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Conserved domains on  [gi|568911642|ref|XP_006497197|]
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tyrosine-protein phosphatase non-receptor type 14 isoform X2 [Mus musculus]

Protein Classification

protein-tyrosine phosphatase family protein( domain architecture ID 13626984)

cys-based protein-tyrosine phosphatase (PTP) family protein may be a PTP or a dual-specificity phosphatase (DUSP or DSP), and may catalyze the dephosphorylation of target phosphoproteins at tyrosine or tyrosine and serine/threonine residues, respectively; similar to Mus musculus myotubularin-related protein 14 (MTMR14) which is a phosphoinositide phosphatase which specifically dephosphorylates PtdIns(3,5)P2) and PI3P; contains a pleckstrin homology-like (PH-like) domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 799-1085 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: 625.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  799 RLRALKKKLEDGMVFTEYEQIPNKKANGVFSTATLPENAERSRIREVVPYEENRVELIPTKENNTGYINASHIKVVVGGS 878
Cdd:cd14599     1 RCKTLERKLEEGMVFTEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  879 EWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTG 958
Cdd:cd14599    81 EWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  959 LKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSVLEGIRTRHPPIVVHCSAGVGRTGVVILSE 1038
Cdd:cd14599   161 LKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSMLDSTKNCNPPIVVHCSAGVGRTGVVILTE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 568911642 1039 LMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQFLQ 1085
Cdd:cd14599   241 LMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 5-121 3.12e-34

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


:

Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 127.00  E-value: 3.12e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642     5 PNVSRLQQEATRYQYYLQVKKDVLEGRLRCSLEQVIRLAGLAVQADFGDYNQFDSQ-EFLREYVLFPMDLaMEEAALEEL 83
Cdd:pfam00373    1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTsEYLSLESFLPKQL-LRKMKSKEL 79

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 568911642    84 TQKVAQEHKAHSGILPAEAELMYINEVERLDGFGQEIF 121
Cdd:pfam00373   80 EKRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_C_PTPN14_PTPN21 cd13188
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and ...
 116-206 4.54e-29

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: 111.61  E-value: 4.54e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  116 FGQEIFPVKDSHGNSVHLGIFFMGIFVRNRVGRQAVIYRWNDIGSVTHSKAAILLELIDKEETALFHTDDIENAKYISRL 195
Cdd:cd13188     1 YGEESFPAKDEQGNEVLIGASLEGIFVKHDNGRPPVFFRWEDIKNVINHKRTFSIECQNSEETVQFQFEDAETAKYVWKL 80

                          90
                  ....*....|.
gi 568911642  196 FTTRHKFYKQN 206
Cdd:cd13188    81 CVLQHKFYRQN 91
 
Name Accession Description Interval E-value
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 799-1085 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: 625.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  799 RLRALKKKLEDGMVFTEYEQIPNKKANGVFSTATLPENAERSRIREVVPYEENRVELIPTKENNTGYINASHIKVVVGGS 878
Cdd:cd14599     1 RCKTLERKLEEGMVFTEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  879 EWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTG 958
Cdd:cd14599    81 EWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  959 LKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSVLEGIRTRHPPIVVHCSAGVGRTGVVILSE 1038
Cdd:cd14599   161 LKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSMLDSTKNCNPPIVVHCSAGVGRTGVVILTE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 568911642 1039 LMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQFLQ 1085
Cdd:cd14599   241 LMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
836-1082 3.22e-92

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 294.15  E-value: 3.22e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642   836 NAERSRIREVVPYEENRVELIPTKENNtGYINASHIKVVVGgsEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEE 915
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPS-DYINASYIDGYKK--PKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642   916 EGGRTKSHRYWPKlgSKHSSATYGKFKVTTK-FRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLS 994
Cdd:pfam00102   78 EKGREKCAQYWPE--EEGESLEYGDFTVTLKkEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLD 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642   995 YLEEIQSVRRHTnsvlegirtRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYK 1074
Cdd:pfam00102  156 LLRKVRKSSLDG---------RSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYI 226


                   ....*...
gi 568911642  1075 FVYQVLVQ 1082
Cdd:pfam00102  227 FLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
812-1082 7.66e-92

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 294.18  E-value: 7.66e-92
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642    812 VFTEYEQIP-NKKANGVFSTATLPENAERSRIREVVPYEENRVELIPTKENNTGYINASHIKVVvgGSEWHYIATQGPLP 890
Cdd:smart00194    2 LEEEFEKLDrLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGP--NGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642    891 HTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhsSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQER 970
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGE--PLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETR 157

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642    971 TVWHLQYTDWPHHGCPEDVQGFLSYLEEIqsvrRHTNSVLEGirtrhpPIVVHCSAGVGRTGVVILSELMIYCLEHNEKV 1050
Cdd:smart00194  158 TVTHYHYTNWPDHGVPESPESILDLIRAV----RKSQSTSTG------PIVVHCSAGVGRTGTFIAIDILLQQLEAGKEV 227

                           250       260       270
                    ....*....|....*....|....*....|..
gi 568911642   1051 EVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 1082
Cdd:smart00194  228 DIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
PHA02738 PHA02738
hypothetical protein; Provisional
 815-1085 2.32e-46

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 169.34  E-value: 2.32e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  815 EYEQIPNKKANGVFSTATlpENAERSRIREVVPYEENRVELiPTKENNTGYINASHikvvVGGSEW--HYIATQGPLPHT 892
Cdd:PHA02738   30 EHQKVISEKVDGTFNAEK--KNRKLNRYLDAVCFDHSRVIL-PAERNRGDYINANY----VDGFEYkkKFICGQAPTRQT 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  893 CHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLgsKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLlSGQERTV 972
Cdd:PHA02738  103 CYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDV--EQGSIRFGKFKITTTQVETHPHYVKSTLLLTDG-TSATQTV 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  973 WHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRR--HTNSVLEG-IRTRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEK 1049
Cdd:PHA02738  180 THFNFTAWPDHDVPKNTSEFLNFVLEVRQCQKelAQESLQIGhNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACAT 259

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 568911642 1050 VEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQFLQ 1085
Cdd:PHA02738  260 VSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRYVN 295
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 5-121 3.12e-34

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 127.00  E-value: 3.12e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642     5 PNVSRLQQEATRYQYYLQVKKDVLEGRLRCSLEQVIRLAGLAVQADFGDYNQFDSQ-EFLREYVLFPMDLaMEEAALEEL 83
Cdd:pfam00373    1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTsEYLSLESFLPKQL-LRKMKSKEL 79

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 568911642    84 TQKVAQEHKAHSGILPAEAELMYINEVERLDGFGQEIF 121
Cdd:pfam00373   80 EKRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 2-121 3.80e-32

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: 124.33  E-value: 3.80e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642      2 FYVPNVSRLQQEATRY-QYYLQVKKDVLEGRLRCSLEQVIRLAGLAVQADFGDYNQFDS--QEFLREYVLFPMDLAMEEa 78
Cdd:smart00295   80 FYPPDPNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdlRGELSLKRFLPKQLLDSR- 158

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 568911642     79 ALEELTQKVAQEHKAHSGILPAEAELMYINEVERLDGFGQEIF 121
Cdd:smart00295  159 KLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
796-1086 1.24e-29

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 119.81  E-value: 1.24e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  796 IDERLRALKKKLEDGMVFTEYEQIPNkkangvfstatlpeNAERSRIREVVPYEENRVEliptkeNNTGYINASHIKVvv 875
Cdd:COG5599    16 INSRLSTLTNELAPSHNDPQYLQNIN--------------GSPLNRFRDIQPYKETALR------ANLGYLNANYIQV-- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  876 gGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGG--RTKSHRYWpklgskHSSATYGKFKVTTK------F 947
Cdd:COG5599    74 -IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISkpKVKMPVYF------RQDGEYGKYEVSSEltesiqL 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  948 RTDSGCYAttgLKVKHLLSGQE-RTVWHLQYTDWPHHGCP--EDVQGFLSYLEEIQSVRRHTNSvlegirtrhpPIVVHC 1024
Cdd:COG5599   147 RDGIEART---YVLTIKGTGQKkIEIPVLHVKNWPDHGAIsaEALKNLADLIDKKEKIKDPDKL----------LPVVHC 213

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568911642 1025 SAGVGRTGVVILselmIYCLE------HNEKVEVPTMLRFLREQR-MFMIQTIAQykfvYQVLVQFLQN 1086
Cdd:COG5599   214 RAGVGRTGTLIA----CLALSksinalVQITLSVEEIVIDMRTSRnGGMVQTSEQ----LDVLVKLAEQ 274
FERM_C_PTPN14_PTPN21 cd13188
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and ...
 116-206 4.54e-29

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: 111.61  E-value: 4.54e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  116 FGQEIFPVKDSHGNSVHLGIFFMGIFVRNRVGRQAVIYRWNDIGSVTHSKAAILLELIDKEETALFHTDDIENAKYISRL 195
Cdd:cd13188     1 YGEESFPAKDEQGNEVLIGASLEGIFVKHDNGRPPVFFRWEDIKNVINHKRTFSIECQNSEETVQFQFEDAETAKYVWKL 80

                          90
                  ....*....|.
gi 568911642  196 FTTRHKFYKQN 206
Cdd:cd13188    81 CVLQHKFYRQN 91
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 15-113 1.33e-27

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: 107.72  E-value: 1.33e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642   15 TRYQYYLQVKKDVLEGRLRCSLEQVIRLAGLAVQADFGDYNQ-FDSQEFLREYVLFPMDLaMEEAALEELTQKVAQEHKA 93
Cdd:cd14473     1 TRYLLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPsEHKPKYLSLKRFLPKQL-LKQRKPEEWEKRIVELHKK 79

                          90       100
                  ....*....|....*....|
gi 568911642   94 HSGILPAEAELMYINEVERL 113
Cdd:cd14473    80 LRGLSPAEAKLKYLKIARKL 99
FERM_C pfam09380
FERM C-terminal PH-like domain;
125-207 2.00e-10

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 58.03  E-value: 2.00e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642   125 DSHGNSVHLGIFFMGIFVRNRVGRQAVIYRWNDIGSVTHSKAAILLELIDK--EETALFHTDDIENAKYISRLFTTRHKF 202
Cdd:pfam09380    1 DKEGTDLWLGVSAKGILVYEDNNKILNLFPWREIRKISFKRKKFLIKLRDKssEETLGFYTESSRACKYLWKLCVEQHTF 80


                   ....*
gi 568911642   203 YKQNK 207
Cdd:pfam09380   81 FRLRR 85
 
Name Accession Description Interval E-value
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 799-1085 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: 625.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  799 RLRALKKKLEDGMVFTEYEQIPNKKANGVFSTATLPENAERSRIREVVPYEENRVELIPTKENNTGYINASHIKVVVGGS 878
Cdd:cd14599     1 RCKTLERKLEEGMVFTEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  879 EWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTG 958
Cdd:cd14599    81 EWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  959 LKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSVLEGIRTRHPPIVVHCSAGVGRTGVVILSE 1038
Cdd:cd14599   161 LKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSMLDSTKNCNPPIVVHCSAGVGRTGVVILTE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 568911642 1039 LMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQFLQ 1085
Cdd:cd14599   241 LMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 865-1085 1.66e-143

