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Conserved domains on  [gi|25149237|ref|NP_494864|]
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Tyrosine-protein phosphatase domain-containing protein [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;
164-406 5.10e-65

Protein tyrosine phosphatase, catalytic domain;


:

Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 210.21  E-value: 5.10e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237    164 PTSRSDAFHGNTFKNQRKDVPCIDDTRVKLADP--NIVYYIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVET 241
Cdd:smart00194  17 ESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPpgEGSDYINASYIDGPNGPKAYIATQGPLPSTVEDFWRMVWEQKVTV 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237    242 IVsLTSSSSASNPNVYPMYYPNKPETFNNFGQFFVYCKTVTQPKtkyGCKEYKFELVVQaDNEERRSVRLYHYPHWTKNM 321
Cdd:smart00194  97 IV-MLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVD---DYTIRTLEVTNT-GCSETRTVTHYHYTNWPDHG 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237    322 VPASSKVVLNLVKKIGKKKSQ--APVVVQCETGVNQSAELVFVDAMCTLLTRQVEVNFDVLFRQMRSQKALaMTQLLHFL 399
Cdd:smart00194 172 VPESPESILDLIRAVRKSQSTstGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQRPG-MVQTEEQY 250


                   ....*..
gi 25149237    400 HSIATVM 406
Cdd:smart00194 251 IFLYRAI 257
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
164-406 5.10e-65

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 210.21  E-value: 5.10e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237    164 PTSRSDAFHGNTFKNQRKDVPCIDDTRVKLADP--NIVYYIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVET 241
Cdd:smart00194  17 ESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPpgEGSDYINASYIDGPNGPKAYIATQGPLPSTVEDFWRMVWEQKVTV 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237    242 IVsLTSSSSASNPNVYPMYYPNKPETFNNFGQFFVYCKTVTQPKtkyGCKEYKFELVVQaDNEERRSVRLYHYPHWTKNM 321
Cdd:smart00194  97 IV-MLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVD---DYTIRTLEVTNT-GCSETRTVTHYHYTNWPDHG 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237    322 VPASSKVVLNLVKKIGKKKSQ--APVVVQCETGVNQSAELVFVDAMCTLLTRQVEVNFDVLFRQMRSQKALaMTQLLHFL 399
Cdd:smart00194 172 VPESPESILDLIRAVRKSQSTstGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQRPG-MVQTEEQY 250


                   ....*..
gi 25149237    400 HSIATVM 406
Cdd:smart00194 251 IFLYRAI 257
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
174-407 3.14e-61

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 199.39  E-value: 3.14e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237   174 NTFKNQRKDVPCIDDTRVKLADPNIVY-YIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVsLTSSSSAS 252
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPGPSdYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIV-MLTELEEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237   253 NPNVYPMYYPNKPETFNNFGQFFVYCKtvtqpKTKYGCKEYKF-ELVVQADN-EERRSVRLYHYPHWTKNMVPASSKVVL 330
Cdd:pfam00102  80 GREKCAQYWPEEEGESLEYGDFTVTLK-----KEKEDEKDYTVrTLEVSNGGsEETRTVKHFHYTGWPDHGVPESPNSLL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237   331 NLVKKIGKKKS---QAPVVVQCETGVNQSAELVFVDAMCTLLTRQVEVNFDVLFRQMRSQKALAMTQLLHFLHSIATVMK 407
Cdd:pfam00102 155 DLLRKVRKSSLdgrSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 201-400 1.42e-39

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: 141.27  E-value: 1.42e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 201 YIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASNPNVYPmYYPNKPETFNNFGQFFVYCKT 280
Cdd:cd00047   1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCER-YWPEEGGKPLEYGDITVTLVS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 281 VTQpktKYGCKEYKFELVVQaDNEERRSVRLYHYPHWTKNMVPASSKVVLNLVKKIGK--KKSQAPVVVQCETGVNQSAE 358
Cdd:cd00047  80 EEE---LSDYTIRTLELSPK-GCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKeaRKPNGPIVVHCSAGVGRTGT 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 25149237 359 LVFVDAMCTLLTRQVEVNFDVLFRQMRSQKALA---MTQLLhFLH 400
Cdd:cd00047 156 FIAIDILLERLEAEGEVDVFEIVKALRKQRPGMvqtLEQYE-FIY 199
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 174-388 1.94e-15

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 76.99  E-value: 1.94e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237  174 NTFKNQRKDVPCIDDTRVKLA-------------DP---------NIVYYIHANHIM-FDHLKKtYITTQHPLPGTLNDF 230
Cdd:PHA02746  51 NLKKNRFHDIPCWDHSRVVINaheslkmfdvgdsDGkkievtsedNAENYIHANFVDgFKEANK-FICAQGPKEDTSEDF 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237  231 WAMVADQKVETIVSLTSSSSASNPNVYPMYYPNKPETfnNFGQFFVycktvtqpKTKYGCKEYKFE----LVVQADNEER 306
Cdd:PHA02746 130 FKLISEHESQVIVSLTDIDDDDEKCFELWTKEEDSEL--AFGRFVA--------KILDIIEELSFTktrlMITDKISDTS 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237  307 RSVRLYHYPHWTKNMVPASSKVVLNLVKKIGKKKSQ------------APVVVQCETGVNQSAELVFVDAMCTLLTRQVE 374
Cdd:PHA02746 200 REIHHFWFPDWPDNGIPTGMAEFLELINKVNEEQAElikqadndpqtlGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKE 279

                        250
                 ....*....|....
gi 25149237  375 VNFDVLFRQMRSQK 388
Cdd:PHA02746 280 VCLGEIVLKIRKQR 293
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
164-406 5.10e-65

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 210.21  E-value: 5.10e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237    164 PTSRSDAFHGNTFKNQRKDVPCIDDTRVKLADP--NIVYYIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVET 241
Cdd:smart00194  17 ESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPpgEGSDYINASYIDGPNGPKAYIATQGPLPSTVEDFWRMVWEQKVTV 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237    242 IVsLTSSSSASNPNVYPMYYPNKPETFNNFGQFFVYCKTVTQPKtkyGCKEYKFELVVQaDNEERRSVRLYHYPHWTKNM 321
Cdd:smart00194  97 IV-MLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVD---DYTIRTLEVTNT-GCSETRTVTHYHYTNWPDHG 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237    322 VPASSKVVLNLVKKIGKKKSQ--APVVVQCETGVNQSAELVFVDAMCTLLTRQVEVNFDVLFRQMRSQKALaMTQLLHFL 399
Cdd:smart00194 172 VPESPESILDLIRAVRKSQSTstGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQRPG-MVQTEEQY 250


                   ....*..
gi 25149237    400 HSIATVM 406
Cdd:smart00194 251 IFLYRAI 257
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
174-407 3.14e-61

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 199.39  E-value: 3.14e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237   174 NTFKNQRKDVPCIDDTRVKLADPNIVY-YIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVsLTSSSSAS 252
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPGPSdYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIV-MLTELEEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237   253 NPNVYPMYYPNKPETFNNFGQFFVYCKtvtqpKTKYGCKEYKF-ELVVQADN-EERRSVRLYHYPHWTKNMVPASSKVVL 330
Cdd:pfam00102  80 GREKCAQYWPEEEGESLEYGDFTVTLK-----KEKEDEKDYTVrTLEVSNGGsEETRTVKHFHYTGWPDHGVPESPNSLL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237   331 NLVKKIGKKKS---QAPVVVQCETGVNQSAELVFVDAMCTLLTRQVEVNFDVLFRQMRSQKALAMTQLLHFLHSIATVMK 407
Cdd:pfam00102 155 DLLRKVRKSSLdgrSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 201-400 1.42e-39

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: 141.27  E-value: 1.42e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 201 YIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASNPNVYPmYYPNKPETFNNFGQFFVYCKT 280
Cdd:cd00047   1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCER-YWPEEGGKPLEYGDITVTLVS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 281 VTQpktKYGCKEYKFELVVQaDNEERRSVRLYHYPHWTKNMVPASSKVVLNLVKKIGK--KKSQAPVVVQCETGVNQSAE 358
Cdd:cd00047  80 EEE---LSDYTIRTLELSPK-GCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKeaRKPNGPIVVHCSAGVGRTGT 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 25149237 359 LVFVDAMCTLLTRQVEVNFDVLFRQMRSQKALA---MTQLLhFLH 400
Cdd:cd00047 156 FIAIDILLERLEAEGEVDVFEIVKALRKQRPGMvqtLEQYE-FIY 199
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 174-394 5.91e-23

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: 97.82  E-value: 5.91e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 174 NTFKNQRKDVPCIDDTRVKLADPN---IVYYIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTssss 250
Cdd:cd14543  29 NQEKNRYGDVLCLDQSRVKLPKRNgdeRTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMTT---- 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 251 asnpNVYP-------MYYPNKPETFNNFGQFFVYCKTVTqpktkygCKEYKFELVVQADNE---ERRSVRLYHYPHWTKN 320
Cdd:cd14543 105 ----RVVErgrvkcgQYWPLEEGSSLRYGDLTVTNLSVE-------NKEHYKKTTLEIHNTetdESRQVTHFQFTSWPDF 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 321 MVPASSKVVLNLVKKIGKKKSQA---------------PVVVQCETGVNQSAELVFVDAMCTLL--TRQVEVNFDVlfRQ 383
Cdd:cd14543 174 GVPSSAAALLDFLGEVRQQQALAvkamgdrwkghppgpPIVVHCSAGIGRTGTFCTLDICLSQLedVGTLNVMQTV--RR 251

