 5.94e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  48 DVGEQEENVKKNRYKDILPFDHSRVKVTLKTSNQDTDYINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIV 127
Cdd:cd14621  45 EAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIV 124

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 128 MACREFEMGRKKCERYFPLFGdePMTFGPFRISCESEQPRTDYCVRTLTVE-----FDQECRRL-TQFHYVNWPDHDVPS 201
Cdd:cd14621 125 MVTNLKERKECKCAQYWPDQG--CWTYGNIRVSVEDVTVLVDYTVRKFCIQqvgdvTNKKPQRLiTQFHFTSWPDFGVPF 202

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 202 SFDSILDMIELMRKHQQRDTTPICVHCSAGCGRTGAICAIDYTWNLLKAGRiseDFNVFQLIQEMRTQRHSAVQTKEQYE 281
Cdd:cd14621 203 TPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAER---KVDVYGFVSRIRAQRCQMVQTDMQYV 279


                ....*...
gi 41054756 282 LVHRAIAQ 289
Cdd:cd14621 280 FIYQALLE 287
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
41-290 5.96e-49

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 171.04  E-value: 5.96e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  41 TEKIYPTDVGEQEE----NVKKNRYKDILPFDHSRVkvtlktsNQDTDYINANFIKGIDgPQAYIATQGPLPNTVLDFWR 116
Cdd:COG5599  24 TNELAPSHNDPQYLqninGSPLNRFRDIQPYKETAL-------RANLGYLNANYIQVIG-NHRYIATQYPLEEQLEDFFQ 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 117 MIWEYKVAVIVM--ACREFEMGRKKCERYFPLFGDEpmtfgpFRISCESEQPRTDYC-----VRTLTV---EFDQECRRL 186
Cdd:COG5599  96 MLFDNNTPVLVVlaSDDEISKPKVKMPVYFRQDGEY------GKYEVSSELTESIQLrdgieARTYVLtikGTGQKKIEI 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 187 TQFHYVNWPDHDVPSS--FDSILDMIELMRKHQQRDTTPICVHCSAGCGRTGAICAIDYTWNLLKAGrISEDFNVFQLIQ 264
Cdd:COG5599 170 PVLHVKNWPDHGAISAeaLKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINAL-VQITLSVEEIVI 248

                       250       260
                ....*....|....*....|....*...
gi 41054756 265 EMRTQR-HSAVQTKEQY-ELVHRAIAQI 290
Cdd:COG5599 249 DMRTSRnGGMVQTSEQLdVLVKLAEQQI 276
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 84-293 6.36e-49

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: 168.97  E-value: 6.36e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  84 DYINANFIKgIDGPQA-----YIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRKKCERYFPlfgdEPM---TFG 155
Cdd:cd14601   1 DYINANYIN-MEIPSSsiinrYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWP----EPSgssSYG 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 156 PFRISCESEQPRTDYCVR--TLTVEFDQECRRLTQFHYVNWPDHDVPSSFDSILDMIELMRKHQQRDTTPICVHCSAGCG 233
Cdd:cd14601  76 GFQVTCHSEEGNPAYVFRemTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIG 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41054756 234 RTGAICAIDYTWNLLKAGRisedfNVFQL--IQEMRTQRHSAVQTKEQYELVHRAIAQIFQK 293
Cdd:cd14601 156 RTGVLITMETAMCLIECNQ-----PVYPLdiVRTMRDQRAMMIQTPSQYRFVCEAILKVYEE 212
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 56-288 1.18e-48

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: 169.66  E-value: 1.18e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  56 VKKNRYKDILPFDHSRVkvTLKTSNQD---TDYINANFIKGIDGPQ-AYIATQGPLPNTVLDFWRMIWEYKVAVIVMACR 131
Cdd:cd14613  26 VRKNRYKTILPNPHSRV--CLTSPDQDdplSSYINANYIRGYGGEEkVYIATQGPTVNTVGDFWRMVWQERSPIIVMITN 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 132 EFEMgRKKCERYFPlfgDEPMTFGPFRISCESEQPRTDYCVRTLTVEFDQECRRLTQFHYVNWPDHDVPSSFDSILDM-- 209
Cdd:cd14613 104 IEEM-NEKCTEYWP---EEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEERGLKHYWYTSWPDQKTPDNAPPLLQLvq 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 210 -IELMRKHQQRDTTPICVHCSAGCGRTGAICAIDYTWNLLKAGRIsedFNVFQLIQEMRTQRHSAVQTKEQYELVHRAIA 288
Cdd:cd14613 180 eVEEARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGV---VDILRTTCQLRLDRGGMIQTCEQYQFVHHVLS 256
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 61-287 2.66e-48

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: 167.81  E-value: 2.66e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  61 YKDILPFDHSRVKVTLKTSNQDTDYINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRKKC 140
Cdd:cd14620   1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 141 ERYFPLFGdePMTFGPFRISCESEQPRTDYCVRTLTV--EFDQEC---RRLTQFHYVNWPDHDVPSSFDSILDMIELMRK 215
Cdd:cd14620  81 YQYWPDQG--CWTYGNIRVAVEDCVVLVDYTIRKFCIqpQLPDGCkapRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKS 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41054756 216 HQQRDTTPICVHCSAGCGRTGAICAIDYTWNLLKAgriSEDFNVFQLIQEMRTQRHSAVQTKEQYELVHRAI 287
Cdd:cd14620 159 VNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHA---EQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQAL 227
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 84-287 2.91e-48

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


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 166.72  E-value: 2.91e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  84 DYINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRKKCERYFPLFGDepMTFGPFRISCES 163
Cdd:cd14622   1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGS--VTHGEITIEIKN 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 164 EQPRTDYCVRTLTVEFDQE--CRRLTQFHYVNWPDHDVPSSFDSILDMIELMRKHQQRD-TTPICVHCSAGCGRTGAICA 240
Cdd:cd14622  79 DTLLETISIRDFLVTYNQEkqTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTgNHPIVVHCSAGAGRTGTFIA 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 41054756 241 IDytwNLLKAGRISEDFNVFQLIQEMRTQRHSAVQTKEQYELVHRAI 287
Cdd:cd14622 159 LS---NILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 53-289 2.32e-47

