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Conserved domains on  [gi|17539216|ref|NP_501277|]
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Tyrosine-protein phosphatase domain-containing protein [Caenorhabditis elegans]

Protein Classification

tyrosine-protein phosphatase( domain architecture ID 11987518)

tyrosine-protein phosphatase catalyzes the dephosphorylation of phosphotyrosine groups in phosphoproteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
243-468 1.31e-69

Protein-tyrosine phosphatase;


:

Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 222.12  E-value: 1.31e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216   243 NMDKNRFVDVICMDHSRVKLTD----SSYIHANWVDLNSSKKA-ILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEFN 317
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGdpgpSDYINASYIDGYKKPKKyIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216   318 KFGGNSVFPQ-NQDFLKFEDRFIRVGEFKQVElgKGWNLKVLSVSNGTYKT--FIHVHHYKNWPHGSIPSDVKQIWQVQS 394
Cdd:pfam00102  81 REKCAQYWPEeEGESLEYGDFTVTLKKEKEDE--KDYTVRTLEVSNGGSEEtrTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17539216   395 YLRKYT---DGHPPVYMSMSGCGRAGTFALFETAHMSLHNEQPsLNMVKCLENVRNGRLHSVQNLSQFSVVYTLIAE 468
Cdd:pfam00102 159 KVRKSSldgRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGE-VDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
 
Name Accession Description Interval E-value
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
243-468 1.31e-69

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 222.12  E-value: 1.31e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216   243 NMDKNRFVDVICMDHSRVKLTD----SSYIHANWVDLNSSKKA-ILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEFN 317
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGdpgpSDYINASYIDGYKKPKKyIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216   318 KFGGNSVFPQ-NQDFLKFEDRFIRVGEFKQVElgKGWNLKVLSVSNGTYKT--FIHVHHYKNWPHGSIPSDVKQIWQVQS 394
Cdd:pfam00102  81 REKCAQYWPEeEGESLEYGDFTVTLKKEKEDE--KDYTVRTLEVSNGGSEEtrTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17539216   395 YLRKYT---DGHPPVYMSMSGCGRAGTFALFETAHMSLHNEQPsLNMVKCLENVRNGRLHSVQNLSQFSVVYTLIAE 468
Cdd:pfam00102 159 KVRKSSldgRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGE-VDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
222-468 1.85e-69

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 222.53  E-value: 1.85e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216    222 NEFEKVSGYLPPHISKNH--FVSNMDKNRFVDVICMDHSRVKLTD-----SSYIHANWVDLNSSKKA-ILTQLPLSHTAS 293
Cdd:smart00194   4 EEFEKLDRLKPDDESCTVaaFPENRDKNRYKDVLPYDHTRVKLKPppgegSDYINASYIDGPNGPKAyIATQGPLPSTVE 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216    294 DFWQMIIDQKIKCVLLIMTDGEFNKFGGNSVFPQNQ-DFLKFEDRFIrvgEFKQVELGKGWNLKVLSVSNGT--YKTFIH 370
Cdd:smart00194  84 DFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgEPLTYGDITV---TLKSVEKVDDYTIRTLEVTNTGcsETRTVT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216    371 VHHYKNWPHGSIPSD-------VKQIWQVQSYLRKytdghPPVYMSMSGCGRAGTFALFETAHMSLHNEQPsLNMVKCLE 443
Cdd:smart00194 161 HYHYTNWPDHGVPESpesildlIRAVRKSQSTSTG-----PIVVHCSAGVGRTGTFIAIDILLQQLEAGKE-VDIFEIVK 234

                          250       260
                   ....*....|....*....|....*
gi 17539216    444 NVRNGRLHSVQNLSQFSVVYTLIAE 468
Cdd:smart00194 235 ELRSQRPGMVQTEEQYIFLYRAILE 259
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 267-463 5.90e-36

