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Conserved domains on  [gi|2462538648|ref|XP_054231263|]
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tyrosine-protein phosphatase non-receptor type 21 isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 760-1046 0e+00

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


The actual alignment was detected with superfamily member cd14599:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 287  Bit Score: 541.51  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  760 RCKILEQRLEQGMVFTEYERILKKRlVDGECSTARLPENAERNRFQDVLPYDDVRVELVPTKENNTGYINASHIKVSVSG 839
Cdd:cd14599      1 RCKTLERKLEEGMVFTEYEQIPKKK-ADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  840 IEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSRHNTVTYGRFKITTRFRTDSGCYATT 919
Cdd:cd14599     80 EEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATT 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  920 GLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTSD-PQSPNPPLLVHCSAGVGRTGVVILS 998
Cdd:cd14599    160 GLKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSMLDsTKNCNPPIVVHCSAGVGRTGVVILT 239

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2462538648  999 EIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQFLK 1046
Cdd:cd14599    240 ELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
FERM_C_PTPN14_PTPN21 cd13188
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and ...
 94-184 6.55e-53

FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and 21); This CD contains PTP members: pez/PTPN14 and PTPN21. A number of mutations in Pez have been shown to be associated with breast and colorectal cancer. The PTPN protein family belong to larger family of PTPs. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. The members are composed of a N-terminal FERM domain and a C-terminal PTP catalytic domain. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. Like most other ERM members they have a phosphoinositide-binding site in their FERM domain. The FERM C domain is the third structural domain within the FERM domain. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


:

Pssm-ID: 270009  Cd Length: 91  Bit Score: 179.41  E-value: 6.55e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648   94 YGEESYPAKDSQGSDISIGACLEGIFVKHKNGRHPVVFRWHDIANMSHNKSFFALELANKEETIQFQTEDMETAKYIWRL 173
Cdd:cd13188      1 YGEESFPAKDEQGNEVLIGASLEGIFVKHDNGRPPVFFRWEDIKNVINHKRTFSIECQNSEETVQFQFEDAETAKYVWKL 80

                           90
                   ....*....|.
gi 2462538648  174 CVARHKFYRLN 184
Cdd:cd13188     81 CVLQHKFYRQN 91
B41 super family cl33382
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 27-99 8.08e-09

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


The actual alignment was detected with superfamily member smart00295:

Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 56.53  E-value: 8.08e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462538648    27 ADFGDFDQYES--QDFLQKFALFPVGWLQDEKvLEEATQKVALLHQKYRGLTAPDAEMLYMQEVERMDGYGEESY 99
Cdd:smart00295  128 AEFGDYDEELHdlRGELSLKRFLPKQLLDSRK-LKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
 
Name Accession Description Interval E-value
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 760-1046 0e+00

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: 541.51  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  760 RCKILEQRLEQGMVFTEYERILKKRlVDGECSTARLPENAERNRFQDVLPYDDVRVELVPTKENNTGYINASHIKVSVSG 839
Cdd:cd14599      1 RCKTLERKLEEGMVFTEYEQIPKKK-ADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  840 IEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSRHNTVTYGRFKITTRFRTDSGCYATT 919
Cdd:cd14599     80 EEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATT 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  920 GLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTSD-PQSPNPPLLVHCSAGVGRTGVVILS 998
Cdd:cd14599    160 GLKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSMLDsTKNCNPPIVVHCSAGVGRTGVVILT 239

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2462538648  999 EIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQFLK 1046
Cdd:cd14599    240 ELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
773-1043 7.51e-100

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 314.98  E-value: 7.51e-100
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648   773 VFTEYERILKKRLVDGECSTARLPENAERNRFQDVLPYDDVRVELVPTKENNTGYINASHIKVSVSgiEWDYIATQGPLQ 852
Cdd:smart00194    2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNG--PKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648   853 NTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSRhnTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQER 932
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGE--PLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETR 157

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648   933 TVWHLQYTDWPEHGCPEDLKGFLSYLEEIqsvrRHTNSTSDPqspnpPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLD 1012
Cdd:smart00194  158 TVTHYHYTNWPDHGVPESPESILDLIRAV----RKSQSTSTG-----PIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVD 228

                           250       260       270
                    ....*....|....*....|....*....|.
gi 2462538648  1013 IPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQ 1043
Cdd:smart00194  229 IFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
798-1043 1.84e-91

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 291.45  E-value: 1.84e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  798 NAERNRFQDVLPYDDVRVELVPTKENNtGYINASHIKVSvsGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEE 877
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPS-DYINASYIDGY--KKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  878 EGGREKSFRYWPRlgSRHNTVTYGRFKITTR-FRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLS 956
Cdd:pfam00102   78 EKGREKCAQYWPE--EEGESLEYGDFTVTLKkEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLD 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  957 YLEEIQSVRrhtnstsdPQSPNPPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTF 1036
Cdd:pfam00102  156 LLRKVRKSS--------LDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIF 227


                   ....*..
gi 2462538648 1037 VYRVLIQ 1043
Cdd:pfam00102  228 LYDAILE 234
FERM_C_PTPN14_PTPN21 cd13188
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and ...
 94-184 6.55e-53

FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and 21); This CD contains PTP members: pez/PTPN14 and PTPN21. A number of mutations in Pez have been shown to be associated with breast and colorectal cancer. The PTPN protein family belong to larger family of PTPs. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. The members are composed of a N-terminal FERM domain and a C-terminal PTP catalytic domain. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. Like most other ERM members they have a phosphoinositide-binding site in their FERM domain. The FERM C domain is the third structural domain within the FERM domain. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270009  Cd Length: 91  Bit Score: 179.41  E-value: 6.55e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648   94 YGEESYPAKDSQGSDISIGACLEGIFVKHKNGRHPVVFRWHDIANMSHNKSFFALELANKEETIQFQTEDMETAKYIWRL 173
Cdd:cd13188      1 YGEESFPAKDEQGNEVLIGASLEGIFVKHDNGRPPVFFRWEDIKNVINHKRTFSIECQNSEETVQFQFEDAETAKYVWKL 80

                           90
                   ....*....|.
gi 2462538648  174 CVARHKFYRLN 184
Cdd:cd13188     81 CVLQHKFYRQN 91
PHA02738 PHA02738
hypothetical protein; Provisional
 776-1048 2.57e-50

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 180.89  E-value: 2.57e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  776 EYERILKKRlVDGECSTARlpENAERNRFQDVLPYDDVRVELvPTKENNTGYINASHikvsVSGIEWD--YIATQGPLQN 853
Cdd:PHA02738    30 EHQKVISEK-VDGTFNAEK--KNRKLNRYLDAVCFDHSRVIL-PAERNRGDYINANY----VDGFEYKkkFICGQAPTRQ 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  854 TCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLgsRHNTVTYGRFKITTRFRTDSGCYATTGLKMKHLlTGQERT 933
Cdd:PHA02738   102 TCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDV--EQGSIRFGKFKITTTQVETHPHYVKSTLLLTDG-TSATQT 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  934 VWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRR--HTNS--TSDPQSPNPPLLVHCSAGVGRTGVVILSEIMIACLEHNE 1009
Cdd:PHA02738   179 VTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCQKelAQESlqIGHNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACA 258

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 2462538648 1010 VLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQFLKSS 1048
Cdd:PHA02738   259 TVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRYVNLT 297
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
796-1043 7.48e-31

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 123.28  E-value: 7.48e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  796 PENAERNRFQDVLPYDDVRVElvptkeNNTGYINASHIKVsvsGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTA 875
Cdd:COG5599     40 INGSPLNRFRDIQPYKETALR------ANLGYLNANYIQV---IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLAS 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  876 EEEGG--REKSFRYWPRLGSrhntvtYGRFKI------TTRFRTDSGCYATTgLKMKHllTGQE-RTVWHLQYTDWPEHG 946
Cdd:COG5599    111 DDEISkpKVKMPVYFRQDGE------YGKYEVsselteSIQLRDGIEARTYV-LTIKG--TGQKkIEIPVLHVKNWPDHG 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  947 CPEDlkgflSYLEEIQSVRRHTNSTSDPqsPNPPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDI---PRVLDMLRQQ 1023
Cdd:COG5599    182 AISA-----EALKNLADLIDKKEKIKDP--DKLLPVVHCRAGVGRTGTLIACLALSKSINALVQITLsveEIVIDMRTSR 254

                          250       260
                   ....*....|....*....|
gi 2462538648 1024 RMMLVQTLCQYTFVYRVLIQ 1043
Cdd:COG5599    255 NGGMVQTSEQLDVLVKLAEQ 274
FERM_C pfam09380
FERM C-terminal PH-like domain;
103-185 2.18e-27

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 106.18  E-value: 2.18e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  103 DSQGSDISIGACLEGIFVKHKNGRHPVVFRWHDIANMSHNKSFFALELANK--EETIQFQTEDMETAKYIWRLCVARHKF 180
Cdd:pfam09380    1 DKEGTDLWLGVSAKGILVYEDNNKILNLFPWREIRKISFKRKKFLIKLRDKssEETLGFYTESSRACKYLWKLCVEQHTF 80


                   ....*
gi 2462538648  181 YRLNQ 185
Cdd:pfam09380   81 FRLRR 85
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 27-99 8.08e-09

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 56.53  E-value: 8.08e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462538648    27 ADFGDFDQYES--QDFLQKFALFPVGWLQDEKvLEEATQKVALLHQKYRGLTAPDAEMLYMQEVERMDGYGEESY 99
Cdd:smart00295  128 AEFGDYDEELHdlRGELSLKRFLPKQLLDSRK-LKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 27-91 5.60e-08

FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases, the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 271216  Cd Length: 99  Bit Score: 51.48  E-value: 5.60e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462538648   27 ADFGDFDQYESQD-FLQKFALFPVgWLQDEKVLEEATQKVALLHQKYRGLTAPDAEMLYMQEVERM 91
Cdd:cd14473     35 AEYGDYDPSEHKPkYLSLKRFLPK-QLLKQRKPEEWEKRIVELHKKLRGLSPAEAKLKYLKIARKL 99
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 27-97 2.18e-07

FERM central domain; This domain is the central structural domain of the FERM domain.


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 50.35  E-value: 2.18e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462538648   27 ADFGDFDQYESQ-DFLQKFALFPVgWLQDEKVLEEATQKVALLHQKYRGLTAPDAEMLYMQEVERMDGYGEE 97
Cdd:pfam00373   45 AEFGDYQPSSHTsEYLSLESFLPK-QLLRKMKSKELEKRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVE 115
 
Name Accession Description Interval E-value
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 760-1046 0e+00

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: 541.51  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  760 RCKILEQRLEQGMVFTEYERILKKRlVDGECSTARLPENAERNRFQDVLPYDDVRVELVPTKENNTGYINASHIKVSVSG 839
Cdd:cd14599      1 RCKTLERKLEEGMVFTEYEQIPKKK-ADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  840 IEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSRHNTVTYGRFKITTRFRTDSGCYATT 919
Cdd:cd14599     80 EEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATT 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  920 GLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTSD-PQSPNPPLLVHCSAGVGRTGVVILS 998
Cdd:cd14599    160 GLKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSMLDsTKNCNPPIVVHCSAGVGRTGVVILT 239

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2462538648  999 EIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQFLK 1046
Cdd:cd14599    240 ELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 827-1046 1.55e-178

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: 518.76  E-value: 1.55e-178
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  827 YINASHIKVSVSGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSRHNTVTYGRFKIT 906
Cdd:cd14598      1 YINASHIKVTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRHNTVTYGRFKIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  907 TRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTSDPQSPNPPLLVHCS 986
Cdd:cd14598     81 TRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTIDPKSPNPPVLVHCS 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  987 AGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQFLK 1046
Cdd:cd14598    161 AGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 827-1045 3.56e-143

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: 427.26  E-value: 3.56e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  827 YINASHIKVSVSGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSRHNTVTYGRFKIT 906
Cdd:cd14540      1 YINASHITATVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHDALTFGEYKVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  907 TRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTSDPQSPNPPLLVHCS 986
Cdd:cd14540     81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRRHTNQDVAGHNRNPPTLVHCS 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462538648  987 AGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQFL 1045
Cdd:cd14540    161 AGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
773-1043 7.51e-100

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 314.98  E-value: 7.51e-100
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648   773 VFTEYERILKKRLVDGECSTARLPENAERNRFQDVLPYDDVRVELVPTKENNTGYINASHIKVSVSgiEWDYIATQGPLQ 852
Cdd:smart00194    2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNG--PKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648   853 NTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSRhnTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQER 932
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGE--PLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETR 157

