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Conserved domains on  [gi|86575091|ref|NP_500128|]
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Protein-tyrosine-phosphatase [Caenorhabditis elegans]

Protein Classification

protein tyrosine phosphatase family protein( domain architecture ID 12193126)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
102-365 6.91e-99

Protein tyrosine phosphatase, catalytic domain;


:

Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 297.26  E-value: 6.91e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091    102 QIRVEQEKLRMEAEYRSECAVA--PQHYARNRYRDILPYDKNRVEIQKDSENPEGYMNASLIQLPGGKTEFIAAQAPLPA 179
Cdd:smart00194   1 GLEEEFEKLDRLKPDDESCTVAafPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091    180 TLDEWWKMIDEHRVSLVVILCKLVELNKIKCERYWPEQVGESELFGDYEITLEEEKLFDDdeYLMRCLKMENQTTGECRK 259
Cdd:smart00194  81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDD--YTIRTLEVTNTGCSETRT 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091    260 VHQLHYREWPDHGCPSGEKQLLNMIDLMENIHeevsPQDSSPILVHCSAGVGRTGTIIAINFIREQMKAEtlHSIDIFGL 339
Cdd:smart00194 159 VTHYHYTNWPDHGVPESPESILDLIRAVRKSQ----STSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAG--KEVDIFEI 232

                          250       260
                   ....*....|....*....|....*.
gi 86575091    340 VMTLRKQRASMVQTQDQFQFVHRCIA 365
Cdd:smart00194 233 VKELRSQRPGMVQTEEQYIFLYRAIL 258
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
102-365 6.91e-99

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 297.26  E-value: 6.91e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091    102 QIRVEQEKLRMEAEYRSECAVA--PQHYARNRYRDILPYDKNRVEIQKDSENPEGYMNASLIQLPGGKTEFIAAQAPLPA 179
Cdd:smart00194   1 GLEEEFEKLDRLKPDDESCTVAafPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091    180 TLDEWWKMIDEHRVSLVVILCKLVELNKIKCERYWPEQVGESELFGDYEITLEEEKLFDDdeYLMRCLKMENQTTGECRK 259
Cdd:smart00194  81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDD--YTIRTLEVTNTGCSETRT 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091    260 VHQLHYREWPDHGCPSGEKQLLNMIDLMENIHeevsPQDSSPILVHCSAGVGRTGTIIAINFIREQMKAEtlHSIDIFGL 339
Cdd:smart00194 159 VTHYHYTNWPDHGVPESPESILDLIRAVRKSQ----STSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAG--KEVDIFEI 232

                          250       260
                   ....*....|....*....|....*.
gi 86575091    340 VMTLRKQRASMVQTQDQFQFVHRCIA 365
Cdd:smart00194 233 VKELRSQRPGMVQTEEQYIFLYRAIL 258
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
126-365 1.76e-93

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 282.59  E-value: 1.76e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091   126 HYARNRYRDILPYDKNRVEIQkDSENPEGYMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVEL 205
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT-GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091   206 NKIKCERYWPEQVGESELFGDYEITLEEEKlFDDDEYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPSGEKQLLNMID 285
Cdd:pfam00102  80 GREKCAQYWPEEEGESLEYGDFTVTLKKEK-EDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091   286 LMeniHEEVSPQDSSPILVHCSAGVGRTGTIIAINFIREQMKAEtlHSIDIFGLVMTLRKQRASMVQTQDQFQFVHRCIA 365
Cdd:pfam00102 159 KV---RKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAE--GEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 155-362 5.25e-86

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: 262.22  E-value: 5.25e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 155 YMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKIKCERYWPEQVGESELFGDYEITLEEE 234
Cdd:cd00047   1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLVSE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 235 KlfDDDEYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPSGekqLLNMIDLMENIHEEvSPQDSSPILVHCSAGVGRTG 314
Cdd:cd00047  81 E--ELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSS---PEDLLALVRRVRKE-ARKPNGPIVVHCSAGVGRTG 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 86575091 315 TIIAINFIREQMKAEtlHSIDIFGLVMTLRKQRASMVQTQDQFQFVHR 362
Cdd:cd00047 155 TFIAIDILLERLEAE--GEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
103-359 6.38e-53

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 179.52  E-value: 6.38e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 103 IRVEQEKLRMEAEYRSE----CAVAPQHYA------RNRYRDILPYDKNRVEIqkdsenPEGYMNASLIQLPGGKTeFIA 172
Cdd:COG5599   9 IKSEEEKINSRLSTLTNelapSHNDPQYLQningspLNRFRDIQPYKETALRA------NLGYLNANYIQVIGNHR-YIA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 173 AQAPLPATLDEWWKMIDEHRVSLVVIL--CKLVELNKIKCERYWPEQvGEselFGDYEITLEEEK---LFDD---DEYLM 244
Cdd:COG5599  82 TQYPLEEQLEDFFQMLFDNNTPVLVVLasDDEISKPKVKMPVYFRQD-GE---YGKYEVSSELTEsiqLRDGieaRTYVL 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 245 RClkmeNQTTGECRKVHQLHYREWPDHGCPSGEkQLLNMIDLMENIHEEVSPqDSSPILVHCSAGVGRTGTIIAINFIRE 324
Cdd:COG5599 158 TI----KGTGQKKIEIPVLHVKNWPDHGAISAE-ALKNLADLIDKKEKIKDP-DKLLPVVHCRAGVGRTGTLIACLALSK 231

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 86575091 325 QMKAETLHSIDIFGLVMTLRKQRAS-MVQTQDQFQF 359
Cdd:COG5599 232 SINALVQITLSVEEIVIDMRTSRNGgMVQTSEQLDV 267
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 124-379 4.22e-32

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 124.76  E-value: 4.22e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091  124 PQHYARNRYRDILPYDKNRVEIQK--------------------DSENPEGYMNASLIQLPGGKTEFIAAQAPLPATLDE 183
Cdd:PHA02746  49 KENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkkievtSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSED 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091  184 WWKMIDEHRVSLVVILCKlVELNKIKCERYWPEQVGESELFGDYEI-TLE--EEKLFDDDEylmrcLKMENQTTGECRKV 260
Cdd:PHA02746 129 FFKLISEHESQVIVSLTD-IDDDDEKCFELWTKEEDSELAFGRFVAkILDiiEELSFTKTR-----LMITDKISDTSREI 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091  261 HQLHYREWPDHGCPSGEKQLLNMIDLMENIHEEV------SPQDSSPILVHCSAGVGRTGTIIAINFIREQMKAEtlHSI 334
Cdd:PHA02746 203 HHFWFPDWPDNGIPTGMAEFLELINKVNEEQAELikqadnDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKE--KEV 280

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 86575091  335 DIFGLVMTLRKQRASMVQTQDQFQFVHRCIasycrrHLGIIEEPK 379
Cdd:PHA02746 281 CLGEIVLKIRKQRHSSVFLPEQYAFCYKAL------KYAIIEEAK 319
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
102-365 6.91e-99

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 297.26  E-value: 6.91e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091    102 QIRVEQEKLRMEAEYRSECAVA--PQHYARNRYRDILPYDKNRVEIQKDSENPEGYMNASLIQLPGGKTEFIAAQAPLPA 179
Cdd:smart00194   1 GLEEEFEKLDRLKPDDESCTVAafPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091    180 TLDEWWKMIDEHRVSLVVILCKLVELNKIKCERYWPEQVGESELFGDYEITLEEEKLFDDdeYLMRCLKMENQTTGECRK 259
Cdd:smart00194  81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDD--YTIRTLEVTNTGCSETRT 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091    260 VHQLHYREWPDHGCPSGEKQLLNMIDLMENIHeevsPQDSSPILVHCSAGVGRTGTIIAINFIREQMKAEtlHSIDIFGL 339
Cdd:smart00194 159 VTHYHYTNWPDHGVPESPESILDLIRAVRKSQ----STSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAG--KEVDIFEI 232

                          250       260
                   ....*....|....*....|....*.
gi 86575091    340 VMTLRKQRASMVQTQDQFQFVHRCIA 365
Cdd:smart00194 233 VKELRSQRPGMVQTEEQYIFLYRAIL 258
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
126-365 1.76e-93

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 282.59  E-value: 1.76e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091   126 HYARNRYRDILPYDKNRVEIQkDSENPEGYMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVEL 205
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT-GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091   206 NKIKCERYWPEQVGESELFGDYEITLEEEKlFDDDEYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPSGEKQLLNMID 285
Cdd:pfam00102  80 GREKCAQYWPEEEGESLEYGDFTVTLKKEK-EDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091   286 LMeniHEEVSPQDSSPILVHCSAGVGRTGTIIAINFIREQMKAEtlHSIDIFGLVMTLRKQRASMVQTQDQFQFVHRCIA 365
Cdd:pfam00102 159 KV---RKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAE--GEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 155-362 5.25e-86

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: 262.22  E-value: 5.25e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 155 YMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKIKCERYWPEQVGESELFGDYEITLEEE 234
Cdd:cd00047   1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLVSE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 235 KlfDDDEYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPSGekqLLNMIDLMENIHEEvSPQDSSPILVHCSAGVGRTG 314
Cdd:cd00047  81 E--ELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSS---PEDLLALVRRVRKE-ARKPNGPIVVHCSAGVGRTG 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 86575091 315 TIIAINFIREQMKAEtlHSIDIFGLVMTLRKQRASMVQTQDQFQFVHR 362
Cdd:cd00047 155 TFIAIDILLERLEAE--GEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 80-372 3.45e-68

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: 219.80  E-value: 3.45e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091  80 LLREFLKEEEAYTPQD------YLRRFYQIRVEQEKLRMEAEYRSECAVAPQHYARNRYRDILPYDKNRVEIQ-KDSENP 152
Cdd:cd14604   5 ILKKFIERVQAMKSTDhngednFASDFMRLRRLSTKYRTEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTlKTSSQD 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 153 EGYMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKIKCERYWPEQVGESELFGDYEITLE 232
Cdd:cd14604  85 SDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPMTFGPFRISCE 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 233 EEKLFDDdeYLMRCLKMENQTtgECRKVHQLHYREWPDHGCPSGEKQLLNMIDLMENIHEevspQDSSPILVHCSAGVGR 312
Cdd:cd14604 165 AEQARTD--YFIRTLLLEFQN--ETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQE----HEDVPICIHCSAGCGR 236

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 86575091 313 TGTIIAINFIREQMKAETL-HSIDIFGLVMTLRKQRASMVQTQDQFQFVHRCIASYCRRHL 372
Cdd:cd14604 237 TGAICAIDYTWNLLKAGKIpEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEKQL 297
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 130-363 1.16e-67

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: 216.22  E-value: 1.16e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 130 NRYRDILPYDKNRVEIQKDSENPEGYMNASLIqlPG--GKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNK 207
Cdd:cd14615   1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYM--PGynSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 208 IKCERYWPEQvgESELFGDYEITLEEEKLFddDEYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPSGEKQLLNMIDLM 287
Cdd:cd14615  79 TKCEEYWPSK--QKKDYGDITVTMTSEIVL--PEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLV 154

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86575091 288 ENIHEEVSPQdsSPILVHCSAGVGRTGTIIAINFIREQMKAEtlHSIDIFGLVMTLRKQRASMVQTQDQFQFVHRC 363
Cdd:cd14615 155 REYMKQNPPN--SPILVHCSAGVGRTGTFIAIDRLIYQIENE--NVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQC 226
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 155-362 1.16e-65

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: 209.97  E-value: 1.16e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 155 YMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKIKCERYWPEQVGESELFGDYEITLEEE 234
Cdd:cd14542   1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKISLEKE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 235 KLFDDDeYLMRCLKMENQTtgECRKVHQLHYREWPDHGCPSGEKQLLNMIDLMENIHEEvspqDSSPILVHCSAGVGRTG 314
Cdd:cd14542  81 KRVGPD-FLIRTLKVTFQK--ESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGS----EDVPICVHCSAGCGRTG 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 86575091 315 TIIAINFIREQMKAETL-HSIDIFGLVMTLRKQRASMVQTQDQFQFVHR 362
Cdd:cd14542 154 TICAIDYVWNLLKTGKIpEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 131-361 1.78e-65