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: 132.41  E-value: 5.90e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 267 YIHANWVDLNSSKKA-ILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEFNKFGGNSVFPQNQD-FLKFEDRFIRVGEF 344
Cdd:cd00047   1 YINASYIDGYRGPKEyIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGkPLEYGDITVTLVSE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 345 KQVElgkGWNLKVLSVSNGTYKT--FIHVHHYKNWPHGSIPSDVKQIWQVQSYLRKYTDG--HPPVYMSMSGCGRAGTFA 420
Cdd:cd00047  81 EELS---DYTIRTLELSPKGCSEsrEVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKpnGPIVVHCSAGVGRTGTFI 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 17539216 421 LFETAHMSLHNEQpSLNMVKCLENVRNGRLHSVQNLSQFSVVY 463
Cdd:cd00047 158 AIDILLERLEAEG-EVDVFEIVKALRKQRPGMVQTLEQYEFIY 199
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
246-469 1.02e-23

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 100.55  E-value: 1.02e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 246 KNRFVDVICMDHSRVKlTDSSYIHANWVDLNSSKKAILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEFNKFGGNSV- 324
Cdd:COG5599  45 LNRFRDIQPYKETALR-ANLGYLNANYIQVIGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISKPKVKMPv 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 325 -FPQNQDFLKFEdrfIRVGEFKQVELGKGWNLKVLSVS---NGTYKTFIHVHHYKNWP-HGSIPSD-----VKQIWQVQS 394
Cdd:COG5599 124 yFRQDGEYGKYE---VSSELTESIQLRDGIEARTYVLTikgTGQKKIEIPVLHVKNWPdHGAISAEalknlADLIDKKEK 200

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 395 YLRKytDGHPPVYMSMSGCGRAGTFalfeTAHMSLHNEQPS-----LNMVKCLENVRNGRLHS-VQNLSQFSVVYTLIAE 468
Cdd:COG5599 201 IKDP--DKLLPVVHCRAGVGRTGTL----IACLALSKSINAlvqitLSVEEIVIDMRTSRNGGmVQTSEQLDVLVKLAEQ 274


                .
gi 17539216 469 H 469
Cdd:COG5599 275 Q 275
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 243-466 2.92e-20

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 91.22  E-value: 2.92e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216  243 NMDKNRFVDVICMDHSRVKLTD----SSYIHANWVD-LNSSKKAILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEFN 317
Cdd:PHA02742  52 NMKKCRYPDAPCFDRNRVILKIedggDDFINASYVDgHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDG 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216  318 KfggNSVFPQnqdFLKFEDRFIRVGEFK----QVELGKGWNLKVLSVSNGTYKTFIHVHH--YKNWPHGSIPSDVKQIWQ 391
Cdd:PHA02742 132 K---EACYPY---WMPHERGKATHGEFKiktkKIKSFRNYAVTNLCLTDTNTGASLDIKHfaYEDWPHGGLPRDPNKFLD 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216  392 VQSYLR------------KYTDGHPPVYM-SMSGCGRAGTFALFETAhMSLHNEQPSLNMVKCLENVRNGRlHSVQNLSQ 458
Cdd:PHA02742 206 FVLAVReadlkadvdikgENIVKEPPILVhCSAGLDRAGAFCAIDIC-ISKYNERAIIPLLSIVRDLRKQR-HNCLSLPQ 283


                 ....*...
gi 17539216  459 FSVVYTLI 466
Cdd:PHA02742 284 QYIFCYFI 291
 
Name Accession Description Interval E-value
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
243-468 1.31e-69

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 222.12  E-value: 1.31e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216   243 NMDKNRFVDVICMDHSRVKLTD----SSYIHANWVDLNSSKKA-ILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEFN 317
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGdpgpSDYINASYIDGYKKPKKyIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216   318 KFGGNSVFPQ-NQDFLKFEDRFIRVGEFKQVElgKGWNLKVLSVSNGTYKT--FIHVHHYKNWPHGSIPSDVKQIWQVQS 394
Cdd:pfam00102  81 REKCAQYWPEeEGESLEYGDFTVTLKKEKEDE--KDYTVRTLEVSNGGSEEtrTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17539216   395 YLRKYT---DGHPPVYMSMSGCGRAGTFALFETAHMSLHNEQPsLNMVKCLENVRNGRLHSVQNLSQFSVVYTLIAE 468
Cdd:pfam00102 159 KVRKSSldgRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGE-VDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
222-468 1.85e-69