                       250
                ....*....|.
gi 25149237 384 MRSQKAlAMTQ 394
Cdd:cd14543 252 MRTQRA-FSIQ 261
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 174-392 1.16e-22

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: 97.70  E-value: 1.16e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 174 NTFKNQRKDVPCIDDTRVKLA---DPNIVYYIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSS 250
Cdd:cd14604  57 NVKKNRYKDILPFDHSRVKLTlktSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFE 136

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 251 ASNPNVyPMYYPNKPETFNNFGQFFVYCKTvTQPKTKYGCKeykfELVVQADNEERRsVRLYHYPHWTKNMVPASSKVVL 330
Cdd:cd14604 137 MGRKKC-ERYWPLYGEEPMTFGPFRISCEA-EQARTDYFIR----TLLLEFQNETRR-LYQFHYVNWPDHDVPSSFDSIL 209

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25149237 331 NLVKKIGKKKSQ--APVVVQCETGVNQSAELVFVDAMCTLLTR-QVEVNFDV--LFRQMRSQKALAM 392
Cdd:cd14604 210 DMISLMRKYQEHedVPICIHCSAGCGRTGAICAIDYTWNLLKAgKIPEEFNVfnLIQEMRTQRHSAV 276
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 173-401 1.32e-21

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: 93.75  E-value: 1.32e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 173 GNTFKNQRKDVPCIDDTRVKLADP----NIVYYIHANHIM-FDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTS 247
Cdd:cd14612  14 GHASKDRYKTILPNPQSRVCLRRAgsqeEEGSYINANYIRgYDGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITK 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 248 SSSASNPNVypMYYPNKPETfnnFGQFFVYCKTVTQpktkygCKEYKF-ELVVQADnEERRSVRLYHYPHWTKNMVPASS 326
Cdd:cd14612  94 LKEKKEKCV--HYWPEKEGT---YGRFEIRVQDMKE------CDGYTIrDLTIQLE-EESRSVKHYWFSSWPDHQTPESA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 327 KVVLNLVKKIGKKK----SQAPVVVQCETGVNQSAELVFVDAMCTLLTRQVEVNFDVLFRQMRSQKAlAMTQL---LHFL 399
Cdd:cd14612 162 GPLLRLVAEVEESRqtaaSPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRG-GMIQTseqYQFL 240


                ..
gi 25149237 400 HS 401
Cdd:cd14612 241 HH 242
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 174-394 1.99e-21

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: 93.16  E-value: 1.99e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 174 NTFKNQRKDVPCIDDTRVKL--ADPN--IVYYIHANHIMFDH--------LKKTYITTQHPLPGTLNDFWAMVADQKVET 241
Cdd:cd14605   2 NKNKNRYKNILPFDHTRVVLhdGDPNepVSDYINANIIMPEFetkcnnskPKKSYIATQGCLQNTVNDFWRMVFQENSRV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 242 IVSLTSSSSASNPNVYPmYYPNKpETFNNFGQFFVycKTVTQ-PKTKYGCKEYKFELVVQADNEerRSVRLYHYPHWTKN 320
Cdd:cd14605  82 IVMTTKEVERGKSKCVK-YWPDE-YALKEYGVMRV--RNVKEsAAHDYILRELKLSKVGQGNTE--RTVWQYHFRTWPDH 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 321 MVPASSKVVLNLVKKIGKKKSQ----APVVVQCETGVNQSAELVFVDAMCTLLTRQ-VEVNFDV--LFRQMRSQKAlAMT 393
Cdd:cd14605 156 GVPSDPGGVLDFLEEVHHKQESimdaGPVVVHCSAGIGRTGTFIVIDILIDIIREKgVDCDIDVpkTIQMVRSQRS-GMV 234


                .
gi 25149237 394 Q 394
Cdd:cd14605 235 Q 235
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 174-394 4.91e-21

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: 92.14  E-value: 4.91e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 174 NTFKNQRKDVPCIDDTRVKL--ADPNIVY--YIHANHIMFDHL-------KKTYITTQHPLPGTLNDFWAMVADQKVETI 242
Cdd:cd14544   1 NKGKNRYKNILPFDHTRVILkdRDPNVPGsdYINANYIRNENEgpttdenAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 243 VSLTSSSSASNPNVYPmYYPNKpetfNNFGQFFVYC-KTVTQPKTK-YGCKEykFELVVQADNEERRSVRLYHYPHWTKN 320
Cdd:cd14544  81 VMTTKEVERGKNKCVR-YWPDE----GMQKQYGPYRvQNVSEHDTTdYTLRE--LQVSKLDQGDPIREIWHYQYLSWPDH 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 321 MVPASSKVVLNLVKKIGKKKS----QAPVVVQCETGVNQSAELVFVDAMCTLLTRQ-VEVNFDV--LFRQMRSQKAlAMT 393
Cdd:cd14544 154 GVPSDPGGVLNFLEDVNQRQEslphAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKgLDCDIDIqkTIQMVRSQRS-GMV 232


                .
gi 25149237 394 Q 394
Cdd:cd14544 233 Q 233
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 201-394 6.64e-20

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: 87.48  E-value: 6.64e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 201 YIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTssssasnpNVYPM-------YYPNKPETFNNFGQ 273
Cdd:cd14542   1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMAC--------REFEMgkkkcerYWPEEGEEQLQFGP 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 274 FfvyckTVTQPKTKYGCKEYKFE-LVVQADNEERRsVRLYHYPHWTKNMVPASSKVVLNLVKKIgkKKSQA----PVVVQ 348
Cdd:cd14542  73 F-----KISLEKEKRVGPDFLIRtLKVTFQKESRT-VYQFHYTAWPDHGVPSSVDPILDLVRLV--RDYQGsedvPICVH 144

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 25149237 349 CETGVNQSAELVFVDAMCTLLTRQ-VEVNFDV--LFRQMRSQKaLAMTQ 394
Cdd:cd14542 145 CSAGCGRTGTICAIDYVWNLLKTGkIPEEFSLfdLVREMRKQR-PAMVQ 192
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 174-394 1.83e-19

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: 87.98  E-value: 1.83e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 174 NTFKNQRKDVPCIDDTRVKLADPNivYYIHANHIMFD----HLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSS 249
Cdd:cd14600  40 NMDKNRYKDVLPYDATRVVLQGNE--DYINASYVNMEipsaNIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLT 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 250 SASNPNVYpMYYPNKPETFnNFGQFFVYCKTvTQPKTKYGCKEYkfeLVVQADNEERRSVRLYHYPHWTKNMVPASSKVV 329
Cdd:cd14600 118 ERGRTKCH-QYWPDPPDVM-EYGGFRVQCHS-EDCTIAYVFREM---LLTNTQTGEERTVTHLQYVAWPDHGVPDDSSDF 191

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25149237 330 LNLVKKIGKKKSQA-PVVVQCETGVNQSAELVFVD-AMCTLLTRQVEVNFDVLfRQMRSQKALaMTQ 394
Cdd:cd14600 192 LEFVNYVRSKRVENePVLVHCSAGIGRTGVLVTMEtAMCLTERNQPVYPLDIV-RKMRDQRAM-MVQ 256
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 201-388 5.47e-19

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: 85.03  E-value: 5.47e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 201 YIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASNPNVyPMYYPNkpETFNNFGQFFVYCKT 280
Cdd:cd17668   1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKC-DQYWPA--DGSEEYGNFLVTQKS 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 281 VtQPKTKYGCKEY-----KFELVVQADNEERRSVRLYHYPHWTKNMVPASSKVVLNLVKKIGKKKSQA--PVVVQCETGV 353
Cdd:cd17668  78 V-QVLAYYTVRNFtlrntKIKKGSQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAvgPVVVHCSAGV 156

                       170       180       190
                ....*....|....*....|....*....|....*
gi 25149237 354 NQSAELVFVDAMCTLLTRQVEVNFDVLFRQMRSQK 388
Cdd:cd17668 157 GRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQR 191
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 178-363 8.03e-19

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: 85.25  E-value: 8.03e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 178 NQRKDVPCIDDTRVKLADPNIVY--YIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASNPN 255
Cdd:cd14615   1 NRYNNVLPYDISRVKLSVQSHSTddYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRTK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 256 VyPMYYPNK-PETFNNFgqffvyckTVTQ----PKTKYGCKEYKFElvvQADNEERRSVRLYHYPHWTKNMVPASSKVVL 330
Cdd:cd14615  81 C-EEYWPSKqKKDYGDI--------TVTMtseiVLPEWTIRDFTVK---NAQTNESRTVRHFHFTSWPDHGVPETTDLLI 148

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 25149237 331 N---LVKKIGKKKS-QAPVVVQCETGVNQSAELVFVD 363
Cdd:cd14615 149 NfrhLVREYMKQNPpNSPILVHCSAGVGRTGTFIAID 185
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 201-400 8.28e-19

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: 84.61  E-value: 8.28e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 201 YIHANHIMFDHL-KKTYITTQHPLPGTLNDFWAMVADQKVETIVsltssssASNPNV-------YPmYYPNKPETFNNFG 272
Cdd:cd18533   1 YINASYITLPGTsSKRYIATQGPLPATIGDFWKMIWQNNVGVIV-------MLTPLVengrekcDQ-YWPSGEYEGEYGD 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 273 QffvyckTVT-QPKTKYGCKEYKF-ELVVQADNEERRSVRLYHYPHWTKNMVPASSKVVLNLVKKIGKKKSQA----PVV 346
Cdd:cd18533  73 L------TVElVSEEENDDGGFIVrEFELSKEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSAsldpPII 146