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: 210.29  E-value: 1.78e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 131 RYRDILPYDKNRVEIQKDSENP-EGYMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKIK 209
Cdd:cd14548   1 RYTNILPYDHSRVKLIPINEEEgSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 210 CERYWPEQVGESElFGDYEITLEEEKLFDDdeYLMRCLKMENQttGECRKVHQLHYREWPDHGCPSGEKQLLNMIDLMen 289
Cdd:cd14548  81 CDHYWPFDQDPVY-YGDITVTMLSESVLPD--WTIREFKLERG--DEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLV-- 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 86575091 290 ihEEVSPQDSSPILVHCSAGVGRTGTIIAINFIREQMKAETLhsIDIFGLVMTLRKQRASMVQTQDQFQFVH 361
Cdd:cd14548 154 --RDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDY--VDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 129-364 6.59e-64

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: 206.60  E-value: 6.59e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 129 RNRYRDILPYDKNRVEIQKDSenpeGYMNASLIQLPGGKTEF--IAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELN 206
Cdd:cd14597   6 KNRYKNILPYDTTRVPLGDEG----GYINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEVEGG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 207 KIKCERYWPEQVGESELFGDyEITLEEEKLFDDDEYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPSGEKQLLNMIDL 286
Cdd:cd14597  82 KIKCQRYWPEILGKTTMVDN-RLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLTFISY 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 86575091 287 MENIHEevspqdSSPILVHCSAGVGRTGTIIAINFIREQMKAETlhSIDIFGLVMTLRKQRASMVQTQDQFQFVHRCI 364
Cdd:cd14597 161 MRHIHK------SGPIITHCSAGIGRSGTLICIDVVLGLISKDL--DFDISDIVRTMRLQRHGMVQTEDQYIFCYQVI 230
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 100-365 7.91e-64

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: 207.37  E-value: 7.91e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 100 FYQIRVEQEKLRMEAEYRSECAVAPQHYARNRYRDILPYDKNRVEIQ-KDSENPEGYMNASLIQLPGGKTEFIAAQAPLP 178
Cdd:cd14603   4 FSEIRACSAAFKADYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSlLQEEGHSDYINANFIKGVDGSRAYIATQGPLS 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 179 ATLDEWWKMIDEHRVSLVVILCKLVELNKIKCERYWPeQVGESELFGDYEIT-LEEEKLfdDDEYLMRCLKMENQTtgEC 257
Cdd:cd14603  84 HTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWA-QEQEPLQTGPFTITlVKEKRL--NEEVILRTLKVTFQK--ES 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 258 RKVHQLHYREWPDHGCPSGEKQLLNMIDLMENIHEEvspqDSSPILVHCSAGVGRTGTIIAINFIREQMKAETLH-SIDI 336
Cdd:cd14603 159 RSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGS----GPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPpDFSI 234

                       250       260
                ....*....|....*....|....*....
gi 86575091 337 FGLVMTLRKQRASMVQTQDQFQFVHRCIA 365
Cdd:cd14603 235 FDVVLEMRKQRPAAVQTEEQYEFLYHTVA 263
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 155-361 6.40e-63

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: 203.25  E-value: 6.40e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 155 YMNASLIQLPGG-KTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKIKCERYWPEQVGESElFGDYEITLEE 233
Cdd:cd18533   1 YINASYITLPGTsSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGE-YGDLTVELVS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 234 EKLFDDDEYLMRCLKMeNQTTGECRKVHQLHYREWPDHGCPSGEKQLLNMIDLmenIHEEV-SPQDSSPILVHCSAGVGR 312
Cdd:cd18533  80 EEENDDGGFIVREFEL-SKEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKL---KRELNdSASLDPPIIVHCSAGVGR 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 86575091 313 TGTIIAINFIREQMKAETLHSID-------IFGLVMTLRKQRASMVQTQDQFQFVH 361
Cdd:cd18533 156 TGTFIALDSLLDELKRGLSDSQDledsedpVYEIVNQLRKQRMSMVQTLRQYIFLY 211
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 130-362 7.47e-62

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: 200.70  E-value: 7.47e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 130 NRYRDILPYDKNRVEIQKDSENPEG-YMNASLIQLPGGKTE-FIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVElNK 207
Cdd:cd14547   1 NRYKTILPNEHSRVCLPSVDDDPLSsYINANYIRGYDGEEKaYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTE-AK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 208 IKCERYWPEQVGESelFGDYEITLEEEKLFDDdeYLMRCLKMENQttGECRKVHQLHYREWPDHGCPSGEKQLLNMIDLM 287
Cdd:cd14547  80 EKCAQYWPEEENET--YGDFEVTVQSVKETDG--YTVRKLTLKYG--GEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEV 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86575091 288 ENIHEEVSPqdSSPILVHCSAGVGRTGTIIAINFIREQMKAETlhSIDIFGLVMTLRKQRASMVQTQDQFQFVHR 362
Cdd:cd14547 154 EEARQTEPH--RGPIVVHCSAGIGRTGCFIATSIGCQQLREEG--VVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 129-364 1.29e-61

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), also called lymphoid phosphatase (LyP), PEST-domain phosphatase (PEP), or hematopoietic cell protein-tyrosine phosphatase 70Z-PEP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. Mutations in the PTPN22 gene are associated with multiple connective tissue and autoimmune diseases including type 1 diabetes mellitus, rheumatoid arthritis, and systemic lupus erythematosus. PTPN22 contains an N-terminal catalytic PTP domain and four proline-rich regions at the C-terminus.


Pssm-ID: 350450 [Multi-domain]  Cd Length: 234  Bit Score: 200.45  E-value: 1.29e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 129 RNRYRDILPYDKNRVEIQK-DSENPEGYMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNK 207
Cdd:cd14602   1 KNRYKDILPYDHSRVELSLiTSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 208 IKCERYWPEqVGESEL-FGDYEITLEEEKlfDDDEYLMRCLKMENQTtgECRKVHQLHYREWPDHGCPSGEKQLLNMIDL 286
Cdd:cd14602  81 KKCERYWAE-PGEMQLeFGPFSVTCEAEK--RKSDYIIRTLKVKFNS--ETRTIYQFHYKNWPDHDVPSSIDPILELIWD 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 86575091 287 MENIHeevsPQDSSPILVHCSAGVGRTGTIIAINFIREQMKAETL-HSIDIFGLVMTLRKQRASMVQTQDQFQFVHRCI 364
Cdd:cd14602 156 VRCYQ----EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIpENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAV 230
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 128-364 6.77e-59

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: 193.77  E-value: 6.77e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 128 ARNRYRDILPYDKNRVEIQKDSENPEG-YMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELN 206
Cdd:cd14553   5 PKNRYANVIAYDHSRVILQPIEGVPGSdYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEERS 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 207 KIKCERYWPEQVgeSELFGDYEITLEEEklFDDDEYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPSGEKQLLNMIDL 286
Cdd:cd14553  85 RVKCDQYWPTRG--TETYGLIQVTLLDT--VELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRR 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 86575091 287 MENIHeevsPQDSSPILVHCSAGVGRTGTIIAINFIREQMKAEtlHSIDIFGLVMTLRKQRASMVQTQDQFQFVHRCI 364
Cdd:cd14553 161 VKACN----PPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHE--KTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDAL 232
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 102-361 4.34e-58

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: 192.58  E-value: 4.34e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 102 QIRVEQEKLRMEAEYRS-ECAVAPQHYARNRYRDILPYDKNRVEIQKDSENPEG-YMNASLIQLPGGKTEFIAAQAPLPA 179
Cdd:cd14543   4 GIYEEYEDIRREPPAGTfLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTdYINANFMDGYKQKNAYIATQGPLPK 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 180 TLDEWWKMIDEHRVSLVVILCKLVELNKIKCERYWPEQVGESELFGDYEITLEEEKLFDDdeYLMRCLKMENQTTGECRK 259
Cdd:cd14543  84 TYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEH--YKKTTLEIHNTETDESRQ 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 260 VHQLHYREWPDHGCPSGEKQLLNMIDLMENiHEEVSPQDSS----------PILVHCSAGVGRTGTIIAINFIREQMkaE 329
Cdd:cd14543 162 VTHFQFTSWPDFGVPSSAAALLDFLGEVRQ-QQALAVKAMGdrwkghppgpPIVVHCSAGIGRTGTFCTLDICLSQL--E 238

                       250       260       270
                ....*....|....*....|....*....|..
gi 86575091 330 TLHSIDIFGLVMTLRKQRASMVQTQDQFQFVH 361
Cdd:cd14543 239 DVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 155-361 1.21e-57

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: 189.10  E-value: 1.21e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 155 YMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKIKCERYWPEQVGESelFGDYEITLEEE 234
Cdd:cd14549   1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTET--YGNIQVTLLST 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 235 KLFddDEYLMR--CLKMENQTTG----ECRKVHQLHYREWPDHGCPSGEKQLLNMIDLMENIHeevsPQDSSPILVHCSA 308
Cdd:cd14549  79 EVL--ATYTVRtfSLKNLKLKKVkgrsSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAAN----PPGAGPIVVHCSA 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 86575091 309 GVGRTGTIIAINFIREQMKAEtlHSIDIFGLVMTLRKQRASMVQTQDQFQFVH 361
Cdd:cd14549 153 GVGRTGTYIVIDSMLQQIQDK--GTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 155-364 1.40e-57

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: 189.12  E-value: 1.40e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 155 YMNASLIQLPGGKTEF--IAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKIKCERYWPEQVGESELF-GDYEITL 231
Cdd:cd14538   1 YINASHIRIPVGGDTYhyIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPLICgGRLEVSL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 232 EEEKLFDDdeYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPSGEKQLLNMIDLMENIHeevspqDSSPILVHCSAGVG 311
Cdd:cd14538  81 EKYQSLQD--FVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIH------NSGPIVVHCSAGIG 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 86575091 312 RTGTIIAINFIREQMkaETLHSIDIFGLVMTLRKQRASMVQTQDQFQFVHRCI 364
Cdd:cd14538 153 RTGVLITIDVALGLI--ERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKAC 203
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 128-367 2.31e-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: 189.98  E-value: 2.31e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 128 ARNRYRDILPYDKNRVEIQKDSENPEG--YMNASLIQLPG--------GKTeFIAAQAPLPATLDEWWKMIDEHRVSLVV 197
Cdd:cd14544   3 GKNRYKNILPFDHTRVILKDRDPNVPGsdYINANYIRNENegpttdenAKT-YIATQGCLENTVSDFWSMVWQENSRVIV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 198 ILCKLVELNKIKCERYWPEqVGESELFGDYEITLEEEKlfDDDEYLMRCLKMENQTTGE-CRKVHQLHYREWPDHGCPSG 276
Cdd:cd14544  82 MTTKEVERGKNKCVRYWPD-EGMQKQYGPYRVQNVSEH--DTTDYTLRELQVSKLDQGDpIREIWHYQYLSWPDHGVPSD 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 277 EKQLLNmidLMENIHEEVSP-QDSSPILVHCSAGVGRTGTIIAINFIREQMKAETLH-SIDIFGLVMTLRKQRASMVQTQ 354
Cdd:cd14544 159 PGGVLN---FLEDVNQRQESlPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDcDIDIQKTIQMVRSQRSGMVQTE 235

                       250
                ....*....|...
gi 86575091 355 DQFQFVHRCIASY 367
Cdd:cd14544 236 AQYKFIYVAVAQY 248
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 130-364 2.52e-56