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 222.53  E-value: 1.85e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216    222 NEFEKVSGYLPPHISKNH--FVSNMDKNRFVDVICMDHSRVKLTD-----SSYIHANWVDLNSSKKA-ILTQLPLSHTAS 293
Cdd:smart00194   4 EEFEKLDRLKPDDESCTVaaFPENRDKNRYKDVLPYDHTRVKLKPppgegSDYINASYIDGPNGPKAyIATQGPLPSTVE 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216    294 DFWQMIIDQKIKCVLLIMTDGEFNKFGGNSVFPQNQ-DFLKFEDRFIrvgEFKQVELGKGWNLKVLSVSNGT--YKTFIH 370
Cdd:smart00194  84 DFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgEPLTYGDITV---TLKSVEKVDDYTIRTLEVTNTGcsETRTVT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216    371 VHHYKNWPHGSIPSD-------VKQIWQVQSYLRKytdghPPVYMSMSGCGRAGTFALFETAHMSLHNEQPsLNMVKCLE 443
Cdd:smart00194 161 HYHYTNWPDHGVPESpesildlIRAVRKSQSTSTG-----PIVVHCSAGVGRTGTFIAIDILLQQLEAGKE-VDIFEIVK 234

                          250       260
                   ....*....|....*....|....*
gi 17539216    444 NVRNGRLHSVQNLSQFSVVYTLIAE 468
Cdd:smart00194 235 ELRSQRPGMVQTEEQYIFLYRAILE 259
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 267-463 5.90e-36

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: 132.41  E-value: 5.90e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 267 YIHANWVDLNSSKKA-ILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEFNKFGGNSVFPQNQD-FLKFEDRFIRVGEF 344
Cdd:cd00047   1 YINASYIDGYRGPKEyIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGkPLEYGDITVTLVSE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 345 KQVElgkGWNLKVLSVSNGTYKT--FIHVHHYKNWPHGSIPSDVKQIWQVQSYLRKYTDG--HPPVYMSMSGCGRAGTFA 420
Cdd:cd00047  81 EELS---DYTIRTLELSPKGCSEsrEVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKpnGPIVVHCSAGVGRTGTFI 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 17539216 421 LFETAHMSLHNEQpSLNMVKCLENVRNGRLHSVQNLSQFSVVY 463
Cdd:cd00047 158 AIDILLERLEAEG-EVDVFEIVKALRKQRPGMVQTLEQYEFIY 199
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 243-464 3.45e-24

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: 101.67  E-value: 3.45e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 243 NMDKNRFVDVICMDHSRVKLT------DSSYIHANWVDLNSSKKA-ILTQLPLSHTASDFWQMIIDQkiKCVLLIMT--- 312
Cdd:cd14543  29 NQEKNRYGDVLCLDQSRVKLPkrngdeRTDYINANFMDGYKQKNAyIATQGPLPKTYSDFWRMVWEQ--KVLVIVMTtrv 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 313 -DGEFNKFGgnSVFPQNQDFLkfeDRF--IRVgEFKQVELGKGWNLKVLSVSNGTYKTFIHVHHYK--NWPHGSIPSDV- 386
Cdd:cd14543 107 vERGRVKCG--QYWPLEEGSS---LRYgdLTV-TNLSVENKEHYKKTTLEIHNTETDESRQVTHFQftSWPDFGVPSSAa 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 387 -----------KQIWQVQSYLRKYTdGHPP-----VYMSmSGCGRAGTFALFETAhMSLHNEQPSLNMVKCLENVRNGRL 450
Cdd:cd14543 181 alldflgevrqQQALAVKAMGDRWK-GHPPgppivVHCS-AGIGRTGTFCTLDIC-LSQLEDVGTLNVMQTVRRMRTQRA 257

                       250
                ....*....|....
gi 17539216 451 HSVQNLSQFSVVYT 464
Cdd:cd14543 258 FSIQTPDQYYFCYK 271
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
246-469 1.02e-23