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: 167.22  E-value: 2.32e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  53 EENVKKNRYKDILPFDHSRVKVTLKTSNQDTDYINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACRE 132
Cdd:cd14624  45 EVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKL 124

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 133 FEMGRKKCERYFPLFGDEpmTFGPFRISCESEQPRTDYCVRTLTV--EFDQECRRLTQFHYVNWPDHDVPSSFDSILDMI 210
Cdd:cd14624 125 EERSRVKCDQYWPSRGTE--TYGLIQVTLLDTVELATYCVRTFALykNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFL 202

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41054756 211 ELMRKHQQRDTTPICVHCSAGCGRTGAICAIDytwNLLKAGRISEDFNVFQLIQEMRTQRHSAVQTKEQYELVHRAIAQ 289
Cdd:cd14624 203 RRVKTCNPPDAGPMVVHCSAGVGRTGCFIVID---AMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 85-285 5.09e-47

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: 163.46  E-value: 5.09e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  85 YINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRKKCERYFPLFGDEPMTFGPFRISCESE 164
Cdd:cd14557   1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 165 QPRTDYCVRTLTVEFDQE---CRRLTQFHYVNWPDHDVPSSFDSILDMIELMRKHQQRDTTPICVHCSAGCGRTGAICAI 241
Cdd:cd14557  81 KICPDYIIRKLNINNKKEkgsGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIGI 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 41054756 242 DYTWNLLKA-GRIsedfNVFQLIQEMRTQRHSAVQTKEQYELVHR 285
Cdd:cd14557 161 DAMLEGLEAeGRV----DVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 7-286 5.67e-47

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: 166.45  E-value: 5.67e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756   7 LKKFIEELRSGEqTGEDNFSSDFMRLRRLSTKYRTEKIYPTDVgeqEENVKKNRYKDILPFDHSRVKVTLKTSNQDTDYI 86
Cdd:cd14628   8 LYAYIQKLTQIE-TGENVTGMELEFKRLASSKAHTSRFISANL---PCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYI 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  87 NANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRKKCERYFPlfGDEPMTFGPFRISCESEQP 166
Cdd:cd14628  84 NASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWP--AERSARYQYFVVDPMAEYN 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 167 RTDYCVRTLTV--EFDQECRRLTQFHYVNWPDHDVPSSFDSILDMIELMRKHQQR--DTTPICVHCSAGCGRTGAICAID 242
Cdd:cd14628 162 MPQYILREFKVtdARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLS 241

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 41054756 243 YtwnLLKAGRISEDFNVFQLIQEMRTQRHSAVQTKEQYELVHRA 286
Cdd:cd14628 242 I---VLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRA 282
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 58-284 3.13e-46

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: 162.01  E-value: 3.13e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  58 KNRYKDILPFDHSRVKVTLKTSNQD-TDYINANFIKGIDGPQ-AYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEM 135
Cdd:cd14611   2 KNRYKTILPNPHSRVCLKPKNSNDSlSTYINANYIRGYGGKEkAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 136 GrKKCERYFPlfgDEPMTFGPFRISCESEQPRTDYCVRTLTVEFDQECRRLTQFHYVNWPDHDVPSSFDSILDMIELMRK 215
Cdd:cd14611  82 N-EKCVLYWP---EKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDVEE 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41054756 216 HQQRDTT--PICVHCSAGCGRTGAICAIDYTWNLLKAGRIsedFNVFQLIQEMRTQRHSAVQTKEQYELVH 284
Cdd:cd14611 158 DRLASPGrgPVVVHCSAGIGRTGCFIATTIGCQQLKEEGV---VDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 85-289 4.63e-46

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: 160.99  E-value: 4.63e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  85 YINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRKKCERYFPlfgDEPMTFGPFRISCESE 164
Cdd:cd14632   1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP---DDSDTYGDIKITLLKT 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 165 QPRTDYCVRTLTVEFDQECRR--LTQFHYVNWPDHDVPSSFDSILDMIELMRKHQQRDTTPICVHCSAGCGRTGAICAID 242
Cdd:cd14632  78 ETLAEYSVRTFALERRGYSARheVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVLD 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 41054756 243 YTWNLLKAGRISEDFNVfqlIQEMRTQRHSAVQTKEQYELVHRAIAQ 289
Cdd:cd14632 158 VMLDMAECEGVVDIYNC---VKTLCSRRINMIQTEEQYIFIHDAILE 201
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 85-284 1.41e-45

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


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 159.47  E-value: 1.41e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  85 YINANFIKGIDgPQA--YIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRKKCERYFPLFGDEPMTFGPFRISCE 162
Cdd:cd14539   1 YINASLIEDLT-PYCprFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAITVSLQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 163 SEQPRTDYCVRTLTVEF--DQECRRLTQFHYVNWPDHDVPSSFDSILDMIELMRKH--QQRDT-TPICVHCSAGCGRTGA 237
Cdd:cd14539  80 SVRTTPTHVERIISIQHkdTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHylQQRSLqTPIVVHCSSGVGRTGA 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 41054756 238 ICAIDYTWNLLKAGRisEDFNVFQLIQEMRTQRHSAVQTKEQYELVH 284
Cdd:cd14539 160 FCLLYAAVQEIEAGN--GIPDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 51-284 2.42e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 162.48  E-value: 2.42e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756   51 EQEENVKKNRYKDILPFDHSRVkvTLKT-SNQDTDYINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMA 129
Cdd:PHA02747  47 EKPENQPKNRYWDIPCWDHNRV--ILDSgGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVML 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  130 C-REFEMGRKKCERYFPLFGDEPMTFGPFRISCESEQPRTDYcVRTL---TVEFDQECRRLTQFHYVNWPDHDVPSS--- 202
Cdd:PHA02747 125 TpTKGTNGEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKY-ILTLieiTDKILKDSRKISHFQCSEWFEDETPSDhpd 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  203 FDSILDMIELMRK-------HQQRDTTPICVHCSAGCGRTGAICAIDYTWN-LLKAGRISedfnVFQLIQEMRTQRHSAV 274
Cdd:PHA02747 204 FIKFIKIIDINRKksgklfnPKDALLCPIVVHCSDGVGKTGIFCAVDICLNqLVKRKAIC----LAKTAEKIREQRHAGI 279