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25149237 347 VQCETGVNQSAELVFVDAMCTLLTRQ------VEVNFDVLFR---QMRSQKaLAMTQLLH---FLH 400
Cdd:cd18533 147 VHCSAGVGRTGTFIALDSLLDELKRGlsdsqdLEDSEDPVYEivnQLRKQR-MSMVQTLRqyiFLY 211
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 201-394 8.63e-19

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: 84.69  E-value: 8.63e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 201 YIHANHI-MF---DHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASNPNVYpMYYPNKPETfNNFGQFFV 276
Cdd:cd14541   2 YINANYVnMEipgSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCH-QYWPDLGET-MQFGNLQI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 277 YCKTvTQPKTKYGCKEykFELVVQADNEERRSVRLyHYPHWTKNMVPASSKVVLNLVKKIGKKKSQA--PVVVQCETGVN 354
Cdd:cd14541  80 TCVS-EEVTPSFAFRE--FILTNTNTGEERHITQM-QYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMvePTVVHCSAGIG 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 25149237 355 QSAELVFVD-AMCTLLTRQVEVNFDVLfRQMRSQKALaMTQ 394
Cdd:cd14541 156 RTGVLITMEtAMCLIEANEPVYPLDIV-RTMRDQRAM-LIQ 194
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 177-390 8.88e-19

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: 85.28  E-value: 8.88e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 177 KNQRKDVPCIDDTRVKLA---DPNIVYYIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSssasn 253
Cdd:cd14602   1 KNRYKDILPYDHSRVELSlitSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACME----- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 254 pnvYPM-------YYPNKPETFNNFGQFFVYCKTVTQpKTKYGCKEYKFELvvqadNEERRSVRLYHYPHWTKNMVPASS 326
Cdd:cd14602  76 ---FEMgkkkcerYWAEPGEMQLEFGPFSVTCEAEKR-KSDYIIRTLKVKF-----NSETRTIYQFHYKNWPDHDVPSSI 146

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25149237 327 KVVLNLVKKIG--KKKSQAPVVVQCETGVNQSAELVFVDAMCTLLTRQ-VEVNFDV--LFRQMRSQKAL 390
Cdd:cd14602 147 DPILELIWDVRcyQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGiIPENFSVfsLIQEMRTQRPS 215
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 201-388 9.60e-19

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: 84.32  E-value: 9.60e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 201 YIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASNPNVyPMYYPNK-PETFNNFgqffvyck 279
Cdd:cd14549   1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKC-DQYWPKEgTETYGNI-------- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 280 TVTQPKTK---------YGCKEYKFELVVQADNEerRSVRLYHYPHWTKNMVPASSKVVLNLVKKIGKKKSQA--PVVVQ 348
Cdd:cd14549  72 QVTLLSTEvlatytvrtFSLKNLKLKKVKGRSSE--RVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGagPIVVH 149

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 25149237 349 CETGVNQSAELVFVDAMCTLLTRQVEVNFDVLFRQMRSQK 388
Cdd:cd14549 150 CSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQR 189
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 201-394 5.42e-18

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: 82.30  E-value: 5.42e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 201 YIHANHIMFDHLKKT----YITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASNPNVYpMYYPNkPETFNNFGQFFV 276
Cdd:cd14601   2 YINANYINMEIPSSSiinrYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCH-QYWPE-PSGSSSYGGFQV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 277 YCktvtqpKTKYGCKEYKFE--LVVQADNEERRSVRLYHYPHWTKNMVPASSKVVLNLVKKIGKKKS--QAPVVVQCETG 352
Cdd:cd14601  80 TC------HSEEGNPAYVFRemTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAgkDEPVVVHCSAG 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 25149237 353 VNQSAELVFVD-AMCTLLTRQVEVNFDVLfRQMRSQKALaMTQ 394
Cdd:cd14601 154 IGRTGVLITMEtAMCLIECNQPVYPLDIV-RTMRDQRAM-MIQ 194
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
308-407 9.43e-18

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 78.55  E-value: 9.43e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237    308 SVRLYHYPHWTKNMVPASSKVVLNLVKKIGKKKSQ----APVVVQCETGVNQSAELVFVDAMCTLLT-RQVEVNFDVLFR 382
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQsessGPVVVHCSAGVGRTGTFVAIDILLQQLEaEAGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 25149237    383 QMRSQKALAMTQLLHFLHSIATVMK 407
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 308-407 9.43e-18

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: 78.55  E-value: 9.43e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237    308 SVRLYHYPHWTKNMVPASSKVVLNLVKKIGKKKSQ----APVVVQCETGVNQSAELVFVDAMCTLLT-RQVEVNFDVLFR 382
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQsessGPVVVHCSAGVGRTGTFVAIDILLQQLEaEAGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 25149237    383 QMRSQKALAMTQLLHFLHSIATVMK 407
Cdd:smart00012  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 187-411 1.23e-17

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: 81.89  E-value: 1.23e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 187 DDTRVKLA---DPNIVYYIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASNPNVyPMYYPN 263
Cdd:cd14617  10 DSTRVKLSnvdDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKC-DHYWPA 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 264 KPETfnnfgqfFVYCKTVTQPKTKYGCKEY---KFELVVQADNEERRSVRLYHYPHWTKNMVPASSKVVLNLVKK----I 336
Cdd:cd14617  89 DQDS-------LYYGDLIVQMLSESVLPEWtirEFKICSEEQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTvrdyI 161

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25149237 337 GKKKSQAPVVVQCETGVNQSAELVFVDAMCTLLTRQVEVNFDVLFRQMRsqkalamtqlLHFLHSIATVMKFIKI 411
Cdd:cd14617 162 NRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLR----------LHRVHMVQTECQYVYL 226
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 187-401 1.59e-17

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: 81.25  E-value: 1.59e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 187 DDTRVKLADPNIVY---YIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVsltssssasnpnvypM---- 259
Cdd:cd14548   9 DHSRVKLIPINEEEgsdYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIV---------------Mltqc 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 260 ----------YYPNK--PETFNNFgqffvyckTVTQPK----TKYGCKEYKFELVvqadnEERRSVRLYHYPHWTKNMVP 323
Cdd:cd14548  74 mekgrvkcdhYWPFDqdPVYYGDI--------TVTMLSesvlPDWTIREFKLERG-----DEVRSVRQFHFTAWPDHGVP 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 324 ASSKVVLNLVKKI--GKKKSQAPVVVQCETGVNQSAELVFVDAMCTLLTRQVEVNFDVLFRQMRSQKALaMTQLLH---F 398
Cdd:cd14548 141 EAPDSLLRFVRLVrdYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPL-MVQTEAqyiF 219


                ...
gi 25149237 399 LHS 401
Cdd:cd14548 220 LHQ 222
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 174-394 1.77e-17

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: 82.24  E-value: 1.77e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 174 NTFKNQRKDVPCIDDTRVKL--ADPNIVY--YIHANHIM-----FDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVS 244
Cdd:cd14606  18 NKSKNRYKNILPFDHSRVILqgRDSNIPGsdYINANYVKnqllgPDENAKTYIASQGCLEATVNDFWQMAWQENSRVIVM 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 245 LTSSSSASNPNVYPmYYPNKpETFNNFGQFFVycKTVTQPKTkygcKEYK---FELVVQADNEERRSVRLYHYPHWTKNM 321
Cdd:cd14606  98 TTREVEKGRNKCVP-YWPEV-GMQRAYGPYSV--TNCGEHDT----TEYKlrtLQVSPLDNGELIREIWHYQYLSWPDHG 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 322 VPASSKVVLNLVKKIGKKK----SQAPVVVQCETGVNQSAELVFVDAMCTLL-TRQVEVNFDV--LFRQMRSQKAlAMTQ 394
Cdd:cd14606 170 VPSEPGGVLSFLDQINQRQeslpHAGPIIVHCSAGIGRTGTIIVIDMLMENIsTKGLDCDIDIqkTIQMVRAQRS-GMVQ 248
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 174-392 1.93e-17

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: 82.18  E-value: 1.93e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 174 NTFKNQRKDVPCIDDTRVKL---ADPNIVYYIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSS 250
Cdd:cd14603  30 NVKKNRYKDILPYDQTRVILsllQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACREIE 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 251 ASNPNVyPMYYPNKPETFnNFGQFfvyckTVTQPKTKYGCKEYKFELVVQADNEERRSVRLYHYPHWTKNMVPASSKVVL 330
Cdd:cd14603 110 MGKKKC-ERYWAQEQEPL-QTGPF-----TITLVKEKRLNEEVILRTLKVTFQKESRSVSHFQYMAWPDHGIPDSPDCML 182

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25149237 331 NLVKKIGKKK--SQAPVVVQCETGVNQSAELVFVDAMCTLL-TRQVEVNFDV--LFRQMRSQKALAM 392
Cdd:cd14603 183 AMIELARRLQgsGPEPLCVHCSAGCGRTGVICTVDYVRQLLlTQRIPPDFSIfdVVLEMRKQRPAAV 249
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 174-372 2.08e-17

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: 82.00  E-value: 2.08e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 174 NTFKNQRKDVPCIDDTRVKL--ADPNivyYIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSA 251
Cdd:cd14608  25 NKNRNRYRDVSPFDHSRIKLhqEDND---YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEK 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 252 SNPNVyPMYYPNKPETFNNFGQFFVYCKTVTQP-KTKYGCKEYKFElvvQADNEERRSVRLYHYPHWTKNMVPASSKVVL 330
Cdd:cd14608 102 GSLKC-AQYWPQKEEKEMIFEDTNLKLTLISEDiKSYYTVRQLELE---NLTTQETREILHFHYTTWPDFGVPESPASFL 177