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: 429.40  E-value: 1.66e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  865 YINASHIKVVVGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHSSATYGKFKVT 944
Cdd:cd14598     1 YINASHIKVTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRHNTVTYGRFKIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  945 TKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSVLEGiRTRHPPIVVHC 1024
Cdd:cd14598    81 TRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTIDP-KSPNPPVLVHC 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568911642 1025 SAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQFLQ 1085
Cdd:cd14598   160 SAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 865-1084 7.41e-138

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: 414.55  E-value: 7.41e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  865 YINASHIKVVVGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHSSATYGKFKVT 944
Cdd:cd14540     1 YINASHITATVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHDALTFGEYKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  945 TKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSVLEGiRTRHPPIVVHC 1024
Cdd:cd14540    81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRRHTNQDVAG-HNRNPPTLVHC 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642 1025 SAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQFL 1084
Cdd:cd14540   160 SAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
836-1082 3.22e-92

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 294.15  E-value: 3.22e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642   836 NAERSRIREVVPYEENRVELIPTKENNtGYINASHIKVVVGgsEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEE 915
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPS-DYINASYIDGYKK--PKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642   916 EGGRTKSHRYWPKlgSKHSSATYGKFKVTTK-FRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLS 994
Cdd:pfam00102   78 EKGREKCAQYWPE--EEGESLEYGDFTVTLKkEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLD 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642   995 YLEEIQSVRRHTnsvlegirtRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYK 1074
Cdd:pfam00102  156 LLRKVRKSSLDG---------RSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYI 226


                   ....*...
gi 568911642  1075 FVYQVLVQ 1082
Cdd:pfam00102  227 FLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
812-1082 7.66e-92

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 294.18  E-value: 7.66e-92
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642    812 VFTEYEQIP-NKKANGVFSTATLPENAERSRIREVVPYEENRVELIPTKENNTGYINASHIKVVvgGSEWHYIATQGPLP 890
Cdd:smart00194    2 LEEEFEKLDrLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGP--NGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642    891 HTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhsSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQER 970
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGE--PLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETR 157

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642    971 TVWHLQYTDWPHHGCPEDVQGFLSYLEEIqsvrRHTNSVLEGirtrhpPIVVHCSAGVGRTGVVILSELMIYCLEHNEKV 1050
Cdd:smart00194  158 TVTHYHYTNWPDHGVPESPESILDLIRAV----RKSQSTSTG------PIVVHCSAGVGRTGTFIAIDILLQQLEAGKEV 227

                           250       260       270
                    ....*....|....*....|....*....|..
gi 568911642   1051 EVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 1082
Cdd:smart00194  228 DIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 865-1078 1.04e-77

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: 253.36  E-value: 1.04e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  865 YINASHIKVvvGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHssATYGKFKVT 944
Cdd:cd00047     1 YINASYIDG--YRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKP--LEYGDITVT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  945 TKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSvlegirtrhpPIVVHC 1024
Cdd:cd00047    77 LVSEEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNG----------PIVVHC 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568911642 1025 SAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 1078
Cdd:cd00047   147 SAGVGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 797-1076 5.47e-72

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: 240.52  E-value: 5.47e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  797 DERLRALKKKLEDGMVFTEYEQIPNKKANGVFSTATLPENAERSRIREVVPYEENRVELiptkENNTGYINASHIKVVVG 876
Cdd:cd14600     1 EESMAQLKKGLESGTVLIQFEQLYRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVL----QGNEDYINASYVNMEIP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  877 GSEW--HYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLgskHSSATYGKFKVTTKFRTDSGCY 954
Cdd:cd14600    77 SANIvnKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDP---PDVMEYGGFRVQCHSEDCTIAY 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  955 ATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYleeIQSVRRhtnsvlegIRTRHPPIVVHCSAGVGRTGVV 1034
Cdd:cd14600   154 VFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSSDFLEF---VNYVRS--------KRVENEPVLVHCSAGIGRTGVL 222

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 568911642 1035 ILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFV 1076
Cdd:cd14600   223 VTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFV 264
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 865-1084 3.62e-69

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: 229.95  E-value: 3.62e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  865 YINASHIKVVVGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKlGSKHSSATYGKFKVT 944
Cdd:cd14538     1 YINASHIRIPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPD-SLNKPLICGGRLEVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  945 TKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYleeIQSVRRHTNSVlegirtrhpPIVVHC 1024
Cdd:cd14538    80 LEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRF---IRYMRRIHNSG---------PIVVHC 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642 1025 SAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQFL 1084
Cdd:cd14538   148 SAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 812-1077 2.88e-64

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: 218.77  E-value: 2.88e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  812 VFTEYEQIPNKKANGVFSTATLPENAERSRIREVVPYEENRVEL-IPTKENNTGYINASHikvvVGGSEWH--YIATQGP 888
Cdd:cd14543     5 IYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLpKRNGDERTDYINANF----MDGYKQKnaYIATQGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  889 LPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKlgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQ 968
Cdd:cd14543    81 LPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPL--EEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  969 ERTVWHLQYTDWPHHGCPEDVQGFLSYLEEiqsVRRHTNSVLEGIRTR---H---PPIVVHCSAGVGRTGVVILSELMIY 1042
Cdd:cd14543   159 SRQVTHFQFTSWPDFGVPSSAAALLDFLGE---VRQQQALAVKAMGDRwkgHppgPPIVVHCSAGIGRTGTFCTLDICLS 235

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 568911642 1043 CLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVY 1077
Cdd:cd14543   236 QLEDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 865-1076 3.58e-63

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: 213.34  E-value: 3.58e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  865 YINASHIKVVVGGSEW--HYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGskhSSATYGKFK 942
Cdd:cd14541     2 YINANYVNMEIPGSGIvnRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLG---ETMQFGNLQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  943 VTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYleeIQSVRRHTNSVLEgirtrhpPIVV 1022
Cdd:cd14541    79 ITCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDF---VKRVRQNRVGMVE-------PTVV 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568911642 1023 HCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFV 1076
Cdd:cd14541   149 HCSAGIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFV 202
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 865-1078 4.42e-60

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: 204.79  E-value: 4.42e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  865 YINASHIKVVVGGSEwHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPklgSKHSSATYGKFKVT 944
Cdd:cd18533     1 YINASYITLPGTSSK-RYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWP---SGEYEGEYGDLTVE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  945 ----TKFrtDSGCYATTGLKVKHlLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSvlegirtrHPPI 1020
Cdd:cd18533    77 lvseEEN--DDGGFIVREFELSK-EDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASL--------DPPI 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568911642 1021 VVHCSAGVGRTGVVILSELMIYCLE--HNEKVE-------VPTMLRFLREQRMFMIQTIAQYKFVYQ 1078
Cdd:cd18533   146 IVHCSAGVGRTGTFIALDSLLDELKrgLSDSQDledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 835-1084 7.22e-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: 199.29  E-value: 7.22e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  835 ENAERSRIREVVPYEENRVELiptkENNTGYINASHIKVVVGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAE 914
Cdd:cd14597     2 ENRKKNRYKNILPYDTTRVPL----GDEGGYINASFIKMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  915 EEGGRTKSHRYWPKLGSKhSSATYGKFKVT-TKFRTDSGcYATTGLKVKHLLSGQERTVWHLQYTDWPHHGC---PEDVQ 990
Cdd:cd14597    78 VEGGKIKCQRYWPEILGK-TTMVDNRLQLTlVRMQQLKN-FVIRVLELEDIQTREVRHITHLNFTAWPDHDTpsqPEQLL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  991 GFLSYLEEIQsvrrhtnsvlegirtRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTI 1070
Cdd:cd14597   156 TFISYMRHIH---------------KSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTE 220

                         250
                  ....*....|....
gi 568911642 1071 AQYKFVYQVLVQFL 1084
Cdd:cd14597   221 DQYIFCYQVILYVL 234
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 836-1086 1.81e-57

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: 198.84  E-value: 1.81e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  836 NAERSRIREVVPYEENRVELIPTKENNTG--YINASHIKVVVGGS-----EWHYIATQGPLPHTCHDFWQMVWEQGVNVI 908
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRDPNVPGsdYINANYIRNENEGPttdenAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  909 AMVTAEEEGGRTKSHRYWPKLGSKHSsatYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQ-ERTVWHLQYTDWPHHGCPE 987
Cdd:cd14544    81 VMTTKEVERGKNKCVRYWPDEGMQKQ---YGPYRVQNVSEHDTTDYTLRELQVSKLDQGDpIREIWHYQYLSWPDHGVPS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  988 DVQGFLSYLEEIQSVRRHTNSvlEGirtrhpPIVVHCSAGVGRTGVVILSELMIYCLEHNE---KVEVPTMLRFLREQRM 1064
Cdd:cd14544   158 DPGGVLNFLEDVNQRQESLPH--AG------PIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRS 229

                         250       260
                  ....*....|....*....|..
gi 568911642 1065 FMIQTIAQYKFVYQVLVQFLQN 1086
Cdd:cd14544   230 GMVQTEAQYKFIYVAVAQYIET 251
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 865-1082 1.85e-56

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: 194.39  E-value: 1.85e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  865 YINASHIKVVVGGSEW--HYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGskhSSATYGKFK 942
Cdd:cd14601     2 YINANYINMEIPSSSIinRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPS---GSSSYGGFQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  943 VTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHtnsvlegirtRHPPIVV 1022
Cdd:cd14601    79 VTCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAG----------KDEPVVV 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642 1023 HCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 1082
Cdd:cd14601   149 HCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 865-1077 6.85e-54

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: 186.79  E-value: 6.85e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  865 YINASHIkvvvggSEWH----YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhssaTYGK 940
Cdd:cd14549     1 YINANYV------DGYNkaraYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTE----TYGN 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  941 FKVTTKFRTDSGCYATTGLKVKHL------LSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSvlegir 1014
Cdd:cd14549    71 IQVTLLSTEVLATYTVRTFSLKNLklkkvkGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAG------ 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568911642 1015 trhpPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVY 1077
Cdd:cd14549   145 ----PIVVHCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 865-1085 7.34e-53

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: 183.80  E-value: 7.34e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  865 YINASHIKVVVGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKlgSKHSSATYGKFKVT 944
Cdd:cd14596     1 YINASYITMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPE--TLQEPMELENYQLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  945 TKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRhtnsvlEGirtrhpPIVVHC 1024
Cdd:cd14596    79 LENYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHN------TG------PIVVHC 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568911642 1025 SAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQFLQ 1085
Cdd:cd14596   147 SAGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 841-1078 1.36e-52