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: 186.63  E-value: 2.52e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 130 NRYRDILPYDKNRVEIQKDSENPEG-YMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKI 208
Cdd:cd14619   1 NRFRNVLPYDWSRVPLKPIHEEPGSdYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 209 KCERYWPEQVGESeLFGDYEITLEEEKLFDDdeYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPSGEKQLLNMIDLME 288
Cdd:cd14619  81 KCEHYWPLDYTPC-TYGHLRVTVVSEEVMEN--WTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLR 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86575091 289 NIHEevSPQDSSPILVHCSAGVGRTGTIIAINFIREQMKAETLhsIDIFGLVMTLRKQRASMVQTQDQFQFVHRCI 364
Cdd:cd14619 158 QWLD--QTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGL--LGPFSFVQKMRENRPLMVQTESQYVFLHQCI 229
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 129-368 4.80e-56

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: 186.06  E-value: 4.80e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 129 RNRYRDILPYDKNRVEIQKDSENPEgYMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKI 208
Cdd:cd14545   1 LNRYRDRDPYDHDRSRVKLKQGDND-YINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 209 KCERYWPEQVGESELFGD--YEITLEEEKLFDDdeYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPSGEKQLLNMIDL 286
Cdd:cd14545  80 KCAQYWPQGEGNAMIFEDtgLKVTLLSEEDKSY--YTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQK 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 287 MENiHEEVSPqDSSPILVHCSAGVGRTGTIIAINFIREQMKAETLHSIDIFGLVMTLRKQRASMVQTQDQFQFvhrciaS 366
Cdd:cd14545 158 VRE-SGSLSS-DVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPSSVDVKKVLLEMRKYRMGLIQTPDQLRF------S 229


                ..
gi 86575091 367 YC 368
Cdd:cd14545 230 YL 231
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 130-364 2.89e-54

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: 181.29  E-value: 2.89e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 130 NRYRDILPYDKNRVEIQKDSENPEG-YMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKI 208
Cdd:cd14618   1 NRYPHVLPYDHSRVRLSQLGGEPHSdYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 209 KCERYWPEQVGESElFGDYEITLEEEKlfDDDEYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPSGEKQLLNMIDLme 288
Cdd:cd14618  81 LCDHYWPSESTPVS-YGHITVHLLAQS--SEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFREL-- 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86575091 289 nIHEEV-SPQDSSPILVHCSAGVGRTGTIIAINFIREQMKAETLhsIDIFGLVMTLRKQRASMVQTQDQFQFVHRCI 364
Cdd:cd14618 156 -VREHVqATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKV--VDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 130-362 4.65e-54

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: 180.89  E-value: 4.65e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 130 NRYRDILPYDKNRVEIQKDSENP-EGYMNASLIqlPGG--KTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELN 206
Cdd:cd14617   1 NRYNNILPYDSTRVKLSNVDDDPcSDYINASYI--PGNnfRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 207 KIKCERYWPEQvGESELFGDYEITLEEEKLFddDEYLMRCLKMENQTTGEC-RKVHQLHYREWPDHGCPSGEKQLLNMID 285
Cdd:cd14617  79 RVKCDHYWPAD-QDSLYYGDLIVQMLSESVL--PEWTIREFKICSEEQLDApRLVRHFHYTVWPDHGVPETTQSLIQFVR 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86575091 286 LMENiHEEVSPqDSSPILVHCSAGVGRTGTIIAINFIREQMkaETLHSIDIFGLVMTLRKQRASMVQTQDQFQFVHR 362
Cdd:cd14617 156 TVRD-YINRTP-GSGPTVVHCSAGVGRTGTFIALDRILQQL--DSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
103-359 6.38e-53

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 179.52  E-value: 6.38e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 103 IRVEQEKLRMEAEYRSE----CAVAPQHYA------RNRYRDILPYDKNRVEIqkdsenPEGYMNASLIQLPGGKTeFIA 172
Cdd:COG5599   9 IKSEEEKINSRLSTLTNelapSHNDPQYLQningspLNRFRDIQPYKETALRA------NLGYLNANYIQVIGNHR-YIA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 173 AQAPLPATLDEWWKMIDEHRVSLVVIL--CKLVELNKIKCERYWPEQvGEselFGDYEITLEEEK---LFDD---DEYLM 244
Cdd:COG5599  82 TQYPLEEQLEDFFQMLFDNNTPVLVVLasDDEISKPKVKMPVYFRQD-GE---YGKYEVSSELTEsiqLRDGieaRTYVL 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 245 RClkmeNQTTGECRKVHQLHYREWPDHGCPSGEkQLLNMIDLMENIHEEVSPqDSSPILVHCSAGVGRTGTIIAINFIRE 324
Cdd:COG5599 158 TI----KGTGQKKIEIPVLHVKNWPDHGAISAE-ALKNLADLIDKKEKIKDP-DKLLPVVHCRAGVGRTGTLIACLALSK 231

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 86575091 325 QMKAETLHSIDIFGLVMTLRKQRAS-MVQTQDQFQF 359
Cdd:COG5599 232 SINALVQITLSVEEIVIDMRTSRNGgMVQTSEQLDV 267
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 124-367 1.36e-52

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: 177.34  E-value: 1.36e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 124 PQHYARNRYRDILPYDKNRVEIQ--KDSENPEGYMNASLIQLPGGK-TEFIAAQAPLPATLDEWWKMIDEHRVSLVVILC 200
Cdd:cd14612  13 PGHASKDRYKTILPNPQSRVCLRraGSQEEEGSYINANYIRGYDGKeKAYIATQGPMLNTVSDFWEMVWQEECPIIVMIT 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 201 KLVElNKIKCERYWPEQVGEselFGDYEITLEEEKlfDDDEYLMRCLKMenQTTGECRKVHQLHYREWPDHGCPSGEKQL 280
Cdd:cd14612  93 KLKE-KKEKCVHYWPEKEGT---YGRFEIRVQDMK--ECDGYTIRDLTI--QLEEESRSVKHYWFSSWPDHQTPESAGPL 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 281 LNMIDLMENiHEEVSPQdSSPILVHCSAGVGRTGTIIAINFIREQMKAETlhSIDIFGLVMTLRKQRASMVQTQDQFQFV 360
Cdd:cd14612 165 LRLVAEVEE-SRQTAAS-PGPIVVHCSAGIGRTGCFIATSIGCQQLKDTG--KVDILGIVCQLRLDRGGMIQTSEQYQFL 240


                ....*..
gi 86575091 361 HRCIASY 367
Cdd:cd14612 241 HHTLALY 247
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 129-362 2.24e-52

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: 176.56  E-value: 2.24e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 129 RNRYRDILPYDKNRVEIQKdSENPEG--YMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELN 206
Cdd:cd14554   9 KNRLVNILPYESTRVCLQP-IRGVEGsdYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLREMG 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 207 KIKCERYWPEQvgESELFGDYEITLEEEklFDDDEYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPSGEKQLLNMIDL 286
Cdd:cd14554  88 REKCHQYWPAE--RSARYQYFVVDPMAE--YNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQ 163

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86575091 287 MENIHEEVSpqDSSPILVHCSAGVGRTGTIIAINFIREQMKAEtlHSIDIFGLVMTLRKQRASMVQTQDQFQFVHR 362
Cdd:cd14554 164 VHKTKEQFG--QEGPITVHCSAGVGRTGVFITLSIVLERMRYE--GVVDVFQTVKLLRTQRPAMVQTEDQYQFCYR 235
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 129-368 9.89e-52

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: 174.83  E-value: 9.89e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 129 RNRYRDILPYDKNRVEIQKDSENPEG-YMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNK 207
Cdd:cd14630   6 KNRYGNIISYDHSRVRLQLLDGDPHSdYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVEVGR 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 208 IKCERYWPEqvgESELFGDYEITL-EEEKLfddDEYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPSGEKQLLNMIDL 286
Cdd:cd14630  86 VKCVRYWPD---DTEVYGDIKVTLiETEPL---AEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQ 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 287 MENIheevSPQDSSPILVHCSAGVGRTGTIIAINFIREQMKAETLhsIDIFGLVMTLRKQRASMVQTQDQFQFVHRCIAS 366
Cdd:cd14630 160 VKFL----NPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGV--VDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233


                ..
gi 86575091 367 YC 368
Cdd:cd14630 234 AC 235
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 130-362 1.63e-51

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: 173.94  E-value: 1.63e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 130 NRYRDILPYDKNRVEIQKDSENP-EGYMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKI 208
Cdd:cd14616   1 NRFPNIKPYNNNRVKLIADAGVPgSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 209 KCERYWPEQVGESELFGDYEITleeeKLFDD--DEYLMRCLKMENQttGECRKVHQLHYREWPDHGCPSGEKQLLNMIDL 286
Cdd:cd14616  81 RCHQYWPEDNKPVTVFGDIVIT----KLMEDvqIDWTIRDLKIERH--GDYMMVRQCNFTSWPEHGVPESSAPLIHFVKL 154

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86575091 287 MenihEEVSPQDSSPILVHCSAGVGRTGTIIAINFIREQMKAETLhsIDIFGLVMTLRKQRASMVQTQDQFQFVHR 362
Cdd:cd14616 155 V----RASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDF--VDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 155-362 1.70e-50

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: 170.70  E-value: 1.70e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 155 YMNASLIQLPGGKTE--FIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKIKCERYWPEQVGESELFGDYEITLE 232
Cdd:cd14596   1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 233 EEKLFDDdeYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPSGEKQLLNMIDLMENIHEEvspqdsSPILVHCSAGVGR 312
Cdd:cd14596  81 NYQALQY--FIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNT------GPIVVHCSAGIGR 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 86575091 313 TGTIIAINFIREQMKAETlhSIDIFGLVMTLRKQRASMVQTQDQFQFVHR 362
Cdd:cd14596 153 AGVLICVDVLLSLIEKDL--SFNIKDIVREMRQQRYGMIQTKDQYLFCYK 200
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 155-365 3.12e-50

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: 169.93  E-value: 3.12e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 155 YMNASLI-----QLPGgkteFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKIKCERYWPEQvgESELFGDYEI 229
Cdd:cd14546   1 YINASTIydhdpRNPA----YIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEE--GSEVYHIYEV 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 230 TLEEEKLFDDDeYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPSGEKQLLnmiDLMENIHEEVSPQdSSPILVHCSAG 309
Cdd:cd14546  75 HLVSEHIWCDD-YLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLL---EFRRKVNKSYRGR-SCPIVVHCSDG 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 86575091 310 VGRTGTIIAINFIREQMkAETLHSIDIFGLVMTLRKQRASMVQTQDQFQFVHRCIA 365
Cdd:cd14546 150 AGRTGTYILIDMVLNRM-AKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVA 204
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 120-379 4.80e-50

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: 171.75  E-value: 4.80e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 120 CAVA--PQHYARNRYRDILPYDKNRVEIQKDSENpegYMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVV 197
Cdd:cd14608  17 CRVAklPKNKNRNRYRDVSPFDHSRIKLHQEDND---YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVV 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 198 ILCKLVELNKIKCERYWPEQVGESELFGD--YEITLEEEKLfdDDEYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPS 275
Cdd:cd14608  94 MLNRVMEKGSLKCAQYWPQKEEKEMIFEDtnLKLTLISEDI--KSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPE 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 276 GEKQLLNmidLMENIHEE--VSPQdSSPILVHCSAGVGRTGTIIAINFIREQM-KAETLHSIDIFGLVMTLRKQRASMVQ 352
Cdd:cd14608 172 SPASFLN---FLFKVRESgsLSPE-HGPVVVHCSAGIGRSGTFCLADTCLLLMdKRKDPSSVDIKKVLLEMRKFRMGLIQ 247

                       250       260
                ....*....|....*....|....*..
gi 86575091 353 TQDQFQFvhrciaSYcrrhLGIIEEPK 379
Cdd:cd14608 248 TADQLRF------SY----LAVIEGAK 264
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 124-367 1.04e-49