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648   933 TVWHLQYTDWPEHGCPEDLKGFLSYLEEIqsvrRHTNSTSDPqspnpPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLD 1012
Cdd:smart00194  158 TVTHYHYTNWPDHGVPESPESILDLIRAV----RKSQSTSTG-----PIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVD 228

                           250       260       270
                    ....*....|....*....|....*....|.
gi 2462538648  1013 IPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQ 1043
Cdd:smart00194  229 IFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
798-1043 1.84e-91

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 291.45  E-value: 1.84e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  798 NAERNRFQDVLPYDDVRVELVPTKENNtGYINASHIKVSvsGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEE 877
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPS-DYINASYIDGY--KKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  878 EGGREKSFRYWPRlgSRHNTVTYGRFKITTR-FRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLS 956
Cdd:pfam00102   78 EKGREKCAQYWPE--EEGESLEYGDFTVTLKkEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLD 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  957 YLEEIQSVRrhtnstsdPQSPNPPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTF 1036
Cdd:pfam00102  156 LLRKVRKSS--------LDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIF 227


                   ....*..
gi 2462538648 1037 VYRVLIQ 1043
Cdd:pfam00102  228 LYDAILE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 827-1039 5.70e-76

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: 248.35  E-value: 5.70e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  827 YINASHIKVSvsGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSrhNTVTYGRFKIT 906
Cdd:cd00047      1 YINASYIDGY--RGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGG--KPLEYGDITVT 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  907 TRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHtnstsdpqsPNPPLLVHCS 986
Cdd:cd00047     77 LVSEEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARK---------PNGPIVVHCS 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462538648  987 AGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYR 1039
Cdd:cd00047    148 AGVGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 758-1037 5.21e-69

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: 232.05  E-value: 5.21e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  758 DERCKILEQRLEQGMVFTEYERILKKRlvDGECST-ARLPENAERNRFQDVLPYDDVRVELvptkENNTGYINASHIKVS 836
Cdd:cd14600      1 EESMAQLKKGLESGTVLIQFEQLYRKK--PGLAITcAKLPQNMDKNRYKDVLPYDATRVVL----QGNEDYINASYVNME 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  837 VSG--IEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLgsrHNTVTYGRFKITTRFRTDSG 914
Cdd:cd14600     75 IPSanIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDP---PDVMEYGGFRVQCHSEDCTI 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  915 CYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHtnstsdpqspNPPLLVHCSAGVGRTGV 994
Cdd:cd14600    152 AYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRVE----------NEPVLVHCSAGIGRTGV 221

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 2462538648  995 VILSEIMIACLEHNE---VLDIPRvldMLRQQRMMLVQTLCQYTFV 1037
Cdd:cd14600    222 LVTMETAMCLTERNQpvyPLDIVR---KMRDQRAMMVQTSSQYKFV 264
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 798-1047 2.21e-64

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: 218.10  E-value: 2.21e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  798 NAERNRFQDVLPYDDVRVEL--VPTKENNTGYINASHIKVSVSGIEWD-----YIATQGPLQNTCQDFWQMVWEQGIAII 870
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILkdRDPNVPGSDYINANYIRNENEGPTTDenaktYIATQGCLENTVSDFWSMVWQENSRVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  871 AMVTAEEEGGREKSFRYWPRLGsrhNTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQ-ERTVWHLQYTDWPEHGCPE 949
Cdd:cd14544     81 VMTTKEVERGKNKCVRYWPDEG---MQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDpIREIWHYQYLSWPDHGVPS 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  950 DLKGFLSYLEEIqsvrrHTNSTSDPQSpnPPLLVHCSAGVGRTGVVILSEIMIACLEHNEVL---DIPRVLDMLRQQRMM 1026
Cdd:cd14544    158 DPGGVLNFLEDV-----NQRQESLPHA--GPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDcdiDIQKTIQMVRSQRSG 230

                          250       260
                   ....*....|....*....|.
gi 2462538648 1027 LVQTLCQYTFVYRVLIQFLKS 1047
Cdd:cd14544    231 MVQTEAQYKFIYVAVAQYIET 251
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 827-1037 2.87e-61

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: 207.95  E-value: 2.87e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  827 YINASHIKVSVSGIEW--DYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGsrhNTVTYGRFK 904
Cdd:cd14541      2 YINANYVNMEIPGSGIvnRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLG---ETMQFGNLQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  905 ITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYleeIQSVRRHTnstsdpQSPNPPLLVH 984
Cdd:cd14541     79 ITCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDF---VKRVRQNR------VGMVEPTVVH 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462538648  985 CSAGVGRTGVVILSEIMIACLEHNE---VLDIPRvlDMlRQQRMMLVQTLCQYTFV 1037
Cdd:cd14541    150 CSAGIGRTGVLITMETAMCLIEANEpvyPLDIVR--TM-RDQRAMLIQTPSQYRFV 202
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 827-1038 3.22e-61

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: 207.87  E-value: 3.22e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  827 YINASHIKVSVSGIEwDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRlgsrhNTVTYGRFKIT 906
Cdd:cd18533      1 YINASYITLPGTSSK-RYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPS-----GEYEGEYGDLT 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  907 TRFRT----DSGCYATTGLKMKHlLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNStsdpqspNPPLL 982
Cdd:cd18533     75 VELVSeeenDDGGFIVREFELSK-EDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASL-------DPPII 146

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462538648  983 VHCSAGVGRTGVVILSEIMIACLE--HNEVLD-------IPRVLDMLRQQRMMLVQTLCQYTFVY 1038
Cdd:cd18533    147 VHCSAGVGRTGTFIALDSLLDELKrgLSDSQDledsedpVYEIVNQLRKQRMSMVQTLRQYIFLY 211
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 827-1045 1.52e-60

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: 205.69  E-value: 1.52e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  827 YINASHIKVSVSGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRlGSRHNTVTYGRFKIT 906
Cdd:cd14538      1 YINASHIRIPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPD-SLNKPLICGGRLEVS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  907 TRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYleeIQSVRRHTNSTsdpqspnpPLLVHCS 986
Cdd:cd14538     80 LEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRF---IRYMRRIHNSG--------PIVVHCS 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462538648  987 AGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQFL 1045
Cdd:cd14538    149 AGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 773-1038 6.21e-59

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: 203.36  E-value: 6.21e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  773 VFTEYERIlKKRLVDGECSTARLPENAERNRFQDVLPYDDVRVELVPTKEN-NTGYINASHikvsVSGIEWD--YIATQG 849
Cdd:cd14543      5 IYEEYEDI-RREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDeRTDYINANF----MDGYKQKnaYIATQG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  850 PLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGsrHNTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTG 929
Cdd:cd14543     80 PLPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEE--GSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETD 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  930 QERTVWHLQYTDWPEHGCPEDLKGFLSYLEEiqsVRRHTNS-------TSDPQSPNPPLLVHCSAGVGRTGVVILSEIMI 1002
Cdd:cd14543    158 ESRQVTHFQFTSWPDFGVPSSAAALLDFLGE---VRQQQALavkamgdRWKGHPPGPPIVVHCSAGIGRTGTFCTLDICL 234

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 2462538648 1003 ACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVY 1038
Cdd:cd14543    235 SQLEDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 797-1045 9.56e-58

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: 198.90  E-value: 9.56e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  797 ENAERNRFQDVLPYDDVRVELvptkENNTGYINASHIKVSVSGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAE 876
Cdd:cd14597      2 ENRKKNRYKNILPYDTTRVPL----GDEGGYINASFIKMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  877 EEGGREKSFRYWPRLGSRhNTVTYGRFKIT-TRFRTDSGcYATTGLKMKHLLTGQERTVWHLQYTDWPEHGC---PEDLK 952
Cdd:cd14597     78 VEGGKIKCQRYWPEILGK-TTMVDNRLQLTlVRMQQLKN-FVIRVLELEDIQTREVRHITHLNFTAWPDHDTpsqPEQLL 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  953 GFLSYLeeiqsvrRHTNSTSdpqspnpPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLC 1032
Cdd:cd14597    156 TFISYM-------RHIHKSG-------PIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTED 221

                          250
                   ....*....|...
gi 2462538648 1033 QYTFVYRVLIQFL 1045
Cdd:cd14597    222 QYIFCYQVILYVL 234
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 797-1047 2.52e-53

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: 187.15  E-value: 2.52e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  797 ENAERNRFQDVLPYDDVRVELVPTKENNTG--YINASHI------KVSVSGIEWDYIATQGPLQNTCQDFWQMVWEQGIA 868
Cdd:cd14605      1 ENKNKNRYKNILPFDHTRVVLHDGDPNEPVsdYINANIImpefetKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  869 IIAMVTAEEEGGREKSFRYWPRLGSRHNtvtYGRFKITTRFRTDSGCYATTGLKMKHLLTGQ-ERTVWHLQYTDWPEHGC 947
Cdd:cd14605     81 VIVMTTKEVERGKSKCVKYWPDEYALKE---YGVMRVRNVKESAAHDYILRELKLSKVGQGNtERTVWQYHFRTWPDHGV 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  948 PEDLKGFLSYLEEIqsvrrhtNSTSDPQSPNPPLLVHCSAGVGRTGVVILSEIMIACLEHNEV---LDIPRVLDMLRQQR 1024
Cdd:cd14605    158 PSDPGGVLDFLEEV-------HHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQR 230

                          250       260
                   ....*....|....*....|...
gi 2462538648 1025 MMLVQTLCQYTFVYRVLIQFLKS 1047
Cdd:cd14605    231 SGMVQTEAQYRFIYMAVQHYIET 253
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 796-1047 3.26e-53

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: 187.01  E-value: 3.26e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  796 PENAERNRFQDVLPYDDVRVELVPTKENNTG--YINASHIKVSVSGIEWD---YIATQGPLQNTCQDFWQMVWEQGIAII 870
Cdd:cd14606     16 PENKSKNRYKNILPFDHSRVILQGRDSNIPGsdYINANYVKNQLLGPDENaktYIASQGCLEATVNDFWQMAWQENSRVI 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  871 AMVTAEEEGGREKSFRYWPRLGSrhnTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQE-RTVWHLQYTDWPEHGCPE 949
Cdd:cd14606     96 VMTTREVEKGRNKCVPYWPEVGM---QRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGELiREIWHYQYLSWPDHGVPS 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  950 DLKGFLSYLEEIqsvrrhtNSTSDPQSPNPPLLVHCSAGVGRTGVVILSEIMIACLEHNEV---LDIPRVLDMLRQQRMM 1026
Cdd:cd14606    173 EPGGVLSFLDQI-------NQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSG 245

                          250       260
                   ....*....|....*....|.
gi 2462538648 1027 LVQTLCQYTFVYRVLIQFLKS 1047
Cdd:cd14606    246 MVQTEAQYKFIYVAIAQFIET 266
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 787-1043 4.41e-53

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: 186.57  E-value: 4.41e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  787 DGECST--ARLPENAERNRFQDVLPYDDVRVELVP-TKENNTGYINASHIKVSVsgIEWDYIATQGPLQNTCQDFWQMVW 863
Cdd:cd14603     17 DYVCSTvaGGRKENVKKNRYKDILPYDQTRVILSLlQEEGHSDYINANFIKGVD--GSRAYIATQGPLSHTVLDFWRMIW 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  864 EQGIAIIAMVTAEEEGGREKSFRYWPrlgSRHNTVTYGRFKITTrfRTDSGCYATTGLKMKHLLTGQE-RTVWHLQYTDW 942
Cdd:cd14603     95 QYGVKVILMACREIEMGKKKCERYWA---QEQEPLQTGPFTITL--VKEKRLNEEVILRTLKVTFQKEsRSVSHFQYMAW 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  943 PEHGCPEDLKGFLSYLEEiqsVRRHTNSTSDpqspnpPLLVHCSAGVGRTGVVILSEIMIACL------EHNEVLDIprV 1016
Cdd:cd14603    170 PDHGIPDSPDCMLAMIEL---ARRLQGSGPE------PLCVHCSAGCGRTGVICTVDYVRQLLltqripPDFSIFDV--V 238

                          250       260
                   ....*....|....*....|....*..
gi 2462538648 1017 LDMlRQQRMMLVQTLCQYTFVYRVLIQ 1043
Cdd:cd14603    239 LEM-RKQRPAAVQTEEQYEFLYHTVAQ 264
FERM_C_PTPN14_PTPN21 cd13188
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and ...
 94-184 6.55e-53

FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and 21); This CD contains PTP members: pez/PTPN14 and PTPN21. A number of mutations in Pez have been shown to be associated with breast and colorectal cancer. The PTPN protein family belong to larger family of PTPs. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. The members are composed of a N-terminal FERM domain and a C-terminal PTP catalytic domain. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. Like most other ERM members they have a phosphoinositide-binding site in their FERM domain. The FERM C domain is the third structural domain within the FERM domain. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270009  Cd Length: 91  Bit Score: 179.41  E-value: 6.55e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648   94 YGEESYPAKDSQGSDISIGACLEGIFVKHKNGRHPVVFRWHDIANMSHNKSFFALELANKEETIQFQTEDMETAKYIWRL 173
Cdd:cd13188      1 YGEESFPAKDEQGNEVLIGASLEGIFVKHDNGRPPVFFRWEDIKNVINHKRTFSIECQNSEETVQFQFEDAETAKYVWKL 80

                           90
                   ....*....|.
gi 2462538648  174 CVARHKFYRLN 184
Cdd:cd13188     81 CVLQHKFYRQN 91
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 793-1039 1.83e-51

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: 181.18  E-value: 1.83e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  793 ARLPENAERNRFQDVLPYDDVRVELVPTKE-NNTGYINASHIkvsvSGIEWD--YIATQGPLQNTCQDFWQMVWEQGIAI 869
Cdd:cd14554      1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGvEGSDYINASFI----DGYRQRgaYIATQGPLAETTEDFWRMLWEHNSTI 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  870 IAMVTAEEEGGREKSFRYWPrlgsRHNTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPE 949
Cdd:cd14554     77 IVMLTKLREMGREKCHQYWP----AERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPK 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  950 DLKGFLSYLEEIQsvrrhtnSTSDPQSPNPPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQ 1029
Cdd:cd14554    153 SGEGFIDFIGQVH-------KTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQ 225

                          250
                   ....*....|
gi 2462538648 1030 TLCQYTFVYR 1039
Cdd:cd14554    226 TEDQYQFCYR 235
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 827-1037 7.31e-51

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: 178.21  E-value: 7.31e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  827 YINASHIKVSV--SGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSrhnTVTYGRFK 904
Cdd:cd14601      2 YINANYINMEIpsSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSG---SSSYGGFQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  905 ITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNStsdpqspnpPLLVH 984
Cdd:cd14601     79 VTCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDE---------PVVVH 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462538648  985 CSAGVGRTGVVILSEIMIACLEHNEV---LDIPRVldmLRQQRMMLVQTLCQYTFV 1037
Cdd:cd14601    150 CSAGIGRTGVLITMETAMCLIECNQPvypLDIVRT---MRDQRAMMIQTPSQYRFV 202
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 827-1038 1.59e-50

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


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 177.16  E-value: 1.59e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  827 YINASHikvsVSGIEWD--YIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSRhntvTYGRFK 904
Cdd:cd14549      1 YINANY----VDGYNKAraYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTE----TYGNIQ 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  905 ITTRFRTDSGCYATTGLKMKHL------LTGQERTVWHLQYTDWPEHGCPEDLKGFLSYleeiqsVRRhtNSTSDPQSPN 978
Cdd:cd14549     73 VTLLSTEVLATYTVRTFSLKNLklkkvkGRSSERVVYQYHYTQWPDHGVPDYTLPVLSF------VRK--SSAANPPGAG 144

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  979 pPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVY 1038
Cdd:cd14549    145 -PIVVHCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 798-1043 2.51e-50

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350401 [Multi-domain]  Cd Length: 238  Bit Score: 177.97  E-value: 2.51e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  798 NAERNRFQDVLPYDDVRVELVPTK-ENNTGYINASHIkvsvSGI--EWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVT 874
Cdd:cd14553      3 NKPKNRYANVIAYDHSRVILQPIEgVPGSDYINANYC----DGYrkQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  875 AEEEGGREKSFRYWPRLGsrhnTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGF 954
Cdd:cd14553     79 KLEERSRVKCDQYWPTRG----TETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPF 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  955 LSYLeeiQSVRRHTNSTSDpqspnpPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQY 1034
Cdd:cd14553    155 LAFL---RRVKACNPPDAG------PIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQY 225


                   ....*....
gi 2462538648 1035 TFVYRVLIQ 1043
Cdd:cd14553    226 IFIHDALLE 234
PHA02738 PHA02738
hypothetical protein; Provisional
 776-1048 2.57e-50

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 180.89  E-value: 2.57e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  776 EYERILKKRlVDGECSTARlpENAERNRFQDVLPYDDVRVELvPTKENNTGYINASHikvsVSGIEWD--YIATQGPLQN 853
Cdd:PHA02738    30 EHQKVISEK-VDGTFNAEK--KNRKLNRYLDAVCFDHSRVIL-PAERNRGDYINANY----VDGFEYKkkFICGQAPTRQ 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  854 TCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLgsRHNTVTYGRFKITTRFRTDSGCYATTGLKMKHLlTGQERT 933
Cdd:PHA02738   102 TCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDV--EQGSIRFGKFKITTTQVETHPHYVKSTLLLTDG-TSATQT 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  934 VWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRR--HTNS--TSDPQSPNPPLLVHCSAGVGRTGVVILSEIMIACLEHNE 1009
Cdd:PHA02738   179 VTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCQKelAQESlqIGHNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACA 258

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 2462538648 1010 VLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQFLKSS 1048
Cdd:PHA02738   259 TVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRYVNLT 297
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 776-1047 7.33e-50

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: 178.39  E-value: 7.33e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  776 EYERILKKRLVDGECSTARLPENAERNRFQDVLPYDDVRVELVPTKE-NNTGYINASHIKVSVSgiEWDYIATQGPLQNT 854
Cdd:cd14628     30 EFKRLASSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGvEGSDYINASFIDGYRQ--QKAYIATQGPLAET 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  855 CQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRlgsrHNTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQERTV 934
Cdd:cd14628    108 TEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPA----ERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTV 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  935 WHLQYTDWPEHGCPEDLKGFLSYLEEIqsvrrhtNSTSDPQSPNPPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIP 1014
Cdd:cd14628    184 RQFQFTDWPEQGVPKSGEGFIDFIGQV-------HKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIF 256

                          250       260       270
                   ....*....|....*....|....*....|...
gi 2462538648 1015 RVLDMLRQQRMMLVQTLCQYTFVYRVLIQFLKS 1047
Cdd:cd14628    257 QTVKMLRTQRPAMVQTEDQYQFCYRAALEYLGS 289
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 802-1039 7.43e-50

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: 176.05  E-value: 7.43e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  802 NRFQDVLPYDDVRVELvPTKENN--TGYINASHIKvSVSGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEG 879
Cdd:cd14547      1 NRYKTILPNEHSRVCL-PSVDDDplSSYINANYIR-GYDGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  880 gREKSFRYWPRLgsrhNTVTYGRFKITTRFRTDSGCYATTGLKMKHllTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLE 959
Cdd:cd14547     79 -KEKCAQYWPEE----ENETYGDFEVTVQSVKETDGYTVRKLTLKY--GGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQ 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  960 EIQSVRRHTNSTsdpqspnPPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYR 1039
Cdd:cd14547    152 EVEEARQTEPHR-------GPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 803-1038 5.29e-49

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar proteins; R3 subfamily receptor-type phosphotyrosine phosphatases (RPTP) are characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. Vertebrate members include receptor-type tyrosine-protein phosphatase-like O (PTPRO), J (PTPRJ), Q (PTPRQ), B (PTPRB), V (PTPRV) and H (PTPRH). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Most members are PTPs, except for PTPRQ, which dephosphorylates phosphatidylinositide substrates. PTPRV is characterized only in rodents; its function has been lost in humans. Both vertebrate and invertebrate R3 subfamily RPTPs are involved in the control of a variety of cellular processes, including cell growth, differentiation, mitotic cycle and oncogenic transformation.


Pssm-ID: 350396 [Multi-domain]  Cd Length: 222  Bit Score: 173.31  E-value: 5.29e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  803 RFQDVLPYDDVRVELVP-TKENNTGYINASHIKVSVSGIEwdYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGR 881
Cdd:cd14548      1 RYTNILPYDHSRVKLIPiNEEEGSDYINANYIPGYNSPRE--FIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  882 EKSFRYWPrlgSRHNTVTYGrfKITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYleeI 961
Cdd:cd14548     79 VKCDHYWP---FDQDPVYYG--DITVTMLSESVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRF---V 150

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462538648  962 QSVRRHTNstsdpqSPNPPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVY 1038
Cdd:cd14548    151 RLVRDYIK------QEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 777-1046 6.84e-49

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: 175.21  E-value: 6.84e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  777 YERIlKKRLVDGECSTARLPENAERNRFQDVLPYDDVRVELvpTKENNTgYINASHIKVSVSgiEWDYIATQGPLQNTCQ 856
Cdd:cd14608      5 YQDI-RHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKL--HQEDND-YINASLIKMEEA--QRSYILTQGPLPNTCG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  857 DFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSRHNTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQERTVWH 936
Cdd:cd14608     79 HFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILH 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  937 LQYTDWPEHGCPEDLKGFLSYLEEIqsvrRHTNSTSdPQspNPPLLVHCSAGVGRTGVVILSEIMIACLEHNE---VLDI 1013
Cdd:cd14608    159 FHYTTWPDFGVPESPASFLNFLFKV----RESGSLS-PE--HGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKdpsSVDI 231

                          250       260       270
                   ....*....|....*....|....*....|...
gi 2462538648 1014 PRVLDMLRQQRMMLVQTLCQYTFVYRVLIQFLK 1046
Cdd:cd14608    232 KKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAK 264
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 783-1047 7.79e-49

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: 175.31  E-value: 7.79e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  783 KRLVDGECSTAR-----LPENAERNRFQDVLPYDDVRVELVPTKE-NNTGYINASHIKVSVSgiEWDYIATQGPLQNTCQ 856
Cdd:cd14627     33 KRLANSKAHTSRfisanLPCNKFKNRLVNIMPYETTRVCLQPIRGvEGSDYINASFIDGYRQ--QKAYIATQGPLAETTE 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  857 DFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPrlgsRHNTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQERTVWH 936
Cdd:cd14627    111 DFWRMLWENNSTIVVMLTKLREMGREKCHQYWP----AERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQ 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  937 LQYTDWPEHGCPEDLKGFLSYLEEIqsvrrhtNSTSDPQSPNPPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRV 1016
Cdd:cd14627    187 FQFTDWPEQGVPKSGEGFIDFIGQV-------HKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQT 259

                          250       260       270
                   ....*....|....*....|....*....|.
gi 2462538648 1017 LDMLRQQRMMLVQTLCQYTFVYRVLIQFLKS 1047
Cdd:cd14627    260 VKMLRTQRPAMVQTEDEYQFCYQAALEYLGS 290
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 827-1046 6.47e-48

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: 169.93  E-value: 6.47e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  827 YINASHIKVSVSGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRlgSRHNTVTYGRFKIT 906
Cdd:cd14596      1 YINASYITMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPE--TLQEPMELENYQLR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  907 TRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCP---EDLKGFLSYLeeiqsvrRHTNSTSdpqspnpPLLV 983
Cdd:cd14596     79 LENYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPqssDQLVKFICYM-------RKVHNTG-------PIVV 144

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462538648  984 HCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQFLK 1046
Cdd:cd14596    145 HCSAGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 802-1042 2.15e-47

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: 168.97  E-value: 2.15e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  802 NRFQDVLPYDDVRVELVP-TKENNTGYINASHIKVSVSGIEwdYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGG 880
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQlGGEPHSDYINANFIPGYTSPQE--FIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  881 REKSFRYWPrlgSRHNTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEe 960
Cdd:cd14618     79 RVLCDHYWP---SESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRE- 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  961 iqSVRRHTNSTSDpqspNPPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRV 1040
Cdd:cd14618    155 --LVREHVQATKG----KGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSC 228


                   ..
gi 2462538648 1041 LI 1042
Cdd:cd14618    229 IL 230
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 801-1043 2.67e-47

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: 168.87  E-value: 2.67e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  801 RNRFQDVLPYDDVRVEL-VPTKENNTGYINASHIKvSVSGIEwDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEG 879
Cdd:cd14602      1 KNRYKDILPYDHSRVELsLITSDEDSDYINANFIK-GVYGPR-AYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEM 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  880 GREKSFRYWPRLGSrhNTVTYGRFKITTRFRTDSGCYATTGLKMKhlLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLE 959
Cdd:cd14602     79 GKKKCERYWAEPGE--MQLEFGPFSVTCEAEKRKSDYIIRTLKVK--FNSETRTIYQFHYKNWPDHDVPSSIDPILELIW 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  960 EIQSVRRHTnstsdpqspNPPLLVHCSAGVGRTGVVILSEIMIACLEHN---EVLDIPRVLDMLRQQRMMLVQTLCQYTF 1036
Cdd:cd14602    155 DVRCYQEDD---------SVPICIHCSAGCGRTGVICAIDYTWMLLKDGiipENFSVFSLIQEMRTQRPSLVQTKEQYEL 225