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: 183.71  E-value: 1.36e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  841 RIREVVPYEENRVELIP-TKENNTGYINASHIKvvvgG--SEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEG 917
Cdd:cd14548     1 RYTNILPYDHSRVKLIPiNEEEGSDYINANYIP----GynSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  918 GRTKSHRYWPKlgsKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHllSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLE 997
Cdd:cd14548    77 GRVKCDHYWPF---DQDPVYYGDITVTMLSESVLPDWTIREFKLER--GDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVR 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  998 EIQSVRRHTNSvlegirtrhpPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVY 1077
Cdd:cd14548   152 LVRDYIKQEKG----------PTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221


                  .
gi 568911642 1078 Q 1078
Cdd:cd14548   222 Q 222
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 814-1082 5.50e-52

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: 183.87  E-value: 5.50e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  814 TEYEQIPNK----KANGVFST--ATLPENAERSRIREVVPYEENRVELIP-TKENNTGYINASHIKVVVGgsEWHYIATQ 886
Cdd:cd14603     2 GEFSEIRACsaafKADYVCSTvaGGRKENVKKNRYKDILPYDQTRVILSLlQEEGHSDYINANFIKGVDG--SRAYIATQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  887 GPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPklgSKHSSATYGKFKVTT--KFRTDSGCYATTgLKVKHl 964
Cdd:cd14603    80 GPLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWA---QEQEPLQTGPFTITLvkEKRLNEEVILRT-LKVTF- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  965 lSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEiqsVRRHTNSVLEgirtrhpPIVVHCSAGVGRTGVVILSElMIYCL 1044
Cdd:cd14603   155 -QKESRSVSHFQYMAWPDHGIPDSPDCMLAMIEL---ARRLQGSGPE-------PLCVHCSAGCGRTGVICTVD-YVRQL 222

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 568911642 1045 EHNEKVEvPTMLRF-----LREQRMFMIQTIAQYKFVYQVLVQ 1082
Cdd:cd14603   223 LLTQRIP-PDFSIFdvvleMRKQRPAAVQTEEQYEFLYHTVAQ 264
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 834-1085 8.84e-52

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: 183.16  E-value: 8.84e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  834 PENAERSRIREVVPYEENRVELIPTKENNTG--YINASHIK---VVVGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVI 908
Cdd:cd14606    16 PENKSKNRYKNILPFDHSRVILQGRDSNIPGsdYINANYVKnqlLGPDENAKTYIASQGCLEATVNDFWQMAWQENSRVI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  909 AMVTAEEEGGRTKSHRYWPKLGSKHSsatYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQE-RTVWHLQYTDWPHHGCPE 987
Cdd:cd14606    96 VMTTREVEKGRNKCVPYWPEVGMQRA---YGPYSVTNCGEHDTTEYKLRTLQVSPLDNGELiREIWHYQYLSWPDHGVPS 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  988 DVQGFLSYLEEIqsvrrhtNSVLEGIRtRHPPIVVHCSAGVGRTGVVILSELMIYCLEH---NEKVEVPTMLRFLREQRM 1064
Cdd:cd14606   173 EPGGVLSFLDQI-------NQRQESLP-HAGPIIVHCSAGIGRTGTIIVIDMLMENISTkglDCDIDIQKTIQMVRAQRS 244

                         250       260
                  ....*....|....*....|.
gi 568911642 1065 FMIQTIAQYKFVYQVLVQFLQ 1085
Cdd:cd14606   245 GMVQTEAQYKFIYVAIAQFIE 265
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 865-1078 9.10e-52

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: 180.66  E-value: 9.10e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  865 YINASHIKVVVGGSEwHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKlgSKHSSATYGKFKVT 944
Cdd:cd14539     1 YINASLIEDLTPYCP-RFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPT--ERGQALVYGAITVS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  945 TKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHtnsvlegIRTRHPPIVVHC 1024
Cdd:cd14539    78 LQSVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQ-------QRSLQTPIVVHC 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568911642 1025 SAGVGRTGV-VILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 1078
Cdd:cd14539   151 SSGVGRTGAfCLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 836-1082 2.22e-51

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: 181.06  E-value: 2.22e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  836 NAERSRIREVVPYEENRVELIPTK-ENNTGYINASHIKvvvgGSEWH--YIATQGPLPHTCHDFWQMVWEQGVNVIAMVT 912
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVILQPIEgVPGSDYINANYCD----GYRKQnaYIATQGPLPETFGDFWRMVWEQRSATIVMMT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  913 AEEEGGRTKSHRYWPKLGskhsSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGF 992
Cdd:cd14553    79 KLEERSRVKCDQYWPTRG----TETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPF 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  993 LSYLeeiqsvRRhtnsvlegIRTRHP----PIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQ 1068
Cdd:cd14553   155 LAFL------RR--------VKACNPpdagPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQ 220

                         250
                  ....*....|....
gi 568911642 1069 TIAQYKFVYQVLVQ 1082
Cdd:cd14553   221 TEDQYIFIHDALLE 234
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 831-1078 3.32e-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: 180.41  E-value: 3.32e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  831 ATLPENAERSRIREVVPYEENRVELIPTK-ENNTGYINASHIKvvvgGSEWH--YIATQGPLPHTCHDFWQMVWEQGVNV 907
Cdd:cd14554     1 ANLPCNKFKNRLVNILPYESTRVCLQPIRgVEGSDYINASFID----GYRQRgaYIATQGPLAETTEDFWRMLWEHNSTI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  908 IAMVTAEEEGGRTKSHRYWPklgsKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPE 987
Cdd:cd14554    77 IVMLTKLREMGREKCHQYWP----AERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPK 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  988 DVQGFLSYLEEIQSVRRHTNSvlEGirtrhpPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMI 1067
Cdd:cd14554   153 SGEGFIDFIGQVHKTKEQFGQ--EG------PITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMV 224

                         250
                  ....*....|.
gi 568911642 1068 QTIAQYKFVYQ 1078
Cdd:cd14554   225 QTEDQYQFCYR 235
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 841-1078 9.65e-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: 175.66  E-value: 9.65e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  841 RIREVVPYEENRVeLIPTKENN--TGYINASHIKVVvGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGg 918
Cdd:cd14547     2 RYKTILPNEHSRV-CLPSVDDDplSSYINANYIRGY-DGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  919 RTKSHRYWPKLgskhSSATYGKFKVTTKFRTDSGCYATTGLKVKHllSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEE 998
Cdd:cd14547    79 KEKCAQYWPEE----ENETYGDFEVTVQSVKETDGYTVRKLTLKY--GGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQE 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  999 IQSVRRHTNSvlegirtrHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 1078
Cdd:cd14547   153 VEEARQTEPH--------RGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 815-1084 5.36e-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: 176.08  E-value: 5.36e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  815 EYEQIPNKKAN-GVFSTATLPENAERSRIREVVPYEENRVELIPTKE-NNTGYINASHIKVVvgGSEWHYIATQGPLPHT 892
Cdd:cd14627    31 EFKRLANSKAHtSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGvEGSDYINASFIDGY--RQQKAYIATQGPLAET 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  893 CHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPklgsKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTV 972
Cdd:cd14627   109 TEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWP----AERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTV 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  973 WHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNsvlegirtRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEV 1052
Cdd:cd14627   185 RQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFG--------QDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDI 256

                         250       260       270
                  ....*....|....*....|....*....|..
gi 568911642 1053 PTMLRFLREQRMFMIQTIAQYKFVYQVLVQFL 1084
Cdd:cd14627   257 FQTVKMLRTQRPAMVQTEDEYQFCYQAALEYL 288
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 840-1084 5.60e-49

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: 173.92  E-value: 5.60e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  840 SRIREVVPYEENRVELIPTKENNTG-YINASHIKVVvgGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGG 918
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPGSdYINANYMPGY--WSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  919 RTKSHRYWPklgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEe 998
Cdd:cd14619    79 RVKCEHYWP---LDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRR- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  999 iqSVRRHTNSVLEGirtrhPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 1078
Cdd:cd14619   155 --LLRQWLDQTMSG-----GPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQ 227


                  ....*.
gi 568911642 1079 VLVQFL 1084
Cdd:cd14619   228 CILDFL 233
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 835-1085 8.11e-49

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: 174.05  E-value: 8.11e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  835 ENAERSRIREVVPYEENRVELIPTKENNTG--YINASHI------KVVVGGSEWHYIATQGPLPHTCHDFWQMVWEQGVN 906
Cdd:cd14605     1 ENKNKNRYKNILPFDHTRVVLHDGDPNEPVsdYINANIImpefetKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  907 VIAMVTAEEEGGRTKSHRYWPklgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQ-ERTVWHLQYTDWPHHGC 985
Cdd:cd14605    81 VIVMTTKEVERGKSKCVKYWP---DEYALKEYGVMRVRNVKESAAHDYILRELKLSKVGQGNtERTVWQYHFRTWPDHGV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  986 PEDVQGFLSYLEEIqsvrrhtNSVLEGIrTRHPPIVVHCSAGVGRTGVVILSELMIYCLEhnEK-----VEVPTMLRFLR 1060
Cdd:cd14605   158 PSDPGGVLDFLEEV-------HHKQESI-MDAGPVVVHCSAGIGRTGTFIVIDILIDIIR--EKgvdcdIDVPKTIQMVR 227

                         250       260
                  ....*....|....*....|....*
gi 568911642 1061 EQRMFMIQTIAQYKFVYQVLVQFLQ 1085
Cdd:cd14605   228 SQRSGMVQTEAQYRFIYMAVQHYIE 252
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 839-1082 8.79e-49

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: 173.49  E-value: 8.79e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  839 RSRIREVVPYEENRVEL-IPTKENNTGYINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEG 917
Cdd:cd14602     1 KNRYKDILPYDHSRVELsLITSDEDSDYINANFIKGVYGPRA--YIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  918 GRTKSHRYWPKLGSkhSSATYGKFKVTTKFRTDSGCYATTGLKVKhlLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLE 997
Cdd:cd14602    79 GKKKCERYWAEPGE--MQLEFGPFSVTCEAEKRKSDYIIRTLKVK--FNSETRTIYQFHYKNWPDHDVPSSIDPILELIW 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  998 EIQSVRRHTNsvlegirtrhPPIVVHCSAGVGRTGVVILSELMIYCLEHN---EKVEVPTMLRFLREQRMFMIQTIAQYK 1074
Cdd:cd14602   155 DVRCYQEDDS----------VPICIHCSAGCGRTGVICAIDYTWMLLKDGiipENFSVFSLIQEMRTQRPSLVQTKEQYE 224


                  ....*...
gi 568911642 1075 FVYQVLVQ 1082
Cdd:cd14602   225 LVYNAVIE 232
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 815-1084 5.60e-48