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: 170.45  E-value: 1.04e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 124 PQHYARNRYRDILPYDKNRVEIQKDSENPEG--YMNASLI--QLPGG----KTeFIAAQAPLPATLDEWWKMIDEHRVSL 195
Cdd:cd14606  16 PENKSKNRYKNILPFDHSRVILQGRDSNIPGsdYINANYVknQLLGPdenaKT-YIASQGCLEATVNDFWQMAWQENSRV 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 196 VVILCKLVELNKIKCERYWPEqVGESELFGDYEITLEEEKlfDDDEYLMRCLKMENQTTGEC-RKVHQLHYREWPDHGCP 274
Cdd:cd14606  95 IVMTTREVEKGRNKCVPYWPE-VGMQRAYGPYSVTNCGEH--DTTEYKLRTLQVSPLDNGELiREIWHYQYLSWPDHGVP 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 275 SGEKQLLNMIDLMENIHEEVspQDSSPILVHCSAGVGRTGTIIAINFIREQMKAETLHS-IDIFGLVMTLRKQRASMVQT 353
Cdd:cd14606 172 SEPGGVLSFLDQINQRQESL--PHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLDCdIDIQKTIQMVRAQRSGMVQT 249

                       250
                ....*....|....
gi 86575091 354 QDQFQFVHRCIASY 367
Cdd:cd14606 250 EAQYKFIYVAIAQF 263
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 132-364 1.04e-49

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: 169.35  E-value: 1.04e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 132 YRDILPYDKNRVEI-QKDSENPEGYMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKIKC 210
Cdd:cd14620   1 YPNILPYDHSRVILsQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 211 ERYWPEQvgESELFGDYEITLEEEKLFDDdeYLMRCLKMENQTTGEC---RKVHQLHYREWPDHGCPSGEKQLLNMIDLM 287
Cdd:cd14620  81 YQYWPDQ--GCWTYGNIRVAVEDCVVLVD--YTIRKFCIQPQLPDGCkapRLVTQLHFTSWPDFGVPFTPIGMLKFLKKV 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86575091 288 ENiheeVSPQDSSPILVHCSAGVGRTGTIIAINFIREQMKAEtlHSIDIFGLVMTLRKQRASMVQTQDQFQFVHRCI 364
Cdd:cd14620 157 KS----VNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAE--QKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQAL 227
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 129-368 1.34e-49

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: 170.60  E-value: 1.34e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 129 RNRYRDILPYDKNRVEIQK-DSENPEGYMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNK 207
Cdd:cd14626  44 KNRYANVIAYDHSRVILTSvDGVPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSR 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 208 IKCERYWPEQvgESELFGDYEITLEEEklFDDDEYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPSGEKQLLNMIDLM 287
Cdd:cd14626 124 VKCDQYWPIR--GTETYGMIQVTLLDT--VELATYSVRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRV 199

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 288 enihEEVSPQDSSPILVHCSAGVGRTGTIIAINFIREQMKAETlhSIDIFGLVMTLRKQRASMVQTQDQFQFVHRCI--A 365
Cdd:cd14626 200 ----KACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEK--TVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALleA 273


                ...
gi 86575091 366 SYC 368
Cdd:cd14626 274 ATC 276
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 94-365 1.40e-49

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: 170.60  E-value: 1.40e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091  94 QDYLRRFYQIRVEQEKLRMEAEYRSECAVAPQ--HYARNRYRDILPYDKNRVEIQKDSeNPE--GYMNASLI-----QLP 164
Cdd:cd14609   8 EDHLRNRDRLAKEWQALCAYQAEPNTCSTAQGeaNVKKNRNPDFVPYDHARIKLKAES-NPSrsDYINASPIiehdpRMP 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 165 GgkteFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKIKCERYWPEQvgESELFGDYEITLEEEKLFDDDeYLM 244
Cdd:cd14609  87 A----YIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDE--GSSLYHIYEVNLVSEHIWCED-FLV 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 245 RCLKMENQTTGECRKVHQLHYREWPDHGCPSGEKQLLnmiDLMENIHEEVSPQdSSPILVHCSAGVGRTGTIIAINFIRE 324
Cdd:cd14609 160 RSFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLL---DFRRKVNKCYRGR-SCPIIVHCSDGAGRTGTYILIDMVLN 235

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 86575091 325 QMkAETLHSIDIFGLVMTLRKQRASMVQTQDQFQFVHRCIA 365
Cdd:cd14609 236 RM-AKGVKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVA 275
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 120-364 2.02e-49

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: 170.03  E-value: 2.02e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 120 CAVAPQHYARNRYRDILPYDKNRVEIQKDsenpEGYMNASLI--QLPGGK--TEFIAAQAPLPATLDEWWKMIDEHRVSL 195
Cdd:cd14600  34 CAKLPQNMDKNRYKDVLPYDATRVVLQGN----EDYINASYVnmEIPSANivNKYIATQGPLPHTCAQFWQVVWEQKLSL 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 196 VVILCKLVELNKIKCERYWPE--QVGEselFGDYEITLEEEKLfdDDEYLMRCLKMENQTTGECRKVHQLHYREWPDHGC 273
Cdd:cd14600 110 IVMLTTLTERGRTKCHQYWPDppDVME---YGGFRVQCHSEDC--TIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGV 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 274 PSGEKQLLNMIDLMENIHeevspQDSSPILVHCSAGVGRTGTIIAINFIREQM-KAETLHSIDIfglVMTLRKQRASMVQ 352
Cdd:cd14600 185 PDDSSDFLEFVNYVRSKR-----VENEPVLVHCSAGIGRTGVLVTMETAMCLTeRNQPVYPLDI---VRKMRDQRAMMVQ 256

                       250
                ....*....|..
gi 86575091 353 TQDQFQFVHRCI 364
Cdd:cd14600 257 TSSQYKFVCEAI 268
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 155-367 4.48e-49

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: 167.25  E-value: 4.48e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 155 YMNASLIQLP-GGKTEF-IAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKIKCERYWPEQVGE--SELFGDYEIT 230
Cdd:cd14540   1 YINASHITATvGGKQRFyIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEhdALTFGEYKVS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 231 LEeeKLFDDDEYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPSGEKQLLNMIDLMENIH----EEVSPQDSS-PILVH 305
Cdd:cd14540  81 TK--FSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRrhtnQDVAGHNRNpPTLVH 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86575091 306 CSAGVGRTGTII----AINFIREQMKaetlhsIDIFGLVMTLRKQRASMVQTQDQFQFVHRCIASY 367
Cdd:cd14540 159 CSAGVGRTGVVIladlMLYCLDHNEE------LDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQY 218
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 155-364 1.25e-48

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: 165.97  E-value: 1.25e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 155 YMNASLI--QLPGGK--TEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKIKCERYWPEqVGESELFGDYEIT 230
Cdd:cd14541   2 YINANYVnmEIPGSGivNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPD-LGETMQFGNLQIT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 231 LEEEKlfDDDEYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPSGEKQLLNMIdlMENIHEEVSPQDssPILVHCSAGV 310
Cdd:cd14541  81 CVSEE--VTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFV--KRVRQNRVGMVE--PTVVHCSAGI 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 86575091 311 GRTGTIIAINFIREQMKA-ETLHSIDIfglVMTLRKQRASMVQTQDQFQFVHRCI 364
Cdd:cd14541 155 GRTGVLITMETAMCLIEAnEPVYPLDI---VRTMRDQRAMLIQTPSQYRFVCEAI 206
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 121-367 1.34e-48

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: 168.25  E-value: 1.34e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 121 AVAPQHYARNRYRDILPYDKNRVEIQKDSENPEGYMNASLIQLPGGKTE--FIAAQAPLPATLDEWWKMIDEHRVSLVVI 198
Cdd:cd14599  33 ATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAM 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 199 LCKLVELNKIKCERYWPeQVG---ESELFGDYEITLEeeklFDDDE--YLMRCLKMENQTTGECRKVHQLHYREWPDHGC 273
Cdd:cd14599 113 VTAEEEGGRSKSHRYWP-KLGskhSSATYGKFKVTTK----FRTDSgcYATTGLKVKHLLSGQERTVWHLQYTDWPDHGC 187

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 274 PSGEKQLLNMIDLMENIHEEVSPQ-DSS-----PILVHCSAGVGRTGTIIainfIREQMKA--ETLHSIDIFGLVMTLRK 345
Cdd:cd14599 188 PEEVQGFLSYLEEIQSVRRHTNSMlDSTkncnpPIVVHCSAGVGRTGVVI----LTELMIGclEHNEKVEVPVMLRHLRE 263

                       250       260
                ....*....|....*....|..
gi 86575091 346 QRASMVQTQDQFQFVHRCIASY 367
Cdd:cd14599 264 QRMFMIQTIAQYKFVYQVLIQF 285
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 107-365 2.14e-48

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: 167.54  E-value: 2.14e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 107 QEKLRMEAEYRSECAVAP-----------QHYARNRYRDILPYDKNRVEIQ-KDSENPEGYMNASLIQLPGGKT-EFIAA 173
Cdd:cd14610  14 KNKNRLEKEWEALCAYQAepnatnvaqreENVQKNRSLAVLPYDHSRIILKaENSHSHSDYINASPIMDHDPRNpAYIAT 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 174 QAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKIKCERYWPEQvgESELFGDYEITLEEEKLFDDDeYLMRCLKMENQT 253
Cdd:cd14610  94 QGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDE--GSNLYHIYEVNLVSEHIWCED-FLVRSFYLKNLQ 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 254 TGECRKVHQLHYREWPDHGCPSGEKQLLnmiDLMENIHEEVSPQdSSPILVHCSAGVGRTGTIIAINFIREQMkAETLHS 333
Cdd:cd14610 171 TNETRTVTQFHFLSWNDQGVPASTRSLL---DFRRKVNKCYRGR-SCPIIVHCSDGAGRSGTYILIDMVLNKM-AKGAKE 245

                       250       260       270
                ....*....|....*....|....*....|..
gi 86575091 334 IDIFGLVMTLRKQRASMVQTQDQFQFVHRCIA 365
Cdd:cd14610 246 IDIAATLEHLRDQRPGMVQTKEQFEFALTAVA 277
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 96-367 3.04e-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: 167.60  E-value: 3.04e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091  96 YLRRFYQIRVEQEKLRMEAEYRsECAVAPQHYAR------------NRYRDILPYDKNRVEIQ--KDSENPEgYMNASLI 161
Cdd:cd14628  11 YIQKLTQIETGENVTGMELEFK-RLASSKAHTSRfisanlpcnkfkNRLVNIMPYESTRVCLQpiRGVEGSD-YINASFI 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 162 QLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKIKCERYWP-EQVGESELFgdyeiTLEEEKLFDDD 240
Cdd:cd14628  89 DGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPaERSARYQYF-----VVDPMAEYNMP 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 241 EYLMRCLKMENQTTGECRKVHQLHYREWPDHGCP-SGEkqllNMIDLMENIH--EEVSPQDsSPILVHCSAGVGRTGTII 317
Cdd:cd14628 164 QYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPkSGE----GFIDFIGQVHktKEQFGQD-GPISVHCSAGVGRTGVFI 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 86575091 318 AINFIREQMKAETLhsIDIFGLVMTLRKQRASMVQTQDQFQFVHRCIASY 367
Cdd:cd14628 239 TLSIVLERMRYEGV--VDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEY 286
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 129-367 5.63e-48

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: 165.58  E-value: 5.63e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 129 RNRYRDILPYDKNRVEIQKDSENPEG--YMNASLIqLPGGKTE---------FIAAQAPLPATLDEWWKMIDEHRVSLVV 197
Cdd:cd14605   5 KNRYKNILPFDHTRVVLHDGDPNEPVsdYINANII-MPEFETKcnnskpkksYIATQGCLQNTVNDFWRMVFQENSRVIV 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 198 ILCKLVELNKIKCERYWPEQVGESElFGDYEITLEEEKLFDDdeYLMRCLKMENQTTGEC-RKVHQLHYREWPDHGCPSG 276
Cdd:cd14605  84 MTTKEVERGKSKCVKYWPDEYALKE-YGVMRVRNVKESAAHD--YILRELKLSKVGQGNTeRTVWQYHFRTWPDHGVPSD 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 277 EKQLLnmiDLMENI-HEEVSPQDSSPILVHCSAGVGRTGTIIAINFIREQMKAETLH-SIDIFGLVMTLRKQRASMVQTQ 354
Cdd:cd14605 161 PGGVL---DFLEEVhHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDcDIDVPKTIQMVRSQRSGMVQTE 237