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 100.55  E-value: 1.02e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 246 KNRFVDVICMDHSRVKlTDSSYIHANWVDLNSSKKAILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEFNKFGGNSV- 324
Cdd:COG5599  45 LNRFRDIQPYKETALR-ANLGYLNANYIQVIGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISKPKVKMPv 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 325 -FPQNQDFLKFEdrfIRVGEFKQVELGKGWNLKVLSVS---NGTYKTFIHVHHYKNWP-HGSIPSD-----VKQIWQVQS 394
Cdd:COG5599 124 yFRQDGEYGKYE---VSSELTESIQLRDGIEARTYVLTikgTGQKKIEIPVLHVKNWPdHGAISAEalknlADLIDKKEK 200

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 395 YLRKytDGHPPVYMSMSGCGRAGTFalfeTAHMSLHNEQPS-----LNMVKCLENVRNGRLHS-VQNLSQFSVVYTLIAE 468
Cdd:COG5599 201 IKDP--DKLLPVVHCRAGVGRTGTL----IACLALSKSINAlvqitLSVEEIVIDMRTSRNGGmVQTSEQLDVLVKLAEQ 274


                .
gi 17539216 469 H 469
Cdd:COG5599 275 Q 275
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 246-468 1.83e-22

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: 96.06  E-value: 1.83e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 246 KNRFVDVICMDHSRVKL------TDSSYIHANWVDLNSSKKA-ILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEFNK 318
Cdd:cd14602   1 KNRYKDILPYDHSRVELslitsdEDSDYINANFIKGVYGPRAyIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 319 fggnsvfpqnqdfLKFEDRFIRVGEFK----------QVELGKG-WNLKVLSVSNGTYKTFIHVHHYKNWPHGSIPSDVK 387
Cdd:cd14602  81 -------------KKCERYWAEPGEMQlefgpfsvtcEAEKRKSdYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSID 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 388 QIWQVQSYLRKYT-DGHPPVYMSMS-GCGRAGTFALFETAHMSLHNEQPSLN--MVKCLENVRNGRLHSVQNLSQFSVVY 463
Cdd:cd14602 148 PILELIWDVRCYQeDDSVPICIHCSaGCGRTGVICAIDYTWMLLKDGIIPENfsVFSLIQEMRTQRPSLVQTKEQYELVY 227


                ....*
gi 17539216 464 TLIAE 468
Cdd:cd14602 228 NAVIE 232
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 243-468 2.67e-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: 96.93  E-value: 2.67e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 243 NMDKNRFVDVICMDHSRVKLT------DSSYIHANWVD-LNSSKKAILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGE 315
Cdd:cd14604  57 NVKKNRYKDILPFDHSRVKLTlktssqDSDYINANFIKgVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFE 136

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 316 FNKFGGNSVFPQnqdflkFEDRFIRVGEFK----QVELGKGWNLKVLSVSNGTYKTFIHVHHYKNWPHGSIPSDVKQIWQ 391
Cdd:cd14604 137 MGRKKCERYWPL------YGEEPMTFGPFRisceAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPDHDVPSSFDSILD 210

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 392 VQSYLRKYTDgHPPVYMSM---SGCGRAG-------TFALFETAHMSlhneqPSLNMVKCLENVRNGRLHSVQNLSQFSV 461
Cdd:cd14604 211 MISLMRKYQE-HEDVPICIhcsAGCGRTGaicaidyTWNLLKAGKIP-----EEFNVFNLIQEMRTQRHSAVQTKEQYEL 284


                ....*..
gi 17539216 462 VYTLIAE 468
Cdd:cd14604 285 VHRAIAQ 291
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
368-468 7.78e-22

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 90.11  E-value: 7.78e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216    368 FIHVHHYKNWPHGSIPSD----VKQIWQVQSYLRKYTDGHPPVYMSMSGCGRAGTFALFETAHMSLHNEQPSLNMVKCLE 443
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESpdsiLELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 17539216    444 NVRNGRLHSVQNLSQFSVVYTLIAE 468
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 368-468 7.78e-22

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: 90.11  E-value: 7.78e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216    368 FIHVHHYKNWPHGSIPSD----VKQIWQVQSYLRKYTDGHPPVYMSMSGCGRAGTFALFETAHMSLHNEQPSLNMVKCLE 443
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESpdsiLELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 17539216    444 NVRNGRLHSVQNLSQFSVVYTLIAE 468
Cdd:smart00012  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 243-468 1.54e-21