                        250
                 ....*....|
gi 41054756  275 QTKEQYELVH 284
Cdd:PHA02747 280 MNFDDYLFIQ 289
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 55-286 6.23e-45

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: 160.66  E-value: 6.23e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  55 NVKKNRYKDILPFDHSRVKVTLKTSNQDTDYINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFE 134
Cdd:cd14629  53 NKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLRE 132

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 135 MGRKKCERYFPlfGDEPMTFGPFRISCESEQPRTDYCVRTLTV--EFDQECRRLTQFHYVNWPDHDVPSSFDSILDMIEL 212
Cdd:cd14629 133 MGREKCHQYWP--AERSARYQYFVVDPMAEYNMPQYILREFKVtdARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQ 210

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41054756 213 MRKHQQR--DTTPICVHCSAGCGRTGAICAIDYtwnLLKAGRISEDFNVFQLIQEMRTQRHSAVQTKEQYELVHRA 286
Cdd:cd14629 211 VHKTKEQfgQDGPITVHCSAGVGRTGVFITLSI---VLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRA 283
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 54-292 1.38e-44

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: 159.78  E-value: 1.38e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  54 ENVKKNRYKDILPFDHSRVKVtLKTSNQDTDYINANFIKGIDGPQA--YIATQGPLPNTVLDFWRMIWEYKVAVIVMACR 131
Cdd:cd14599  37 ENAERNRIREVVPYEENRVEL-VPTKENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTA 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 132 EFEMGRKKCERYFPLFGDE--PMTFGPFRISCESeqpRTD---YCVRTLTVEF---DQEcRRLTQFHYVNWPDHDVP--- 200
Cdd:cd14599 116 EEEGGRSKSHRYWPKLGSKhsSATYGKFKVTTKF---RTDsgcYATTGLKVKHllsGQE-RTVWHLQYTDWPDHGCPeev 191

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 201 SSFDSILDMIELMRKHQQR--DTT-----PICVHCSAGCGRTGAICAIDYTWNLLKAgriSEDFNVFQLIQEMRTQRHSA 273
Cdd:cd14599 192 QGFLSYLEEIQSVRRHTNSmlDSTkncnpPIVVHCSAGVGRTGVVILTELMIGCLEH---NEKVEVPVMLRHLREQRMFM 268

                       250
                ....*....|....*....
gi 41054756 274 VQTKEQYELVHRAIAQIFQ 292
Cdd:cd14599 269 IQTIAQYKFVYQVLIQFLK 287
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 55-286 1.90e-44

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: 159.51  E-value: 1.90e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  55 NVKKNRYKDILPFDHSRVKVTLKTSNQDTDYINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFE 134
Cdd:cd14627  53 NKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLRE 132

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 135 MGRKKCERYFPlfGDEPMTFGPFRISCESEQPRTDYCVRTLTV--EFDQECRRLTQFHYVNWPDHDVPSSFDSILDMIEL 212
Cdd:cd14627 133 MGREKCHQYWP--AERSARYQYFVVDPMAEYNMPQYILREFKVtdARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQ 210

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41054756 213 MRKHQQR--DTTPICVHCSAGCGRTGAICAIDYtwnLLKAGRISEDFNVFQLIQEMRTQRHSAVQTKEQYELVHRA 286
Cdd:cd14627 211 VHKTKEQfgQDGPISVHCSAGVGRTGVFITLSI---VLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQA 283
PHA02738 PHA02738
hypothetical protein; Provisional
 38-287 8.28e-43

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 155.85  E-value: 8.28e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756   38 KYRTEKIYPTdVGEQEENVKKNRYKDILPFDHSRVkvTLKTSNQDTDYINANFIKGIDGPQAYIATQGPLPNTVLDFWRM 117
Cdd:PHA02738  33 KVISEKVDGT-FNAEKKNRKLNRYLDAVCFDHSRV--ILPAERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRM 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  118 IWEYKVAVIVMACREFEMGRKKCERYFPLFGDEPMTFGPFRISCESEQPRTDYCVRTLTVEFDQEC-RRLTQFHYVNWPD 196
Cdd:PHA02738 110 LWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDGTSAtQTVTHFNFTAWPD 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  197 HDVPSSFDSILDMIELMRK-------------HQQRDTTPICVHCSAGCGRTGAICAIDYTWNLLKAgriSEDFNVFQLI 263
Cdd:PHA02738 190 HDVPKNTSEFLNFVLEVRQcqkelaqeslqigHNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDA---CATVSIPSIV 266

                        250       260
                 ....*....|....*....|....
gi 41054756  264 QEMRTQRHSAVQTKEQYELVHRAI 287
Cdd:PHA02738 267 SSIRNQRYYSLFIPFQYFFCYRAV 290
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 85-285 1.13e-41

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: 148.91  E-value: 1.13e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  85 YINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRKKCERYFPLFGDEpmTFGPFRISCESE 164
Cdd:cd14551   1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCW--TYGNLRVRVEDT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 165 QPRTDYCVRTLTVE---FDQECRR---LTQFHYVNWPDHDVPSSFDSILDMIELMRKHQQRDTTPICVHCSAGCGRTGAI 238
Cdd:cd14551  79 VVLVDYTTRKFCIQkvnRGIGEKRvrlVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGTF 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 41054756 239 CAIDYTWNLLKAGRiseDFNVFQLIQEMRTQRHSAVQTKEQYELVHR 285
Cdd:cd14551 159 IVIDAMLDMMHAEG---KVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 85-284 1.81e-39