                   ....*..
gi 2462538648 1037 VYRVLIQ 1043
Cdd:cd14602    226 VYNAVIE 232
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 802-1039 4.74e-47

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: 168.07  E-value: 4.74e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  802 NRFQDVLPYDDVRVELVPTKENNTGYINASHIKVSVSGIEwdYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGR 881
Cdd:cd14615      1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKE--FIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  882 EKSFRYWPRLGSRhntvTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEei 961
Cdd:cd14615     79 TKCEEYWPSKQKK----DYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRH-- 152

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462538648  962 qSVRRHtnstSDPQSPNPPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYR 1039
Cdd:cd14615    153 -LVREY----MKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 225
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 802-1039 5.51e-47

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: 167.79  E-value: 5.51e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  802 NRFQDVLPYDDVRVELVPTKENN-TGYINASHIkvSVSGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGG 880
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPcSDYINASYI--PGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  881 REKSFRYWPrlgSRHNTVTYGrfKITTRFRTDSGCYATTGLKMKHLLTGQ---ERTVWHLQYTDWPEHGCPEDLKGFLSY 957
Cdd:cd14617     79 RVKCDHYWP---ADQDSLYYG--DLIVQMLSESVLPEWTIREFKICSEEQldaPRLVRHFHYTVWPDHGVPETTQSLIQF 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  958 leeIQSVRRHTNSTSDPQspnpPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFV 1037
Cdd:cd14617    154 ---VRTVRDYINRTPGSG----PTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYL 226


                   ..
gi 2462538648 1038 YR 1039
Cdd:cd14617    227 HQ 228
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 801-1038 6.13e-47

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: 167.95  E-value: 6.13e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  801 RNRFQDVLPYDDVRVELvptKENNTGYINASHIKVSVSGIEwdYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGG 880
Cdd:cd14545      3 RYRDRDPYDHDRSRVKL---KQGDNDYINASLVEVEEAKRS--YILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  881 REKSFRYWPRLGSRHNTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLee 960
Cdd:cd14545     78 QIKCAQYWPQGEGNAMIFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFL-- 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  961 iQSVRRHTNSTSDPQspnpPLLVHCSAGVGRTGVVILSEIMIACLEHNEV--LDIPRVLDMLRQQRMMLVQTLCQYTFVY 1038
Cdd:cd14545    156 -QKVRESGSLSSDVG----PPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 827-1038 8.80e-47

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: 166.41  E-value: 8.80e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  827 YINASHIKvSVSGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRlgSRHNTVTYGRFKIT 906
Cdd:cd14539      1 YINASLIE-DLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPT--ERGQALVYGAITVS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  907 TRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTsdpqspNPPLLVHCS 986
Cdd:cd14539     78 LQSVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSL------QTPIVVHCS 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462538648  987 AGVGRTGV-VILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVY 1038
Cdd:cd14539    152 SGVGRTGAfCLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 802-1045 2.62e-46

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: 166.22  E-value: 2.62e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  802 NRFQDVLPYDDVRVELVPTKENNTG-YINASHIKVSVSGIEwdYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGG 880
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIHEEPGSdYINANYMPGYWSSQE--FIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  881 REKSFRYWPRlgsRHNTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEe 960
Cdd:cd14619     79 RVKCEHYWPL---DYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRR- 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  961 iqSVRRHTNSTsdpQSPNPPlLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRV 1040
Cdd:cd14619    155 --LLRQWLDQT---MSGGPT-VVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQC 228


                   ....*
gi 2462538648 1041 LIQFL 1045
Cdd:cd14619    229 ILDFL 233
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 795-1044 1.06e-45

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: 165.01  E-value: 1.06e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  795 LPENAERNRFQDVLPYDDVRVEL--VPTKENNTGYINASHIKvSVSGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAM 872
Cdd:cd14612     12 IPGHASKDRYKTILPNPQSRVCLrrAGSQEEEGSYINANYIR-GYDGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVM 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  873 VTAEEEgGREKSFRYWPRLGSrhntvTYGRFKITTRFRTDSGCYATTGLKMKHllTGQERTVWHLQYTDWPEHGCPEDLK 952
Cdd:cd14612     91 ITKLKE-KKEKCVHYWPEKEG-----TYGRFEIRVQDMKECDGYTIRDLTIQL--EEESRSVKHYWFSSWPDHQTPESAG 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  953 GFLSYLEEIQSVRRhtnstsdpQSPNP-PLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTL 1031
Cdd:cd14612    163 PLLRLVAEVEESRQ--------TAASPgPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTS 234

                          250
                   ....*....|...
gi 2462538648 1032 CQYTFVYRVLIQF 1044
Cdd:cd14612    235 EQYQFLHHTLALY 247
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 773-1043 1.10e-45

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: 165.98  E-value: 1.10e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  773 VFTEYERILKKRLVDGECSTArlPENAERNRFQDVLPYDDVRVELVP---TKENNTGYINASHikvsVSGIEWD--YIAT 847
Cdd:cd17667      4 DFEEVQRCTADMNITAEHSNH--PDNKHKNRYINILAYDHSRVKLRPlpgKDSKHSDYINANY----VDGYNKAkaYIAT 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  848 QGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPrlgsRHNTVTYGRFKITTRFRTDSGCYATTGL-----K 922
Cdd:cd17667     78 QGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWP----TENSEEYGNIIVTLKSTKIHACYTVRRFsirntK 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  923 MKHLLTGQ------ERTVWHLQYTDWPEHGCPEDLKGFLSYleeiqsVRRhtnsTSDPQSPN-PPLLVHCSAGVGRTGVV 995
Cdd:cd17667    154 VKKGQKGNpkgrqnERTVIQYHYTQWPDMGVPEYALPVLTF------VRR----SSAARTPEmGPVLVHCSAGVGRTGTY 223

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2462538648  996 ILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQ 1043
Cdd:cd17667    224 IVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 271
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 792-1047 1.75e-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: 165.67  E-value: 1.75e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  792 TARLPENAERNRFQDVLPYDDVRVELVPTKE-NNTGYINASHIKVSVSgiEWDYIATQGPLQNTCQDFWQMVWEQGIAII 870
Cdd:cd14629     47 SANLPCNKFKNRLVNIMPYELTRVCLQPIRGvEGSDYINASFIDGYRQ--QKAYIATQGPLAETTEDFWRMLWEHNSTIV 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  871 AMVTAEEEGGREKSFRYWPrlgsRHNTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPED 950
Cdd:cd14629    125 VMLTKLREMGREKCHQYWP----AERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKT 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  951 LKGFLSYLEEIqsvrrhtNSTSDPQSPNPPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQT 1030
Cdd:cd14629    201 GEGFIDFIGQV-------HKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQT 273

                          250
                   ....*....|....*..
gi 2462538648 1031 LCQYTFVYRVLIQFLKS 1047
Cdd:cd14629    274 EDQYQLCYRAALEYLGS 290
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 793-1038 2.12e-45

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: 164.37  E-value: 2.12e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  793 ARLPENAERNRFQDVLPYDDVRVELVPTkENNtgYINAShiKVSVSGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAM 872
Cdd:cd14607     19 AKYPENRNRNRYRDVSPYDHSRVKLQNT-END--YINAS--LVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVM 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  873 VTAEEEGGREKSFRYWPRLGSRHNTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLK 952
Cdd:cd14607     94 LNRIVEKDSVKCAQYWPTDEEEVLSFKETGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTTWPDFGVPESPA 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  953 GFLSYLEEIqsvrRHTNSTSdPQspNPPLLVHCSAGVGRTGVVILSEIMIACLEHNE--VLDIPRVLDMLRQQRMMLVQT 1030
Cdd:cd14607    174 SFLNFLFKV----RESGSLS-PE--HGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGLIQT 246


                   ....*...
gi 2462538648 1031 LCQYTFVY 1038
Cdd:cd14607    247 PDQLRFSY 254
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 797-1046 5.23e-45

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: 164.72  E-value: 5.23e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  797 ENAERNRFQDVLPYDDVRVEL-VPTKENNTGYINASHIKvSVSGIEwDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTA 875
Cdd:cd14604     56 ENVKKNRYKDILPFDHSRVKLtLKTSSQDSDYINANFIK-GVYGPK-AYIATQGPLANTVIDFWRMIWEYNVAIIVMACR 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  876 EEEGGREKSFRYWPRLGSrhNTVTYGRFKIT---TRFRTDSgCYATTGLKMKHlltgQERTVWHLQYTDWPEHGCPEDlk 952
Cdd:cd14604    134 EFEMGRKKCERYWPLYGE--EPMTFGPFRISceaEQARTDY-FIRTLLLEFQN----ETRRLYQFHYVNWPDHDVPSS-- 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  953 gFLSYLEEIQSVRRHTnstsdpQSPNPPLLVHCSAGVGRTGVVILSEIMIACLEHN---EVLDIPRVLDMLRQQRMMLVQ 1029
Cdd:cd14604    205 -FDSILDMISLMRKYQ------EHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGkipEEFNVFNLIQEMRTQRHSAVQ 277

                          250
                   ....*....|....*..
gi 2462538648 1030 TLCQYTFVYRVLIQFLK 1046
Cdd:cd14604    278 TKEQYELVHRAIAQLFE 294
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 802-1039 1.00e-43

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: 158.53  E-value: 1.00e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  802 NRFQDVLPYDDVRVELVPTKEN-NTGYINASHIKVSVSGIEwdYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGG 880
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGVpGSDYINASYISGYLCPNE--FIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  881 REKSFRYWPRlgSRHNTVTYGRFKITTRFRTDSGCYATTGLKM-KHlltGQERTVWHLQYTDWPEHGCPEDLKGFLSYLE 959
Cdd:cd14616     79 RIRCHQYWPE--DNKPVTVFGDIVITKLMEDVQIDWTIRDLKIeRH---GDYMMVRQCNFTSWPEHGVPESSAPLIHFVK 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  960 EIQSVRRHTNStsdpqspnpPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYR 1039
Cdd:cd14616    154 LVRASRAHDNT---------PMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 755-1043 1.63e-43

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: 159.82  E-value: 1.63e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  755 ATNDERCKIleqrlEQGMVFT-EYERILKKRLVDGECSTarLPENAERNRFQDVLPYDDVRVELVPTKE-NNTGYINASH 832
Cdd:cd14626      4 ADNIERLKA-----NDGLKFSqEYESIDPGQQFTWENSN--LEVNKPKNRYANVIAYDHSRVILTSVDGvPGSDYINANY 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  833 IKVSVSgiEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSRhntvTYGRFKITTRFRTD 912
Cdd:cd14626     77 IDGYRK--QNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTE----TYGMIQVTLLDTVE 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  913 SGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVrrhtnstsdpqspNP----PLLVHCSAG 988
Cdd:cd14626    151 LATYSVRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKAC-------------NPpdagPMVVHCSAG 217

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462538648  989 VGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQ 1043
Cdd:cd14626    218 VGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 827-1039 2.19e-43

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: 156.53  E-value: 2.19e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  827 YINASHIKVSVSGIEwdYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLgsRHNTVTYGRFKIT 906
Cdd:cd14557      1 YINASYIDGFKEPRK--YIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSM--EEGSRAFGDVVVK 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  907 TRFRTDSGCYATTGLKMKHLL-TGQERTVWHLQYTDWPEHGCPEDLKGFLsyleeiqSVRRHTNSTSDPQSpnPPLLVHC 985
Cdd:cd14557     77 INEEKICPDYIIRKLNINNKKeKGSGREVTHIQFTSWPDHGVPEDPHLLL-------KLRRRVNAFNNFFS--GPIVVHC 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462538648  986 SAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYR 1039
Cdd:cd14557    148 SAGVGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 827-1041 1.97e-42

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: 153.96  E-value: 1.97e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  827 YINASHIkvsvSGIEWD--YIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSrhntVTYGRFK 904
Cdd:cd14552      1 YINASFI----DGYRQKdaYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGS----VSSGDIT 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  905 ITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNstsdpqspNPPLLVH 984
Cdd:cd14552     73 VELKDQTDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSG--------NHPITVH 144

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462538648  985 CSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVL 1041
Cdd:cd14552    145 CSAGAGRTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 757-1046 2.07e-42