                       250
                ....*....|...
gi 86575091 355 DQFQFVHRCIASY 367
Cdd:cd14605 238 AQYRFIYMAVQHY 250
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 155-368 7.19e-48

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: 163.55  E-value: 7.19e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 155 YMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKIKCERYWPEqvgESELFGDYEITLEEE 234
Cdd:cd14555   1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPD---DTEVYGDIKVTLVET 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 235 KLFddDEYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPSGEKQLLNMIDLMENIheevSPQDSSPILVHCSAGVGRTG 314
Cdd:cd14555  78 EPL--AEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKAS----NPPSAGPIVVHCSAGAGRTG 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 86575091 315 TIIAINFIREQMKAETLhsIDIFGLVMTLRKQRASMVQTQDQFQFVHRCIASYC 368
Cdd:cd14555 152 CYIVIDIMLDMAEREGV--VDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEAC 203
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 155-364 1.30e-47

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: 162.82  E-value: 1.30e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 155 YMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKIKCERYWPEQVGESelFGDYEITLEEE 234
Cdd:cd14552   1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVS--SGDITVELKDQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 235 KLFDDdeYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPSGEKqllNMIDLMENIHEEVSPQDSSPILVHCSAGVGRTG 314
Cdd:cd14552  79 TDYED--YTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGK---GMIDLIAAVQKQQQQSGNHPITVHCSAGAGRTG 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 86575091 315 TIIAINFIREQMKAETLhsIDIFGLVMTLRKQRASMVQTQDQFQFVHRCI 364
Cdd:cd14552 154 TFCALSTVLERVKAEGV--LDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 115-364 2.21e-47

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: 2.21e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 115 EYRSECAVAPQHYARNRYRDILPYDKNRVEIQkDSENpeGYMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVS 194
Cdd:cd14607  13 DYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQ-NTEN--DYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTK 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 195 LVVILCKLVELNKIKCERYWPEQvGESELFgdYEITLEEEKLFDDD---EYLMRCLKMENQTTGECRKVHQLHYREWPDH 271
Cdd:cd14607  90 AVVMLNRIVEKDSVKCAQYWPTD-EEEVLS--FKETGFSVKLLSEDvksYYTVHLLQLENINSGETRTISHFHYTTWPDF 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 272 GCPSGEKQLLNmidLMENIHEEVS-PQDSSPILVHCSAGVGRTGTIIAINFIREQMKAETLHSIDIFGLVMTLRKQRASM 350
Cdd:cd14607 167 GVPESPASFLN---FLFKVRESGSlSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDPDSVDIKQVLLDMRKYRMGL 243

                       250
                ....*....|....
gi 86575091 351 VQTQDQFQFVHRCI 364
Cdd:cd14607 244 IQTPDQLRFSYMAV 257
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 119-364 2.22e-47

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: 163.91  E-value: 2.22e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 119 ECAVAPQHYARNRYRDILPYDKNRVE-IQKDSENPEGYMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVV 197
Cdd:cd14614   5 FAADLPVNRCKNRYTNILPYDFSRVKlVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIV 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 198 ILCKLVELNKIKCERYWPEQvGESELFGDyeITLEEEKLFDDDEYLMRCLKMenQTTGECRKVHQLHYREWPDHGCPSGE 277
Cdd:cd14614  85 MLTQCNEKRRVKCDHYWPFT-EEPVAYGD--ITVEMLSEEEQPDWAIREFRV--SYADEVQDVMHFNYTAWPDHGVPTAN 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 278 KqLLNMIDLMENIHEEVSpQDSSPILVHCSAGVGRTGTIIAINFIREQMKAETLhsIDIFGLVMTLRKQRASMVQTQDQF 357
Cdd:cd14614 160 A-AESILQFVQMVRQQAV-KSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEF--VDILGLVSEMRSYRMSMVQTEEQY 235


                ....*..
gi 86575091 358 QFVHRCI 364
Cdd:cd14614 236 IFIHQCV 242
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 155-368 4.73e-46

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


Pssm-ID: 350480 [Multi-domain]  Cd Length: 205  Bit Score: 159.06  E-value: 4.73e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 155 YMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKIKCERYWPEqvgESELFGDYEITL-EE 233
Cdd:cd14632   1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPD---DSDTYGDIKITLlKT 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 234 EKLfddDEYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPSGEKQLLNMIDLMENiheeVSPQDSSPILVHCSAGVGRT 313
Cdd:cd14632  78 ETL---AEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKA----STPPDAGPVVVHCSAGAGRT 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 86575091 314 GTIIAINFIREQMKAETLhsIDIFGLVMTLRKQRASMVQTQDQFQFVHRCIASYC 368
Cdd:cd14632 151 GCYIVLDVMLDMAECEGV--VDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEAC 203
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 155-362 1.16e-45

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: 1.16e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 155 YMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKIKCERYWPEQVGESELFGDYEITLEEE 234
Cdd:cd14557   1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 235 KLFDDdeYLMRCLKMEN-QTTGECRKVHQLHYREWPDHGCPSGEKQLLNM---IDLMENIHeevspqdSSPILVHCSAGV 310
Cdd:cd14557  81 KICPD--YIIRKLNINNkKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLrrrVNAFNNFF-------SGPIVVHCSAGV 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 86575091 311 GRTGTIIAINFIREQMKAETlhSIDIFGLVMTLRKQRASMVQTQDQFQFVHR 362
Cdd:cd14557 152 GRTGTYIGIDAMLEGLEAEG--RVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 155-367 1.40e-45

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: 157.86  E-value: 1.40e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 155 YMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKIKCERYWPEQvgESELFGDYEITLEEE 234
Cdd:cd14622   2 YINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSE--GSVTHGEITIEIKND 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 235 KLFddDEYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPSGEKqllNMIDLMENIHEEVSPQDSSPILVHCSAGVGRTG 314
Cdd:cd14622  80 TLL--ETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGK---GMIDLIAAVQKQQQQTGNHPIVVHCSAGAGRTG 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 86575091 315 TIIAINFIREQMKAETLhsIDIFGLVMTLRKQRASMVQTQDQFQFVHRCIASY 367
Cdd:cd14622 155 TFIALSNILERVKAEGL--LDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 124-361 2.12e-45

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


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 159.43  E-value: 2.12e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 124 PQHYARNRYRDILPYDKNRVEIQ----KDSENPEgYMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVIL 199
Cdd:cd17667  25 PDNKHKNRYINILAYDHSRVKLRplpgKDSKHSD-YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMI 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 200 CKLVELNKIKCERYWPEQvgESELFGDYEITLEEEKL---FDDDEYLMRCLKMENQTTGEC------RKVHQLHYREWPD 270
Cdd:cd17667 104 TNLVEKGRRKCDQYWPTE--NSEEYGNIIVTLKSTKIhacYTVRRFSIRNTKVKKGQKGNPkgrqneRTVIQYHYTQWPD 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 271 HGCPsgeKQLLNMIDLMENIHEEVSPqDSSPILVHCSAGVGRTGTIIAINFIREQMKAETlhSIDIFGLVMTLRKQRASM 350
Cdd:cd17667 182 MGVP---EYALPVLTFVRRSSAARTP-EMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKS--TVNVLGFLKHIRTQRNYL 255

                       250
                ....*....|.
gi 86575091 351 VQTQDQFQFVH 361
Cdd:cd17667 256 VQTEEQYIFIH 266
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 129-364 2.55e-45

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: 159.49  E-value: 2.55e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 129 RNRYRDILPYDKNRVEIQK-DSENPEGYMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNK 207
Cdd:cd14625  50 KNRYANVIAYDHSRVILQPiEGIMGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSR 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 208 IKCERYWPEQvgESELFGDYEITLEEEklFDDDEYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPSGEKQLLNMIDLM 287
Cdd:cd14625 130 IKCDQYWPSR--GTETYGMIQVTLLDT--IELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRV 205

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86575091 288 ENiheeVSPQDSSPILVHCSAGVGRTGTIIAINFIREQMKAETlhSIDIFGLVMTLRKQRASMVQTQDQFQFVHRCI 364
Cdd:cd14625 206 KT----CNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEK--TVDIYGHVTLMRSQRNYMVQTEDQYSFIHDAL 276
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 96-367 4.96e-45

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 159.13  E-value: 4.96e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091  96 YLRRFYQIRVEQEKLRMEAEY-----------RSECAVAPQHYARNRYRDILPYDKNRVEIQ--KDSENPEgYMNASLIQ 162
Cdd:cd14627  12 YIQKLAQVEVGEHVTGMELEFkrlanskahtsRFISANLPCNKFKNRLVNIMPYETTRVCLQpiRGVEGSD-YINASFID 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 163 LPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKIKCERYWP-EQVGESELFgdyeiTLEEEKLFDDDE 241
Cdd:cd14627  91 GYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPaERSARYQYF-----VVDPMAEYNMPQ 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 242 YLMRCLKMENQTTGECRKVHQLHYREWPDHGCP-SGEkqllNMIDLMENIH--EEVSPQDsSPILVHCSAGVGRTGTIIA 318
Cdd:cd14627 166 YILREFKVTDARDGQSRTVRQFQFTDWPEQGVPkSGE----GFIDFIGQVHktKEQFGQD-GPISVHCSAGVGRTGVFIT 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 86575091 319 INFIREQMKAETLhsIDIFGLVMTLRKQRASMVQTQDQFQFVHRCIASY 367
Cdd:cd14627 241 LSIVLERMRYEGV--VDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEY 287
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 129-361 5.04e-45

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: 157.00  E-value: 5.04e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 129 RNRYRDILPYDKNRVEIQ-KDSENP-EGYMNASLIQLPGGKTE-FIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVEL 205
Cdd:cd14611   2 KNRYKTILPNPHSRVCLKpKNSNDSlSTYINANYIRGYGGKEKaFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 206 NKiKCERYWPEQVGeseLFGDYEITLEEEKlfDDDEYLMRCLKMENqtTGECRKVHQLHYREWPDHGCPSGEKQLLN-MI 284
Cdd:cd14611  82 NE-KCVLYWPEKRG---IYGKVEVLVNSVK--ECDNYTIRNLTLKQ--GSQSRSVKHYWYTSWPDHKTPDSAQPLLQlML 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86575091 285 DLMEnihEEVSPQDSSPILVHCSAGVGRTGTIIAINFIREQMKAETLhsIDIFGLVMTLRKQRASMVQTQDQFQFVH 361
Cdd:cd14611 154 DVEE---DRLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGV--VDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 129-368 5.96e-45

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: 158.28  E-value: 5.96e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 129 RNRYRDILPYDKNRVEIQK-DSENPEGYMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNK 207
Cdd:cd14633  43 KNRYGNIIAYDHSRVRLQPiEGETSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGR 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 208 IKCERYWPEqvgESELFGDYEITLEEEKLFddDEYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPSGEKQLLNMIDLM 287
Cdd:cd14633 123 VKCCKYWPD---DTEIYKDIKVTLIETELL--AEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQV 197

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 288 ENiheeVSPQDSSPILVHCSAGVGRTGTIIAINFIREQMKAETLhsIDIFGLVMTLRKQRASMVQTQDQFQFVHRCIASY 367
Cdd:cd14633 198 KS----KSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGV--VDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEA 271


                .
gi 86575091 368 C 368
Cdd:cd14633 272 C 272
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 131-364 1.39e-44

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: 155.97  E-value: 1.39e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 131 RYRDILPYDKNRVEIQ-KDSENPEGYMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKIK 209
Cdd:cd14623   1 RVLQIIPYEFNRVIIPvKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 210 CERYWPEQvgESELFGDYEITLEEEKlfDDDEYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPSGEKQLLNMIDLMEN 289
Cdd:cd14623  81 CAQYWPSD--GSVSYGDITIELKKEE--ECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQK 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86575091 290 IHEEvspQDSSPILVHCSAGVGRTGTIIAINFIREQMKAETLhsIDIFGLVMTLRKQRASMVQTQDQFQFVHRCI 364
Cdd:cd14623 157 QQQQ---SGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGI--LDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 129-361 2.68e-44