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: 142.93  E-value: 1.81e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  85 YINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMaCREFEMGRKKCERYFPlfgDEPM-TFGPFRISCES 163
Cdd:cd14556   1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVM-LNQLDPKDQSCPQYWP---DEGSgTYGPIQVEFVS 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 164 EQPRTDYCVRTL----TVEFDQECRRLTQFHYVNWPDH-DVPSSFDSILDMIELMRKHQQR-DTTPICVHCSAGCGRTGA 237
Cdd:cd14556  77 TTIDEDVISRIFrlqnTTRPQEGYRMVQQFQFLGWPRDrDTPPSKRALLKLLSEVEKWQEQsGEGPIVVHCLNGVGRSGV 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 41054756 238 ICAIDYTWNLLKAGRIsedFNVFQLIQEMRTQRHSAVQTKEQYELVH 284
Cdd:cd14556 157 FCAISSVCERIKVENV---VDVFQAVKTLRNHRPNMVETEEQYKFCY 200
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 54-280 9.49e-39

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 144.37  E-value: 9.49e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756   54 ENVKKNRYKDILPFDHSRVkvTLKTSNQDTDYINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREF 133
Cdd:PHA02742  51 KNMKKCRYPDAPCFDRNRV--ILKIEDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIM 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  134 EMGRKKCERYFPLFGDEPMTFGPFRISCESEQPRTDYCVRTLTVEFDQECRRL--TQFHYVNWPDHDVPSSFDSILDMIE 211
Cdd:PHA02742 129 EDGKEACYPYWMPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLdiKHFAYEDWPHGGLPRDPNKFLDFVL 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  212 LMRKHQQR-----------DTTPICVHCSAGCGRTGAICAIDYTWNLLKAGRIsedFNVFQLIQEMRTQRHSAVQTKEQY 280
Cdd:PHA02742 209 AVREADLKadvdikgenivKEPPILVHCSAGLDRAGAFCAIDICISKYNERAI---IPLLSIVRDLRKQRHNCLSLPQQY 285
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
186-289 1.36e-38

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 137.10  E-value: 1.36e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756    186 LTQFHYVNWPDHDVPSSFDSILDMIELMRKHQQ--RDTTPICVHCSAGCGRTGAICAIDYTWNLLKAGRISedFNVFQLI 263
Cdd:smart00404   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNqsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGE--VDIFDTV 79

                           90       100
                   ....*....|....*....|....*.
gi 41054756    264 QEMRTQRHSAVQTKEQYELVHRAIAQ 289
Cdd:smart00404  80 KELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 186-289 1.36e-38

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


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 137.10  E-value: 1.36e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756    186 LTQFHYVNWPDHDVPSSFDSILDMIELMRKHQQ--RDTTPICVHCSAGCGRTGAICAIDYTWNLLKAGRISedFNVFQLI 263
Cdd:smart00012   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNqsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGE--VDIFDTV 79

                           90       100
                   ....*....|....*....|....*.
gi 41054756    264 QEMRTQRHSAVQTKEQYELVHRAIAQ 289
Cdd:smart00012  80 KELRSQRPGMVQTEEQYLFLYRALLE 105
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 52-300 2.06e-38

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 144.02  E-value: 2.06e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756   52 QEENVKKNRYKDILPFDHSRV-------------------KVTLKTSNQDTDYINANFIKGIDGPQAYIATQGPLPNTVL 112
Cdd:PHA02746  48 KKENLKKNRFHDIPCWDHSRVvinaheslkmfdvgdsdgkKIEVTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSE 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  113 DFWRMIWEYKVAVIVmACREFEMGRKKCERYFPLFGDEPMTFGPF-----RISCESEQPRTDYcvrTLTVEFDQECRRLT 187
Cdd:PHA02746 128 DFFKLISEHESQVIV-SLTDIDDDDEKCFELWTKEEDSELAFGRFvakilDIIEELSFTKTRL---MITDKISDTSREIH 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  188 QFHYVNWPDHDVPSSFDSILDMIELMRKHQQR----------DTTPICVHCSAGCGRTGAICAIDytwNLLKAGRISEDF 257
Cdd:PHA02746 204 HFWFPDWPDNGIPTGMAEFLELINKVNEEQAElikqadndpqTLGPIVVHCSAGIGRAGTFCAID---NALEQLEKEKEV 280

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 41054756  258 NVFQLIQEMRTQRHSAVQTKEQYELVHRAIAQIFQKQLKLLES 300
Cdd:PHA02746 281 CLGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAIIEEAKKKFF 323
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 85-280 8.83e-38

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: 138.37  E-value: 8.83e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  85 YINANFIKG---IDGPQaYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRK-KCERYFPLFGDEPMTFGPFRIS 160
Cdd:cd17658   1 YINASLVETpasESLPK-FIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEENESREFGRISVT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 161 CESEQ-PRTDYCVRTLTV---EFDQECRRLTQFHYVNWPDHDVPSSFDSILdmiELMRK--HQQRDTTPICVHCSAGCGR 234
Cdd:cd17658  80 NKKLKhSQHSITLRVLEVqyiESEEPPLSVLHIQYPEWPDHGVPKDTRSVR---ELLKRlyGIPPSAGPIVVHCSAGIGR 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 41054756 235 TGAICAIDYTWNLLKAGRISEdFNVFQLIQEMRTQRHSAVQTKEQY 280
Cdd:cd17658 157 TGAYCTIHNTIRRILEGDMSA-VDLSKTVRKFRSQRIGMVQTQDQY 201
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 85-292 3.56e-37

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: 137.41  E-value: 3.56e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  85 YINANFIK-GIDGPQ-AYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRKKCERYFPLFGDE--PMTFGPFRIS 160
Cdd:cd14598   1 YINASHIKvTVGGKEwDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRhnTVTYGRFKIT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 161 CESeqpRTD---YCVRTLTVEF---DQEcRRLTQFHYVNWPDHDVPSS---FDSILDMIELMRKHQQRDT------TPIC 225
Cdd:cd14598  81 TRF---RTDsgcYATTGLKIKHlltGQE-RTVWHLQYTDWPEHGCPEDlkgFLSYLEEIQSVRRHTNSTIdpkspnPPVL 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41054756 226 VHCSAGCGRTGAICAIDYTWNLLKAgriSEDFNVFQLIQEMRTQRHSAVQTKEQYELVHRAIAQIFQ 292
Cdd:cd14598 157 VHCSAGVGRTGVVILSEIMIACLEH---NEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 85-284 2.04e-27