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 25149237 331 NLVKKIGKKKS----QAPVVVQCETGVNQSAELVFVDAmCTLLTRQ 372
Cdd:cd14608 178 NFLFKVRESGSlspeHGPVVVHCSAGIGRSGTFCLADT-CLLLMDK 222
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 174-385 7.85e-17

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: 80.01  E-value: 7.85e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 174 NTFKNQRKDVPCIDDTRVKLADPNiVYYIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASN 253
Cdd:cd14607  24 NRNRNRYRDVSPYDHSRVKLQNTE-NDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKDS 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 254 PNVyPMYYPNKPETFNNFGQFFVYCKTVTQP-KTKYGCKEYKFElvvQADNEERRSVRLYHYPHWTKNMVPASSKVVLNL 332
Cdd:cd14607 103 VKC-AQYWPTDEEEVLSFKETGFSVKLLSEDvKSYYTVHLLQLE---NINSGETRTISHFHYTTWPDFGVPESPASFLNF 178

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 25149237 333 VKKIGKKKS----QAPVVVQCETGVNQSAELVFVDAMCTLLTRQ--VEVNFDVLFRQMR 385
Cdd:cd14607 179 LFKVRESGSlspeHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKdpDSVDIKQVLLDMR 237
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 160-388 1.01e-16

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: 80.08  E-value: 1.01e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 160 MNIapTSRSDAFHGNTFKNQRKDVPCIDDTRVKL-----ADPNIVYYIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMV 234
Cdd:cd17667  15 MNI--TAEHSNHPDNKHKNRYINILAYDHSRVKLrplpgKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMI 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 235 ADQKVETIVSLTSSSSASNPNVyPMYYPNkpETFNNFGQFFVY--------CKTVTqpktKYGCKEYKFELVVQADNEER 306
Cdd:cd17667  93 WEQNTGIIVMITNLVEKGRRKC-DQYWPT--ENSEEYGNIIVTlkstkihaCYTVR----RFSIRNTKVKKGQKGNPKGR 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 307 ---RSVRLYHYPHWTKNMVPASSKVVLNLVKK--IGKKKSQAPVVVQCETGVNQSAELVFVDAMCTLLTRQVEVNFDVLF 381
Cdd:cd17667 166 qneRTVIQYHYTQWPDMGVPEYALPVLTFVRRssAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFL 245


                ....*..
gi 25149237 382 RQMRSQK 388
Cdd:cd17667 246 KHIRTQR 252
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 189-394 1.33e-16

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: 78.59  E-value: 1.33e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 189 TRVKL----ADPnIVYYIHANHIM-FDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASNPNVypMYYPN 263
Cdd:cd14547  12 SRVCLpsvdDDP-LSSYINANYIRgYDGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKEKCA--QYWPE 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 264 K-PETFNNFgqffvyckTVTQPKTKYgCKEYKFELVVQADNEERRSVRLYHYPHWTKNMVPASSKVVLNLVKKIGKKKSQ 342
Cdd:cd14547  89 EeNETYGDF--------EVTVQSVKE-TDGYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEARQT 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 25149237 343 A----PVVVQCETGVNQSAELVFVDAMCTLLTRQVEVnfDVL--FRQMRSQKAlAMTQ 394
Cdd:cd14547 160 EphrgPIVVHCSAGIGRTGCFIATSIGCQQLREEGVV--DVLgiVCQLRLDRG-GMVQ 214
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 201-388 1.34e-16

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: 78.03  E-value: 1.34e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 201 YIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASNPNVYpMYYPNKPETFNNFGQFFVYckt 280
Cdd:cd14555   1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCS-RYWPDDTEVYGDIKVTLVE--- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 281 vTQPKTKYGCKEYKFElvvQADNEERRSVRLYHYPHWTKNMVPASSKVVLNLVKKIGKKK--SQAPVVVQCETGVNQSAE 358
Cdd:cd14555  77 -TEPLAEYVVRTFALE---RRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNppSAGPIVVHCSAGAGRTGC 152

                       170       180       190
                ....*....|....*....|....*....|
gi 25149237 359 LVFVDAMCTLLTRQVEVNFDVLFRQMRSQK 388
Cdd:cd14555 153 YIVIDIMLDMAEREGVVDIYNCVKELRSRR 182
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 201-394 1.65e-16

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: 77.80  E-value: 1.65e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 201 YIHANHIMFDHLKKT--YITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASNPNVYpMYYPNKPETfnnfgqffvyc 278
Cdd:cd14538   1 YINASHIRIPVGGDTyhYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCH-RYWPDSLNK----------- 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 279 ktvtqPKTKYGCKEYKFE-------------LVVQADNEERRSVRLYHYPHWTKNMVPASSKVVLNLVKKIGKKKSQAPV 345
Cdd:cd14538  69 -----PLICGGRLEVSLEkyqslqdfvirriSLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHNSGPI 143

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 25149237 346 VVQCETGVNQSAELVFVDAMCTLLTRQVEVNFDVLFRQMRSQKAlAMTQ 394
Cdd:cd14538 144 VVHCSAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQ-GMIQ 191
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 201-388 1.67e-16

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: 77.81  E-value: 1.67e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 201 YIHANHImfDHLKKT---YITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASNPNVYpMYYPNKPETFNNFGQFFVy 277
Cdd:cd14539   1 YINASLI--EDLTPYcprFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVH-RYWPTERGQALVYGAITV- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 278 ckTVTQPKTKYGCKEYKFELVVQaDNEERRSVRLYHYPHWTKNMVPASSKVVLNLVKKI-----GKKKSQAPVVVQCETG 352
Cdd:cd14539  77 --SLQSVRTTPTHVERIISIQHK-DTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVhshylQQRSLQTPIVVHCSSG 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 25149237 353 VNQSAelvfvdAMCTLLTRQVEV-------NFDVLFRQMRSQK 388
Cdd:cd14539 154 VGRTG------AFCLLYAAVQEIeagngipDLPQLVRKMRQQR 190
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 174-388 2.29e-16

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: 78.14  E-value: 2.29e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 174 NTFKNQRKDVPCIDDTRVKL----ADPNiVYYIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSS 249
Cdd:cd14630   3 NRNKNRYGNIISYDHSRVRLqlldGDPH-SDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 250 SASNPNVYpMYYPNKPETFNNFGQFFVYcktvTQPKTKYGCKEYKfelVVQADNEERRSVRLYHYPHWTKNMVPASSKVV 329
Cdd:cd14630  82 EVGRVKCV-RYWPDDTEVYGDIKVTLIE----TEPLAEYVIRTFT---VQKKGYHEIREIRQFHFTSWPDHGVPCYATGL 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25149237 330 LNLVKKIG--KKKSQAPVVVQCETGVNQSAELVFVDAMCTLLTRQVEVNFDVLFRQMRSQK 388
Cdd:cd14630 154 LGFVRQVKflNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQR 214
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 178-394 2.39e-16

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: 78.01  E-value: 2.39e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 178 NQRKDVPCIDDTRVKL----ADPNiVYYIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASN 253
Cdd:cd14619   1 NRFRNVLPYDWSRVPLkpihEEPG-SDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 254 ---PNVYPMYYpnKPETFNNFgQFFVYCKTVTQPKTkygCKEYkfeLVVQADNEERRSVRLYHYPHWTKNMVPASSKVVL 330
Cdd:cd14619  80 vkcEHYWPLDY--TPCTYGHL-RVTVVSEEVMENWT---VREF---LLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLL 150

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25149237 331 ---NLVKK-IGKKKSQAPVVVQCETGVNQSAELVFVDAMCTLLTRQVEVNFDVLFRQMRSQKALaMTQ 394
Cdd:cd14619 151 afrRLLRQwLDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPL-MVQ 217
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 174-410 2.96e-16

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: 78.89  E-value: 2.96e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 174 NTFKNQRKDVPCIDDTRVKL--ADPNIVYYIHANHI--MFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSS 249
Cdd:cd14599  38 NAERNRIREVVPYEENRVELvpTKENNTGYINASHIkvTVGGEEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEE 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 250 SASNPNVYpMYYPNKPETFNN--FGQFfvycKTVTQPKTKYGCKEYKFELVVQADNEERRSVRLYHYPHWTKNMVPASSK 327
Cdd:cd14599 118 EGGRSKSH-RYWPKLGSKHSSatYGKF----KVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQ 192

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 328 VVLNLVKKI------------GKKKSQAPVVVQCETGVNQSAELVFVDAMCTLLTRQVEVNFDVLFRQMRSQKALAMTQL 395
Cdd:cd14599 193 GFLSYLEEIqsvrrhtnsmldSTKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTI 272

                       250
                ....*....|....*
gi 25149237 396 LHFLHSIATVMKFIK 410
Cdd:cd14599 273 AQYKFVYQVLIQFLK 287
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 201-356 3.15e-16

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: 77.05  E-value: 3.15e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 201 YIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASNPNVYPmYYPNKPETF----------NN 270
Cdd:cd14558   1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQ-YWGDEKKTYgdievelkdtEK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 271 FGQFFVYCKTVTQPKTKygckeykfelvvqadneERRSVRLYHYPHWTKNMVPASSKVVLNLVKKIGKKKSQ-------- 342
Cdd:cd14558  80 SPTYTVRVFEITHLKRK-----------------DSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYknskhgrs 142

                       170
                ....*....|....
gi 25149237 343 APVVVQCETGVNQS 356
Cdd:cd14558 143 VPIVVHCSDGSSRT 156
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 201-385 3.33e-16