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 157.47  E-value: 2.07e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  757 NDERCKILEQRLEQGMVF----TEYERILKKrLVDGECSTARLPENAERNRFQDVLPYDDVRVeLVPTKENNTGYINASH 832
Cdd:PHA02742     8 KNSFAKNCEQLIEESNLAeilkEEHEHIMQE-IVAFSCNESLELKNMKKCRYPDAPCFDRNRV-ILKIEDGGDDFINASY 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  833 ikVSVSGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWprLGSRHNTVTYGRFKITTR---- 908
Cdd:PHA02742    86 --VDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYW--MPHERGKATHGEFKIKTKkiks 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  909 FRTdsgcYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIqsvrRHTNSTSD-PQS-----PNPPLL 982
Cdd:PHA02742   162 FRN----YAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLAV----READLKADvDIKgenivKEPPIL 233

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462538648  983 VHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQFLK 1046
Cdd:PHA02742   234 VHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLIFAK 297
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 743-1043 2.72e-42

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: 156.41  E-value: 2.72e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  743 PLPdegkeVATRATNDERCKILEQ-RLEQgmvftEYERILKKRLVDGECSTarLPENAERNRFQDVLPYDDVRVELVPTK 821
Cdd:cd14625      3 PIP-----ISELAEHTERLKANDNlKLSQ-----EYESIDPGQQFTWEHSN--LEVNKPKNRYANVIAYDHSRVILQPIE 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  822 E-NNTGYINASHIKVSVSgiEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGsrhnTVTY 900
Cdd:cd14625     71 GiMGSDYINANYIDGYRK--QNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRG----TETY 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  901 GRFKITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQsvrrhtnsTSDPQSPNpP 980
Cdd:cd14625    145 GMIQVTLLDTIELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVK--------TCNPPDAG-P 215

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462538648  981 LLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQ 1043
Cdd:cd14625    216 IVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 771-1045 3.86e-42

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 156.70  E-value: 3.86e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  771 GMVFTEYERILKKRlVDGECSTARLPENAERNRFQDVLPYDDVRVELVPTKENNTGYINASHIkvsvSGIEWD--YIATQ 848
Cdd:PHA02747    25 GIIRDEHHQIILKP-FDGLIANFEKPENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWI----DGFEDDkkFIATQ 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  849 GPLQNTCQDFWQMVWEQGIAIIAMVT-AEEEGGREKSFRYWPrLGSRHNTVTYGrFKITTRFRTDSGCYATTGLKMKHLL 927
Cdd:PHA02747   100 GPFAETCADFWKAVWQEHCSIIVMLTpTKGTNGEEKCYQYWC-LNEDGNIDMED-FRIETLKTSVRAKYILTLIEITDKI 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  928 TGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTSDPQSP-NPPLLVHCSAGVGRTGVVILSEIMIACLE 1006
Cdd:PHA02747   178 LKDSRKISHFQCSEWFEDETPSDHPDFIKFIKIIDINRKKSGKLFNPKDAlLCPIVVHCSDGVGKTGIFCAVDICLNQLV 257

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 2462538648 1007 HNEVLDIPRVLDMLRQQRMMLVQTLCQYTFV---YRVLIQFL 1045
Cdd:PHA02747   258 KRKAICLAKTAEKIREQRHAGIMNFDDYLFIqpgYEVLHYFL 299
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 827-1039 5.01e-42

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: 152.58  E-value: 5.01e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  827 YINASHIKvSVSGiEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSrhNTVTYGRFKIT 906
Cdd:cd14542      1 YINANFIK-GVSG-SKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGE--EQLQFGPFKIS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  907 ---TRFRTDSgcYATTGLKMKhlLTGQERTVWHLQYTDWPEHGCPEDLKgflSYLEEIQSVRRHTNSTSdpqspnPPLLV 983
Cdd:cd14542     77 lekEKRVGPD--FLIRTLKVT--FQKESRTVYQFHYTAWPDHGVPSSVD---PILDLVRLVRDYQGSED------VPICV 143

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462538648  984 HCSAGVGRTGVV--------ILSEIMIAclEHNEVLDIprVLDMlRQQRMMLVQTLCQYTFVYR 1039
Cdd:cd14542    144 HCSAGCGRTGTIcaidyvwnLLKTGKIP--EEFSLFDL--VREM-RKQRPAMVQTKEQYELVYR 202
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 792-1039 1.19e-41

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: 153.12  E-value: 1.19e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  792 TARLPENAERNRFQDVLPYDDVRVELVPT-KENNTGYINASHIKVSVSGIEwdYIATQGPLQNTCQDFWQMVWEQGIAII 870
Cdd:cd14614      6 AADLPVNRCKNRYTNILPYDFSRVKLVSMhEEEGSDYINANYIPGYNSPQE--YIATQGPLPETRNDFWKMVLQQKSQII 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  871 AMVTAEEEGGREKSFRYWPrlgSRHNTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQErtVWHLQYTDWPEHGCPeD 950
Cdd:cd14614     84 VMLTQCNEKRRVKCDHYWP---FTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQD--VMHFNYTAWPDHGVP-T 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  951 LKGFLSYLEEIQSVRRHTNSTSDpqspnpPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQT 1030
Cdd:cd14614    158 ANAAESILQFVQMVRQQAVKSKG------PMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQT 231


                   ....*....
gi 2462538648 1031 LCQYTFVYR 1039
Cdd:cd14614    232 EEQYIFIHQ 240
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 803-1041 1.47e-41

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: 152.51  E-value: 1.47e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  803 RFQDVLPYDDVRVeLVPTK--ENNTGYINASHIKVSVSgiEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGG 880
Cdd:cd14623      1 RVLQIIPYEFNRV-IIPVKrgEENTDYVNASFIDGYRQ--KDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  881 REKSFRYWPRLGSrhntVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEE 960
Cdd:cd14623     78 QEKCAQYWPSDGS----VSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAA 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  961 IQSVRRhtnstsdpQSPNPPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRV 1040
Cdd:cd14623    154 VQKQQQ--------QSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKV 225


                   .
gi 2462538648 1041 L 1041
Cdd:cd14623    226 V 226
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 795-1041 7.58e-41

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: 151.17  E-value: 7.58e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  795 LPENAERNRFQDVLPYDDVRVELVPTKENN--TGYINASHIKvSVSGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAM 872
Cdd:cd14613     22 IPGLVRKNRYKTILPNPHSRVCLTSPDQDDplSSYINANYIR-GYGGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVM 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  873 VTAEEEGGrEKSFRYWPRlgsrhNTVTYGRFKITTRFRTDSGCYATTGLKMKHllTGQERTVWHLQYTDWPEHGCPEDLK 952
Cdd:cd14613    101 ITNIEEMN-EKCTEYWPE-----EQVTYEGIEITVKQVIHADDYRLRLITLKS--GGEERGLKHYWYTSWPDQKTPDNAP 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  953 GFLSYLEEIQSVRRHTnstsdpQSPNPPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLC 1032
Cdd:cd14613    173 PLLQLVQEVEEARQQA------EPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCE 246


                   ....*....
gi 2462538648 1033 QYTFVYRVL 1041
Cdd:cd14613    247 QYQFVHHVL 255
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 804-1043 3.56e-40

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: 148.55  E-value: 3.56e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  804 FQDVLPYDDVRVELVPTKEN-NTGYINASHIKVSVSgiEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGRE 882
Cdd:cd14620      1 YPNILPYDHSRVILSQLDGIpCSDYINASYIDGYKE--KNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  883 KSFRYWPRLGSRhntvTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQ---ERTVWHLQYTDWPEHGCPEDLKGFLSYLE 959
Cdd:cd14620     79 KCYQYWPDQGCW----TYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGckaPRLVTQLHFTSWPDFGVPFTPIGMLKFLK 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  960 EIQSVrrhtnstsdpqspNP----PLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYT 1035
Cdd:cd14620    155 KVKSV-------------NPvhagPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYS 221


                   ....*...
gi 2462538648 1036 FVYRVLIQ 1043
Cdd:cd14620    222 FIYQALLE 229
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 801-1038 4.26e-40

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: 148.14  E-value: 4.26e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  801 RNRFQDVLPYDDVRVELVPTKENN--TGYINASHIKvSVSGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEE 878
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPKNSNDslSTYINANYIR-GYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  879 GGrEKSFRYWPrlgsrHNTVTYGRFKITTRFRTDSGCYATTGLKMKHllTGQERTVWHLQYTDWPEHGCPEDLKGFLSYL 958
Cdd:cd14611     81 KN-EKCVLYWP-----EKRGIYGKVEVLVNSVKECDNYTIRNLTLKQ--GSQSRSVKHYWYTSWPDHKTPDSAQPLLQLM 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  959 EEIQSVRRHTNSTSdpqspnpPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVY 1038
Cdd:cd14611    153 LDVEEDRLASPGRG-------PVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 827-1042 7.64e-40

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: 146.66  E-value: 7.64e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  827 YINASHikvsVSGI--EWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSRHntvtYGRFK 904
Cdd:cd17668      1 YINANY----VDGYnkPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEE----YGNFL 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  905 ITTRFRTDSGCYA--TTGLKMKHLLTG------QERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNStsdpqs 976
Cdd:cd17668     73 VTQKSVQVLAYYTvrNFTLRNTKIKKGsqkgrpSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVG------ 146

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462538648  977 pnpPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLI 1042
Cdd:cd17668    147 ---PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 776-1043 1.95e-39

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: 147.96  E-value: 1.95e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  776 EYERILKKRLVDGECSTarLPENAERNRFQDVLPYDDVRVeLVPTKENNTG--YINASHIKVSVSgiEWDYIATQGPLQN 853
Cdd:cd14624     27 EYESIDPGQQFTWEHSN--LEVNKPKNRYANVIAYDHSRV-LLSAIEGIPGsdYINANYIDGYRK--QNAYIATQGALPE 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  854 TCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGsrhnTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQERT 933
Cdd:cd14624    102 TFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRG----TETYGLIQVTLLDTVELATYCVRTFALYKNGSSEKRE 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  934 VWHLQYTDWPEHGCPEDLKGFLSYLEEIQsvrrhtnsTSDPQSPNPpLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDI 1013
Cdd:cd14624    178 VRQFQFTAWPDHGVPEHPTPFLAFLRRVK--------TCNPPDAGP-MVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDI 248

                          250       260       270
                   ....*....|....*....|....*....|
gi 2462538648 1014 PRVLDMLRQQRMMLVQTLCQYTFVYRVLIQ 1043
Cdd:cd14624    249 YGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 797-1043 2.45e-39

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: 146.32  E-value: 2.45e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  797 ENAERNRFQDVLPYDDVRVELVPTKEN-NTGYINASHIkvsvSGIEWD--YIATQGPLQNTCQDFWQMVWEQGIAIIAMV 873
Cdd:cd14630      2 ENRNKNRYGNIISYDHSRVRLQLLDGDpHSDYINANYI----DGYHRPrhYIATQGPMQETVKDFWRMIWQENSASVVMV 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  874 TAEEEGGREKSFRYWPrlgsrHNTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKG 953
Cdd:cd14630     78 TNLVEVGRVKCVRYWP-----DDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATG 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  954 FLSYLEEIQSVrrhtnstsdpqspNP----PLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQ 1029
Cdd:cd14630    153 LLGFVRQVKFL-------------NPpdagPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQ 219

                          250
                   ....*....|....
gi 2462538648 1030 TLCQYTFVYRVLIQ 1043
Cdd:cd14630    220 TEEQYVFVHDAILE 233
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 786-1043 3.67e-39

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: 147.86  E-value: 3.67e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  786 VDGECSTARLPENAERNRFQDVLPYDDVRVELVPTKE-NNTGYINASHIkvsvSGIEWD--YIATQGPLQNTCQDFWQMV 862
Cdd:cd14621     40 IQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGvPDSDYINASFI----NGYQEKnkFIAAQGPKEETVNDFWRMI 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  863 WEQGIAIIAMVTAEEEGGREKSFRYWPRLGSRhntvTYGRFKITTRFRTDSGCYATTGLKMKHL--LTGQ--ERTVWHLQ 938
Cdd:cd14621    116 WEQNTATIVMVTNLKERKECKCAQYWPDQGCW----TYGNIRVSVEDVTVLVDYTVRKFCIQQVgdVTNKkpQRLITQFH 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  939 YTDWPEHGCPEDLKGFLSYLEEIQsvrrhtnsTSDPQSPNPpLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLD 1018
Cdd:cd14621    192 FTSWPDFGVPFTPIGMLKFLKKVK--------NCNPQYAGA-IVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVS 262

                          250       260
                   ....*....|....*....|....*
gi 2462538648 1019 MLRQQRMMLVQTLCQYTFVYRVLIQ 1043
Cdd:cd14621    263 RIRAQRCQMVQTDMQYVFIYQALLE 287
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 827-1038 4.29e-39