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: 94.12  E-value: 1.54e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 243 NMDKNRFVDVICMDHSRVKLT------DSSYIHANWVD-LNSSKKAILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGE 315
Cdd:cd14603  30 NVKKNRYKDILPYDQTRVILSllqeegHSDYINANFIKgVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACREIE 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 316 FNKFGGNSVFPQNQDFLKFEDrfIRVGEFKQVELGKGWNLKVLSVSNGTYKTFIHVHHYKNWPHGSIPSDVKQIWQVQSY 395
Cdd:cd14603 110 MGKKKCERYWAQEQEPLQTGP--FTITLVKEKRLNEEVILRTLKVTFQKESRSVSHFQYMAWPDHGIPDSPDCMLAMIEL 187

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17539216 396 LRKY--TDGHPPVYMSMSGCGRAGTFALFETAHMSLHNE--QPSLNMVKCLENVRNGRLHSVQNLSQFSVVYTLIAE 468
Cdd:cd14603 188 ARRLqgSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQriPPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 267-463 2.10e-21

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: 92.31  E-value: 2.10e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 267 YIHANWVDL--NSSKKAILTQLPLSHTASDFWQMIIDQKIKCVllIMtdgeFNKFGGNSV------FPQNQDFLKFEDrf 338
Cdd:cd18533   1 YINASYITLpgTSSKRYIATQGPLPATIGDFWKMIWQNNVGVI--VM----LTPLVENGRekcdqyWPSGEYEGEYGD-- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 339 IRVGEFKQVELGKGW-NLKVLSVSNGTYKTFIhVHH--YKNWPHGSIPSDVKQIWQVQSYLRKYTDGH---PPVYMSMS- 411
Cdd:cd18533  73 LTVELVSEEENDDGGfIVREFELSKEDGKVKK-VYHiqYKSWPDFGVPDSPEDLLTLIKLKRELNDSAsldPPIIVHCSa 151

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 412 GCGRAGTF-ALFETAHM--SLHNEQPSLNM-----VKCLENVRNGRLHSVQNLSQFSVVY 463
Cdd:cd18533 152 GVGRTGTFiALDSLLDElkRGLSDSQDLEDsedpvYEIVNQLRKQRMSMVQTLRQYIFLY 211
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 223-466 2.45e-21

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: 93.49  E-value: 2.45e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 223 EFEKVSGYLPPHISKnhFVSNMDKNRFVDVICMDHSRVKL--TDSSYIHANWVDLNSSKKA-ILTQLPLSHTASDFWQMI 299
Cdd:cd14607   6 EIRNESHDYPHRVAK--YPENRNRNRYRDVSPYDHSRVKLqnTENDYINASLVVIEEAQRSyILTQGPLPNTCCHFWLMV 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 300 IDQKIKCVLLIMTDGEFNKFGGNSVFP-QNQDFLKFEDRFIRVGEFKQvELGKGWNLKVLSVSN---GTYKTFIHVhHYK 375
Cdd:cd14607  84 WQQKTKAVVMLNRIVEKDSVKCAQYWPtDEEEVLSFKETGFSVKLLSE-DVKSYYTVHLLQLENinsGETRTISHF-HYT 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 376 NWPHGSIP----SDVKQIWQVQSYLRKYTDGHPPVYMSMSGCGRAGTFALFETAHMSLHNEQP-SLNMVKCLENVRNGRL 450
Cdd:cd14607 162 TWPDFGVPespaSFLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDPdSVDIKQVLLDMRKYRM 241

                       250
                ....*....|....*.
gi 17539216 451 HSVQNLSQFSVVYTLI 466
Cdd:cd14607 242 GLIQTPDQLRFSYMAV 257
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 247-459 3.75e-21