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: 172.99  E-value: 5.60e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  815 EYEQIPNKKAN-GVFSTATLPENAERSRIREVVPYEENRVELIPTKE-NNTGYINASHIKVVvgGSEWHYIATQGPLPHT 892
Cdd:cd14628    30 EFKRLASSKAHtSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGvEGSDYINASFIDGY--RQQKAYIATQGPLAET 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  893 CHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPklgsKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTV 972
Cdd:cd14628   108 TEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWP----AERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTV 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  973 WHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNsvlegirtRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEV 1052
Cdd:cd14628   184 RQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFG--------QDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDI 255

                         250       260       270
                  ....*....|....*....|....*....|..
gi 568911642 1053 PTMLRFLREQRMFMIQTIAQYKFVYQVLVQFL 1084
Cdd:cd14628   256 FQTVKMLRTQRPAMVQTEDQYQFCYRAALEYL 287
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 816-1082 3.22e-47

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: 170.59  E-value: 3.22e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  816 YEQIPNKKANGVFSTATLPENAERSRIREVVPYEENRVELipTKENNTgYINASHIKVvvGGSEWHYIATQGPLPHTCHD 895
Cdd:cd14608     5 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKL--HQEDND-YINASLIKM--EEAQRSYILTQGPLPNTCGH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  896 FWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHL 975
Cdd:cd14608    80 FWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  976 QYTDWPHHGCPEDVQGFLSYLEEIqsvrRHTNSvlegIRTRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNE---KVEV 1052
Cdd:cd14608   160 HYTTWPDFGVPESPASFLNFLFKV----RESGS----LSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKdpsSVDI 231

                         250       260       270
                  ....*....|....*....|....*....|
gi 568911642 1053 PTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 1082
Cdd:cd14608   232 KKVLLEMRKFRMGLIQTADQLRFSYLAVIE 261
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 840-1078 5.99e-47

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: 167.78  E-value: 5.99e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  840 SRIREVVPYEENRVELIPTKEN-NTGYINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGG 918
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVpGSDYINASYISGYLCPNE--FIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  919 RTKSHRYWPKlgSKHSSATYGKFKVTTKFRTDSGCYATTGLKV-KHllsGQERTVWHLQYTDWPHHGCPEDVQGFLSYLE 997
Cdd:cd14616    79 RIRCHQYWPE--DNKPVTVFGDIVITKLMEDVQIDWTIRDLKIeRH---GDYMMVRQCNFTSWPEHGVPESSAPLIHFVK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  998 EIQSVRRHTNSvlegirtrhpPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVY 1077
Cdd:cd14616   154 LVRASRAHDNT----------PMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223


                  .
gi 568911642 1078 Q 1078
Cdd:cd14616   224 Q 224
PHA02738 PHA02738
hypothetical protein; Provisional
 815-1085 2.32e-46

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 169.34  E-value: 2.32e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  815 EYEQIPNKKANGVFSTATlpENAERSRIREVVPYEENRVELiPTKENNTGYINASHikvvVGGSEW--HYIATQGPLPHT 892
Cdd:PHA02738   30 EHQKVISEKVDGTFNAEK--KNRKLNRYLDAVCFDHSRVIL-PAERNRGDYINANY----VDGFEYkkKFICGQAPTRQT 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  893 CHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLgsKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLlSGQERTV 972
Cdd:PHA02738  103 CYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDV--EQGSIRFGKFKITTTQVETHPHYVKSTLLLTDG-TSATQTV 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  973 WHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRR--HTNSVLEG-IRTRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEK 1049
Cdd:PHA02738  180 THFNFTAWPDHDVPKNTSEFLNFVLEVRQCQKelAQESLQIGhNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACAT 259

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 568911642 1050 VEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQFLQ 1085
Cdd:PHA02738  260 VSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRYVN 295
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 798-1082 2.84e-46

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: 167.52  E-value: 2.84e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  798 ERLRAlkkklEDGMVFT-EYEQI-PNKKANgvFSTATLPENAERSRIREVVPYEENRVELIPTKE-NNTGYINASHIKvv 874
Cdd:cd14626     8 ERLKA-----NDGLKFSqEYESIdPGQQFT--WENSNLEVNKPKNRYANVIAYDHSRVILTSVDGvPGSDYINANYID-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  875 vGGSEWH-YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhssaTYGKFKVTTKFRTDSGC 953
Cdd:cd14626    79 -GYRKQNaYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTE----TYGMIQVTLLDTVELAT 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  954 YATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVrrhtNSVLEGirtrhpPIVVHCSAGVGRTGV 1033
Cdd:cd14626   154 YSVRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKAC----NPPDAG------PMVVHCSAGVGRTGC 223

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 568911642 1034 VILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 1082
Cdd:cd14626   224 FIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 839-1078 3.59e-46

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: 165.64  E-value: 3.59e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  839 RSRIREVVPYEENRVELiptKENNTGYINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGG 918
Cdd:cd14545     3 RYRDRDPYDHDRSRVKL---KQGDNDYINASLVEVEEAKRS--YILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  919 RTKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLee 998
Cdd:cd14545    78 QIKCAQYWPQGEGNAMIFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFL-- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  999 iQSVRRHtnSVLEgirTRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNE--KVEVPTMLRFLREQRMFMIQTIAQYKFV 1076
Cdd:cd14545   156 -QKVRES--GSLS---SDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKYRMGLIQTPDQLRFS 229


                  ..
gi 568911642 1077 YQ 1078
Cdd:cd14545   230 YL 231
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 840-1078 1.25e-45

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: 163.94  E-value: 1.25e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  840 SRIREVVPYEENRVELIPTKENN-TGYINASHIKvvvGGS-EWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEG 917
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPcSDYINASYIP---GNNfRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  918 GRTKSHRYWPklgSKHSSATYGKFKVttKFRTDSGCYATTGLKVKhlLSGQE-----RTVWHLQYTDWPHHGCPEDVQGF 992
Cdd:cd14617    78 GRVKCDHYWP---ADQDSLYYGDLIV--QMLSESVLPEWTIREFK--ICSEEqldapRLVRHFHYTVWPDHGVPETTQSL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  993 LSYleeIQSVRRHTNsvlegiRTRHP-PIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIA 1071
Cdd:cd14617   151 IQF---VRTVRDYIN------RTPGSgPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTEC 221


                  ....*..
gi 568911642 1072 QYKFVYQ 1078
Cdd:cd14617   222 QYVYLHQ 228
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 841-1078 1.72e-45

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: 163.83  E-value: 1.72e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  841 RIREVVPYEENRVELIPTKENNTGYINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRT 920
Cdd:cd14615     2 RYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKE--FIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  921 KSHRYWPKLGSKhssaTYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEeiq 1000
Cdd:cd14615    80 KCEEYWPSKQKK----DYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRH--- 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568911642 1001 SVRRHTNSVLegirtRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 1078
Cdd:cd14615   153 LVREYMKQNP-----PNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 225
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 816-1077 3.15e-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: 163.98  E-value: 3.15e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  816 YEQIPNKKANGVFSTATLPENAERSRIREVVPYEENRVELIPTkENNtgYINAShiKVVVGGSEWHYIATQGPLPHTCHD 895
Cdd:cd14607     4 YLEIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNT-END--YINAS--LVVIEEAQRSYILTQGPLPNTCCH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  896 FWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHL 975
Cdd:cd14607    79 FWLMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKETGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  976 QYTDWPHHGCPEDVQGFLSYLEEIQSVRrhtnsvleGIRTRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNE--KVEVP 1053
Cdd:cd14607   159 HYTTWPDFGVPESPASFLNFLFKVRESG--------SLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIK 230

                         250       260
                  ....*....|....*....|....
gi 568911642 1054 TMLRFLREQRMFMIQTIAQYKFVY 1077
Cdd:cd14607   231 QVLLDMRKYRMGLIQTPDQLRFSY 254
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 833-1083 4.48e-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: 163.08  E-value: 4.48e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  833 LPENAERSRIREVVPYEENRVEL--IPTKENNTGYINASHIKVVvGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAM 910
Cdd:cd14612    12 IPGHASKDRYKTILPNPQSRVCLrrAGSQEEEGSYINANYIRGY-DGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVM 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  911 VTAEEEGgRTKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCYATTGLKVKHllSGQERTVWHLQYTDWPHHGCPEDVQ 990
Cdd:cd14612    91 ITKLKEK-KEKCVHYWPE-----KEGTYGRFEIRVQDMKECDGYTIRDLTIQL--EEESRSVKHYWFSSWPDHQTPESAG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  991 GFLSYLEEIQSVRRHTNSVlegirtrhPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTI 1070
Cdd:cd14612   163 PLLRLVAEVEESRQTAASP--------GPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTS 234

                         250
                  ....*....|...
gi 568911642 1071 AQYKFVYQVLVQF 1083
Cdd:cd14612   235 EQYQFLHHTLALY 247
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 815-1084 6.81e-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: 164.13  E-value: 6.81e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  815 EYEQIPNKKAN-GVFSTATLPENAERSRIREVVPYEENRVELIPTKE-NNTGYINASHIKVVvgGSEWHYIATQGPLPHT 892
Cdd:cd14629    31 EFKLLANSKAHtSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGvEGSDYINASFIDGY--RQQKAYIATQGPLAET 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  893 CHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPklgsKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTV 972
Cdd:cd14629   109 TEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWP----AERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTI 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  973 WHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNsvlegirtRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEV 1052
Cdd:cd14629   185 RQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEQFG--------QDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDM 256

                         250       260       270
                  ....*....|....*....|....*....|..
gi 568911642 1053 PTMLRFLREQRMFMIQTIAQYKFVYQVLVQFL 1084
Cdd:cd14629   257 FQTVKTLRTQRPAMVQTEDQYQLCYRAALEYL 288
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 865-1078 6.71e-44

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: 157.97  E-value: 6.71e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  865 YINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhsSATYGKFKVT 944
Cdd:cd14542     1 YINANFIKGVSGSKA--YIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEE--QLQFGPFKIS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  945 ---TKFRTDSgcYATTGLKVKhlLSGQERTVWHLQYTDWPHHGCPEDVQgflSYLEEIQSVRRHTNSvlegirtRHPPIV 1021
Cdd:cd14542    77 lekEKRVGPD--FLIRTLKVT--FQKESRTVYQFHYTAWPDHGVPSSVD---PILDLVRLVRDYQGS-------EDVPIC 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568911642 1022 VHCSAGVGRTGVV--------ILSELMIyclehNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 1078
Cdd:cd14542   143 VHCSAGCGRTGTIcaidyvwnLLKTGKI-----PEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 865-1078 1.02e-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: 157.68  E-value: 1.02e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  865 YINASHIKvvvGGSE-WHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLgsKHSSATYGkfKV 943
Cdd:cd14557     1 YINASYID---GFKEpRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSM--EEGSRAFG--DV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  944 TTKFRTDSGC--YATTGLKVKHLL-SGQERTVWHLQYTDWPHHGCPEDVQGFLsyleeiqSVRRHTNSVLEGIRTrhpPI 1020
Cdd:cd14557    74 VVKINEEKICpdYIIRKLNINNKKeKGSGREVTHIQFTSWPDHGVPEDPHLLL-------KLRRRVNAFNNFFSG---PI 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568911642 1021 VVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 1078
Cdd:cd14557   144 VVHCSAGVGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 798-1085 7.46e-43