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: 109.73  E-value: 2.04e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  85 YINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACrefEMGRKK-CERYFPlfGDEPMTFGPFR---IS 160
Cdd:cd14634   1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLN---EMDAAQlCMQYWP--EKTSCCYGPIQvefVS 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 161 CESEQPRTDYCVRTLTVEFDQECRRLTQ-FHYVNWPDH-DVPSSFDSILDMIELMRKHQQ----RDTTPIcVHCSAGCGR 234
Cdd:cd14634  76 ADIDEDIISRIFRICNMARPQDGYRIVQhLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEqydgREGRTV-VHCLNGGGR 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 41054756 235 TGAICAIDYTWNLLKAGRIsedFNVFQLIQEMRTQRHSAVQTKEQYELVH 284
Cdd:cd14634 155 SGTFCAICSVCEMIQQQNI---IDVFHTVKTLRNNKSNMVETLEQYKFVY 201
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 85-284 1.27e-25

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: 104.72  E-value: 1.27e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  85 YINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMaCREFEMGrKKCERYFPLFGdePMTFGPFRISCESE 164
Cdd:cd14636   1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVM-LNEVDLA-QGCPQYWPEEG--MLRYGPIQVECMSC 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 165 QPRTDYCVRTLTV---EFDQECRRLT-QFHYVNWPDH-DVPSSFDSILDMIELMRKHQQR----DTTPIcVHCSAGCGRT 235
Cdd:cd14636  77 SMDCDVISRIFRIcnlTRPQEGYLMVqQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEEcdegEGRTI-IHCLNGGGRS 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 41054756 236 GAICAIDYTWNLLKAGRIsedFNVFQLIQEMRTQRHSAVQTKEQYELVH 284
Cdd:cd14636 156 GMFCAISIVCEMIKRQNV---VDVFHAVKTLRNSKPNMVETPEQYRFCY 201
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 85-282 1.57e-21

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


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 92.77  E-value: 1.57e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  85 YINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVM--ACREFEmgrkKCERYFPLfGDEPMTFGPFRISC- 161
Cdd:cd14550   1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMltDNELNE----DEPIYWPT-KEKPLECETFKVTLs 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 162 -ESEQPRTDYC---VRTLTVEFDQECRRLT--QFHYVNWPDHDVPSSfdSILDMIELMRKHQQRDTTPICVHCSAGCGRT 235
Cdd:cd14550  76 gEDHSCLSNEIrliVRDFILESTQDDYVLEvrQFQCPSWPNPCSPIH--TVFELINTVQEWAQQRDGPIVVHDRYGGVQA 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 41054756 236 GAICAidytWNLLKAGRISED-FNVFQLIQEMRTQRHSAVQTKEQYEL 282
Cdd:cd14550 154 ATFCA----LTTLHQQLEHESsVDVYQVAKLYHLMRPGVFTSKEDYQF 197
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 85-287 9.69e-20

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: 87.74  E-value: 9.69e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  85 YINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRKKCErYFPlFGDEPMTFGPFRISCESE 164
Cdd:cd17669   1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWP-NKDEPINCETFKVTLIAE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 165 QPR-----TDYCVRTLTVEFDQECRRLTQFHYV--NWPDHDVPSSfdSILDMIELMRKHQQRDTTPICVHCSAGCGRTGA 237
Cdd:cd17669  79 EHKclsneEKLIIQDFILEATQDDYVLEVRHFQcpKWPNPDSPIS--KTFELISIIKEEAANRDGPMIVHDEHGGVTAGT 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 41054756 238 ICAIdytWNLLKAGRISEDFNVFQLIQEMRTQRHSAVQTKEQYELVHRAI 287
Cdd:cd17669 157 FCAL---TTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 85-284 1.77e-19

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: 87.05  E-value: 1.77e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  85 YINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMaCREFEMGrKKCERYFPLFGDEpmTFGPFR---ISC 161
Cdd:cd14635   1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVM-LNDVDPA-QLCPQYWPENGVH--RHGPIQvefVSA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 162 ESEQPRTDYCVRTLTVEFDQECRRLT-QFHYVNWPDH-DVPSSFDSILDMIELMRKHQQR---DTTPICVHCSAGCGRTG 236
Cdd:cd14635  77 DLEEDIISRIFRIYNAARPQDGYRMVqQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEyngGEGRTVVHCLNGGGRSG 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 41054756 237 AICAIDYTWNLLKAgriSEDFNVFQLIQEMRTQRHSAVQTKEQYELVH 284
Cdd:cd14635 157 TFCAISIVCEMLRH---QRAVDVFHAVKTLRNNKPNMVDLLDQYKFCY 201
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 85-287 8.25e-19

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: 85.12  E-value: 8.25e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  85 YINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRKKCErYFPlFGDEPMTFGPFRIS---- 160
Cdd:cd17670   1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFV-YWP-SREESMNCEAFTVTlisk 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 161 ---CESEQPRT---DYCVRTLTVEFDQECRrltQFHYVNWPDHDVPSSfdSILDMIELMRKHQQRDTTPICVHCSAGCGR 234
Cdd:cd17670  79 drlCLSNEEQIiihDFILEATQDDYVLEVR---HFQCPKWPNPDAPIS--STFELINVIKEEALTRDGPTIVHDEFGAVS 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 41054756 235 TGAICAIDYTWNLLKAGRISEDFNVFQLIQEMRTQRHSAVqtkEQYELVHRAI 287
Cdd:cd17670 154 AGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDI---EQYQFLYKAM 203
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 85-280 5.13e-18