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: 144.46  E-value: 4.29e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  827 YINASHIkvsvSGIeW---DYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSrhntvTYGRF 903
Cdd:cd14558      1 YINASFI----DGY-WgpkSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKK-----TYGDI 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  904 KITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYleeIQSVRRHTNSTSDPQSPNPPLLV 983
Cdd:cd14558     71 EVELKDTEKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDM---IKSIKQKLPYKNSKHGRSVPIVV 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462538648  984 HCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVY 1038
Cdd:cd14558    148 HCSDGSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 827-1038 4.93e-39

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: 144.12  E-value: 4.93e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  827 YINASHIkvsvsgIEWD-----YIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSRhntvTYG 901
Cdd:cd14546      1 YINASTI------YDHDprnpaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSE----VYH 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  902 RFKITTrFRTDSGC--YATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYleeiqsvRRHTNSTSDPQSpnP 979
Cdd:cd14546     71 IYEVHL-VSEHIWCddYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEF-------RRKVNKSYRGRS--C 140

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  980 PLLVHCSAGVGRTGVVILSEIMIACLEHN-EVLDIPRVLDMLRQQRMMLVQTLCQYTFVY 1038
Cdd:cd14546    141 PIVVHCSDGAGRTGTYILIDMVLNRMAKGaKEIDIAATLEHLRDQRPGMVKTKDQFEFVL 200
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 790-1036 7.42e-39

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: 146.34  E-value: 7.42e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  790 CSTARLPENAERNRFQDVLPYDDVRVEL-VPTKENNTGYINASHIkvsvsgIEWD-----YIATQGPLQNTCQDFWQMVW 863
Cdd:cd14609     34 CSTAQGEANVKKNRNPDFVPYDHARIKLkAESNPSRSDYINASPI------IEHDprmpaYIATQGPLSHTIADFWQMVW 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  864 EQGIAIIAMVTAEEEGGREKSFRYWPRLGSRhntvTYGRFKITTrFRTDSGC--YATTGLKMKHLLTGQERTVWHLQYTD 941
Cdd:cd14609    108 ENGCTVIVMLTPLVEDGVKQCDRYWPDEGSS----LYHIYEVNL-VSEHIWCedFLVRSFYLKNVQTQETRTLTQFHFLS 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  942 WPEHGCPEDLKGFLSYleeiqsvRRHTNSTSDPQSpnPPLLVHCSAGVGRTGVVILSEIMIACLEHN-EVLDIPRVLDML 1020
Cdd:cd14609    183 WPAEGIPSSTRPLLDF-------RRKVNKCYRGRS--CPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDIAATLEHV 253

                          250
                   ....*....|....*.
gi 2462538648 1021 RQQRMMLVQTLCQYTF 1036
Cdd:cd14609    254 RDQRPGMVRTKDQFEF 269
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 827-1044 2.11e-38

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: 142.45  E-value: 2.11e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  827 YINASHIKvsvSGIEWDY-IATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSrhntVTYGrfKI 905
Cdd:cd14622      2 YINASFID---GYRQKDYfIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGS----VTHG--EI 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  906 TTRFRTDSGCYATTGLKMkhLLT----GQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRhtnstsdpQSPNPPL 981
Cdd:cd14622     73 TIEIKNDTLLETISIRDF--LVTynqeKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQ--------QTGNHPI 142

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462538648  982 LVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQF 1044
Cdd:cd14622    143 VVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 765-1036 3.68e-38

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: 144.43  E-value: 3.68e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  765 EQRLEQgmvftEYERILKKRLVDGECSTARLPENAERNRFQDVLPYDDVRVEL-VPTKENNTGYINASHIkvsvsgIEWD 843
Cdd:cd14610     16 KNRLEK-----EWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILkAENSHSHSDYINASPI------MDHD 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  844 -----YIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSRHNTVtYGRFKITTRFRTDSgcYAT 918
Cdd:cd14610     85 prnpaYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHI-YEVNLVSEHIWCED--FLV 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  919 TGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYleeiqsvRRHTNSTSDPQSpnPPLLVHCSAGVGRTGVVILS 998
Cdd:cd14610    162 RSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDF-------RRKVNKCYRGRS--CPIIVHCSDGAGRSGTYILI 232

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 2462538648  999 EIMIACLEHN-EVLDIPRVLDMLRQQRMMLVQTLCQYTF 1036
Cdd:cd14610    233 DMVLNKMAKGaKEIDIAATLEHLRDQRPGMVQTKEQFEF 271
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 763-1043 3.85e-38

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: 144.03  E-value: 3.85e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  763 ILEQRLEQGMVFTE-YERILKKRlvDGECSTARLPENAERNRFQDVLPYDDVRVELVPTK-ENNTGYINASHIkvsvSGI 840
Cdd:cd14633      6 ITQMKCAEGYGFKEeYESFFEGQ--SAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEgETSSDYINGNYI----DGY 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  841 EW--DYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPrlgsrHNTVTYGRFKITTRFRTDSGCYAT 918
Cdd:cd14633     80 HRpnHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWP-----DDTEIYKDIKVTLIETELLAEYVI 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  919 TGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSvrrhtnstSDPQSPNpPLLVHCSAGVGRTGVVILS 998
Cdd:cd14633    155 RTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS--------KSPPNAG-PLVVHCSAGAGRTGCFIVI 225

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 2462538648  999 EIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQ 1043
Cdd:cd14633    226 DIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 827-1043 4.58e-38

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: 141.21  E-value: 4.58e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  827 YINASHIkvsvSGIEWD--YIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPrlgsrHNTVTYGRFK 904
Cdd:cd14555      1 YINANYI----DGYHRPnhYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP-----DDTEVYGDIK 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  905 ITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSvrrhtnstSDPQSPNpPLLVH 984
Cdd:cd14555     72 VTLVETEPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKA--------SNPPSAG-PIVVH 142

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462538648  985 CSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQ 1043
Cdd:cd14555    143 CSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 827-1039 7.09e-38

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: 140.82  E-value: 7.09e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  827 YINASHIkvsvSGIEWD--YIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSRhntvTYGRFK 904
Cdd:cd14551      1 YINASYI----DGYQEKnkFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCW----TYGNLR 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  905 ITTRFRTDSGCYATTGLKMKHLLTG----QERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVrrhtnstsDPQSPNpP 980
Cdd:cd14551     73 VRVEDTVVLVDYTTRKFCIQKVNRGigekRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSA--------NPPRAG-P 143

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462538648  981 LLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYR 1039
Cdd:cd14551    144 IVVHCSAGVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 814-1043 9.95e-38

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: 140.93  E-value: 9.95e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  814 RVELVPTKENNTG-YINASHIkvsvSGIEW--DYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPr 890
Cdd:cd14631      1 RVILQPVEDDPSSdYINANYI----DGYQRpsHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  891 lgsrHNTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQsvrrhtns 970
Cdd:cd14631     76 ----DDTEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVK-------- 143

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462538648  971 TSDPQSPNpPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQ 1043
Cdd:cd14631    144 LSNPPSAG-PIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 827-1038 1.11e-35

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: 134.51  E-value: 1.11e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  827 YINASHIKVSVSGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGR-EKSFRYWPRlgSRHNTVTYGRFKI 905
Cdd:cd17658      1 YINASLVETPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPA--EENESREFGRISV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  906 TTR-FRTDSGCYATTGLKMKHL-LTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVrrhtnstsdPQSPNpPLLV 983
Cdd:cd17658     79 TNKkLKHSQHSITLRVLEVQYIeSEEPPLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGI---------PPSAG-PIVV 148

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  984 HCSAGVGRTGVVI-----LSEIMIACLehnEVLDIPRVLDMLRQQRMMLVQTLCQYTFVY 1038
Cdd:cd17658    149 HCSAGIGRTGAYCtihntIRRILEGDM---SAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 827-1043 5.42e-34

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350480 [Multi-domain]  Cd Length: 205  Bit Score: 129.79  E-value: 5.42e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  827 YINASHIkvsvSGIEWD--YIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPrlgsrHNTVTYGRFK 904
Cdd:cd14632      1 YINANYI----DGYHRSnhFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP-----DDSDTYGDIK 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  905 ITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLeeiqsvrRHTNSTSDPQSpnPPLLVH 984
Cdd:cd14632     72 ITLLKTETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFI-------RRVKASTPPDA--GPVVVH 142

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462538648  985 CSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQ 1043
Cdd:cd14632    143 CSAGAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 786-1041 7.02e-34

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 133.23  E-value: 7.02e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  786 VDGECSTARLPENAERNRFQDVLPYDDVRVEL--------------------VPTKENNTGYINASHikvsVSGIEW--D 843
Cdd:PHA02746    39 IRGTTNHFLKKENLKKNRFHDIPCWDHSRVVInaheslkmfdvgdsdgkkieVTSEDNAENYIHANF----VDGFKEanK 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  844 YIATQGPLQNTCQDFWQMVWEQGIAIIAMVTaEEEGGREKSFRYWPRlgSRHNTVTYGRFKITTRFRTDSGCYATTGLKM 923
Cdd:PHA02746   115 FICAQGPKEDTSEDFFKLISEHESQVIVSLT-DIDDDDEKCFELWTK--EEDSELAFGRFVAKILDIIEELSFTKTRLMI 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  924 KHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTSDPQSPNP-PLLVHCSAGVGRTGVVILSEIMI 1002
Cdd:PHA02746   192 TDKISDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEEQAELIKQADNDPQTLgPIVVHCSAGIGRAGTFCAIDNAL 271

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 2462538648 1003 ACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVL 1041
Cdd:PHA02746   272 EQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
933-1043 6.17e-32

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 120.16  E-value: 6.17e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648   933 TVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHtnstsdpQSPNPPLLVHCSAGVGRTGVVILSEIMIACLEH-NEVL 1011
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQ-------SESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEV 73

                            90       100       110
                    ....*....|....*....|....*....|..
gi 2462538648  1012 DIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQ 1043
Cdd:smart00404   74 DIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 933-1043 6.17e-32

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: 120.16  E-value: 6.17e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648   933 TVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHtnstsdpQSPNPPLLVHCSAGVGRTGVVILSEIMIACLEH-NEVL 1011
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQ-------SESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEV 73

                            90       100       110
                    ....*....|....*....|....*....|..
gi 2462538648  1012 DIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQ 1043
Cdd:smart00012   74 DIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
796-1043 7.48e-31

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 123.28  E-value: 7.48e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  796 PENAERNRFQDVLPYDDVRVElvptkeNNTGYINASHIKVsvsGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTA 875
Cdd:COG5599     40 INGSPLNRFRDIQPYKETALR------ANLGYLNANYIQV---IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLAS 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  876 EEEGG--REKSFRYWPRLGSrhntvtYGRFKI------TTRFRTDSGCYATTgLKMKHllTGQE-RTVWHLQYTDWPEHG 946
Cdd:COG5599    111 DDEISkpKVKMPVYFRQDGE------YGKYEVsselteSIQLRDGIEARTYV-LTIKG--TGQKkIEIPVLHVKNWPDHG 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  947 CPEDlkgflSYLEEIQSVRRHTNSTSDPqsPNPPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDI---PRVLDMLRQQ 1023
Cdd:COG5599    182 AISA-----EALKNLADLIDKKEKIKDP--DKLLPVVHCRAGVGRTGTLIACLALSKSINALVQITLsveEIVIDMRTSR 254

                          250       260
                   ....*....|....*....|
gi 2462538648 1024 RMMLVQTLCQYTFVYRVLIQ 1043
Cdd:COG5599    255 NGGMVQTSEQLDVLVKLAEQ 274
FERM_C pfam09380
FERM C-terminal PH-like domain;
103-185 2.18e-27

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 106.18  E-value: 2.18e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  103 DSQGSDISIGACLEGIFVKHKNGRHPVVFRWHDIANMSHNKSFFALELANK--EETIQFQTEDMETAKYIWRLCVARHKF 180
Cdd:pfam09380    1 DKEGTDLWLGVSAKGILVYEDNNKILNLFPWREIRKISFKRKKFLIKLRDKssEETLGFYTESSRACKYLWKLCVEQHTF 80


                   ....*
gi 2462538648  181 YRLNQ 185
Cdd:pfam09380   81 FRLRR 85
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 827-1038 4.79e-25

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The type IIb (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 103.64  E-value: 4.79e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  827 YINA----SHIKVSVsgiewdYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTaEEEGGREKSFRYWPRLGSRhntvTYGR 902
Cdd:cd14556      1 YINAalldSYKQPAA------FIVTQHPLPNTVTDFWRLVYDYGCTSIVMLN-QLDPKDQSCPQYWPDEGSG----TYGP 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  903 FKITTRFRTDSGCYATTGLKMKHLLTGQE--RTVWHLQYTDWPEHG-CPEDLKGFLSYLEEIQSVRRhtnstsdpQSPNP 979
Cdd:cd14556     70 IQVEFVSTTIDEDVISRIFRLQNTTRPQEgyRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQE--------QSGEG 141