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: 92.26  E-value: 3.75e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 247 NRFVDVICMDHSRVKLT------DSSYIHANWV-DLNSSKKAILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEFNKF 319
Cdd:cd14619   1 NRFRNVLPYDWSRVPLKpiheepGSDYINANYMpGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 320 GGNSVFPQNQDFLKFEDRFIRVgefKQVELGKGWNLKVLSVSNGTYKTFIHVH--HYKNWPHGSIPSDVKQIWQVQSYLR 397
Cdd:cd14619  81 KCEHYWPLDYTPCTYGHLRVTV---VSEEVMENWTVREFLLKQVEEQKTLSVRhfHFTAWPDHGVPSSTDTLLAFRRLLR 157

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17539216 398 KYTDGH----PPVYMSMSGCGRAGTFALFETAHMSLHNEQpSLNMVKCLENVRNGRLHSVQNLSQF 459
Cdd:cd14619 158 QWLDQTmsggPTVVHCSAGVGRTGTLIALDVLLQQLQSEG-LLGPFSFVQKMRENRPLMVQTESQY 222
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 243-462 8.88e-21

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: 92.22  E-value: 8.88e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 243 NMDKNRFVDVICMDHSRVKLT-DSSYIHANWVDL-----NSSKKAILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEF 316
Cdd:cd14600  40 NMDKNRYKDVLPYDATRVVLQgNEDYINASYVNMeipsaNIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTER 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 317 NKFGGNSVFPQNQDFLKFEDRFIRVgefKQVELGKGWNLKVLSVSN---GTYKTFIHVhHYKNWPHGSIPSDVKQIWQVQ 393
Cdd:cd14600 120 GRTKCHQYWPDPPDVMEYGGFRVQC---HSEDCTIAYVFREMLLTNtqtGEERTVTHL-QYVAWPDHGVPDDSSDFLEFV 195

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17539216 394 SYLRKYTDGHPPVYMSMS-GCGRAGTFALFETAHMSLHNEQP--SLNMVKCLenvRNGRLHSVQNLSQFSVV 462
Cdd:cd14600 196 NYVRSKRVENEPVLVHCSaGIGRTGVLVTMETAMCLTERNQPvyPLDIVRKM---RDQRAMMVQTSSQYKFV 264
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 243-466 2.92e-20

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 91.22  E-value: 2.92e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216  243 NMDKNRFVDVICMDHSRVKLTD----SSYIHANWVD-LNSSKKAILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEFN 317
Cdd:PHA02742  52 NMKKCRYPDAPCFDRNRVILKIedggDDFINASYVDgHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDG 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216  318 KfggNSVFPQnqdFLKFEDRFIRVGEFK----QVELGKGWNLKVLSVSNGTYKTFIHVHH--YKNWPHGSIPSDVKQIWQ 391
Cdd:PHA02742 132 K---EACYPY---WMPHERGKATHGEFKiktkKIKSFRNYAVTNLCLTDTNTGASLDIKHfaYEDWPHGGLPRDPNKFLD 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216  392 VQSYLR------------KYTDGHPPVYM-SMSGCGRAGTFALFETAhMSLHNEQPSLNMVKCLENVRNGRlHSVQNLSQ 458
Cdd:PHA02742 206 FVLAVReadlkadvdikgENIVKEPPILVhCSAGLDRAGAFCAIDIC-ISKYNERAIIPLLSIVRDLRKQR-HNCLSLPQ 283


                 ....*...
gi 17539216  459 FSVVYTLI 466
Cdd:PHA02742 284 QYIFCYFI 291
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 245-463 9.02e-20

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: 88.22  E-value: 9.02e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 245 DKNRFVDVICMDHSRVKLT--DSSYIHANWVDLNSSKKA-ILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEFNKFGG 321
Cdd:cd14545   2 NRYRDRDPYDHDRSRVKLKqgDNDYINASLVEVEEAKRSyILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQIKC 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 322 NSVFPQNQDF-LKFEDRFIRVgEFKQVELGKGWNLKVLSVSN-GTYKTFIHVH-HYKNWPHGSIPSD----VKQIWQVQS 394
Cdd:cd14545  82 AQYWPQGEGNaMIFEDTGLKV-TLLSEEDKSYYTVRTLELENlKTQETREVLHfHYTTWPDFGVPESpaafLNFLQKVRE 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 395 YLRKYTDGHPPVYMSMSGCGRAGTFALFETAHMSLHNEQPS-LNMVKCLENVRNGRLHSVQNLSQFSVVY 463
Cdd:cd14545 161 SGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPSsVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 248-459 1.96e-19