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: 158.56  E-value: 7.46e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  798 ERLRALKKKLEDG-----MVFTEYEQIPNK-KANGVFSTAT--LPENAERSRIREVVPYEENRVEL-IPTKENNTGYINA 868
Cdd:cd14604    11 ERVQAMKSTDHNGednfaSDFMRLRRLSTKyRTEKIYPTATgeKEENVKKNRYKDILPFDHSRVKLtLKTSSQDSDYINA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  869 SHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhsSATYGKFKVT---T 945
Cdd:cd14604    91 NFIKGVYGPKA--YIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGEE--PMTFGPFRISceaE 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  946 KFRTDsgcYATTGLKVKhlLSGQERTVWHLQYTDWPHHGCPedvQGFLSYLEEIQSVRRHTNSvlegirtRHPPIVVHCS 1025
Cdd:cd14604   167 QARTD---YFIRTLLLE--FQNETRRLYQFHYVNWPDHDVP---SSFDSILDMISLMRKYQEH-------EDVPICIHCS 231

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568911642 1026 AGVGRTGVVILSELMIYCLEHN---EKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQFLQ 1085
Cdd:cd14604   232 AGCGRTGAICAIDYTWNLLKAGkipEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFE 294
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 815-1082 7.72e-43

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: 157.95  E-value: 7.72e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  815 EYEQI-PNKKANgvFSTATLPENAERSRIREVVPYEENRVELIPTKE-NNTGYINASHIKVVvgGSEWHYIATQGPLPHT 892
Cdd:cd14625    27 EYESIdPGQQFT--WEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGiMGSDYINANYIDGY--RKQNAYIATQGPLPET 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  893 CHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhssaTYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTV 972
Cdd:cd14625   103 FGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTE----TYGMIQVTLLDTIELATFCVRTFSLHKNGSSEKREV 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  973 WHLQYTDWPHHGCPEDVQGFLSYLEEIQSVrrhtNSVLEGirtrhpPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEV 1052
Cdd:cd14625   179 RQFQFTAWPDHGVPEYPTPFLAFLRRVKTC----NPPDAG------PIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDI 248

                         250       260       270
                  ....*....|....*....|....*....|
gi 568911642 1053 PTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 1082
Cdd:cd14625   249 YGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 834-1082 9.86e-43

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: 157.50  E-value: 9.86e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  834 PENAERSRIREVVPYEENRVEL--IPTKEN-NTGYINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAM 910
Cdd:cd17667    25 PDNKHKNRYINILAYDHSRVKLrpLPGKDSkHSDYINANYVDGYNKAKA--YIATQGPLKSTFEDFWRMIWEQNTGIIVM 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  911 VTAEEEGGRTKSHRYWPklgsKHSSATYGKFKVTTKFRTDSGCYATTGL-----KVKHLLSGQ------ERTVWHLQYTD 979
Cdd:cd17667   103 ITNLVEKGRRKCDQYWP----TENSEEYGNIIVTLKSTKIHACYTVRRFsirntKVKKGQKGNpkgrqnERTVIQYHYTQ 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  980 WPHHGCPEDVQGFLSYleeiqsVRRHTNSvlegiRTRH-PPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRF 1058
Cdd:cd17667   179 WPDMGVPEYALPVLTF------VRRSSAA-----RTPEmGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKH 247

                         250       260
                  ....*....|....*....|....
gi 568911642 1059 LREQRMFMIQTIAQYKFVYQVLVQ 1082
Cdd:cd17667   248 IRTQRNYLVQTEEQYIFIHDALLE 271
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 840-1081 2.75e-42

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: 154.72  E-value: 2.75e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  840 SRIREVVPYEENRVELIP-TKENNTGYINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGG 918
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQlGGEPHSDYINANFIPGYTSPQE--FIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  919 RTKSHRYWPklgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEE 998
Cdd:cd14618    79 RVLCDHYWP---SESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFREL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  999 IQSVRRHTNSvlegirtrHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 1078
Cdd:cd14618   156 VREHVQATKG--------KGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHS 227


                  ...
gi 568911642 1079 VLV 1081
Cdd:cd14618   228 CIL 230
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 865-1077 5.82e-42

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


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 152.60  E-value: 5.82e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  865 YINASHIKVvvggsewH------YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhssaTY 938
Cdd:cd14546     1 YINASTIYD-------HdprnpaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSE----VY 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  939 GKFKVTTkFRTDSGC--YATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYleeiqsvRRHTNSVLEGirtR 1016
Cdd:cd14546    70 HIYEVHL-VSEHIWCddYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEF-------RRKVNKSYRG---R 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568911642 1017 HPPIVVHCSAGVGRTGVVILSELMIYCLEHNEK-VEVPTMLRFLREQRMFMIQTIAQYKFVY 1077
Cdd:cd14546   139 SCPIVVHCSDGAGRTGTYILIDMVLNRMAKGAKeIDIAATLEHLRDQRPGMVKTKDQFEFVL 200
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 830-1084 6.46e-42

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: 153.89  E-value: 6.46e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  830 TATLPENAERSRIREVVPYEENRVELIPT-KENNTGYINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVI 908
Cdd:cd14614     6 AADLPVNRCKNRYTNILPYDFSRVKLVSMhEEEGSDYINANYIPGYNSPQE--YIATQGPLPETRNDFWKMVLQQKSQII 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  909 AMVTAEEEGGRTKSHRYWPklgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQErtVWHLQYTDWPHHGCPeD 988
Cdd:cd14614    84 VMLTQCNEKRRVKCDHYWP---FTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQD--VMHFNYTAWPDHGVP-T 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  989 VQGFLSYLEEIQSVRRHTNSvlegirtRHPPIVVHCSAGVGRTGVVI-LSELMIYCLEHnEKVEVPTMLRFLREQRMFMI 1067
Cdd:cd14614   158 ANAAESILQFVQMVRQQAVK-------SKGPMIIHCSAGVGRTGTFIaLDRLLQHIRDH-EFVDILGLVSEMRSYRMSMV 229

                         250
                  ....*....|....*..
gi 568911642 1068 QTIAQYKFVYQVlVQFL 1084
Cdd:cd14614   230 QTEEQYIFIHQC-VQLM 245
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 865-1081 7.98e-42

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: 152.44  E-value: 7.98e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  865 YINASHIKVVvgGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHssatYGKFKVT 944
Cdd:cd17668     1 YINANYVDGY--NKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEE----YGNFLVT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  945 TKFRTDSGCYATTGLKVKH--LLSG------QERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSvlegirtr 1016
Cdd:cd17668    75 QKSVQVLAYYTVRNFTLRNtkIKKGsqkgrpSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVG-------- 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568911642 1017 hpPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLV 1081
Cdd:cd17668   147 --PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 815-1083 4.73e-41

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 153.62  E-value: 4.73e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  815 EYEQIpnKKANGVFSTATLPENAERSRIR--EVVPYEENRVeLIPTKENNTGYINASHikvvVGG--SEWHYIATQGPLP 890
Cdd:PHA02742   31 EHEHI--MQEIVAFSCNESLELKNMKKCRypDAPCFDRNRV-ILKIEDGGDDFINASY----VDGhnAKGRFICTQAPLE 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  891 HTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWpkLGSKHSSATYGKFKVTTK----FRTdsgcYATTGLKVKHLLS 966
Cdd:PHA02742  104 ETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYW--MPHERGKATHGEFKIKTKkiksFRN----YAVTNLCLTDTNT 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  967 GQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSVLEG-IRTRHPPIVVHCSAGVGRTGVVILSELMIYclE 1045
Cdd:PHA02742  178 GASLDIKHFAYEDWPHGGLPRDPNKFLDFVLAVREADLKADVDIKGeNIVKEPPILVHCSAGLDRAGAFCAIDICIS--K 255

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 568911642 1046 HNEKVEVP--TMLRFLREQRMFMIQTIAQYKFVYQVLVQF 1083
Cdd:PHA02742  256 YNERAIIPllSIVRDLRKQRHNCLSLPQQYIFCYFIVLIF 295
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 845-1082 8.43e-41

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: 150.09  E-value: 8.43e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  845 VVPYEENRVELIPTKEN-NTGYINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSH 923
Cdd:cd14620     4 ILPYDHSRVILSQLDGIpCSDYINASYIDGYKEKNK--FIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKCY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  924 RYWPKLGSkhssATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQ---ERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQ 1000
Cdd:cd14620    82 QYWPDQGC----WTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGckaPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642 1001 SVrrhtNSVLEGirtrhpPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVL 1080
Cdd:cd14620   158 SV----NPVHAG------PIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQAL 227


                  ..
gi 568911642 1081 VQ 1082
Cdd:cd14620   228 LE 229
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 865-1078 1.71e-40

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


Pssm-ID: 350399 [Multi-domain]  Cd Length: 202  Bit Score: 148.52  E-value: 1.71e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  865 YINASHIKvvvGGSEWH-YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhssaTYGKFKV 943
Cdd:cd14551     1 YINASYID---GYQEKNkFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCW----TYGNLRV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  944 TTKFRTDSGCYATTGLKVKHLLSG----QERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVrrhtNSVLEGirtrhpP 1019
Cdd:cd14551    74 RVEDTVVLVDYTTRKFCIQKVNRGigekRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSA----NPPRAG------P 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568911642 1020 IVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 1078
Cdd:cd14551   144 IVVHCSAGVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 798-1082 2.23e-40

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: 151.04  E-value: 2.23e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  798 ERLRAlkkklEDGMVFT-EYEQI-PNKKANgvFSTATLPENAERSRIREVVPYEENRVeLIPTKENNTG--YINASHIKV 873
Cdd:cd14624    14 ERLKA-----NDNLKFSqEYESIdPGQQFT--WEHSNLEVNKPKNRYANVIAYDHSRV-LLSAIEGIPGsdYINANYIDG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  874 VvgGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhssaTYGKFKVTTKFRTDSGC 953
Cdd:cd14624    86 Y--RKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTE----TYGLIQVTLLDTVELAT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  954 YATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVrrhtNSVLEGirtrhpPIVVHCSAGVGRTGV 1033
Cdd:cd14624   160 YCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTC----NPPDAG------PMVVHCSAGVGRTGC 229

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 568911642 1034 VILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 1082
Cdd:cd14624   230 FIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 865-1081 2.40e-40

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: 147.80  E-value: 2.40e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  865 YINASHIKVVvgGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGskhsSATYGKFKVT 944
Cdd:cd14552     1 YINASFIDGY--RQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDG----SVSSGDITVE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  945 TKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNsvlegirtrHPPIVVHC 1024
Cdd:cd14552    75 LKDQTDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSG---------NHPITVHC 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568911642 1025 SAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLV 1081
Cdd:cd14552   146 SAGAGRTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVVQ 202
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 865-1077 2.80e-40