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: 82.65  E-value: 5.13e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  85 YINANFIKGIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRK-KCERYFPlfgdEP--MTFGPFRISC 161
Cdd:cd14637   1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWP----EPglQQYGPMEVEF 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 162 ESEQPRTDYCVRTLTVE----FDQECRRLTQFHYVNW-PDHDVPSSFDSILDMIELMRKHQQ--RDTTPIcVHCSAGCGR 234
Cdd:cd14637  77 VSGSADEDIVTRLFRVQnitrLQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQResGEGRTV-VHCLNGGGR 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 41054756 235 TGAICAIDYTWNLLKAGRISEdfnVFQLIQEMRTQRHSAVQTKEQY 280
Cdd:cd14637 156 SGTYCASAMILEMIRCHNIVD---VFYAVKTLRNYKPNMVETLEQY 198
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 59-282 1.19e-15

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: 76.28  E-value: 1.19e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  59 NRYKDIlpfdHSRVkvtlktSNQDTDYINANFIKgIDGPQAYIATQGPLPNTVLDFWRMIWEYKVAVIVMACREFEMGRK 138
Cdd:cd14559   1 NRFTNI----QTRV------STPVGKNLNANRVQ-IGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRK 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 139 KCERYFPLFGdepmTFGpfRISCESEQPRTDYCVRTLTVefDQECRRLTQ---------FHYVNWPDHDVPSSfDSILDM 209
Cdd:cd14559  70 GLPPYFRQSG----TYG--SVTVKSKKTGKDELVDGLKA--DMYNLKITDgnktitipvVHVTNWPDHTAISS-EGLKEL 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 210 IELMRKHQQRDTT-----------------PIcVHCSAGCGRTGAICAidyTWNLLKAgriSEDFNVFQLIQEMRTQR-H 271
Cdd:cd14559 141 ADLVNKSAEEKRNfykskgssaindknkllPV-IHCRAGVGRTGQLAA---AMELNKS---PNNLSVEDIVSDMRTSRnG 213

                       250
                ....*....|.
gi 41054756 272 SAVQTKEQYEL 282
Cdd:cd14559 214 KMVQKDEQLDT 224
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 32-298 2.44e-14

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 73.85  E-value: 2.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756   32 LRRLSTKYRTEKIYPTDVGEQEENVKKNRYKD------ILPFDHSRVKVtlktsNQDTDYINANFIKGIDGPQAYIATQG 105
Cdd:PHA02740  24 LSCIIKEYRAIVPEHEDEANKACAQAENKAKDenlalhITRLLHRRIKL-----FNDEKVLDARFVDGYDFEQKFICIIN 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  106 PLPNTVLDFWRMIWEYKVAVIVMACREFEmgrKKC-ERYFPLFGDEPMTFGPFRISCES--EQPRTDYCVRTLTVEFDQE 182
Cdd:PHA02740  99 LCEDACDKFLQALSDNKVQIIVLISRHAD---KKCfNQFWSLKEGCVITSDKFQIETLEiiIKPHFNLTLLSLTDKFGQA 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  183 cRRLTQFHYVNWP----DHDVPSSFD---SILDMIELMRKHQQ-RDTTPICVHCSAGCGRTGAICAIDYTWNLL-KAGRI 253
Cdd:PHA02740 176 -QKISHFQYTAWPadgfSHDPDAFIDffcNIDDLCADLEKHKAdGKIAPIIIDCIDGISSSAVFCVFDICATEFdKTGML 254

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 41054756  254 SedfnVFQLIQEMRTQRHSAVQTKEQYELVHRAIAQIFQKQLKLL 298
Cdd:PHA02740 255 S----IANALKKVRQKKYGCMNCLDDYVFCYHLIAAYLKEKFDIL 295
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 97-285 3.85e-10

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: 57.36  E-value: 3.85e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  97 PQAYIATQGPLPNtVLDFWRMIWEYKVAVIVMACrefemgrkkceryfplfgdepmtfgpfrisceseqprtdycvrtlt 176
Cdd:cd14494   6 PLRLIAGALPLSP-LEADSRFLKQLGVTTIVDLT---------------------------------------------- 38

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 177 vefdqecrrltqfhyvnwpdhdvpssfDSILDMIELMRKHQQRDTTPICVHCSAGCGRTGAICAIDytwnLLKAGRISed 256
Cdd:cd14494  39 ---------------------------LAMVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACY----LVLLGGMS-- 85

                       170       180       190
                ....*....|....*....|....*....|
gi 41054756 257 fnVFQLIQEMRTQR-HSAVQTKEQYELVHR 285
Cdd:cd14494  86 --AEEAVRIVRLIRpGGIPQTIEQLDFLIK 113
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 189-284 3.91e-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: 59.67  E-value: 3.91e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 189 FHYVNWPDHDVPSsFDSILDMIELMRKHQQRDTTpICVHCSAGCGRTG-AICAIdytwnLLKAGRISEDfnvfQLIQEMR 267
Cdd:cd14506  79 FYNFGWKDYGVPS-LTTILDIVKVMAFALQEGGK-VAVHCHAGLGRTGvLIACY-----LVYALRMSAD----QAIRLVR 147

                        90
                ....*....|....*..
gi 41054756 268 TQRHSAVQTKEQYELVH 284
Cdd:cd14506 148 SKRPNSIQTRGQVLCVR 164
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
188-285 1.51e-09

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 56.52  E-value: 1.51e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 188 QFHYVNWPDHDVPS--SFDSILDMIElmrkHQQRDTTPICVHCSAGCGRTGAICAIdytwnLLkagrISEDFNVFQLIQE 265
Cdd:COG2453  49 EYLHLPIPDFGAPDdeQLQEAVDFID----EALREGKKVLVHCRGGIGRTGTVAAA-----YL----VLLGLSAEEALAR 115