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: 87.02  E-value: 1.96e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 248 RFVDVICMDHSRVKLTD------SSYIHANWVD-LNSSKKAILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEFNKFG 320
Cdd:cd14548   1 RYTNILPYDHSRVKLIPineeegSDYINANYIPgYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 321 GNSVFPQNQDFLKFEDrfIRVGEFKQVELgKGWNLKVLSVSNGTYKTFIHVHHYKNWP-HG--SIPSDVKQIWQ-VQSYL 396
Cdd:cd14548  81 CDHYWPFDQDPVYYGD--ITVTMLSESVL-PDWTIREFKLERGDEVRSVRQFHFTAWPdHGvpEAPDSLLRFVRlVRDYI 157

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17539216 397 RKytDGHPPVYMSMSGCGRAGTF-AL-FETAHMSLHNEQPSLNMVKCLenvRNGRLHSVQNLSQF 459
Cdd:cd14548 158 KQ--EKGPTIVHCSAGVGRTGTFiALdRLLQQIESEDYVDIFGIVYDL---RKHRPLMVQTEAQY 217
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 247-463 3.47e-19

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: 86.51  E-value: 3.47e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 247 NRFVDVICMDHSRVKLTD------SSYIHANWVDLNSSKKA-ILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEFNKF 319
Cdd:cd14617   1 NRYNNILPYDSTRVKLSNvdddpcSDYINASYIPGNNFRREyIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 320 GGNSVFPQNQDFLKFEDRFIRVGEFKQVELGKGWNLKVLSVSNGTYKTFIHVHHYKNWPHGSIPSDVKQIWQ----VQSY 395
Cdd:cd14617  81 KCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQLDAPRLVRHFHYTVWPDHGVPETTQSLIQfvrtVRDY 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17539216 396 LRKYTDGHPPVYMSMSGCGRAGTFALFETAHMSLhNEQPSLNMVKCLENVRNGRLHSVQNLSQFSVVY 463
Cdd:cd14617 161 INRTPGSGPTVVHCSAGVGRTGTFIALDRILQQL-DSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 243-483 4.33e-19

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: 87.39  E-value: 4.33e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 243 NMDKNRFVDVICMDHSRVKLT--DSSYIHANWVDLNSSKKA-ILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEFNKF 319
Cdd:cd14608  25 NKNRNRYRDVSPFDHSRIKLHqeDNDYINASLIKMEEAQRSyILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSL 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 320 GGNSVFPQNQDF-LKFEDRFIRVGEFKQvELGKGWNLKVLSVSN-GTYKTFIHVH-HYKNWPHGSIPSDVKQIWQVQSYL 396
Cdd:cd14608 105 KCAQYWPQKEEKeMIFEDTNLKLTLISE-DIKSYYTVRQLELENlTTQETREILHfHYTTWPDFGVPESPASFLNFLFKV 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 397 RK---YTDGHPPVYMSMS-GCGRAGTFALFETA--HMSLHNEQPSLNMVKCLENVRNGRLHSVQNLSQFSVVYTLI---A 467
Cdd:cd14608 184 REsgsLSPEHGPVVVHCSaGIGRSGTFCLADTCllLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAViegA 263

                       250
                ....*....|....*.
gi 17539216 468 EHVLGNgigkKDVEEQ 483
Cdd:cd14608 264 KFIMGD----SSVQDQ 275
PHA02738 PHA02738
hypothetical protein; Provisional
 243-470 4.65e-19