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


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 76.98  E-value: 3.33e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 201 YIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASNpnvYPMYYPNKPET--FNNFgqffvyc 278
Cdd:cd14550   1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNED---EPIYWPTKEKPleCETF------- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 279 kTVTQPKTKYGCKEYKFELVV-----QADNEERR-SVRLYHYPHWTKNMVPASSkvVLNLVKKIGKKKSQ--APVVVQCE 350
Cdd:cd14550  71 -KVTLSGEDHSCLSNEIRLIVrdfilESTQDDYVlEVRQFQCPSWPNPCSPIHT--VFELINTVQEWAQQrdGPIVVHDR 147

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 25149237 351 TGVNQSAELVFVDAMCTLLTRQVEVN---FDVLFRQMR 385
Cdd:cd14550 148 YGGVQAATFCALTTLHQQLEHESSVDvyqVAKLYHLMR 185
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 155-388 4.78e-16

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: 78.15  E-value: 4.78e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 155 FSNHLMNIAP----TSRSDAFHGNTFKNQRKDVPCIDDTRVKLADPNIVY---YIHANHIMFDHLKKTYITTQHPLPGTL 227
Cdd:cd14626  18 FSQEYESIDPgqqfTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPgsdYINANYIDGYRKQNAYIATQGPLPETL 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 228 NDFWAMVADQKVETIVSLTSSSSASNPNVyPMYYPNK-PETfnnFGQFFVYCKTVTQPKTkYGCKEYKfelVVQADNEER 306
Cdd:cd14626  98 SDFWRMVWEQRTATIVMMTRLEEKSRVKC-DQYWPIRgTET---YGMIQVTLLDTVELAT-YSVRTFA---LYKNGSSEK 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 307 RSVRLYHYPHWTKNMVPASSKVVLNLVKKIG--KKKSQAPVVVQCETGVNQSAELVFVDAMCTLLTRQVEVNFDVLFRQM 384
Cdd:cd14626 170 REVRQFQFMAWPDHGVPEYPTPILAFLRRVKacNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCM 249


                ....
gi 25149237 385 RSQK 388
Cdd:cd14626 250 RSQR 253
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 174-394 8.38e-16

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type tyrosine-protein phosphatase N2 (PTPRN2 or R-PTP-N2), also called islet cell autoantigen-related protein (IAR), ICAAR, phogrin, or IA-2beta, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. It is mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells. It may function as a phosphatidylinositol phosphatase to regulate insulin secretion. It is also required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain.


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 77.40  E-value: 8.38e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 174 NTFKNQRKDVPCIDDTRVKLADPNI---VYYIHANHIMfDHLKKT--YITTQHPLPGTLNDFWAMVADQKVETIVSLTSS 248
Cdd:cd14610  44 NVQKNRSLAVLPYDHSRIILKAENShshSDYINASPIM-DHDPRNpaYIATQGPLPATVADFWQMVWESGCVVIVMLTPL 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 249 SSASNPNVYpMYYPNKpetfnnfGQFFVYCKTVTQPKTKYGCKEY---KFELVVQADNEErRSVRLYHYPHWTKNMVPAS 325
Cdd:cd14610 123 AENGVKQCY-HYWPDE-------GSNLYHIYEVNLVSEHIWCEDFlvrSFYLKNLQTNET-RTVTQFHFLSWNDQGVPAS 193

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25149237 326 SKVVLNLVKKIGK--KKSQAPVVVQCETGVNQSAELVFVDAMCTLLTRQV-EVNFDVLFRQMRSQKAlAMTQ 394
Cdd:cd14610 194 TRSLLDFRRKVNKcyRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKGAkEIDIAATLEHLRDQRP-GMVQ 264
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 201-394 9.04e-16

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: 76.21  E-value: 9.04e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 201 YIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASNPNVYPmYYPNKPETFNNFGQFFVYckt 280
Cdd:cd14631  15 YINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYK-YWPDDTEVYGDFKVTCVE--- 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 281 vTQPKTKYGCKEYKFElvvQADNEERRSVRLYHYPHWTKNMVPASSKVVLNLVK--KIGKKKSQAPVVVQCETGVNQSAE 358
Cdd:cd14631  91 -MEPLAEYVVRTFTLE---RRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRrvKLSNPPSAGPIVVHCSAGAGRTGC 166

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 25149237 359 LVFVDAMCTLLTRQVEVNFDVLFRQMRSQKaLAMTQ 394
Cdd:cd14631 167 YIVIDIMLDMAEREGVVDIYNCVKALRSRR-INMVQ 201
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 201-388 1.89e-15

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: 74.78  E-value: 1.89e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 201 YIHANHIMFD--HLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASNPNVYpMYYP---NKPETFNNFGQFF 275
Cdd:cd14596   1 YINASYITMPvgEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCH-RYWPetlQEPMELENYQLRL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 276 VYCKTVtqpktkygckEY---KFELVVQADNEERRSVRLYHYPHWTKNMVPASSKVVLNLVKKIGKKKSQAPVVVQCETG 352
Cdd:cd14596  80 ENYQAL----------QYfiiRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNTGPIVVHCSAG 149

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 25149237 353 VNQSAELVFVDAMCTLLTRQVEVNFDVLFRQMRSQK 388
Cdd:cd14596 150 IGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQR 185
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 174-388 1.94e-15

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 76.99  E-value: 1.94e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237  174 NTFKNQRKDVPCIDDTRVKLA-------------DP---------NIVYYIHANHIM-FDHLKKtYITTQHPLPGTLNDF 230
Cdd:PHA02746  51 NLKKNRFHDIPCWDHSRVVINaheslkmfdvgdsDGkkievtsedNAENYIHANFVDgFKEANK-FICAQGPKEDTSEDF 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237  231 WAMVADQKVETIVSLTSSSSASNPNVYPMYYPNKPETfnNFGQFFVycktvtqpKTKYGCKEYKFE----LVVQADNEER 306
Cdd:PHA02746 130 FKLISEHESQVIVSLTDIDDDDEKCFELWTKEEDSEL--AFGRFVA--------KILDIIEELSFTktrlMITDKISDTS 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237  307 RSVRLYHYPHWTKNMVPASSKVVLNLVKKIGKKKSQ------------APVVVQCETGVNQSAELVFVDAMCTLLTRQVE 374
Cdd:PHA02746 200 REIHHFWFPDWPDNGIPTGMAEFLELINKVNEEQAElikqadndpqtlGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKE 279

                        250
                 ....*....|....
gi 25149237  375 VNFDVLFRQMRSQK 388
Cdd:PHA02746 280 VCLGEIVLKIRKQR 293
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 174-403 8.72e-15

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: 73.71  E-value: 8.72e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 174 NTFKNQRKDVPCIDDTRVKLADPNIVY---YIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSS 250
Cdd:cd14554   6 NKFKNRLVNILPYESTRVCLQPIRGVEgsdYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLRE 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 251 ASNPNVYpMYYPNkpETFNNFGQFfvycktVTQPKTKYGCKEYKFE--LVVQADNEERRSVRLYHYPHWTKNMVPASSKV 328
Cdd:cd14554  86 MGREKCH-QYWPA--ERSARYQYF------VVDPMAEYNMPQYILRefKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEG 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 329 VLNLVKKIGKKKSQ----APVVVQCETGVNQSAelVFVDAMCTLLTRQVEVNFDVL--FRQMRSQKAlAMTQL---LHFL 399
Cdd:cd14554 157 FIDFIGQVHKTKEQfgqeGPITVHCSAGVGRTG--VFITLSIVLERMRYEGVVDVFqtVKLLRTQRP-AMVQTedqYQFC 233


                ....
gi 25149237 400 HSIA 403
Cdd:cd14554 234 YRAA 237
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 201-396 1.17e-14

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: 72.73  E-value: 1.17e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 201 YIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASNPNVYpMYYPNkpETFNNFGQFFVYCKT 280
Cdd:cd14622   2 YINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCV-QYWPS--EGSVTHGEITIEIKN 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 281 VTQPKTkYGCKEYkfeLVVQADNEERRSVRLYHYPHWTKNMVPASSKVVLNLVKKIGKKKSQA---PVVVQCETGVNQSA 357
Cdd:cd14622  79 DTLLET-ISIRDF---LVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTgnhPIVVHCSAGAGRTG 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 25149237 358 ELVfvdAMCTLLTR-QVEVNFDVL--FRQMRSQKAlAMTQLL 396
Cdd:cd14622 155 TFI---ALSNILERvKAEGLLDVFqtVKSLRLQRP-HMVQTL 192
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 174-406 1.32e-14

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: 73.38  E-value: 1.32e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 174 NTFKNQRKDVPCIDDTRVKLA---DPNIVYYIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSS 250
Cdd:cd14614  12 NRCKNRYTNILPYDFSRVKLVsmhEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNE 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 251 ASNPNVyPMYYPNKPETFnNFGQFFVYCKTVTQpKTKYGCKEYKfelVVQADneERRSVRLYHYPHWTKNMVPA--SSKV 328
Cdd:cd14614  92 KRRVKC-DHYWPFTEEPV-AYGDITVEMLSEEE-QPDWAIREFR---VSYAD--EVQDVMHFNYTAWPDHGVPTanAAES 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 329 VLNLVKKIGKK--KSQAPVVVQCETGVNQSAELVFVDAMCTLLTRQVEVNFDVLFRQMRSQKaLAMTQLLH---FLHSIA 403
Cdd:cd14614 164 ILQFVQMVRQQavKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYR-MSMVQTEEqyiFIHQCV 242