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: 156.82  E-value: 2.68e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 129 RNRYRDILPYDKNRVEIQKDSENP-EGYMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNK 207
Cdd:cd14624  50 KNRYANVIAYDHSRVLLSAIEGIPgSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSR 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 208 IKCERYWPEQvgESELFGDYEITLEEEklFDDDEYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPSGEKQLLNMIDLM 287
Cdd:cd14624 130 VKCDQYWPSR--GTETYGLIQVTLLDT--VELATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRV 205

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86575091 288 ENiheeVSPQDSSPILVHCSAGVGRTGTIIAINFIREQMKAETlhSIDIFGLVMTLRKQRASMVQTQDQFQFVH 361
Cdd:cd14624 206 KT----CNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEK--TVDIYGHVTLMRAQRNYMVQTEDQYIFIH 273
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 124-367 2.74e-44

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: 157.19  E-value: 2.74e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 124 PQHYARNRYRDILPYDKNRVEIQ--KDSENPEgYMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCK 201
Cdd:cd14629  51 PCNKFKNRLVNIMPYELTRVCLQpiRGVEGSD-YINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTK 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 202 LVELNKIKCERYWP-EQVGESELFgdyeiTLEEEKLFDDDEYLMRCLKMENQTTGECRKVHQLHYREWPDHGCP-SGEkq 279
Cdd:cd14629 130 LREMGREKCHQYWPaERSARYQYF-----VVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPkTGE-- 202

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 280 llNMIDLMENIH--EEVSPQDsSPILVHCSAGVGRTGTIIAINFIREQMKAETLhsIDIFGLVMTLRKQRASMVQTQDQF 357
Cdd:cd14629 203 --GFIDFIGQVHktKEQFGQD-GPITVHCSAGVGRTGVFITLSIVLERMRYEGV--VDMFQTVKTLRTQRPAMVQTEDQY 277

                       250
                ....*....|
gi 86575091 358 QFVHRCIASY 367
Cdd:cd14629 278 QLCYRAALEY 287
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 119-364 7.22e-44

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: 155.95  E-value: 7.22e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 119 ECAVAPQHYARNRYRDILPYDKNRVEIQKDSENPEG-YMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVV 197
Cdd:cd14621  45 EAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSdYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIV 124

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 198 ILCKLVELNKIKCERYWPEQvgESELFGDYEITLEEEKLFDDDEYLMRCLKMENQTTGE--CRKVHQLHYREWPDHGCPS 275
Cdd:cd14621 125 MVTNLKERKECKCAQYWPDQ--GCWTYGNIRVSVEDVTVLVDYTVRKFCIQQVGDVTNKkpQRLITQFHFTSWPDFGVPF 202

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 276 GEKQLLNMIDLMENiheeVSPQDSSPILVHCSAGVGRTGTIIAINFIREQMKAEtlHSIDIFGLVMTLRKQRASMVQTQD 355
Cdd:cd14621 203 TPIGMLKFLKKVKN----CNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAE--RKVDVYGFVSRIRAQRCQMVQTDM 276


                ....*....
gi 86575091 356 QFQFVHRCI 364
Cdd:cd14621 277 QYVFIYQAL 285
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 142-368 7.29e-44

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: 153.64  E-value: 7.29e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 142 RVEIQKDSENPEG-YMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKIKCERYWPEqvgE 220
Cdd:cd14631   1 RVILQPVEDDPSSdYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPD---D 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 221 SELFGDYEIT-LEEEKLfddDEYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPSGEKQLLNMIDLMenihEEVSPQDS 299
Cdd:cd14631  78 TEVYGDFKVTcVEMEPL---AEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRV----KLSNPPSA 150

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 86575091 300 SPILVHCSAGVGRTGTIIAINFIREQMKAETLhsIDIFGLVMTLRKQRASMVQTQDQFQFVHRCIASYC 368
Cdd:cd14631 151 GPIVVHCSAGAGRTGCYIVIDIMLDMAEREGV--VDIYNCVKALRSRRINMVQTEEQYIFIHDAILEAC 217
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 129-367 1.01e-43

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: 154.64  E-value: 1.01e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 129 RNRYRDILPYDKNRVE-IQKDSENP-EGYMNASLIQLPGGKTE-FIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVEL 205
Cdd:cd14613  28 KNRYKTILPNPHSRVClTSPDQDDPlSSYINANYIRGYGGEEKvYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 206 NKiKCERYWPEqvgESELFGDYEITLEEEklFDDDEYLMRCLKMenQTTGECRKVHQLHYREWPDHGCPSGEKQLLNMID 285
Cdd:cd14613 108 NE-KCTEYWPE---EQVTYEGIEITVKQV--IHADDYRLRLITL--KSGGEERGLKHYWYTSWPDQKTPDNAPPLLQLVQ 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 286 LMENIHEEvSPQDSSPILVHCSAGVGRTGTIIAINFIREQMKAETLhsIDIFGLVMTLRKQRASMVQTQDQFQFVHRCIA 365
Cdd:cd14613 180 EVEEARQQ-AEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGV--VDILRTTCQLRLDRGGMIQTCEQYQFVHHVLS 256


                ..
gi 86575091 366 SY 367
Cdd:cd14613 257 LY 258
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 155-359 3.10e-43

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: 151.39  E-value: 3.10e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 155 YMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKIKCERYWPEqvgESELFGDYEITLEEE 234
Cdd:cd14558   1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGD---EKKTYGDIEVELKDT 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 235 KLFddDEYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPSGEKQLLNMID-LMENIHEEVSPQD-SSPILVHCSAGVGR 312
Cdd:cd14558  78 EKS--PTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKsIKQKLPYKNSKHGrSVPIVVHCSDGSSR 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 86575091 313 TGTIIAINFIREQmkAETLHSIDIFGLVMTLRKQRASMVQTQDQFQF 359
Cdd:cd14558 156 TGIFCALWNLLES--AETEKVVDVFQVVKALRKQRPGMVSTLEQYQF 200
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 155-362 5.19e-43

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: 150.83  E-value: 5.19e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 155 YMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKIKCERYWPEQvGEsELFGDYEITLEEE 234
Cdd:cd14551   1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQ-GC-WTYGNLRVRVEDT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 235 KLFDDdeYLMR--CLKMENQTTGE--CRKVHQLHYREWPDHGCPsgeKQLLNMIDLMENIhEEVSPQDSSPILVHCSAGV 310
Cdd:cd14551  79 VVLVD--YTTRkfCIQKVNRGIGEkrVRLVTQFHFTSWPDFGVP---FTPIGMLKFLKKV-KSANPPRAGPIVVHCSAGV 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 86575091 311 GRTGTIIAINFIREQMKAEtlHSIDIFGLVMTLRKQRASMVQTQDQFQFVHR 362
Cdd:cd14551 153 GRTGTFIVIDAMLDMMHAE--GKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 155-364 8.57e-42

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: 147.78  E-value: 8.57e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 155 YMNASLI--QLPGGK--TEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKIKCERYWPEQVGESElFGDYEIT 230
Cdd:cd14601   2 YINANYInmEIPSSSiiNRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSS-YGGFQVT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 231 LEEEKlfDDDEYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPSGEKQLLNMIDLMENI---HEEvspqdssPILVHCS 307
Cdd:cd14601  81 CHSEE--GNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKragKDE-------PVVVHCS 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 86575091 308 AGVGRTGTIIAINFIREQMK-AETLHSIDIfglVMTLRKQRASMVQTQDQFQFVHRCI 364
Cdd:cd14601 152 AGIGRTGVLITMETAMCLIEcNQPVYPLDI---VRTMRDQRAMMIQTPSQYRFVCEAI 206
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 155-359 2.36e-41

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: 146.46  E-value: 2.36e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 155 YMNASLIQLP--GGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNK-IKCERYWPEQVGESELFGDYEITL 231
Cdd:cd17658   1 YINASLVETPasESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPAEENESREFGRISVTN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 232 EEEKLfDDDEYLMRCLKME-NQTTGECRKVHQLHYREWPDHGCPSGEKQLLNMIDLMENIheevsPQDSSPILVHCSAGV 310
Cdd:cd17658  81 KKLKH-SQHSITLRVLEVQyIESEEPPLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGI-----PPSAGPIVVHCSAGI 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 86575091 311 GRTGTIIAI-NFIREQMKAEtLHSIDIFGLVMTLRKQRASMVQTQDQFQF 359
Cdd:cd17658 155 GRTGAYCTIhNTIRRILEGD-MSAVDLSKTVRKFRSQRIGMVQTQDQYIF 203
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 155-361 2.42e-40

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: 143.68  E-value: 2.42e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 155 YMNASLIQ-LPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKIKCERYWPEQVGESELFGDYEITLEE 233
Cdd:cd14539   1 YINASLIEdLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAITVSLQS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 234 EKlfDDDEYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPSGEKQLLNMIdlmENIHEEVSPQDSS--PILVHCSAGVG 311
Cdd:cd14539  81 VR--TTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFI---EEVHSHYLQQRSLqtPIVVHCSSGVG 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 86575091 312 RTGTI-IAINFIREqmkAETLHSI-DIFGLVMTLRKQRASMVQTQDQFQFVH 361
Cdd:cd14539 156 RTGAFcLLYAAVQE---IEAGNGIpDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 155-361 3.94e-40

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


Pssm-ID: 350506 [Multi-domain]  Cd Length: 209  Bit Score: 143.20  E-value: 3.94e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 155 YMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKIKCERYWPEQvgESELFGDYEITLEEE 234
Cdd:cd17668   1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPAD--GSEEYGNFLVTQKSV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 235 KLFddDEYLMRCLKMEN--------QTTGECRKVHQLHYREWPDHGCPSGEKQLLNMIdlmeNIHEEVSPQDSSPILVHC 306
Cdd:cd17668  79 QVL--AYYTVRNFTLRNtkikkgsqKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFV----RKASYAKRHAVGPVVVHC 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 86575091 307 SAGVGRTGTIIAINFIREQMKAETlhSIDIFGLVMTLRKQRASMVQTQDQFQFVH 361
Cdd:cd17668 153 SAGVGRTGTYIVLDSMLQQIQHEG--TVNIFGFLKHIRSQRNYLVQTEEQYVFIH 205
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 155-369 3.44e-38

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: 138.57  E-value: 3.44e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 155 YMNASLIQLPGGKTE--FIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKIKCERYWPeQVGE---SELFGDYEI 229
Cdd:cd14598   1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWP-RLGSrhnTVTYGRFKI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 230 TLEeeklFDDDE--YLMRCLKMENQTTGECRKVHQLHYREWPDHGCPSGEKQLLNMIDLMENI----HEEVSPQDS-SPI 302
Cdd:cd14598  80 TTR----FRTDSgcYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVrrhtNSTIDPKSPnPPV 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 86575091 303 LVHCSAGVGRTGTIIainfIREQMKAETLHS--IDIFGLVMTLRKQRASMVQTQDQFQFVHRCIASYCR 369
Cdd:cd14598 156 LVHCSAGVGRTGVVI----LSEIMIACLEHNemLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
259-366 1.18e-33

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 122.47  E-value: 1.18e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091    259 KVHQLHYREWPDHGCPSGEKQLLNMIDLMENIHEEVSPqdSSPILVHCSAGVGRTGTIIAINFIREQMKAETLhSIDIFG 338
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSES--SGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAG-EVDIFD 77

                           90       100
                   ....*....|....*....|....*...
gi 86575091    339 LVMTLRKQRASMVQTQDQFQFVHRCIAS 366
Cdd:smart00404  78 TVKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 259-366 1.18e-33

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: 122.47  E-value: 1.18e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091    259 KVHQLHYREWPDHGCPSGEKQLLNMIDLMENIHEEVSPqdSSPILVHCSAGVGRTGTIIAINFIREQMKAETLhSIDIFG 338
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSES--SGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAG-EVDIFD 77