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: 147.92  E-value: 2.80e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  865 YINASHIKvvvggSEWH---YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKlgskhSSATYGKF 941
Cdd:cd14558     1 YINASFID-----GYWGpksLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGD-----EKKTYGDI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  942 KVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSvRRHTNSVLEGirtRHPPIV 1021
Cdd:cd14558    71 EVELKDTEKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQ-KLPYKNSKHG---RSVPIV 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568911642 1022 VHCSAGVGRTGvvilselmIYC-----LE--HNEK-VEVPTMLRFLREQRMFMIQTIAQYKFVY 1077
Cdd:cd14558   147 VHCSDGSSRTG--------IFCalwnlLEsaETEKvVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 865-1077 3.03e-40

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: 147.61  E-value: 3.03e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  865 YINASHIKVVVGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRT-KSHRYWPKlgSKHSSATYGKFKV 943
Cdd:cd17658     1 YINASLVETPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPA--EENESREFGRISV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  944 TTK-FRTDSGCYATTGLKVKHL-LSGQERTVWHLQYTDWPHHGCPEDVQgflsYLEEIqsVRRhtnsvLEGIRTRHPPIV 1021
Cdd:cd17658    79 TNKkLKHSQHSITLRVLEVQYIeSEEPPLSVLHIQYPEWPDHGVPKDTR----SVREL--LKR-----LYGIPPSAGPIV 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568911642 1022 VHCSAGVGRTGVvilselmiYCLEHN----------EKVEVPTMLRFLREQRMFMIQTIAQYKFVY 1077
Cdd:cd17658   148 VHCSAGIGRTGA--------YCTIHNtirrilegdmSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 841-1080 1.20e-39

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: 146.73  E-value: 1.20e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  841 RIREVVPYEENRVeLIPTK--ENNTGYINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGG 918
Cdd:cd14623     1 RVLQIIPYEFNRV-IIPVKrgEENTDYVNASFIDGYRQKDS--YIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  919 RTKSHRYWPKLGskhsSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEE 998
Cdd:cd14623    78 QEKCAQYWPSDG----SVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  999 IQSVRRHTNSvlegirtrhPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 1078
Cdd:cd14623   154 VQKQQQQSGN---------HPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYK 224


                  ..
gi 568911642 1079 VL 1080
Cdd:cd14623   225 VV 226
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 839-1078 9.25e-39

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: 144.29  E-value: 9.25e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  839 RSRIREVVPYEENRVELIPTKENN--TGYINASHIKVVvGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEE 916
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKNSNDslSTYINANYIRGY-GGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  917 GGRtKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCYATTGLKVKHllSGQERTVWHLQYTDWPHHGCPEDVQGFLSYL 996
Cdd:cd14611    81 KNE-KCVLYWPE-----KRGIYGKVEVLVNSVKECDNYTIRNLTLKQ--GSQSRSVKHYWYTSWPDHKTPDSAQPLLQLM 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  997 EEIQSVRRhtNSVLEGirtrhpPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFV 1076
Cdd:cd14611   153 LDVEEDRL--ASPGRG------PVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFV 224


                  ..
gi 568911642 1077 YQ 1078
Cdd:cd14611   225 HH 226
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 794-1082 1.74e-38

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: 145.94  E-value: 1.74e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  794 VPIDERLRALKKKL-EDGMVF-TEYEQIPNKKANGVFSTATLPENAERSRIREVVPYEENRVELIPTKE-NNTGYINASH 870
Cdd:cd14621     8 LPVDKLEEEINRRMaDDNKLFrEEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGvPDSDYINASF 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  871 IKvvvGGSEWH-YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSkhssATYGKFKVTTKFRT 949
Cdd:cd14621    88 IN---GYQEKNkFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGC----WTYGNIRVSVEDVT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  950 DSGCYATTGLKVKHL--LSGQ--ERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVrrhtNSVLEGirtrhpPIVVHCS 1025
Cdd:cd14621   161 VLVDYTVRKFCIQQVgdVTNKkpQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNC----NPQYAG------AIVVHCS 230

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568911642 1026 AGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 1082
Cdd:cd14621   231 AGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLE 287
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 810-1084 1.83e-38

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 146.30  E-value: 1.83e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  810 GMVFTEYEQIPNKKANGVFSTATLPENAERSRIREVVPYEENRVELIPTKENNTGYINASHIKvvvgGSE--WHYIATQG 887
Cdd:PHA02747   25 GIIRDEHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWID----GFEddKKFIATQG 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  888 PLPHTCHDFWQMVWEQGVNVIAMVT-AEEEGGRTKSHRYWPKlgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLS 966
Cdd:PHA02747  101 PFAETCADFWKAVWQEHCSIIVMLTpTKGTNGEEKCYQYWCL--NEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKIL 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  967 GQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSVLEGIRTRHPPIVVHCSAGVGRTGVVILSELMIYCLEH 1046
Cdd:PHA02747  179 KDSRKISHFQCSEWFEDETPSDHPDFIKFIKIIDINRKKSGKLFNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVK 258

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 568911642 1047 NEKVEVPTMLRFLREQRMFMIQTIAQYKFV---YQVLVQFL 1084
Cdd:PHA02747  259 RKAICLAKTAEKIREQRHAGIMNFDDYLFIqpgYEVLHYFL 299
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 796-1075 1.95e-38

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: 145.18  E-value: 1.95e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  796 IDERLRALKKKLEDGMVFTEYEQIPNKkangvFSTATLPENAERSRIREVVPYEENRVEL-IPTKENNTGYINASHIkVV 874
Cdd:cd14609     7 MEDHLRNRDRLAKEWQALCAYQAEPNT-----CSTAQGEANVKKNRNPDFVPYDHARIKLkAESNPSRSDYINASPI-IE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  875 VGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGskhsSATYGKFKVTTkFRTDSGC- 953
Cdd:cd14609    81 HDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEG----SSLYHIYEVNL-VSEHIWCe 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  954 -YATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYleeiqsvRRHTNSVLEGirtRHPPIVVHCSAGVGRTG 1032
Cdd:cd14609   156 dFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDF-------RRKVNKCYRG---RSCPIIVHCSDGAGRTG 225

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 568911642 1033 VVILSELMIYCLEHNEK-VEVPTMLRFLREQRMFMIQTIAQYKF 1075
Cdd:cd14609   226 TYILIDMVLNRMAKGVKeIDIAATLEHVRDQRPGMVRTKDQFEF 269
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 816-1075 2.75e-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: 144.81  E-value: 2.75e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  816 YEQIPNkkangVFSTATLPENAERSRIREVVPYEENRVEL-IPTKENNTGYINASHIkVVVGGSEWHYIATQGPLPHTCH 894
Cdd:cd14610    29 YQAEPN-----ATNVAQREENVQKNRSLAVLPYDHSRIILkAENSHSHSDYINASPI-MDHDPRNPAYIATQGPLPATVA 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  895 DFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSK--HssaTYGKFKVTTKFRTDSgcYATTGLKVKHLLSGQERTV 972
Cdd:cd14610   103 DFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNlyH---IYEVNLVSEHIWCED--FLVRSFYLKNLQTNETRTV 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  973 WHLQYTDWPHHGCPEDVQGFLSYleeiqsvRRHTNSVLEGirtRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEK-VE 1051
Cdd:cd14610   178 TQFHFLSWNDQGVPASTRSLLDF-------RRKVNKCYRG---RSCPIIVHCSDGAGRSGTYILIDMVLNKMAKGAKeID 247

                         250       260
                  ....*....|....*....|....
gi 568911642 1052 VPTMLRFLREQRMFMIQTIAQYKF 1075
Cdd:cd14610   248 IAATLEHLRDQRPGMVQTKEQFEF 271
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 833-1080 5.24e-38

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: 143.08  E-value: 5.24e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  833 LPENAERSRIREVVPYEENRVELIPTKENN--TGYINASHIKVVvGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAM 910
Cdd:cd14613    22 IPGLVRKNRYKTILPNPHSRVCLTSPDQDDplSSYINANYIRGY-GGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVM 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  911 VTAEEEGGRtKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCYATTGLKVKHllSGQERTVWHLQYTDWPHHGCPEDVQ 990
Cdd:cd14613   101 ITNIEEMNE-KCTEYWPE-----EQVTYEGIEITVKQVIHADDYRLRLITLKS--GGEERGLKHYWYTSWPDQKTPDNAP 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  991 GFLSYLEEIQSVRRHTnsvlegiRTRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTI 1070
Cdd:cd14613   173 PLLQLVQEVEEARQQA-------EPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTC 245

                         250
                  ....*....|
gi 568911642 1071 AQYKFVYQVL 1080
Cdd:cd14613   246 EQYQFVHHVL 255
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 865-1082 1.90e-37

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: 139.67  E-value: 1.90e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  865 YINASHIKVVVGGSewHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKlgskhSSATYGKFKVT 944
Cdd:cd14555     1 YINANYIDGYHRPN--HYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPD-----DTEVYGDIKVT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  945 TKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSvrrhTNSVLEGirtrhpPIVVHC 1024
Cdd:cd14555    74 LVETEPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKA----SNPPSAG------PIVVHC 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568911642 1025 SAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 1082
Cdd:cd14555   144 SAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 835-1082 3.96e-37

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: 139.78  E-value: 3.96e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  835 ENAERSRIREVVPYEENRVELIPTKEN-NTGYINASHIKVVvgGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTA 913
Cdd:cd14630     2 ENRNKNRYGNIISYDHSRVRLQLLDGDpHSDYINANYIDGY--HRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  914 EEEGGRTKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFL 993
Cdd:cd14630    80 LVEVGRVKCVRYWPD-----DTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  994 SYLEEIQSVrrhtNSVLEGirtrhpPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQY 1073
Cdd:cd14630   155 GFVRQVKFL----NPPDAG------PIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQY 224


                  ....*....
gi 568911642 1074 KFVYQVLVQ 1082
Cdd:cd14630   225 VFVHDAILE 233
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 852-1082 2.59e-36

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: 137.07  E-value: 2.59e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  852 RVELIPTKENNTG-YINASHIKVVVGGSewHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKlg 930
Cdd:cd14631     1 RVILQPVEDDPSSdYINANYIDGYQRPS--HYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPD-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  931 skhSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIqsvrRHTNSVL 1010
Cdd:cd14631    77 ---DTEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRV----KLSNPPS 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568911642 1011 EGirtrhpPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 1082
Cdd:cd14631   150 AG------PIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 865-1083 6.78e-36

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: 135.13  E-value: 6.78e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  865 YINASHIKvvvGGSEWHY-IATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGskhsSATYGKFKV 943
Cdd:cd14622     2 YINASFID---GYRQKDYfIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEG----SVTHGEITI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  944 TTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSvlegirtrhPPIVVH 1023
Cdd:cd14622    75 EIKNDTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGN---------HPIVVH 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642 1024 CSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQF 1083
Cdd:cd14622   146 CSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 865-1082 1.90e-35