                ...
gi 25149237 404 TVM 406
Cdd:cd14614 243 QLM 245
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 174-411 1.72e-14

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 73.88  E-value: 1.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237  174 NTFKNQRKDVPCIDDTRVKL-ADPNIVYYIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSAS 252
Cdd:PHA02742  52 NMKKCRYPDAPCFDRNRVILkIEDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDG 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237  253 NPNVYPMYYPNKPETFnNFGQFfvyckTVTQPKTKyGCKEYKFELVVQADNEERRSVRLYH--YPHWTKNMVPASSKVVL 330
Cdd:PHA02742 132 KEACYPYWMPHERGKA-THGEF-----KIKTKKIK-SFRNYAVTNLCLTDTNTGASLDIKHfaYEDWPHGGLPRDPNKFL 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237  331 NLVKKIGKKKSQA-------------PVVVQCETGVNQSAELVFVDAMCTLLTRQVEVNFDVLFRQMRSQKALAMTQLLH 397
Cdd:PHA02742 205 DFVLAVREADLKAdvdikgenivkepPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQ 284

                        250
                 ....*....|....
gi 25149237  398 FLHSIATVMKFIKI 411
Cdd:PHA02742 285 YIFCYFIVLIFAKL 298
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 201-396 1.80e-14

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: 71.92  E-value: 1.80e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 201 YIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASNPNVYpMYYPNkpETFNNFGQFFVYCKT 280
Cdd:cd14552   1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCA-QYWPE--DGSVSSGDITVELKD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 281 VTQpktkygCKEYKFE--LVVQADNEERRSVRLYHYPHWTKNMVPASSKVVLNLVKKIGKKKSQA---PVVVQCETGVNQ 355
Cdd:cd14552  78 QTD------YEDYTLRdfLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSgnhPITVHCSAGAGR 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 25149237 356 SAELVfvdAMCTLLTR-QVEVNFDVL--FRQMRSQKAlAMTQLL 396
Cdd:cd14552 152 TGTFC---ALSTVLERvKAEGVLDVFqvVKSLRLQRP-HMVQTL 191
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 173-388 2.11e-14

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: 73.53  E-value: 2.11e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 173 GNTFKNQRKDVPCIDDTRVKL---ADPNIVYYIHANHIMfDHLKK--TYITTQHPLPGTLNDFWAMVADQKVETIVSLTS 247
Cdd:cd14609  41 ANVKKNRNPDFVPYDHARIKLkaeSNPSRSDYINASPII-EHDPRmpAYIATQGPLSHTIADFWQMVWENGCTVIVMLTP 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 248 SSSASNPNVyPMYYPNKPETFnnfgqFFVYckTVTQPKTKYGCKEY---KFELVvQADNEERRSVRLYHYPHWTKNMVPA 324
Cdd:cd14609 120 LVEDGVKQC-DRYWPDEGSSL-----YHIY--EVNLVSEHIWCEDFlvrSFYLK-NVQTQETRTLTQFHFLSWPAEGIPS 190

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25149237 325 SSKVVLNLVKKIGK--KKSQAPVVVQCETGVNQSAELVFVDAMCTLLTRQV-EVNFDVLFRQMRSQK 388
Cdd:cd14609 191 STRPLLDFRRKVNKcyRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGVkEIDIAATLEHVRDQR 257
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 201-394 2.44e-14

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: 71.73  E-value: 2.44e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 201 YIHANHIM---FDHLKKtYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASNPNVYPMYYPNKPETFNNFGQFFVY 277
Cdd:cd17658   1 YINASLVEtpaSESLPK-FIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTAKCADYFPAEENESREFGRISVT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 278 CKtvtqpktKYGCKEYKFEL----VVQADNEER-RSVRLYHYPHWTKNMVPASSKVVLNLVKKI-GKKKSQAPVVVQCET 351
Cdd:cd17658  80 NK-------KLKHSQHSITLrvleVQYIESEEPpLSVLHIQYPEWPDHGVPKDTRSVRELLKRLyGIPPSAGPIVVHCSA 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 25149237 352 GVNQSAelvfvdAMCTL---LTRQVE-----VNFDVLFRQMRSQKaLAMTQ 394
Cdd:cd17658 153 GIGRTG------AYCTIhntIRRILEgdmsaVDLSKTVRKFRSQR-IGMVQ 196
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 201-389 2.66e-14

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: 71.71  E-value: 2.66e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 201 YIHANHIMfDHLKK--TYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASNPNVYpMYYPNK-PETFNNFgqffvy 277
Cdd:cd14546   1 YINASTIY-DHDPRnpAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCA-RYWPEEgSEVYHIY------ 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 278 ckTVTQPKTKYGCKEY---KFELvVQADNEERRSVRLYHYPHWTKNMVPASSKVVLNLVKKIGK--KKSQAPVVVQCETG 352
Cdd:cd14546  73 --EVHLVSEHIWCDDYlvrSFYL-KNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKsyRGRSCPIVVHCSDG 149

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 25149237 353 VNQSAELVFVDAMCTLLTRQV-EVNFDVLFRQMRSQKA 389
Cdd:cd14546 150 AGRTGTYILIDMVLNRMAKGAkEIDIAATLEHLRDQRP 187
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 201-388 2.66e-14

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: 71.28  E-value: 2.66e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 201 YIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASNPnvYPMYYPNkpETFNNFGQFFVYCKT 280
Cdd:cd14556   1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQS--CPQYWPD--EGSGTYGPIQVEFVS 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 281 VTQPKTkygCKEYKFELV-VQADNEERRSVRLYHYPHWTKN-MVPASSKVVLNLVKKIGKKKSQA---PVVVQCETGVNQ 355
Cdd:cd14556  77 TTIDED---VISRIFRLQnTTRPQEGYRMVQQFQFLGWPRDrDTPPSKRALLKLLSEVEKWQEQSgegPIVVHCLNGVGR 153

                       170       180       190
                ....*....|....*....|....*....|....*
gi 25149237 356 SAELVFVDAMCTLLtrQVEVNFDVLF--RQMRSQK 388
Cdd:cd14556 154 SGVFCAISSVCERI--KVENVVDVFQavKTLRNHR 186
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 201-400 2.98e-14

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: 71.72  E-value: 2.98e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 201 YIHANHIMFDHLKKT--YITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASNPNVYpMYYP--NKPETFNNFGQFFV 276
Cdd:cd14540   1 YINASHITATVGGKQrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCF-RYWPtlGGEHDALTFGEYKV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 277 YCKTvTQPKTKYGCKEYKFELVvqadnEERRSVRLYH--YPHWTKNMVPASSKVVLNLVKKI-----------GKKKSQA 343
Cdd:cd14540  80 STKF-SVSSGCYTTTGLRVKHT-----LSGQSRTVWHlqYTDWPDHGCPEDVSGFLDFLEEInsvrrhtnqdvAGHNRNP 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 344 PVVVQCETGVNQSAELVFVDAMCTLLTRQVEVNFDVLFRQMRSQKALaMTQLL---HFLH 400
Cdd:cd14540 154 PTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRML-LVQTLaqyKFVY 212
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 177-379 4.83e-14

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: 71.27  E-value: 4.83e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 177 KNQRKDVPCIDDTRVKLADPN-IVYYIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASNPN 255
Cdd:cd14545   1 LNRYRDRDPYDHDRSRVKLKQgDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQIK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 256 VYpMYYPNKPETFNNFgQFFVYCKTVTQPKTK--YGCKEYKFE-LVVQadneERRSVRLYHYPHWTKNMVPASSKVVLNL 332
Cdd:cd14545  81 CA-QYWPQGEGNAMIF-EDTGLKVTLLSEEDKsyYTVRTLELEnLKTQ----ETREVLHFHYTTWPDFGVPESPAAFLNF 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 25149237 333 VKKIGKKKS----QAPVVVQCETGVNQSAELVFVDAmCTLLTRQVEVN-FDV 379
Cdd:cd14545 155 LQKVRESGSlssdVGPPVVHCSAGIGRSGTFCLVDT-CLVLIEKGNPSsVDV 205
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 174-388 7.58e-14

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: 71.01  E-value: 7.58e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 174 NTFKNQRKDVPCIDDTRVKLADPNivYYIHANHIMFDHLKK--TYITTQHPLPGTLNDFWAMVADQKvETIVSLTSSSSA 251
Cdd:cd14597   3 NRKKNRYKNILPYDTTRVPLGDEG--GYINASFIKMPVGDEefVYIACQGPLPTTVADFWQMVWEQK-STVIAMMTQEVE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 252 SNPNVYPMYYP---NKPETFNNFGQFFVyckTVTQPKTKYGCKEYKFELVvqaDNEERRSVRLYHYPHWTKNMVPASSKV 328
Cdd:cd14597  80 GGKIKCQRYWPeilGKTTMVDNRLQLTL---VRMQQLKNFVIRVLELEDI---QTREVRHITHLNFTAWPDHDTPSQPEQ 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 329 VLNLVKKIGKKKSQAPVVVQCETGVNQSAELVFVDAMCTLLTRQVEVNFDVLFRQMRSQK 388
Cdd:cd14597 154 LLTFISYMRHIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQR 213
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 174-388 1.02e-13

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: 71.28  E-value: 1.02e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 174 NTFKNQRKDVPCIDDTRVKLADPNIVY---YIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSS 250
Cdd:cd14625  47 NKPKNRYANVIAYDHSRVILQPIEGIMgsdYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEE 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 251 ASNPNVyPMYYPNKPEtfNNFGQFFVYCKTVTQPKTkYGCKEYKFElvvQADNEERRSVRLYHYPHWTKNMVPASSKVVL 330
Cdd:cd14625 127 KSRIKC-DQYWPSRGT--ETYGMIQVTLLDTIELAT-FCVRTFSLH---KNGSSEKREVRQFQFTAWPDHGVPEYPTPFL 199