                           90       100
                   ....*....|....*....|....*...
gi 86575091    339 LVMTLRKQRASMVQTQDQFQFVHRCIAS 366
Cdd:smart00012  78 TVKELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 155-361 7.66e-33

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: 123.29  E-value: 7.66e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 155 YMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLvELNKIKCERYWPEQvgESELFGDYEITLEEE 234
Cdd:cd14556   1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQL-DPKDQSCPQYWPDE--GSGTYGPIQVEFVST 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 235 KLfdDDEYLMRCLKMENQTTGE--CRKVHQLHYREWPDHG-CPSGEKQLLNMIDLMENIHEEvspQDSSPILVHCSAGVG 311
Cdd:cd14556  78 TI--DEDVISRIFRLQNTTRPQegYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQ---SGEGPIVVHCLNGVG 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 86575091 312 RTGTIIAINFIREQMKAEtlHSIDIFGLVMTLRKQRASMVQTQDQFQFVH 361
Cdd:cd14556 153 RSGVFCAISSVCERIKVE--NVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 124-379 4.22e-32

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 124.76  E-value: 4.22e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091  124 PQHYARNRYRDILPYDKNRVEIQK--------------------DSENPEGYMNASLIQLPGGKTEFIAAQAPLPATLDE 183
Cdd:PHA02746  49 KENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkkievtSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSED 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091  184 WWKMIDEHRVSLVVILCKlVELNKIKCERYWPEQVGESELFGDYEI-TLE--EEKLFDDDEylmrcLKMENQTTGECRKV 260
Cdd:PHA02746 129 FFKLISEHESQVIVSLTD-IDDDDEKCFELWTKEEDSELAFGRFVAkILDiiEELSFTKTR-----LMITDKISDTSREI 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091  261 HQLHYREWPDHGCPSGEKQLLNMIDLMENIHEEV------SPQDSSPILVHCSAGVGRTGTIIAINFIREQMKAEtlHSI 334
Cdd:PHA02746 203 HHFWFPDWPDNGIPTGMAEFLELINKVNEEQAELikqadnDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKE--KEV 280

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 86575091  335 DIFGLVMTLRKQRASMVQTQDQFQFVHRCIasycrrHLGIIEEPK 379
Cdd:PHA02746 281 CLGEIVLKIRKQRHSSVFLPEQYAFCYKAL------KYAIIEEAK 319
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 125-369 2.90e-30

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 119.34  E-value: 2.90e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091  125 QHYARNRYRDILPYDKNRVeIQKDSENPEGYMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVE 204
Cdd:PHA02742  51 KNMKKCRYPDAPCFDRNRV-ILKIEDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091  205 LNKIKCERYWPEQVGESELFGDYEITLEEEKLFDDdeYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPSGEKQLLNMI 284
Cdd:PHA02742 130 DGKEACYPYWMPHERGKATHGEFKIKTKKIKSFRN--YAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFV 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091  285 ------DLMENI-HEEVSPQDSSPILVHCSAGVGRTGTIIAINFIREQMKAETLhsIDIFGLVMTLRKQRASMVQTQDQF 357
Cdd:PHA02742 208 lavreaDLKADVdIKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAI--IPLLSIVRDLRKQRHNCLSLPQQY 285

                        250
                 ....*....|..
gi 86575091  358 QFVHRCIASYCR 369
Cdd:PHA02742 286 IFCYFIVLIFAK 297
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 124-361 8.00e-28

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 112.79  E-value: 8.00e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091  124 PQHYARNRYRDILPYDKNRVEIQKDSENPEGYMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLV 203
Cdd:PHA02747  49 PENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTK 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091  204 ELN-KIKCERYWPEQVGESELFGDYEItlEEEKLFDDDEYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPSGEK---Q 279
Cdd:PHA02747 129 GTNgEEKCYQYWCLNEDGNIDMEDFRI--ETLKTSVRAKYILTLIEITDKILKDSRKISHFQCSEWFEDETPSDHPdfiK 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091  280 LLNMIDLMENIH-EEVSPQDS--SPILVHCSAGVGRTGTIIAINFIREQMKAETlhSIDIFGLVMTLRKQRASMVQTQDQ 356
Cdd:PHA02747 207 FIKIIDINRKKSgKLFNPKDAllCPIVVHCSDGVGKTGIFCAVDICLNQLVKRK--AICLAKTAEKIREQRHAGIMNFDD 284


                 ....*
gi 86575091  357 FQFVH 361
Cdd:PHA02747 285 YLFIQ 289
PHA02738 PHA02738
hypothetical protein; Provisional
 130-367 2.37e-26

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 108.86  E-value: 2.37e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091  130 NRYRDILPYDKNRVEIQKDsENPEGYMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKIK 209
Cdd:PHA02738  53 NRYLDAVCFDHSRVILPAE-RNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREK 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091  210 CERYWPEQVGESELFGDYEITLEEEKLFddDEYLMRCLKMENqTTGECRKVHQLHYREWPDHGCPSGEKQLLNMI----- 284
Cdd:PHA02738 132 CFPYWSDVEQGSIRFGKFKITTTQVETH--PHYVKSTLLLTD-GTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVlevrq 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091  285 ---DLMENI----HEEVSPqdsSPILVHCSAGVGRTGTIIAINFIREQMKAETlhSIDIFGLVMTLRKQRASMVQTQDQF 357
Cdd:PHA02738 209 cqkELAQESlqigHNRLQP---PPIVVHCNAGLGRTPCYCVVDISISRFDACA--TVSIPSIVSSIRNQRYYSLFIPFQY 283

                        250
                 ....*....|
gi 86575091  358 QFVHRCIASY 367
Cdd:PHA02738 284 FFCYRAVKRY 293
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 155-361 3.26e-25

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: 102.79  E-value: 3.26e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 155 YMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCklvELNKIK-CERYWPEQvgESELFGDYEITLEE 233
Cdd:cd14634   1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLN---EMDAAQlCMQYWPEK--TSCCYGPIQVEFVS 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 234 EKLfdDDEYLMRCLKMENQTTGE--CRKVHQLHYREWPDH-GCPSGEKQLLNMIDLMENIHEEVSPQDSSPIlVHCSAGV 310
Cdd:cd14634  76 ADI--DEDIISRIFRICNMARPQdgYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQYDGREGRTV-VHCLNGG 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 86575091 311 GRTGTIIAINFIREQMKAETLhsIDIFGLVMTLRKQRASMVQTQDQFQFVH 361
Cdd:cd14634 153 GRSGTFCAICSVCEMIQQQNI--IDVFHTVKTLRNNKSNMVETLEQYKFVY 201
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 143-358 1.11e-20

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: 90.54  E-value: 1.11e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 143 VEIQKDSENPEGY-MNASLIQLpGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKlvelNK-IKCERYwPEQVGE 220
Cdd:cd14559   4 TNIQTRVSTPVGKnLNANRVQI-GNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLAS----NKdIQRKGL-PPYFRQ 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 221 SELFGdyEITLEEEKLFDDDEYLMRCLKMEN-QTTGECRKVH--QLHYREWPDHGcPSGEKQLLNMIDLMENIHEEVSP- 296
Cdd:cd14559  78 SGTYG--SVTVKSKKTGKDELVDGLKADMYNlKITDGNKTITipVVHVTNWPDHT-AISSEGLKELADLVNKSAEEKRNf 154

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86575091 297 ---QDSSPI--------LVHCSAGVGRTGTIIAINFIREQMKAETLHSIdifglVMTLRKQR-ASMVQTQDQFQ 358
Cdd:cd14559 155 yksKGSSAIndknkllpVIHCRAGVGRTGQLAAAMELNKSPNNLSVEDI-----VSDMRTSRnGKMVQKDEQLD 223
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 155-361 6.90e-20

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


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 87.82  E-value: 6.90e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 155 YMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKlVELNKIkCERYWPEQvgESELFGDYEITLEEE 234
Cdd:cd14635   1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLND-VDPAQL-CPQYWPEN--GVHRHGPIQVEFVSA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 235 KLfdDDEYLMRCLKMENQTTGE--CRKVHQLHYREWPDH-GCPSGEKQLLNMIDLMENIHEEVSPQDSSPIlVHCSAGVG 311
Cdd:cd14635  77 DL--EEDIISRIFRIYNAARPQdgYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYNGGEGRTV-VHCLNGGG 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 86575091 312 RTGTIIAINFIREQMKAEtlHSIDIFGLVMTLRKQRASMVQTQDQFQFVH 361
Cdd:cd14635 154 RSGTFCAISIVCEMLRHQ--RAVDVFHAVKTLRNNKPNMVDLLDQYKFCY 201
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 155-361 8.41e-20

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: 87.39  E-value: 8.41e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 155 YMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKlVELNKiKCERYWPEqvgESEL-FGDYEITLEE 233
Cdd:cd14636   1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNE-VDLAQ-GCPQYWPE---EGMLrYGPIQVECMS 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 234 EKLfdDDEYLMRCLKMENQTTGE--CRKVHQLHYREWPDH-GCPSGEKQLLNMIDLMENIHEEVSPQDSSPIlVHCSAGV 310
Cdd:cd14636  76 CSM--DCDVISRIFRICNLTRPQegYLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECDEGEGRTI-IHCLNGG 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 86575091 311 GRTGTIIAINFIREQMKAETLhsIDIFGLVMTLRKQRASMVQTQDQFQFVH 361
Cdd:cd14636 153 GRSGMFCAISIVCEMIKRQNV--VDVFHAVKTLRNSKPNMVETPEQYRFCY 201
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 155-361 3.27e-18

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


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 83.03  E-value: 3.27e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 155 YMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKI-KCERYWPEQvGESElFGDYEItlEE 233
Cdd:cd14637   1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEP-GLQQ-YGPMEV--EF 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 234 EKLFDDDEYLMRCLKMENQT--TGECRKVHQLHYREW-PDHGCPSGEKQLLNMIDLMENIHEEVSPQDSspiLVHCSAGV 310
Cdd:cd14637  77 VSGSADEDIVTRLFRVQNITrlQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRESGEGRT---VVHCLNGG 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 86575091 311 GRTGTIIAINFIREQMKAETLhsIDIFGLVMTLRKQRASMVQTQDQFQFVH 361
Cdd:cd14637 154 GRSGTYCASAMILEMIRCHNI--VDVFYAVKTLRNYKPNMVETLEQYRFCY 202
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 155-359 2.55e-17

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: 80.06  E-value: 2.55e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 155 YMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVElnKIKCERYWPEQVGESElFGDYEITL--- 231
Cdd:cd14550   1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNEL--NEDEPIYWPTKEKPLE-CETFKVTLsge 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 232 EEEKLFDDDEYLMRCLKMENQTTGECRKVHQLHYREWPdHGCPSGEKQLlnmiDLMENIHEEVSPQDsSPILVHCSAGVG 311
Cdd:cd14550  78 DHSCLSNEIRLIVRDFILESTQDDYVLEVRQFQCPSWP-NPCSPIHTVF----ELINTVQEWAQQRD-GPIVVHDRYGGV 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 86575091 312 RTGTIIAINFIREQMKAETlhSIDIFGLVMTLRKQRASMVQTQDQFQF 359
Cdd:cd14550 152 QAATFCALTTLHQQLEHES--SVDVYQVAKLYHLMRPGVFTSKEDYQF 197
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 155-366 8.43e-15