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462538648  980 PLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVY 1038
Cdd:cd14556    142 PIVVHCLNGVGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
FERM_C-lobe cd00836
FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N ...
 95-182 9.98e-18

FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 275389  Cd Length: 93  Bit Score: 78.96  E-value: 9.98e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648   95 GEESYPAKDSQ--GSDISIGACLEGI-FVKHKNGRHPVVFRWHDIANMSHNK-SFFALELAN--KEETIQFQTEDMEtAK 168
Cdd:cd00836      1 GVEFFPVKDKSkkGSPIILGVNPEGIsVYDELTGQPLVLFPWPNIKKISFSGaKKFTIVVADedKQSKLLFQTPSRQ-AK 79

                           90
                   ....*....|....
gi 2462538648  169 YIWRLCVARHKFYR 182
Cdd:cd00836     80 EIWKLIVGYHRFLL 93
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 841-1046 3.70e-17

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 83.48  E-value: 3.70e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  841 EWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEggrEKSF-RYWprlGSRHNTV-TYGRFKITTRFRTDSGCYAT 918
Cdd:PHA02740    90 EQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHAD---KKCFnQFW---SLKEGCViTSDKFQIETLEIIIKPHFNL 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  919 TGLKMKHLLtGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQS----VRRHTNSTSdpqspNPPLLVHCSAGVGRTGV 994
Cdd:PHA02740   164 TLLSLTDKF-GQAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDlcadLEKHKADGK-----IAPIIIDCIDGISSSAV 237

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462538648  995 VILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQFLK 1046
Cdd:PHA02740   238 FCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYLK 289
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 827-1038 9.81e-16

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: 76.98  E-value: 9.81e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  827 YINASHIKVSVSGIEwdYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEggREKSFRYWPrlgSRHNTVTYGRFKIT 906
Cdd:cd14550      1 YINASYLQGYRRSNE--FIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNEL--NEDEPIYWP---TKEKPLECETFKVT 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  907 TRFRTDSGCYATTGLKMKHLL--TGQER---TVWHLQYTDWPeHGCPEDLKGFlsylEEIQSVRRHTNSTsdpqspNPPL 981
Cdd:cd14550     74 LSGEDHSCLSNEIRLIVRDFIleSTQDDyvlEVRQFQCPSWP-NPCSPIHTVF----ELINTVQEWAQQR------DGPI 142

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462538648  982 LVH-----CSAGVgrtgVVILSEIMIAcLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVY 1038
Cdd:cd14550    143 VVHdryggVQAAT----FCALTTLHQQ-LEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLY 199
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 827-1042 2.82e-15

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: 75.87  E-value: 2.82e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  827 YINASHIKVSVSGIEwdYIATQGPLQNTCQDFWQMVWEQGIAIIAMVtAEEEGGREKSFRYWPrlgSRHNTVTYGRFKIT 906
Cdd:cd17670      1 YINASYIMGYYRSNE--FIITQHPLPHTTKDFWRMIWDHNAQIIVML-PDNQGLAEDEFVYWP---SREESMNCEAFTVT 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  907 TrFRTDSGCYATTGLKMKH---LLTGQERTVW---HLQYTDWPEHGCPedlkgfLSYLEEIQSVRRHTNSTSDpqspnPP 980
Cdd:cd17670     75 L-ISKDRLCLSNEEQIIIHdfiLEATQDDYVLevrHFQCPKWPNPDAP------ISSTFELINVIKEEALTRD-----GP 142

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462538648  981 LLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLI 1042
Cdd:cd17670    143 TIVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 844-1043 3.21e-15

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


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 75.72  E-value: 3.21e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  844 YIATQGPLQNTCQDFWQMVWEQGIAIIAMVTA-EEEGGREKSFRYWPRLGSRHntvtYGRFK------------ITTRFR 910
Cdd:cd14637     16 FIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQlNQSNSAWPCLQYWPEPGLQQ----YGPMEvefvsgsadediVTRLFR 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  911 TDSgcyaTTGLKMKHLLtgqertVWHLQYTDW-PEHGCPEDLKGFLSYLEEIQSVRRhtnstsdpQSPNPPLLVHCSAGV 989
Cdd:cd14637     92 VQN----ITRLQEGHLM------VRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQR--------ESGEGRTVVHCLNGG 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462538648  990 GRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQ 1043
Cdd:cd14637    154 GRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
FERM_C_4_1_family cd13184
FERM domain C-lobe of Protein 4.1 family; The protein 4.1 family includes four well-defined ...
 94-183 9.10e-14

FERM domain C-lobe of Protein 4.1 family; The protein 4.1 family includes four well-defined members: erythroid protein 4.1 (4.1R), the best known and characterized member, 4.1G (general), 4.1N (neuronal), and 4.1 B (brain). The less well understood 4.1O/FRMD3 is not a true member of this family and is not included in this hierarchy. Besides three highly conserved domains, FERM, SAB (spectrin and actin binding domain) and CTD (C-terminal domain), the proteins from this family contain several unique domains: U1, U2 and U3. FERM domains like other members of the FERM domain superfamily have a cloverleaf architecture with three distinct lobes: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The brain is a particularly rich source of protein 4.1 isoforms. The various 4.1R, 4.1G, 4.1N, and 4.1B mRNAs are all expressed in distinct patterns within the brain. It is likely that 4.1 proteins play important functional roles in the brain including motor coordination and spatial learning, postmitotic differentiation, and synaptic architecture and function. In addition they are found in nonerythroid, nonneuronal cells where they may play a general structural role in nuclear architecture and/or may interact with splicing factors. The FERM C domain is the third structural domain within the FERM domain. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270005  Cd Length: 94  Bit Score: 67.73  E-value: 9.10e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648   94 YGEESYPAKDSQGSDISIGACLEGIFVkHKNGRHPVVFRWHDIANMSHNKSFFAL-----ELANKEETIQFQTEDMETAK 168
Cdd:cd13184      1 YGVDLHPAKDSEGVDIMLGVCSSGLLV-YRDRLRINRFAWPKVLKISYKRNNFYIkirpgEFEQYETTIGFKLPNHRAAK 79

                           90
                   ....*....|....*
gi 2462538648  169 YIWRLCVARHKFYRL 183
Cdd:cd13184     80 RLWKVCVEHHTFFRL 94
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 827-1042 1.74e-13

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: 70.41  E-value: 1.74e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  827 YINASHIKVSVSGIEwdYIATQGPLQNTCQDFWQMVWEQGIAIIAMVtAEEEGGREKSFRYWPrlgSRHNTVTYGRFKIT 906
Cdd:cd17669      1 YINASYIMGYYQSNE--FIITQHPLLHTIKDFWRMIWDHNAQLIVML-PDGQNMAEDEFVYWP---NKDEPINCETFKVT 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  907 TrFRTDSGCYAT-TGLKMKHLLTGQER-----TVWHLQYTDWPEHGCPedlkgfLSYLEEIQSVRRHTNSTSDpqspnPP 980
Cdd:cd17669     75 L-IAEEHKCLSNeEKLIIQDFILEATQddyvlEVRHFQCPKWPNPDSP------ISKTFELISIIKEEAANRD-----GP 142

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462538648  981 LLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLI 1042
Cdd:cd17669    143 MIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 827-1043 3.20e-13

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 69.66  E-value: 3.20e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  827 YINA----SHIKVSVsgiewdYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTaeEEGGREKSFRYWPRLGSrhntVTYGR 902
Cdd:cd14634      1 YINAalmdSHKQPAA------FIVTQHPLPNTVADFWRLVFDYNCSSVVMLN--EMDAAQLCMQYWPEKTS----CCYGP 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  903 FKITTRFRTDSGCYATTGLKMKHLLTGQE--RTVWHLQYTDWPEH-GCPEDLKGFLsyleeiQSVRRHTNSTSDPQSPNP 979
Cdd:cd14634     69 IQVEFVSADIDEDIISRIFRICNMARPQDgyRIVQHLQYIGWPAYrDTPPSKRSIL------KVVRRLEKWQEQYDGREG 142

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462538648  980 PLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQ 1043
Cdd:cd14634    143 RTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 844-1043 3.26e-12

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: 66.97  E-value: 3.26e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  844 YIATQGPLQNTCQDFWQMVWEQGIAIIAMVTaeEEGGREKSFRYWPRLGsrhnTVTYGRFKITTrFRTDSGCYATTGL-K 922
Cdd:cd14636     16 FIVTQHPLPNTVKDFWRLVYDYGCTSIVMLN--EVDLAQGCPQYWPEEG----MLRYGPIQVEC-MSCSMDCDVISRIfR 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  923 MKHLLTGQE--RTVWHLQYTDWPEH-GCPEDLKGFLSYLEEIQSVRRHTNSTSDPQspnpplLVHCSAGVGRTGVVILSE 999
Cdd:cd14636     89 ICNLTRPQEgyLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECDEGEGRT------IIHCLNGGGRSGMFCAIS 162

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2462538648 1000 IMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQ 1043
Cdd:cd14636    163 IVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 844-1043 8.75e-11

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


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 62.78  E-value: 8.75e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  844 YIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGgrEKSFRYWPRLG-SRHNTVTYGRFK-------ITTRFRTDSGC 915
Cdd:cd14635     16 FIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPA--QLCPQYWPENGvHRHGPIQVEFVSadleediISRIFRIYNAA 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  916 YATTGLKMkhlltgqertVWHLQYTDWPEH-GCPEDLKGFLSYLEEIQSVRRHTNSTSDPQspnpplLVHCSAGVGRTGV 994
Cdd:cd14635     94 RPQDGYRM----------VQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYNGGEGRT------VVHCLNGGGRSGT 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2462538648  995 VILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQ 1043
Cdd:cd14635    158 FCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
FERM_C_FRMD3_FRMD5 cd13192
FERM domain C-lobe of FERM domain-containing protein 3 and 5 (FRMD3 and 5); FRMD3 (also called ...
 80-182 1.15e-09

FERM domain C-lobe of FERM domain-containing protein 3 and 5 (FRMD3 and 5); FRMD3 (also called Band 4.1-like protein 4O/4.1O though it is not a true member of that family) is a novel putative tumor suppressor gene that is implicated in the origin and progression of lung cancer. In humans there are 5 isoforms that are produced by alternative splicing. Less is known about FRMD5, though there are 2 isoforms of the human protein are produced by alternative splicing. Both FRMD3 and FRMD5 contain a N-terminal FERM domain, followed by a FERM adjacent (FA) domain, and 4.1 protein C-terminal domain (CTD). The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270013  Cd Length: 105  Bit Score: 56.63  E-value: 1.15e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648   80 AEMLYMQEVERMDGYGEESYPAKDSQGSDISIGACLEGIFVkHKNGRHPVVFRWHDIANMSHNKSFFALELANKEE---T 156
Cdd:cd13192      1 AEDNFLRKAATLETYGVDPHPVKDHRGNQLYLGFTHTGIVT-FQGGKRVHHFRWNDITKFNYEGKMFILHVMQKEEkkhT 79

                           90       100
                   ....*....|....*....|....*.
gi 2462538648  157 IQFQTEDMETAKYIWRLCVARHKFYR 182
Cdd:cd13192     80 LGFKCPTPAACKHLWKCAVEQQAFYT 105
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 828-1034 1.44e-09

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: 59.34  E-value: 1.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  828 INASHIKVSVSGIewdYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGsrhntvTYGRFKITT 907
Cdd:cd14559     18 LNANRVQIGNKNV---AIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYFRQSG------TYGSVTVKS 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  908 RfRTDSGcYATTGLKMKHL---LTGQERT----VWHLqyTDWPEHGC--PEDLKGFLSYLEeiQSVRRHTN-----STSD 973
Cdd:cd14559     89 K-KTGKD-ELVDGLKADMYnlkITDGNKTitipVVHV--TNWPDHTAisSEGLKELADLVN--KSAEEKRNfykskGSSA 162

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462538648  974 PQSPNPPL-LVHCSAGVGRTGVVILSEIMIaclEHNEVLDIPRVLDMLRQQR-MMLVQTLCQY 1034
Cdd:cd14559    163 INDKNKLLpVIHCRAGVGRTGQLAAAMELN---KSPNNLSVEDIVSDMRTSRnGKMVQKDEQL 222
FERM_C_PTPN4_PTPN3_like cd13189
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 3 and 4 (PTPN4 and ...
 94-183 3.47e-09

FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 3 and 4 (PTPN4 and PTPN3); PTPN4 (also called PTPMEG, protein tyrosine phosphatase, megakaryocyte) is a cytoplasmic protein-tyrosine phosphatase (PTP) thought to play a role in cerebellar function. PTPMEG-knockout mice have impaired memory formation and cerebellar long-term depression. PTPN3/PTPH1 is a membrane-associated PTP that is implicated in regulating tyrosine phosphorylation of growth factor receptors, p97 VCP (valosin-containing protein, or Cdc48 in Saccharomyces cerevisiae), and HBV (Hepatitis B Virus) gene expression; it is mutated in a subset of colon cancers. PTPMEG and PTPN3/PTPH1 contains a N-terminal FERM domain, a middle PDZ domain, and a C-terminal phosphatase domain. PTP1/Tyrosine-protein phosphatase 1 from nematodes and a FERM_C repeat 1 from Tetraodon nigroviridis are also included in this cd. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270010  Cd Length: 95  Bit Score: 55.01  E-value: 3.47e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648   94 YGEESYPAKDSQGSDISIGACLEGIFVKHkNGRHPVVFRWHDIANMSHNKSFFALELANK----EETI-QFQTEDMETAK 168
Cdd:cd13189      2 YGVELHSARDSNNLELQIGVSSAGILVFQ-NGIRINTFPWSKIVKISFKRKQFFIQLRREpnesRDTIlGFNMLSYRACK 80

                           90
                   ....*....|....*
gi 2462538648  169 YIWRLCVARHKFYRL 183
Cdd:cd13189     81 NLWKSCVEHHTFFRL 95
FERM_C_PTPH13 cd13187
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor 13 (PTPH13); There are many ...
 99-180 3.96e-09

FERM domain C-lobe of Protein tyrosine phosphatase non-receptor 13 (PTPH13); There are many functions of PTPN13 (also called PTPL1, PTP-BAS, hPTP1E, FAP1, or PTPL1). Mice lacking PTPN13 activity have abnormal regulation of signal transducer and activator of transcription signaling in their T cells, mild impairment of motor nerve repair, and a significant reduction in the growth of retinal glia cultures. It also plays a role in adipocyte differentiation. PTPN13 contains a kinase non-catalytic C-lobe domain (KIND), a FERM domain with two potential phosphatidylinositol 4,5-biphosphate [PtdIns(4,5)P2]-binding motifs, 5 PDZ domains, and a carboxy-terminal catalytic domain. There is an nteraction between the FERM domain of PTPL1 and PtdIns(4,5)P2 which is thought to regulate the membrane localization of PTPN13. PDZ are protein/protein interaction domains so there is the potential for numerous partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated PTPL1 substrates. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270008  Cd Length: 103  Bit Score: 55.02  E-value: 3.96e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648   99 YPAKDSQGSDISIGACLEGIFV--KHKNGRHPVV-FRWHDIANMSHNKSFFALElANKEETIQ--FQTEDMETAKYIWRL 173
Cdd:cd13187      8 YREKKSSTLSLWLGICSRGIIIyeEKNGARTPVLrFPWRETQKISFDKKKFTIE-SRGGSGIKhtFYTDSYKKSQYLLQL 86


                   ....*..
gi 2462538648  174 CVARHKF 180
Cdd:cd13187     87 CSAQHKF 93
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 27-99 8.08e-09

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 56.53  E-value: 8.08e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462538648    27 ADFGDFDQYES--QDFLQKFALFPVGWLQDEKvLEEATQKVALLHQKYRGLTAPDAEMLYMQEVERMDGYGEESY 99
Cdd:smart00295  128 AEFGDYDEELHdlRGELSLKRFLPKQLLDSRK-LKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 27-91 5.60e-08

FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases, the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 271216  Cd Length: 99  Bit Score: 51.48  E-value: 5.60e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462538648   27 ADFGDFDQYESQD-FLQKFALFPVgWLQDEKVLEEATQKVALLHQKYRGLTAPDAEMLYMQEVERM 91
Cdd:cd14473     35 AEYGDYDPSEHKPkYLSLKRFLPK-QLLKQRKPEEWEKRIVELHKKLRGLSPAEAKLKYLKIARKL 99
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 27-97 2.18e-07

FERM central domain; This domain is the central structural domain of the FERM domain.


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 50.35  E-value: 2.18e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462538648   27 ADFGDFDQYESQ-DFLQKFALFPVgWLQDEKVLEEATQKVALLHQKYRGLTAPDAEMLYMQEVERMDGYGEE 97
Cdd:pfam00373   45 AEFGDYQPSSHTsEYLSLESFLPK-QLLRKMKSKELEKRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVE 115
FERM_C_ERM cd13194
FERM domain C-lobe/F3 of the ERM family; The ERM family includes ezrin, radixin, moesin and ...
 94-181 8.98e-06

FERM domain C-lobe/F3 of the ERM family; The ERM family includes ezrin, radixin, moesin and merlin. They are composed of a N-terminal FERM (ERM) domain (also called N-ERMAD (N-terminal ERM association domain)), a coiled coil region (CRR), and a C-terminal domain CERMAD (C-terminal ERM association domain) which has an F-actin-binding site (ABD). Two actin-binding sites have been identified in the middle and N-terminal domains. Merlin is structurally similar to the ERM proteins, but instead of an actin-binding domain (ABD), it contains a C-terminal domain (CTD), just like the proteins from the 4.1 family. Activated ezrin, radixin and moesin are thought to be involved in the linking of actin filaments to CD43, CD44, ICAM1-3 cell adhesion molecules, various membrane channels and receptors, such as the Na+/H+ exchanger-3 (NHE3), cystic fibrosis transmembrane conductance regulator (CFTR), and the beta2-adrenergic receptor. The ERM proteins exist in two states, a dormant state in which the FERM domain binds to its own C-terminal tail and thereby precludes binding of some partner proteins, and an activated state, in which the FERM domain binds to one of many membrane binding proteins and the C-terminal tail binds to F-actin. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain of ERM is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270015  Cd Length: 97  Bit Score: 45.34  E-value: 8.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648   94 YGEESYPAKDSQGSDISIGACLEGIFVKHKNGR-HPVV-FRWHDIANMS-HNKSFFALELANKEETIQFQTEDMETAKYI 170
Cdd:cd13194      2 YGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKlTPKIgFPWSEIRNISfNDKKFVIKPIDKKAPDFVFYSPRLRINKRI 81

                           90
                   ....*....|.
gi 2462538648  171 WRLCVARHKFY 181
Cdd:cd13194     82 LDLCMGNHELY 92
FERM_C_NBL4_NBL5 cd13186
FERM domain C-lobe of Novel band 4.1-like protein 4 and 5 (NBL4 and 5); NBL4 (also called ...
 95-182 1.01e-05

FERM domain C-lobe of Novel band 4.1-like protein 4 and 5 (NBL4 and 5); NBL4 (also called Erythrocyte protein band 4.1-like 4; Epb4 1l4) plays a role the beta-catenin/Tcf signaling pathway and is thought to be involved in establishing the cell polarity or proliferation. NBL4 may be also involved in adhesion, in cell motility and/or in cell-to-cell communication. No role for NBL5 has been proposed to date. Both NBL4 and NBL5 contain a N-terminal FERM domain which has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe is a member of the PH superfamily. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270007  Cd Length: 92  Bit Score: 44.97  E-value: 1.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648   95 GEESYPAKDSQGSDISIGACLEGIFV---KHKNGrhpvVFRWHDIANMSHNKSFFALELANKEETIQ-----FQTEDMET 166
Cdd:cd13186      1 GVDLHPVKGEDGNEYFLGLTPTGILVfenKTKIG----LFFWPRITKLDFKGKKLKLVVKEKDDQEQehtfvFRLPNKKA 76

                           90
                   ....*....|....*.
gi 2462538648  167 AKYIWRLCVARHKFYR 182
Cdd:cd13186     77 CKHLWKCAVEHHAFFR 92
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 947-1039 1.57e-05

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


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 45.03  E-value: 1.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  947 CPEDLKGFLSYLEEiqsvrrhtnstsdPQSPNPPLLVHCSAGVGRTGVVILseIMIACLEHNEVLDIprvLDMLRQQR-M 1025
Cdd:cd14494     38 TLAMVDRFLEVLDQ-------------AEKPGEPVLVHCKAGVGRTGTLVA--CYLVLLGGMSAEEA---VRIVRLIRpG 99

                           90
                   ....*....|....
gi 2462538648 1026 MLVQTLCQYTFVYR 1039
Cdd:cd14494    100 GIPQTIEQLDFLIK 113
FERM_C_FARP1-like cd13193
FERM domain C-lobe of FERM, RhoGEF and pleckstrin domain-containing protein 1 and related ...
 88-185 3.20e-05

FERM domain C-lobe of FERM, RhoGEF and pleckstrin domain-containing protein 1 and related proteins; Members here include FARP1 (also called Chondrocyte-derived ezrin-like protein; PH domain-containing family C member 2), FARP2 (also called FIR/FERM domain including RhoGEF; FGD1-related Cdc42-GEF/FRG), and FRMD7(FERM domain containing 7). FARP1 and FARP2 are members of the Dbl family guanine nucleotide exchange factors (GEFs) which are upstream positive regulators of Rho GTPases. FARP1 has increased expression in differentiated chondrocytes. FARP2 is thought to regulate neurite remodeling by mediating the signaling pathways from membrane proteins to Rac. It is found in brain, lung, and testis, as well as embryonic hippocampal and cortical neurons. These members are composed of a N-terminal FERM domain, a proline-rich (PR) domain, Dbl-homology (DH), and two C-terminal PH domains. Other members in this family do not contain the DH domains such as the Human FERM domain containing protein 7 and Caenorhabditis elegans CFRM3, both of which have unknown functions. They contain an N-terminal FERM domain, a PH domain, followed by a FA (FERM adjacent) domain. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270014  Cd Length: 122  Bit Score: 44.26  E-value: 3.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648   88 VERMDGYGEESYPAKDSQGSDISIGACLEGIFVKHKNGRHPVvFRWHDIANMSHNKSFFALELANKE-----ETIQFQTE 162
Cdd:cd13193      3 ARRCELYGIRLHPAKDREGVKLNLAVAHMGILVFQGFTKINT-FSWAKIRKLSFKRKRFLIKLHPEAygsykDTVEFSFE 81

                           90       100
                   ....*....|....*....|...
gi 2462538648  163 DMETAKYIWRLCVARHKFYRLNQ 185
Cdd:cd13193     82 SRNECKSFWKKCIEHHAFFRCSE 104
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 981-1039 9.19e-04

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: 41.09  E-value: 9.19e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462538648  981 LLVHCSAGVGRTGVVilseimIAC--LEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYR 1039
Cdd:cd14505    109 VLIHCKGGLGRTGLI------AACllLELGDTLDPEQAIAAVRALRPGAIQTPKQENFLHQ 163
FERM_C_MYLIP_IDOL cd13195
FERM domain C-lobe of E3 ubiquitin ligase myosin regulatory light chain-interacting protein ...
 94-182 1.93e-03

FERM domain C-lobe of E3 ubiquitin ligase myosin regulatory light chain-interacting protein (MYLIP; also called inducible degrader of the LDL receptor, IDOL); MYLIP/IDOL is a regulator of the LDL receptor (LDLR) pathway via the nuclear receptor liver X receptor (LXR). In response to cellular cholesterol loading, the activation of LXR leads to the induction of MYLIP expression. MYLIP stimulates ubiquitination of the LDLR on its cytoplasmic tail, directing its degradation. The LXR-MYLIP-LDLR pathway provides a complementary pathway to sterol regulatory element-binding proteins for the feedback inhibition of cholesterol uptake. MYLIP has an N-terminal FERM domain and in some cases a C-terminal RING domain. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270016  Cd Length: 111  Bit Score: 39.15  E-value: 1.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648   94 YGEESYPAKDSQGSDISIGACLEGIFVKHKNGRHPVVFRWHDI-ANMSHNKSFFA--LELANKEETIQFQTEDMETAKYI 170
Cdd:cd13195      1 YGVEFFEVRNIEGQKLLIGVGPHGITICNDDFEVIERIPYTAIqMATSSGRVFTLtyLSDDGSVKVLEFKLPSTRAASGL 80

                           90
                   ....*....|..
gi 2462538648  171 WRLCVARHKFYR 182
Cdd:cd13195     81 YRAITEKHAFYR 92
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
980-1039 2.04e-03

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 39.57  E-value: 2.04e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538648  980 PLLVHCSAGVGRTGVVilseimIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYR 1039
Cdd:COG2453     82 KVLVHCRGGIGRTGTV------AAAYLVLLGLSAEEALARVRAARPGAVETPAQRAFLER 135
 
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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