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 331 NLVKKIG--KKKSQAPVVVQCETGVNQSAELVFVDAMCTLLTRQVEVNFDVLFRQMRSQK 388
Cdd:cd14625 200 AFLRRVKtcNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQR 259
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 187-400 2.20e-13

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: 69.17  E-value: 2.20e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 187 DDTRVKL-ADPNIVY--YIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASNPNVYpMYYP- 262
Cdd:cd14616  10 NNNRVKLiADAGVPGsdYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRIRCH-QYWPe 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 263 -NKPETFnnFGQfFVYCKTVTQPKTKYGCKEYKFElvvqaDNEERRSVRLYHYPHWTKNMVPASSKVVLNLVKKIGKKKS 341
Cdd:cd14616  89 dNKPVTV--FGD-IVITKLMEDVQIDWTIRDLKIE-----RHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRASRA 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25149237 342 Q--APVVVQCETGVNQSAELVFVDAMCTLLTRQVEVNFDVLFRQMRSQKaLAMTQLLH---FLH 400
Cdd:cd14616 161 HdnTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSER-MCMVQNLAqyiFLH 223
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 174-365 3.27e-13

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: 68.96  E-value: 3.27e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 174 NTFKNQRKDVPCIDDTRVKLADPNIVY---YIHANHImfDHLKK--TYITTQHPLPGTLNDFWAMVADQKVETIVSLTSS 248
Cdd:cd14553   3 NKPKNRYANVIAYDHSRVILQPIEGVPgsdYINANYC--DGYRKqnAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 249 SSASNPNVyPMYYPNK-PETfnnFGQFFVYCkTVTQPKTKYGCKeyKFELVVQADNeERRSVRLYHYPHWTKNMVPASSK 327
Cdd:cd14553  81 EERSRVKC-DQYWPTRgTET---YGLIQVTL-LDTVELATYTVR--TFALHKNGSS-EKREVRQFQFTAWPDHGVPEHPT 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 25149237 328 VVLNLVKKIgkkKS-----QAPVVVQCETGVNQSAELVFVDAM 365
Cdd:cd14553 153 PFLAFLRRV---KAcnppdAGPIVVHCSAGVGRTGCFIVIDSM 192
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 135-394 2.14e-12

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: 67.44  E-value: 2.14e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 135 YIKFMDQVAFIENGTTLSTFFSNHLMNIAPTSR--SDAFHGNTFKNQRKDVPCIDDTRVKLADPNIVY---YIHANHIMF 209
Cdd:cd14629  12 HIQKLTQVPPGESVTAMELEFKLLANSKAHTSRfiSANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEgsdYINASFIDG 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 210 DHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASNPNVYPMYYPNKPETFnnfgQFFVYCKTVTQPKTKYG 289
Cdd:cd14629  92 YRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARY----QYFVVDPMAEYNMPQYI 167

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 290 CKEYKfelVVQADNEERRSVRLYHYPHWTKNMVPASSKVVLNLVKKIGKKKSQ----APVVVQCETGVNQSAELVFVDAM 365
Cdd:cd14629 168 LREFK---VTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEQfgqdGPITVHCSAGVGRTGVFITLSIV 244

                       250       260
                ....*....|....*....|....*....
gi 25149237 366 CTLLTRQVEVNFDVLFRQMRSQKAlAMTQ 394
Cdd:cd14629 245 LERMRYEGVVDMFQTVKTLRTQRP-AMVQ 272
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 201-388 2.30e-12

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: 65.70  E-value: 2.30e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 201 YIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASNPNVYpMYYPNKPE-TFNNfgqfFVYCK 279
Cdd:cd14551   1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCS-QYWPDQGCwTYGN----LRVRV 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 280 TVTQPKTKYGCKEYKFELVVQADNEER-RSVRLYHYPHWTKNMVPASSKVVLNLVKKIGKKKSQ--APVVVQCETGVNQS 356
Cdd:cd14551  76 EDTVVLVDYTTRKFCIQKVNRGIGEKRvRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPraGPIVVHCSAGVGRT 155

                       170       180       190
                ....*....|....*....|....*....|..
gi 25149237 357 AELVFVDAMCTLLTRQVEVNFDVLFRQMRSQK 388
Cdd:cd14551 156 GTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQR 187
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 190-400 3.35e-12

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: 65.71  E-value: 3.35e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 190 RVKLADPNIVYYIHANHIM-FDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASNPNVypMYYPNKPETf 268
Cdd:cd14611  19 KPKNSNDSLSTYINANYIRgYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKNEKCV--LYWPEKRGI- 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 269 nnFGQFFVYCKTVTQpktkygCKEYKFELVVQADNEERRSVRLYHYPHWTKNMVPASSKVVLNLVKKIGKKK----SQAP 344
Cdd:cd14611  96 --YGKVEVLVNSVKE------CDNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRlaspGRGP 167

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 25149237 345 VVVQCETGVNQSAELVFVDAMCTLLTRQVEVNFDVLFRQMRSQKA--LAMTQLLHFLH 400
Cdd:cd14611 168 VVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGgmVQTSEQYEFVH 225
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 201-395 1.57e-11

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: 63.31  E-value: 1.57e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 201 YIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKvETIVSLTSSSSASNPNVYPMYYPNKPETFNNFGQFFVyckT 280
Cdd:cd14557   1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQK-STVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVV---K 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 281 VTQPKTkygCKEYKFELVVQADNEERRSVR-LYH--YPHWTKNMVPASSKVVLNLVKKIGKKKS--QAPVVVQCETGVNQ 355
Cdd:cd14557  77 INEEKI---CPDYIIRKLNINNKKEKGSGReVTHiqFTSWPDHGVPEDPHLLLKLRRRVNAFNNffSGPIVVHCSAGVGR 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 25149237 356 SAELVFVDAMCTLLTRQVEVNFDVLFRQMRSQKALaMTQL 395
Cdd:cd14557 154 TGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCL-MVQV 192
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 201-365 1.63e-11

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: 63.53  E-value: 1.63e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 201 YIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASNPNVyPMYYPNKPETFNNFGQFFVYCKT 280
Cdd:cd14632   1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKC-SKYWPDDSDTYGDIKITLLKTET 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 281 VTQpktkYGCKEYKFElvvQADNEERRSVRLYHYPHWTKNMVPASSKVVLNLVKKIGKKK--SQAPVVVQCETGVNQSAE 358
Cdd:cd14632  80 LAE----YSVRTFALE---RRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTppDAGPVVVHCSAGAGRTGC 152


                ....*..
gi 25149237 359 LVFVDAM 365
Cdd:cd14632 153 YIVLDVM 159
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 201-410 1.78e-11

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: 63.46  E-value: 1.78e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 201 YIHANHIMFD--HLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASNPNVYpMYYPNKPETFN--NFGQFfv 276
Cdd:cd14598   1 YINASHIKVTvgGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSF-RYWPRLGSRHNtvTYGRF-- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 277 ycKTVTQPKTKYGCKEYKFELVVQADNEERRSVRLYHYPHWTKNMVPASSKVVLNLVKKIGK-----------KKSQAPV 345
Cdd:cd14598  78 --KITTRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSvrrhtnstidpKSPNPPV 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25149237 346 VVQCETGVNQSAELVFVDAMCTLLTRQVEVNFDVLFRQMRSQKALAMTQLLHFLHSIATVMKFIK 410
Cdd:cd14598 156 LVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 201-388 3.63e-11

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: 63.04  E-value: 3.63e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 201 YIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASNPNVYpMYYPNKP-ETFNNFGQFFVYCK 279
Cdd:cd14620  25 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKCY-QYWPDQGcWTYGNIRVAVEDCV 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 280 TVTQPKTKYGCKEYKFELVVQADneerRSVRLYHYPHWTKNMVPASSKVVLNLVKKIG--KKKSQAPVVVQCETGVNQSA 357
Cdd:cd14620 104 VLVDYTIRKFCIQPQLPDGCKAP----RLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKsvNPVHAGPIVVHCSAGVGRTG 179

                       170       180       190
                ....*....|....*....|....*....|.
gi 25149237 358 ELVFVDAMCTLLTRQVEVNFDVLFRQMRSQK 388
Cdd:cd14620 180 TFIVIDAMIDMMHAEQKVDVFEFVSRIRNQR 210
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 174-420 4.09e-11

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: 63.89  E-value: 4.09e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 174 NTFKNQRKDVPCIDDTRVKLADPNIVY---YIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSS 250
Cdd:cd14621  52 NKEKNRYVNILPYDHSRVHLTPVEGVPdsdYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKE 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 251 ASNPNVyPMYYPNkpETFNNFGQFFVYCKTVTQpKTKYGCKEYKFELVVQADNEE-RRSVRLYHYPHWTKNMVPASSKVV 329
Cdd:cd14621 132 RKECKC-AQYWPD--QGCWTYGNIRVSVEDVTV-LVDYTVRKFCIQQVGDVTNKKpQRLITQFHFTSWPDFGVPFTPIGM 207

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 330 LNLVKKIGKKKSQ--APVVVQCETGVNQSAELVFVDAMCTLLTRQVEVNFDVLFRQMRSQKAlamtqllhflHSIATVMK 407
Cdd:cd14621 208 LKFLKKVKNCNPQyaGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRC----------QMVQTDMQ 277