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


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 73.17  E-value: 8.43e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 155 YMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKIKCErYWP--EQVGESELFGDYEITLE 232
Cdd:cd17670   1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFV-YWPsrEESMNCEAFTVTLISKD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 233 EEKLFDDDEYLMRCLKMENQTTGECRKVHQLHYREWPDHGCP-SGEKQLLNMIDlmenihEEVSPQDsSPILVHCSAGVG 311
Cdd:cd17670  80 RLCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINVIK------EEALTRD-GPTIVHDEFGAV 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 86575091 312 RTGTIIAINFIREQMKAETlhSIDIFGLVMTLRKQRASMVQTQDQFQFVHRCIAS 366
Cdd:cd17670 153 SAGTLCALTTLSQQLENEN--AVDVYQVAKMINLMRPGVFTDIEQYQFLYKAMLS 205
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 155-364 1.34e-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: 72.33  E-value: 1.34e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 155 YMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKIKCErYWP--EQVGESELFGDYEITLE 232
Cdd:cd17669   1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPnkDEPINCETFKVTLIAEE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 233 EEKLFDDDEYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPsgekqLLNMIDLMENIHEEVSPQDsSPILVHCSAGVGR 312
Cdd:cd17669  80 HKCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSP-----ISKTFELISIIKEEAANRD-GPMIVHDEHGGVT 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 86575091 313 TGTIIAINFIREQMKAEtlHSIDIFGLVMTLRKQRASMVQTQDQFQFVHRCI 364
Cdd:cd17669 154 AGTFCALTTLMHQLEKE--NSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 261-338 1.04e-08

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


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 54.12  E-value: 1.04e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 86575091 261 HQLHYREWPDHGCPSgekqLLNMIDLMENIHEEVSPQDSSPILVHCSAGVGRTGTIIAiNFIREQMKAETLH-SIDIFG 338
Cdd:cd14497  61 GRVLHYGFPDHHPPP----LGLLLEIVDDIDSWLSEDPNNVAVVHCKAGKGRTGTVIC-AYLLYYGQYSTADeALEYFA 134
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
268-362 1.50e-08

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 53.44  E-value: 1.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 268 WPDHGCPSGEkqllNMIDLMENIHEEVspQDSSPILVHCSAGVGRTGTIIAINFIREQMKAEtlhsiDIFGLVmtlRKQR 347
Cdd:COG2453  55 IPDFGAPDDE----QLQEAVDFIDEAL--REGKKVLVHCRGGIGRTGTVAAAYLVLLGLSAE-----EALARV---RAAR 120

                        90
                ....*....|....*
gi 86575091 348 ASMVQTQDQFQFVHR 362
Cdd:COG2453 121 PGAVETPAQRAFLER 135
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 301-362 3.50e-08

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: 51.58  E-value: 3.50e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86575091 301 PILVHCSAGVGRTGTIIAINFIREQMKaetlhsiDIFGLVMTLRKQRAS-MVQTQDQFQFVHR 362
Cdd:cd14494  58 PVLVHCKAGVGRTGTLVACYLVLLGGM-------SAEEAVRIVRLIRPGgIPQTIEQLDFLIK 113
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 269-360 4.82e-08

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: 51.89  E-value: 4.82e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 269 PDHGCPSGEkQLLNMIDLMENiheevSPQDSSPILVHCSAGVGRTGTIIAINFIREQMKAetlhSIDifgLVMTLRKQRA 348
Cdd:cd14504  58 EDYTPPTLE-QIDEFLDIVEE-----ANAKNEAVLVHCLAGKGRTGTMLACYLVKTGKIS----AVD---AINEIRRIRP 124

                        90
                ....*....|..
gi 86575091 349 SMVQTQDQFQFV 360
Cdd:cd14504 125 GSIETSEQEKFV 136
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 268-361 3.23e-07

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: 50.81  E-value: 3.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 268 WPDHGCPSGEKqLLNMIDLMENiheevSPQDSSPILVHCSAGVGRTGTIIAINFI-REQMKAETlhsidifgLVMTLRKQ 346
Cdd:cd14506  84 WKDYGVPSLTT-ILDIVKVMAF-----ALQEGGKVAVHCHAGLGRTGVLIACYLVyALRMSADQ--------AIRLVRSK 149

                        90
                ....*....|....*
gi 86575091 347 RASMVQTQDQFQFVH 361
Cdd:cd14506 150 RPNSIQTRGQVLCVR 164
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 163-362 3.43e-07

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 49.95  E-value: 3.43e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 163 LPGgkTEFIAAQAPLPATLDEWWKmideHRVSLVVILCKLVELNKIKCERYwPEQVGESELfgdyeitleeeklfdddey 242
Cdd:cd14505  20 CPG--CKFKDHRRDLQADLEELKD----QGVDDVVTLCTDGELEELGVPDL-LEQYQQAGI------------------- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 243 lmrclkmenqttgecrKVHQLHYrewPDHGCPSGEKQLLNmidLMENIHEEVSPQDSspILVHCSAGVGRTGTIIAINFI 322
Cdd:cd14505  74 ----------------TWHHLPI---PDGGVPSDIAQWQE---LLEELLSALENGKK--VLIHCKGGLGRTGLIAACLLL 129

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 86575091 323 REQMKAETLHSIDIfglvmtLRKQRASMVQTQDQFQFVHR 362
Cdd:cd14505 130 ELGDTLDPEQAIAA------VRALRPGAIQTPKQENFLHQ 163
PRK15375 PRK15375
type III secretion system effector GTPase-activating protein SptP;
166-329 2.09e-06

type III secretion system effector GTPase-activating protein SptP;


Pssm-ID: 185273 [Multi-domain]  Cd Length: 535  Bit Score: 50.19  E-value: 2.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091  166 GKTEFIAAQAP--LPATLDEWWKMIDEHRVSLVVILCKLVELNKIKCERYWPEQVGESELFGDYEITLEEEKLFDDDEYL 243
Cdd:PRK15375 332 GKPVALAGSYPknTPDALEAHMKMLLEKECSCLVVLTSEDQMQAKQLPPYFRGSYTFGEVHTNSQKVSSASQGEAIDQYN 411

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091  244 MRCLKMENQTTgecrkVHQLHYREWPDHGCPSGEKQLLNMIDLMENIHEEVSPQDSSP----ILVHCSAGVGRTGTIIAI 319
Cdd:PRK15375 412 MQLSCGEKRYT-----IPVLHVKNWPDHQPLPSTDQLEYLADRVKNSNQNGAPGRSSSdkhlPMIHCLGGVGRTGTMAAA 486

                        170
                 ....*....|....*..
gi 86575091  320 NFIR-------EQMKAE 329
Cdd:PRK15375 487 LVLKdnphsnlEQVRAD 503
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 259-371 5.79e-06

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 46.55  E-value: 5.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091  259 KVHqlhyrEWP--DHGCPSgeKQLLNmiDLMENIHEEVSPQDSSP--ILVHCSAGVGRTGTIIAINFIreqmKAETLHSI 334
Cdd:PTZ00242  63 EVH-----DWPfdDGAPPP--KAVID--NWLRLLDQEFAKQSTPPetIAVHCVAGLGRAPILVALALV----EYGGMEPL 129

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 86575091  335 DIFGLVMtlRKQRASMVQTQDQFqfvhrcIASYCRRH 371
Cdd:PTZ00242 130 DAVGFVR--EKRKGAINQTQLQF------LKKYKPRK 158
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 259-318 5.07e-05

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


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 43.60  E-value: 5.07e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 259 KVHQLHYrewPDHGCPSgEKQLLNMIDLMENIheevspqdSSPILVHCSAGVGRTGTIIA 318
Cdd:cd14499  81 RHYDLYF---PDGSTPS-DDIVKKFLDICENE--------KGAIAVHCKAGLGRTGTLIA 128
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 269-361 2.33e-04

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


Pssm-ID: 350360 [Multi-domain]  Cd Length: 177  Bit Score: 41.96  E-value: 2.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 269 PDHGCPSgekqLLNMIDLMENIHEEVSPQDSSPILVHCSAGVGRTGTIIAINFIREQMKAETLHSIDIFGlvmtLRKQRA 348
Cdd:cd14510  82 DDHNVPT----LDEMLSFTAEVREWMAADPKNVVAIHCKGGKGRTGTMVCAWLIYSGQFESAKEALEYFG----ERRTDK 153

                        90
                ....*....|....*....
gi 86575091 349 SM------VQTQDQFQFVH 361
Cdd:cd14510 154 SVsskfqgVETPSQSRYVG 172
PTP-IVa cd14500
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...
 259-347 3.03e-04

protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), also known as protein-tyrosine phosphatases of regenerating liver (PRLs) constitute a family of small, prenylated phosphatases that are the most oncogenic of all PTPs. They stimulate progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. They associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation. Vertebrates contain three members: PRL-1, PRL-2, and PRL-3.


Pssm-ID: 350350 [Multi-domain]  Cd Length: 156  Bit Score: 41.05  E-value: 3.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 259 KVHQLhyrEWPDHGCPSgEKQLLNMIDLMENIHEEVSPQDSSpILVHCSAGVGRTGTIIAINFIREQMKAETlhsidifg 338
Cdd:cd14500  60 KVHDW---PFDDGSPPP-DDVVDDWLDLLKTRFKEEGKPGAC-IAVHCVAGLGRAPVLVAIALIELGMKPED-------- 126


                ....*....
gi 86575091 339 LVMTLRKQR 347
Cdd:cd14500 127 AVEFIRKKR 135
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 269-342 5.79e-04

protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; Phosphatase and tensin homolog (PTEN), also phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN or mutated in multiple advanced cancers 1 (MMAC1), is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It is a critical endogenous inhibitor of phosphoinositide signaling. It dephosphorylates phosphoinositide trisphosphate, and therefore, has the function of negatively regulating Akt. The PTEN/PI3K/AKT pathway regulates the signaling of multiple biological processes such as apoptosis, metabolism, cell proliferation, and cell growth. PTEN contains an N-terminal PIP-binding domain, a protein tyrosine phosphatase (PTP)-like catalytic domain, a regulatory C2 domain responsible for its cellular location, a C-tail containing phosphorylation sites, and a C-terminal PDZ domain.


Pssm-ID: 350359 [Multi-domain]  Cd Length: 158  Bit Score: 40.26  E-value: 5.79e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86575091 269 PDHGCPSgekqlLNMI-DLMENIHEEVSPQDSSPILVHCSAGVGRTGTIIAINFIREQMKAETLHSIDIFGLVMT 342
Cdd:cd14509  68 DDHNPPP-----LELIkPFCEDVDEWLKEDEKNVAAVHCKAGKGRTGVMICCYLLYLGKFPSAKEALDFYGAKRT 137
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 301-326 2.02e-03

bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa TpbA; This subfamily contains bacterial protein tyrosine phosphatases (PTPs) and dual-specificity phosphatases (DUSPs) related to Pseudomonas aeruginosa TpbA, a DUSP that negatively regulates biofilm formation by converting extracellular quorum sensing signals and to Mycobacterium tuberculosis PtpB, a PTP virulence factor that attenuates host immune defenses by interfering with signal transduction pathways in macrophages. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides, while DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and PTPs.


Pssm-ID: 350378 [Multi-domain]  Cd Length: 158  Bit Score: 38.89  E-value: 2.02e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 86575091 301 PILVHCSAGVGRTGTIIAI---------NFIREQM 326
Cdd:cd14529  91 PVLIHCKHGKDRTGLVSALyrivyggskEEANEDY 125
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 297-359 2.48e-03

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: 38.01  E-value: 2.48e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86575091   297 QDSSPILVHCSAGVGRTGTIIaINFIreqMKAETLHSIDIFGLVmtlrKQRASMVQTQDQFQF 359
Cdd:pfam00782  67 QKGGKVLVHCQAGISRSATLI-IAYL---MKTRNLSLNEAYSFV----KERRPGISPNFGFKR 121
Oca4 COG2365
Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];
238-319 7.60e-03

Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];


Pssm-ID: 441932 [Multi-domain]  Cd Length: 248  Bit Score: 38.02  E-value: 7.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86575091 238 DDDEYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPSGEKQLLNMidLMENiheevspqDSSPILVHCSAGVGRTGTII 317
Cdd:COG2365  82 DDAEALLEELRDGDLTPGDAEEFMLELYRAFVDPDAADAYRAAFRA--LADA--------ENGPVLFHCTAGKDRTGVAA 151


                ..
gi 86575091 318 AI 319
Cdd:COG2365 152 AL 153
 
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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