                        90       100
                ....*....|....*....|
gi 41054756 266 MRTQRHSAVQTKEQYELVHR 285
Cdd:COG2453 116 VRAARPGAVETPAQRAFLER 135
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 186-285 7.35e-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: 49.18  E-value: 7.35e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 186 LTQFHYVnWPDHDVPSSFDSILDMIELMRKhQQRDTTPICVHCSAGCGRTGAICAidytwNLLKagRISEDFNVFQLIQE 265
Cdd:cd14505  73 ITWHHLP-IPDGGVPSDIAQWQELLEELLS-ALENGKKVLIHCKGGLGRTGLIAA-----CLLL--ELGDTLDPEQAIAA 143

                        90       100
                ....*....|....*....|
gi 41054756 266 MRTQRHSAVQTKEQYELVHR 285
Cdd:cd14505 144 VRALRPGAIQTPKQENFLHQ 163
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 199-283 3.12e-06

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


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 46.89  E-value: 3.12e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 199 VPSSFDSILDMIELMRKHQQRDTtPICVHCSAGCGRTGAICAIdYtwnLLKAGRISEDfnvfQLIQEMRTQRHSAVQTKE 278
Cdd:cd14504  61 TPPTLEQIDEFLDIVEEANAKNE-AVLVHCLAGKGRTGTMLAC-Y---LVKTGKISAV----DAINEIRRIRPGSIETSE 131


                ....*
gi 41054756 279 QYELV 283
Cdd:cd14504 132 QEKFV 136
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 188-240 2.05e-05

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: 44.88  E-value: 2.05e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 41054756 188 QFHYVNWPDHDVPSsFDSILDMIELMRKHQQRDttP---ICVHCSAGCGRTGAICA 240
Cdd:cd14497  62 RVLHYGFPDHHPPP-LGLLLEIVDDIDSWLSED--PnnvAVVHCKAGKGRTGTVIC 114
PHA03247 PHA03247
large tegument protein UL36; Provisional
 314-566 1.30e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.31  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756   314 DSSPEKHTPNSDEEQWDTPPPKPPRLRSVQGEcavqeeiLQAPEPRPVPPILRPSPASALRTVSSARHSDTYHPKPLLSD 393
Cdd:PHA03247 2606 GDPRGPAPPSPLPPDTHAPDPPPPSPSPAANE-------PDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASS 2678

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756   394 PePSDPEPS---------THFTDPDHHSSDPEPSEPERRVERLAVEIQKVALQEGPR-PLHLLLQSPAHAPALSFT-NPL 462
Cdd:PHA03247 2679 P-PQRPRRRaarptvgslTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPAlPAAPAPPAVPAGPATPGGpARP 2757

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756   463 HTHTHSHTLPDTHPTAAGGTAEqqnQRRATHMSIAGHTLHTESSEEQPAGAADTAPLQAsgdttAAPRENDAEQKSTETP 542
Cdd:PHA03247 2758 ARPPTTAGPPAPAPPAAPAAGP---PRRLTRPAVASLSESRESLPSPWDPADPPAAVLA-----PAAALPPAASPAGPLP 2829

                         250       260
                  ....*....|....*....|....
gi 41054756   543 VSGTKAEIGfgrrCSPPRGPREPP 566
Cdd:PHA03247 2830 PPTSAQPTA----PPPPPGPPPPS 2849
PHA03247 PHA03247
large tegument protein UL36; Provisional
 331-567 6.05e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 6.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756   331 TPPPKPPRLRSVQGECAVQEEILQAPEPRPVPPILRPSPASALRTVSSARHSDTYHPKPLLSDPEPSDPE--PSTHFTDP 408
Cdd:PHA03247 2707 TPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAagPPRRLTRP 2786

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756   409 DHHSSDPE----PSEPERRVERLAVEIQKVALQEGPRPLHLLLQSPAHAPALSFTNPLHTHThshTLPDTHPTAAGGTAE 484
Cdd:PHA03247 2787 AVASLSESreslPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPP---SLPLGGSVAPGGDVR 2863

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756   485 QQNQRRATHMSIAGHTLHTESSEEQPAGAADTAPLQASGDTTAAPRENDAEQKSTETPVSGTKAeigfgRRCSPPRGPRE 564
Cdd:PHA03247 2864 RRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPP-----QPQPPPPPPPR 2938


                  ...
gi 41054756   565 PPS 567
Cdd:PHA03247 2939 PQP 2941
PHA03247 PHA03247
large tegument protein UL36; Provisional
 315-567 1.02e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756   315 SSPEKHTPNSDEEQWDTPPPKPPRLRSVQGECAvqeeilQAPEPRPVPPILRPSPASALRTVSSARHSDTYHPKPLLSDP 394
Cdd:PHA03247 2637 EPDPHPPPTVPPPERPRDDPAPGRVSRPRRARR------LGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEP 2710

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756   395 EPSDPEPSTHFTDPDHHSSDPEPSEPERRVERLAVEIQKVALQEGPRPLHLLLQSPAHAPALSftNPLHTHTHSHTLPDT 474
Cdd:PHA03247 2711 APHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPA--APAAGPPRRLTRPAV 2788

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756   475 HPTAAGGTAEQQNQRRATHMSIAGHTLHTESSEEQPAG--AADTAPLQASGDTTAAPREndaeqksTETPVSGTKAEIGF 552
Cdd:PHA03247 2789 ASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGplPPPTSAQPTAPPPPPGPPP-------PSLPLGGSVAPGGD 2861

                         250
                  ....*....|....*
gi 41054756   553 GRRCSPPRGPREPPS 567
Cdd:PHA03247 2862 VRRRPPSRSPAAKPA 2876
PHA03247 PHA03247
large tegument protein UL36; Provisional
 330-567 1.78e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756   330 DTPPPKPPRLRSVQGECAVqeeilqaPEPRPVPpilRPS-PASALRTVSSARHSDTYHPKPLLSDPEPSDPEPSTHFTDP 408
Cdd:PHA03247 2550 DPPPPLPPAAPPAAPDRSV-------PPPRPAP---RPSePAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPP 2619