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: 134.02  E-value: 1.90e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  865 YINASHIKVVVGGSewHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKlgskhSSATYGKFKVT 944
Cdd:cd14632     1 YINANYIDGYHRSN--HFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPD-----DSDTYGDIKIT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  945 TKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYleeiqsVRRhtnsvlegIRTRHP----PI 1020
Cdd:cd14632    74 LLKTETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAF------IRR--------VKASTPpdagPV 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568911642 1021 VVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 1082
Cdd:cd14632   140 VVHCSAGAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 806-1082 6.07e-35

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: 134.79  E-value: 6.07e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  806 KLEDGMVFTEYEQIPNKKANGVFSTATLPENAERSRIREVVPYEENRVELIPTK-ENNTGYINASHIKVVVGGSewHYIA 884
Cdd:cd14633    10 KCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEgETSSDYINGNYIDGYHRPN--HYIA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  885 TQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCYATTGLKVKHL 964
Cdd:cd14633    88 TQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPD-----DTEIYKDIKVTLIETELLAEYVIRTFAVEKR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  965 LSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSvlegirtrhpPIVVHCSAGVGRTGVVILSELMIYCL 1044
Cdd:cd14633   163 GVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAG----------PLVVHCSAGAGRTGCFIVIDIMLDMA 232

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 568911642 1045 EHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 1082
Cdd:cd14633   233 EREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 5-121 3.12e-34

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 127.00  E-value: 3.12e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642     5 PNVSRLQQEATRYQYYLQVKKDVLEGRLRCSLEQVIRLAGLAVQADFGDYNQFDSQ-EFLREYVLFPMDLaMEEAALEEL 83
Cdd:pfam00373    1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTsEYLSLESFLPKQL-LRKMKSKEL 79

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 568911642    84 TQKVAQEHKAHSGILPAEAELMYINEVERLDGFGQEIF 121
Cdd:pfam00373   80 EKRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 2-121 3.80e-32

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: 124.33  E-value: 3.80e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642      2 FYVPNVSRLQQEATRY-QYYLQVKKDVLEGRLRCSLEQVIRLAGLAVQADFGDYNQFDS--QEFLREYVLFPMDLAMEEa 78
Cdd:smart00295   80 FYPPDPNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdlRGELSLKRFLPKQLLDSR- 158

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 568911642     79 ALEELTQKVAQEHKAHSGILPAEAELMYINEVERLDGFGQEIF 121
Cdd:smart00295  159 KLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
971-1080 2.49e-30

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 115.53  E-value: 2.49e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642    971 TVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRhtnsvlegIRTRHPPIVVHCSAGVGRTGVVILSELMIYCLEH-NEK 1049
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLN--------QSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGE 72

                            90       100       110
                    ....*....|....*....|....*....|.
gi 568911642   1050 VEVPTMLRFLREQRMFMIQTIAQYKFVYQVL 1080
Cdd:smart00404   73 VDIFDTVKELRSQRPGMVQTEEQYLFLYRAL 103
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 971-1080 2.49e-30

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: 115.53  E-value: 2.49e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642    971 TVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRhtnsvlegIRTRHPPIVVHCSAGVGRTGVVILSELMIYCLEH-NEK 1049
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLN--------QSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGE 72

                            90       100       110
                    ....*....|....*....|....*....|.
gi 568911642   1050 VEVPTMLRFLREQRMFMIQTIAQYKFVYQVL 1080
Cdd:smart00012   73 VDIFDTVKELRSQRPGMVQTEEQYLFLYRAL 103
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 811-1080 4.65e-30

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 122.06  E-value: 4.65e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  811 MVFTEYEQIPNKKANGVFSTATLPENAERSRIREVVPYEENRVEL--------------------IPTKENNTGYINASH 870
Cdd:PHA02746   26 FVLLEHAEVMDIPIRGTTNHFLKKENLKKNRFHDIPCWDHSRVVInaheslkmfdvgdsdgkkieVTSEDNAENYIHANF 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  871 IKvvvGGSEWH-YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTaEEEGGRTKSHRYWPKlgSKHSSATYGKFKVTTKFRT 949
Cdd:PHA02746  106 VD---GFKEANkFICAQGPKEDTSEDFFKLISEHESQVIVSLT-DIDDDDEKCFELWTK--EEDSELAFGRFVAKILDII 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  950 DSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSVLEGIRTRHPPIVVHCSAGVG 1029
Cdd:PHA02746  180 EELSFTKTRLMITDKISDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEEQAELIKQADNDPQTLGPIVVHCSAGIG 259

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568911642 1030 RTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVL 1080
Cdd:PHA02746  260 RAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
796-1086 1.24e-29

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 119.81  E-value: 1.24e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  796 IDERLRALKKKLEDGMVFTEYEQIPNkkangvfstatlpeNAERSRIREVVPYEENRVEliptkeNNTGYINASHIKVvv 875
Cdd:COG5599    16 INSRLSTLTNELAPSHNDPQYLQNIN--------------GSPLNRFRDIQPYKETALR------ANLGYLNANYIQV-- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  876 gGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGG--RTKSHRYWpklgskHSSATYGKFKVTTK------F 947
Cdd:COG5599    74 -IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISkpKVKMPVYF------RQDGEYGKYEVSSEltesiqL 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  948 RTDSGCYAttgLKVKHLLSGQE-RTVWHLQYTDWPHHGCP--EDVQGFLSYLEEIQSVRRHTNSvlegirtrhpPIVVHC 1024
Cdd:COG5599   147 RDGIEART---YVLTIKGTGQKkIEIPVLHVKNWPDHGAIsaEALKNLADLIDKKEKIKDPDKL----------LPVVHC 213

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568911642 1025 SAGVGRTGVVILselmIYCLE------HNEKVEVPTMLRFLREQR-MFMIQTIAQykfvYQVLVQFLQN 1086
Cdd:COG5599   214 RAGVGRTGTLIA----CLALSksinalVQITLSVEEIVIDMRTSRnGGMVQTSEQ----LDVLVKLAEQ 274
FERM_C_PTPN14_PTPN21 cd13188
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and ...
 116-206 4.54e-29

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: 111.61  E-value: 4.54e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  116 FGQEIFPVKDSHGNSVHLGIFFMGIFVRNRVGRQAVIYRWNDIGSVTHSKAAILLELIDKEETALFHTDDIENAKYISRL 195
Cdd:cd13188     1 YGEESFPAKDEQGNEVLIGASLEGIFVKHDNGRPPVFFRWEDIKNVINHKRTFSIECQNSEETVQFQFEDAETAKYVWKL 80

                          90
                  ....*....|.
gi 568911642  196 FTTRHKFYKQN 206
Cdd:cd13188    81 CVLQHKFYRQN 91
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 15-113 1.33e-27

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: 107.72  E-value: 1.33e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642   15 TRYQYYLQVKKDVLEGRLRCSLEQVIRLAGLAVQADFGDYNQ-FDSQEFLREYVLFPMDLaMEEAALEELTQKVAQEHKA 93
Cdd:cd14473     1 TRYLLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPsEHKPKYLSLKRFLPKQL-LKQRKPEEWEKRIVELHKK 79

                          90       100
                  ....*....|....*....|
gi 568911642   94 HSGILPAEAELMYINEVERL 113
Cdd:cd14473    80 LRGLSPAEAKLKYLKIARKL 99
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 882-1078 5.46e-26

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: 106.72  E-value: 5.46e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  882 YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTkSHRYWPklgsKHSSATYGKFKVTTKFRTDSGCYATTGLKV 961
Cdd:cd14556    16 FIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQS-CPQYWP----DEGSGTYGPIQVEFVSTTIDEDVISRIFRL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  962 KHLLSGQE--RTVWHLQYTDWPHHG-CPEDVQGFLSYLEEIQSVRRHTNsvlEGirtrhpPIVVHCSAGVGRTGVVILSE 1038
Cdd:cd14556    91 QNTTRPQEgyRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQSG---EG------PIVVHCLNGVGRSGVFCAIS 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 568911642 1039 LMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 1078
Cdd:cd14556   162 SVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 865-1078 1.75e-18

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


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 85.07  E-value: 1.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  865 YINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKShrYWPKLGSKHSSATYGKFKVT 944
Cdd:cd14550     1 YINASYLQGYRRSNE--FIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPI--YWPTKEKPLECETFKVTLSG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  945 TKFRTDSGcyaTTGLKVKHLL--SGQER---TVWHLQYTDWPHHGCPedvqgFLSYLEEIQSVRRHTNSvlegirtRHPP 1019
Cdd:cd14550    77 EDHSCLSN---EIRLIVRDFIleSTQDDyvlEVRQFQCPSWPNPCSP-----IHTVFELINTVQEWAQQ-------RDGP 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568911642 1020 IVVH-----CSAGVgrtgVVILSELMIYcLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 1078
Cdd:cd14550   142 IVVHdryggVQAAT----FCALTTLHQQ-LEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 865-1081 5.65e-18

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: 83.57  E-value: 5.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  865 YINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVtAEEEGGRTKSHRYWPklgSKHSSATYGKFKVT 944
Cdd:cd17670     1 YINASYIMGYYRSNE--FIITQHPLPHTTKDFWRMIWDHNAQIIVML-PDNQGLAEDEFVYWP---SREESMNCEAFTVT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  945 TkFRTDSGCYATTGLKVKH---LLSGQERTVW---HLQYTDWPHHGCPedvqgflsyleeIQSVRRHTNSVLEGIRTRHP 1018
Cdd:cd17670    75 L-ISKDRLCLSNEEQIIIHdfiLEATQDDYVLevrHFQCPKWPNPDAP------------ISSTFELINVIKEEALTRDG 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568911642 1019 PIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLV 1081
Cdd:cd17670   142 PTIVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 865-1082 2.43e-15

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: 75.83  E-value: 2.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  865 YINA----SHIKVVVggsewhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTaeEEGGRTKSHRYWPklgsKHSSATYGK 940
Cdd:cd14634     1 YINAalmdSHKQPAA------FIVTQHPLPNTVADFWRLVFDYNCSSVVMLN--EMDAAQLCMQYWP----EKTSCCYGP 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  941 FKVTTKFRTDSGCYATTGLKVKHLLSGQE--RTVWHLQYTDWP-HHGCPEDVQGFLsyleeiQSVRRhTNSVLEGIRTRH 1017
Cdd:cd14634    69 IQVEFVSADIDEDIISRIFRICNMARPQDgyRIVQHLQYIGWPaYRDTPPSKRSIL------KVVRR-LEKWQEQYDGRE 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568911642 1018 PPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 1082
Cdd:cd14634   142 GRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 865-1082 8.51e-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: 74.56  E-value: 8.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  865 YINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRT-KSHRYWPKLGSKHssatYGKFKV 943
Cdd:cd14637     1 YINAALTDSYTRSAA--FIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQ----YGPMEV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  944 TTKFRTDSGCYATTGLKVKHLLSGQER--TVWHLQYTDW-PHHGCPEDVQGFLSYLEEIQSVRRHTNsvlEGiRTrhppi 1020
Cdd:cd14637    75 EFVSGSADEDIVTRLFRVQNITRLQEGhlMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRESG---EG-RT----- 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568911642 1021 VVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 1082
Cdd:cd14637   146 VVHCLNGGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 865-1081 2.19e-14