                       250
                ....*....|...
gi 25149237 408 FIKIrFSAMPSHY 420
Cdd:cd14621 278 YVFI-YQALLEHY 289
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 177-376 5.48e-11

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: 62.96  E-value: 5.48e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 177 KNQRKDVPCIDDTRVKLADPN----IVYYIHANHIM-FDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTssssa 251
Cdd:cd14613  28 KNRYKTILPNPHSRVCLTSPDqddpLSSYINANYIRgYGGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMIT----- 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 252 snpNVYPM------YYPNKPETFNNFGqffVYCKTVTQPKtkygckEYKFELVVQADNEERRSVRLYHYPHWTKNMVPAS 325
Cdd:cd14613 103 ---NIEEMnekcteYWPEEQVTYEGIE---ITVKQVIHAD------DYRLRLITLKSGGEERGLKHYWYTSWPDQKTPDN 170

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 25149237 326 SKVVLNLVKKIGKKKSQA-----PVVVQCETGVNQSAELVFVDAMCTLLTRQVEVN 376
Cdd:cd14613 171 APPLLQLVQEVEEARQQAepncgPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVD 226
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 201-379 1.10e-10

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: 60.85  E-value: 1.10e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 201 YIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASNPNVypMYYPNKPETFNnfgqffvyCK- 279
Cdd:cd17670   1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEF--VYWPSREESMN--------CEa 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 280 -TVTQPKTKYGCKEYKFELVVQ------ADNEERRSVRLYHYPHWTKNMVPASSKV-VLNLVKKIGKKKSqAPVVVQCET 351
Cdd:cd17670  71 fTVTLISKDRLCLSNEEQIIIHdfileaTQDDYVLEVRHFQCPKWPNPDAPISSTFeLINVIKEEALTRD-GPTIVHDEF 149

                       170       180
                ....*....|....*....|....*...
gi 25149237 352 GVNQSAELVFVdamcTLLTRQVEVNFDV 379
Cdd:cd17670 150 GAVSAGTLCAL----TTLSQQLENENAV 173
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 201-352 1.11e-10

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: 61.16  E-value: 1.11e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 201 YIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASNPNVypMYYPNKPETFNnfgqffvyCK- 279
Cdd:cd17669   1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF--VYWPNKDEPIN--------CEt 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 280 -TVTQPKTKYGCKEYKFELVVQ------ADNEERRSVRLYHYPHWTKNMVPASSKV-VLNLVKKIGKKKSqAPVVVQCET 351
Cdd:cd17669  71 fKVTLIAEEHKCLSNEEKLIIQdfileaTQDDYVLEVRHFQCPKWPNPDSPISKTFeLISIIKEEAANRD-GPMIVHDEH 149


                .
gi 25149237 352 G 352
Cdd:cd17669 150 G 150
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 201-396 1.20e-10

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: 61.21  E-value: 1.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 201 YIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASNPNVyPMYYPNKpetfnnfgQFFVYCKT 280
Cdd:cd14623  26 YVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEKC-AQYWPSD--------GSVSYGDI 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 281 VTQPKTKYGCKEYKFE--LVVQADNEERRSVRLYHYPHWTKNMVPASSKVVLNLVKKIGKKKSQA---PVVVQCETGVNQ 355
Cdd:cd14623  97 TIELKKEEECESYTVRdlLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQQSgnhPITVHCSAGAGR 176

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 25149237 356 SAELVfvdAMCTLLTR-QVEVNFDVL--FRQMRSQKAlAMTQLL 396
Cdd:cd14623 177 TGTFC---ALSTVLERvKAEGILDVFqtVKSLRLQRP-HMVQTL 216
PHA02738 PHA02738
hypothetical protein; Provisional
 178-363 2.01e-10

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 61.86  E-value: 2.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237  178 NQRKDVPCIDDTRVKL-ADPNIVYYIHANHI-MFDHLKKtYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASNPN 255
Cdd:PHA02738  53 NRYLDAVCFDHSRVILpAERNRGDYINANYVdGFEYKKK-FICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREK 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237  256 VYPmYYPNKPETFNNFGQFFVyckTVTQPKT--KYgckeYKFELVVQADNEERRSVRLYHYPHWTKNMVPASSKVVLNLV 333
Cdd:PHA02738 132 CFP-YWSDVEQGSIRFGKFKI---TTTQVEThpHY----VKSTLLLTDGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFV 203

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 25149237  334 K--------------KIGKKKSQ-APVVVQCETGVNQSAELVFVD 363
Cdd:PHA02738 204 LevrqcqkelaqeslQIGHNRLQpPPIVVHCNAGLGRTPCYCVVD 248
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 174-388 9.58e-10

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 59.63  E-value: 9.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237  174 NTFKNQRKDVPCIDDTRVKL--ADPNIVYYIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSA 251
Cdd:PHA02747  51 NQPKNRYWDIPCWDHNRVILdsGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTKGT 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237  252 SNPNV-YPMYYPNKPETFNNFGQFFVYCKTVTQPKtkygckeYKFELVVQADNEERRSVRLYHY--PHWTKNMVPASSKV 328
Cdd:PHA02747 131 NGEEKcYQYWCLNEDGNIDMEDFRIETLKTSVRAK-------YILTLIEITDKILKDSRKISHFqcSEWFEDETPSDHPD 203

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25149237  329 VLNLVKKIGKKKSQ------------APVVVQCETGVNQSAELVFVDAMCTLLTRQVEVNFDVLFRQMRSQK 388
Cdd:PHA02747 204 FIKFIKIIDINRKKsgklfnpkdallCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQR 275
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 216-388 1.94e-07

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: 51.56  E-value: 1.94e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 216 YITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASN-PNVYP-----MYYPNKPETF------NNFGQFFVYCkTVTQ 283
Cdd:cd14636  16 FIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQGcPQYWPeegmlRYGPIQVECMscsmdcDVISRIFRIC-NLTR 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 284 PKTKYgckeykfeLVVQAdneerrsvrlYHYPHWTKNM-VPASSKVVLNLVKKIGK-----KKSQAPVVVQCETGVNQSA 357
Cdd:cd14636  95 PQEGY--------LMVQQ----------FQYLGWASHReVPGSKRSFLKLILQVEKwqeecDEGEGRTIIHCLNGGGRSG 156

                       170       180       190
                ....*....|....*....|....*....|.
gi 25149237 358 ELVFVDAMCTLLTRQVEVNFDVLFRQMRSQK 388
Cdd:cd14636 157 MFCAISIVCEMIKRQNVVDVFHAVKTLRNSK 187
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 201-389 2.20e-07

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: 51.18  E-value: 2.20e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 201 YIHANhIMFDHLK-KTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSAsnpNVYPMYYPNKPETF----------- 268
Cdd:cd14634   1 YINAA-LMDSHKQpAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAA---QLCMQYWPEKTSCCygpiqvefvsa 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 269 ----NNFGQFFVYCkTVTQPKTKYgckeykfelvvqadneerRSVRLYHYPHWTKNM-VPASSKVVLNLVKKIGKKKSQ- 342
Cdd:cd14634  77 dideDIISRIFRIC-NMARPQDGY------------------RIVQHLQYIGWPAYRdTPPSKRSILKVVRRLEKWQEQy 137

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 25149237 343 ----APVVVQCETGVNQSAELVFVDAMCTLLTRQVEVNFDVLFRQMRSQKA 389
Cdd:cd14634 138 dgreGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKS 188
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 203-388 1.62e-05

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: 45.83  E-value: 1.62e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 203 HANHIMFDHLKK--TYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSAsnpNVYPMYYPNkpetfnnfgqffvyckt 280
Cdd:cd14635   1 YINAALMDSYKQpsAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPA---QLCPQYWPE----------------- 60

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237 281 vtQPKTKYGCKEYKFelvVQADNEE---RRSVRLYH--YPHWTKNMV--------------PASSKVVLNLVKKIGKKKS 341
Cdd:cd14635  61 --NGVHRHGPIQVEF---VSADLEEdiiSRIFRIYNaaRPQDGYRMVqqfqflgwpmyrdtPVSKRSFLKLIRQVDKWQE 135

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 25149237 342 -----QAPVVVQCETGVNQSAELVFVDAMCTLLTRQVEVNFDVLFRQMRSQK 388
Cdd:cd14635 136 eynggEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNK 187
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 209-417 1.67e-03

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 40.34  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237  209 FDHlKKTYITTQHPLPGTLNDFWAMVADQKVETIVSLTSSSSASNpnvYPMYYPNKPETFNNFGQFFVYC-KTVTQPktk 287
Cdd:PHA02740  87 YDF-EQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADKKC---FNQFWSLKEGCVITSDKFQIETlEIIIKP--- 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149237  288 ygckEYKFELVVQADNE-ERRSVRLYHYPHWTKNMVPASSKVVLNL----------VKKIGKKKSQAPVVVQCETGVNQS 356
Cdd:PHA02740 160 ----HFNLTLLSLTDKFgQAQKISHFQYTAWPADGFSHDPDAFIDFfcniddlcadLEKHKADGKIAPIIIDCIDGISSS 235

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25149237  357 AELVFVDAMCTLLTRQVEVNFDVLFRQMRSQKALAMTQLLHFLHSIATVMKFIKIRFSAMP 417
Cdd:PHA02740 236 AVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYLKEKFDILK 296
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 201-243 7.18e-03

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: 37.97  E-value: 7.18e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 25149237 201 YIHANHIMFDHLKKTYITTQHPLPGTLNDFWAMVADQKVETIV 243
Cdd:cd14637   1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVV 43
 
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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