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756   409 DHHSSDPEPSEPErrverlaveiqkvalqegPRPLHLLLQSPAHAPalsftnplhththshtlPDTHPTAAGGTAEQQNQ 488
Cdd:PHA03247 2620 DTHAPDPPPPSPS------------------PAANEPDPHPPPTVP-----------------PPERPRDDPAPGRVSRP 2664

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756   489 RRATHMSIAGHTLHTESSEEQPAGAADTAPLQASGDTTAAPRENDAEQKSTETPV-SGTKAEIGFGRRCSPPRGPREPPS 567
Cdd:PHA03247 2665 RRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATpLPPGPAAARQASPALPAAPAPPAV 2744
PHA03132 PHA03132
thymidine kinase; Provisional
 290-429 2.27e-03

thymidine kinase; Provisional


Pssm-ID: 222997 [Multi-domain]  Cd Length: 580  Bit Score: 40.90  E-value: 2.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756  290 IFQKQLKLLESPTNSEvTDGTLQEDSSPEKHTPNSDEEQWDTPPPKPPRLRSVQGECAVQEEILqaPEPRPVPPILRPSP 369
Cdd:PHA03132  29 FDAERDDFLTPLGSTS-EATSEDDDDLYPPRETGSGGGVATSTIYTVPRPPRGPEQTLDKPDSL--PASRELPPGPTPVP 105

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41054756  370 ASALRTVSSAR-HSDTYHPKPLLSDPEPSDPEPSTHFTDPDHHSSDPEPSEPERRVERLAV 429
Cdd:PHA03132 106 PGGFRGASSPRlGADSTSPRFLYQVNFPVILAPIGESNSSSEELSEEEEHSRPPPSESLKV 166
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 189-284 3.43e-03

protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase/transmembrane phosphatase with tensin homology; Voltage-sensitive phosphatase (VSP) proteins comprise a family of phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. This family is conserved in deuterostomes; VSP was first identified as a sperm flagellar plasma membrane protein in Ciona intestinalis. Gene duplication events in primates resulted in the presence of paralogs, transmembrane phosphatase with tensin homology (TPTE) and TPTE2, that retain protein domain architecture but, in the case of TPTE, have lost catalytic activity. TPTE, also called cancer/testis antigen 44 (CT44), may play a role in the signal transduction pathways of the endocrine or spermatogenic function of the testis. TPTE2, also called TPTE and PTEN homologous inositol lipid phosphatase (TPIP), occurs in several differentially spliced forms; TPIP alpha displays phosphoinositide 3-phosphatase activity and is localized on the endoplasmic reticulum, while TPIP beta is cytosolic and lacks detectable phosphatase activity. VSP/TPTE proteins contain an N-terminal voltage sensor consisting of four transmembrane segments, a protein tyrosine phosphatase (PTP)-like phosphoinositide phosphatase catalytic domain, followed by a regulatory C2 domain.


Pssm-ID: 350360 [Multi-domain]  Cd Length: 177  Bit Score: 38.88  E-value: 3.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 189 FHY----VNWPDHDVPSsFDSILDMIELMRKHQQRD-TTPICVHCSAGCGRTG-AICAidytWnLLKAGRISEDFNVFQL 262
Cdd:cd14510  72 FHNrverVPIDDHNVPT-LDEMLSFTAEVREWMAADpKNVVAIHCKGGKGRTGtMVCA----W-LIYSGQFESAKEALEY 145

                        90       100
                ....*....|....*....|....*..
gi 41054756 263 IQEMRT-----QRHSAVQTKEQYELVH 284
Cdd:cd14510 146 FGERRTdksvsSKFQGVETPSQSRYVG 172
DUSP14 cd14572
dual specificity protein phosphatase 14; dual specificity protein phosphatase 14 (DUSP14), ...
 188-254 3.72e-03

dual specificity protein phosphatase 14; dual specificity protein phosphatase 14 (DUSP14), also called mitogen-activated protein kinase (MAPK) phosphatase 6 (MKP-6) or MKP-1-like protein tyrosine phosphatase (MKP-L), 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. DUSP14 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. DUSP14 dephosphorylates JNK, ERK, and p38 in vitro. It also directly interacts and dephosphorylates TGF-beta-activated kinase 1 (TAK1)-binding protein 1 (TAB1) in T cells, and negatively regulates TCR signaling and immune responses.


Pssm-ID: 350420 [Multi-domain]  Cd Length: 150  Bit Score: 38.31  E-value: 3.72e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41054756 188 QFHYVNWPDHDVPSS-----FDSILDMI-ELMRKHQQrdttpICVHCSAGCGRTGAICaIDYtwnLLKAGRIS 254
Cdd:cd14572  51 QFEYVKVPLADMPHApislyFDSVADKIhSVGRKHGA-----TLVHCAAGVSRSATLC-IAY---LMKYHRVS 114
PTP-IVa1 cd18537
protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), ...
 172-278 4.71e-03

protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), also known as protein-tyrosine phosphatase of regenerating liver 1 (PRL-1), stimulates progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. It may play a role in the development and maintenance of differentiating epithelial tissues. PRL-1 promotes cell growth and migration by activating both the ERK1/2 and RhoA pathways. It is a member of the PTP-IVa/PRL family of small, prenylated phosphatases that are the most oncogenic of all PTPs. PRLs associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation.


Pssm-ID: 350513 [Multi-domain]  Cd Length: 167  Bit Score: 38.13  E-value: 4.71e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054756 172 VRTLTVEFDQECRRLTQFHYVNWP-DHDVPSSFDSILDMIELMR-KHQQRDTTPICVHCSAGCGRTGAICAIdytwNLLK 249
Cdd:cd18537  46 VRVCEATYDTTLVEKEGIQVLDWPfDDGAPPSNQIVDDWLNLLKvKFREEPGCCIAVHCVAGLGRAPVLVAL----ALIE 121

                        90       100
                ....*....|....*....|....*....
gi 41054756 250 AGRISEDfnvfqLIQEMRTQRHSAVQTKE 278
Cdd:cd18537 122 CGMKYED-----AVQFIRQKRRGAFNSKQ 145
 
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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