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: 73.10  E-value: 2.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  865 YINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVT-----AEEEggrtksHRYWPklgSKHSSATYG 939
Cdd:cd17669     1 YINASYIMGYYQSNE--FIITQHPLLHTIKDFWRMIWDHNAQLIVMLPdgqnmAEDE------FVYWP---NKDEPINCE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  940 KFKVTTkFRTDSGCYAT-TGLKVKHLL--SGQERTVW---HLQYTDWPHHGCPedvqgflsyleeIQSVRRHTNSVLEGI 1013
Cdd:cd17669    70 TFKVTL-IAEEHKCLSNeEKLIIQDFIleATQDDYVLevrHFQCPKWPNPDSP------------ISKTFELISIIKEEA 136

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568911642 1014 RTRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLV 1081
Cdd:cd17669   137 ANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 790-1085 9.32e-14

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 73.46  E-value: 9.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  790 DATRVPIDERLRALKKKLEDGMVFTEYEQIPNKKANGVFSTATLPENAERSRIR--EVVPYEENRVELIptkeNNTGYIN 867
Cdd:PHA02740    5 DAVDINGMDFINFINKPDLLSCIIKEYRAIVPEHEDEANKACAQAENKAKDENLalHITRLLHRRIKLF----NDEKVLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  868 ASHIKVVvgGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEggRTKSHRYWpklgskhsSATYGKFKVTTKF 947
Cdd:PHA02740   81 ARFVDGY--DFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHAD--KKCFNQFW--------SLKEGCVITSDKF 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  948 RTDSGCYATTGLKVKHLLS-----GQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQS----VRRHTNSVLEGirtrhp 1018
Cdd:PHA02740  149 QIETLEIIIKPHFNLTLLSltdkfGQAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDlcadLEKHKADGKIA------ 222

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568911642 1019 PIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQFLQ 1085
Cdd:PHA02740  223 PIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYLK 289
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 865-1082 1.88e-12

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: 67.41  E-value: 1.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  865 YINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKshRYWPKLGSKHSSATYGKFkVT 944
Cdd:cd14635     1 YINAALMDSYKQPSA--FIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQLCP--QYWPENGVHRHGPIQVEF-VS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  945 TKFRTDsgcYATTGLKVKHLLSGQE--RTVWHLQYTDWP-HHGCPEDVQGFLSYLEEIQSVRRHTNSVlEGiRTrhppiV 1021
Cdd:cd14635    76 ADLEED---IISRIFRIYNAARPQDgyRMVQQFQFLGWPmYRDTPVSKRSFLKLIRQVDKWQEEYNGG-EG-RT-----V 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568911642 1022 VHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 1082
Cdd:cd14635   146 VHCLNGGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 882-1082 2.04e-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: 67.36  E-value: 2.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  882 YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTaeEEGGRTKSHRYWPKLGskhsSATYGKFKVTTkFRTDSGCYATTGL-K 960
Cdd:cd14636    16 FIVTQHPLPNTVKDFWRLVYDYGCTSIVMLN--EVDLAQGCPQYWPEEG----MLRYGPIQVEC-MSCSMDCDVISRIfR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  961 VKHLLSGQE--RTVWHLQYTDWP-HHGCPEDVQGFLSYLEEIQSVRRHTNSVlEGiRTrhppiVVHCSAGVGRTGVVILS 1037
Cdd:cd14636    89 ICNLTRPQEgyLMVQQFQYLGWAsHREVPGSKRSFLKLILQVEKWQEECDEG-EG-RT-----IIHCLNGGGRSGMFCAI 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 568911642 1038 ELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 1082
Cdd:cd14636   162 SIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
FERM_C pfam09380
FERM C-terminal PH-like domain;
125-207 2.00e-10

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 58.03  E-value: 2.00e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642   125 DSHGNSVHLGIFFMGIFVRNRVGRQAVIYRWNDIGSVTHSKAAILLELIDK--EETALFHTDDIENAKYISRLFTTRHKF 202
Cdd:pfam09380    1 DKEGTDLWLGVSAKGILVYEDNNKILNLFPWREIRKISFKRKKFLIKLRDKssEETLGFYTESSRACKYLWKLCVEQHTF 80


                   ....*
gi 568911642   203 YKQNK 207
Cdd:pfam09380   81 FRLRR 85
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 866-1074 2.49e-10

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: 61.65  E-value: 2.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  866 INASHIKVvvgGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWpklgskHSSATYGKFKVTT 945
Cdd:cd14559    18 LNANRVQI---GNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYF------RQSGTYGSVTVKS 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  946 KfRTDSGcYATTGLKVKHL---LSGQERT----VWHLqyTDWPHHGcPEDVQGFLSYLEEIQSVRRHTNSVLEGIRTR-- 1016
Cdd:cd14559    89 K-KTGKD-ELVDGLKADMYnlkITDGNKTitipVVHV--TNWPDHT-AISSEGLKELADLVNKSAEEKRNFYKSKGSSai 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568911642 1017 -----HPPiVVHCSAGVGRTGVVILSELMIyclEHNEKVEVPTMLRFLREQR-MFMIQTIAQYK 1074
Cdd:cd14559   164 ndknkLLP-VIHCRAGVGRTGQLAAAMELN---KSPNNLSVEDIVSDMRTSRnGKMVQKDEQLD 223
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 985-1078 1.50e-07

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: 50.81  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  985 CPEDVQGFLSYLEEIQSvrrhtnsvlegirtRHPPIVVHCSAGVGRTGVVILSELMIYcleHNEKVEVptMLRFLREQRM 1064
Cdd:cd14494    38 TLAMVDRFLEVLDQAEK--------------PGEPVLVHCKAGVGRTGTLVACYLVLL---GGMSAEE--AVRIVRLIRP 98

                          90
                  ....*....|....*
gi 568911642 1065 FMI-QTIAQYKFVYQ 1078
Cdd:cd14494    99 GGIpQTIEQLDFLIK 113
FERM_C_FRMD3_FRMD5 cd13192
FERM domain C-lobe of FERM domain-containing protein 3 and 5 (FRMD3 and 5); FRMD3 (also called ...
 102-204 2.37e-06

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: 47.39  E-value: 2.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  102 AELMYINEVERLDGFGQEIFPVKDSHGNSVHLGIFFMGIFVRnRVGRQAVIYRWNDIGSVTHSKAAILLELIDKEE---T 178
Cdd:cd13192     1 AEDNFLRKAATLETYGVDPHPVKDHRGNQLYLGFTHTGIVTF-QGGKRVHHFRWNDITKFNYEGKMFILHVMQKEEkkhT 79

                          90       100
                  ....*....|....*....|....*.
gi 568911642  179 ALFHTDDIENAKYISRLFTTRHKFYK 204
Cdd:cd13192    80 LGFKCPTPAACKHLWKCAVEQQAFYT 105
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 1020-1076 3.74e-05

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


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 45.80  E-value: 3.74e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568911642 1020 IVVHCSAGVGRTGVVILSELMIYClehneKVEVPTMLRFLREQRMFMIQTIAQYKFV 1076
Cdd:cd14506   112 VAVHCHAGLGRTGVLIACYLVYAL-----RMSADQAIRLVRSKRPNSIQTRGQVLCV 163
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 980-1078 5.21e-05

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: 44.95  E-value: 5.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642  980 WPHH-----GCPEDVQGFLSYLEEIQSVrrhtnsvLEGIRTrhppIVVHCSAGVGRTGVVILSELmiycLEHNEKVEVPT 1054
Cdd:cd14505    75 WHHLpipdgGVPSDIAQWQELLEELLSA-------LENGKK----VLIHCKGGLGRTGLIAACLL----LELGDTLDPEQ 139

                          90       100
                  ....*....|....*....|....
gi 568911642 1055 MLRFLREQRMFMIQTIAQYKFVYQ 1078
Cdd:cd14505   140 AIAAVRALRPGAIQTPKQENFLHQ 163
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1010-1078 3.17e-04

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 41.88  E-value: 3.17e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568911642 1010 LEGIRTRHPPIVVHCSAGVGRTGVVILSeLMIYclehnEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 1078
Cdd:COG2453    73 IDEALREGKKVLVHCRGGIGRTGTVAAA-YLVL-----LGLSAEEALARVRAARPGAVETPAQRAFLER 135
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 989-1063 7.45e-04

Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The enzyme's tertiary fold is highly similar to that of tyrosine-specific phosphatases, except for a "recognition" region.


Pssm-ID: 395632 [Multi-domain]  Cd Length: 127  Bit Score: 40.71  E-value: 7.45e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568911642   989 VQGFLSYLEEIQSVRRHTNSVLEGIRTRHPPIVVHCSAGVGRTGVVILSELMIYclehnEKVEVPTMLRFLREQR 1063
Cdd:pfam00782   41 IPVEDNHETNISKYLEEAVEFIDDARQKGGKVLVHCQAGISRSATLIIAYLMKT-----RNLSLNEAYSFVKERR 110
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
956-1063 1.70e-03

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 39.96  E-value: 1.70e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642    956 TTGLKVKHLLSGQERTVW----HLQYTDWPHHGcpEDVQGFLSYLEEiqsvrrhTNSVLEGIRTRHPPIVVHCSAGVGRT 1031
Cdd:smart00195   22 LKKLGITHVINVTNEVPNyngsDFTYLGVPIDD--NTETKISPYFPE-------AVEFIEDAESKGGKVLVHCQAGVSRS 92

                            90       100       110
                    ....*....|....*....|....*....|..
gi 568911642   1032 GVVILSELMIYclehnEKVEVPTMLRFLREQR 1063
Cdd:smart00195   93 ATLIIAYLMKT-----RNMSLNDAYDFVKDRR 119
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 1019-1078 5.63e-03

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


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 38.41  E-value: 5.63e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911642 1019 PIVVHCSAGVGRTGvVILSELMIYClehnEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 1078
Cdd:cd14504    84 AVLVHCLAGKGRTG-TMLACYLVKT----GKISAVDAINEIRRIRPGSIETSEQEKFVIQ 138
Y_phosphatase3 pfam13350
Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 ...
 1009-1039 6.96e-03

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


Pssm-ID: 463853 [Multi-domain]  Cd Length: 243  Bit Score: 39.53  E-value: 6.96e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 568911642  1009 VLEGIRTRHPPIVVHCSAGVGRTGVV---ILSEL 1039
Cdd:pfam13350  121 LFEALADNDGPVLFHCTAGKDRTGVAaalLLSLL 154
 
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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