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 88.06  E-value: 4.65e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216  243 NMDKNRFVDVICMDHSRVKL----TDSSYIHANWVD-LNSSKKAILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEFN 317
Cdd:PHA02738  49 NRKLNRYLDAVCFDHSRVILpaerNRGDYINANYVDgFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENG 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216  318 KfggNSVFPQNQDflkFEDRFIRVGEFK----QVELGKGWNLKVLSVSNGTYKTFIHVHH-YKNWPHGSIPSDVKQ---- 388
Cdd:PHA02738 129 R---EKCFPYWSD---VEQGSIRFGKFKitttQVETHPHYVKSTLLLTDGTSATQTVTHFnFTAWPDHDVPKNTSEflnf 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216  389 IWQVQS-----YLRKYTDGH-----PPVYMSMS-GCGRAGTFALFETAhMSLHNEQPSLNMVKCLENVRNGRLHSVQNLS 457
Cdd:PHA02738 203 VLEVRQcqkelAQESLQIGHnrlqpPPIVVHCNaGLGRTPCYCVVDIS-ISRFDACATVSIPSIVSSIRNQRYYSLFIPF 281

                        250
                 ....*....|...
gi 17539216  458 QFSVVYTLIAEHV 470
Cdd:PHA02738 282 QYFFCYRAVKRYV 294
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 201-466 5.39e-18

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: 84.28  E-value: 5.39e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 201 KLTKWKLvaqetlkdDANIAVNEFEKVSGYLPPHI-SKNHFVSNMDKNRFVDVICMDHSRVKL-----TDSSYIHANWVD 274
Cdd:cd14599   3 KTLERKL--------EEGMVFTEYEQIPKKKADGVfTTATLPENAERNRIREVVPYEENRVELvptkeNNTGYINASHIK 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 275 LNSSKKA---ILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEFNKFGGNSVFPQnqdfLKFEDRFIRVGEFK-----Q 346
Cdd:cd14599  75 VTVGGEEwhyIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPK----LGSKHSSATYGKFKvttkfR 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 347 VELG--KGWNLKVLSVSNGTYKTFIHVhHYKNWPHGSIPSDVK----QIWQVQSyLRKYTDG--------HPPVYMSMS- 411
Cdd:cd14599 151 TDSGcyATTGLKVKHLLSGQERTVWHL-QYTDWPDHGCPEEVQgflsYLEEIQS-VRRHTNSmldstkncNPPIVVHCSa 228

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17539216 412 GCGRAGTFALFETAHMSL-HNEQPSLNMVkcLENVRNGRLHSVQNLSQFSVVYTLI 466
Cdd:cd14599 229 GVGRTGVVILTELMIGCLeHNEKVEVPVM--LRHLREQRMFMIQTIAQYKFVYQVL 282
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 238-471 1.10e-17

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: 83.16  E-value: 1.10e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 238 NHfVSNMDKNRFVDVICMDHSRVKL--------TDSSYIHANWVD-LNSSKKAILTQLPLSHTASDFWQMIIDQKIKCVL 308
Cdd:cd17667  23 NH-PDNKHKNRYINILAYDHSRVKLrplpgkdsKHSDYINANYVDgYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIV 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 309 LIMTDGEFNKFGGNSVFP--QNQDF--LKFEDRFIRVGEFKQVELGKGWNLKVLSVSNGTYK------TFIHvHHYKNWP 378
Cdd:cd17667 102 MITNLVEKGRRKCDQYWPteNSEEYgnIIVTLKSTKIHACYTVRRFSIRNTKVKKGQKGNPKgrqnerTVIQ-YHYTQWP 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 379 HGSIPsdvKQIWQVQSYLRKYT-----DGHPPVYMSMSGCGRAGTFALFETAHMSLhNEQPSLNMVKCLENVRNGRLHSV 453
Cdd:cd17667 181 DMGVP---EYALPVLTFVRRSSaartpEMGPVLVHCSAGVGRTGTYIVIDSMLQQI-KDKSTVNVLGFLKHIRTQRNYLV 256

                       250
                ....*....|....*...
gi 17539216 454 QNLSQFSVVYTLIAEHVL 471
Cdd:cd17667 257 QTEEQYIFIHDALLEAIL 274
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 267-463 2.00e-17

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: 80.54  E-value: 2.00e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 267 YIHANWVDLNSSKKA-ILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEFNKFGGNSVFPQNQ-DFLKFEDrfIRVGEF 344
Cdd:cd14542   1 YINANFIKGVSGSKAyIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGeEQLQFGP--FKISLE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 345 KQVELGKGWNLKVLSVSNGTYKTFIHVHHYKNWPHGSIPSDVKQIWQVQSYLRKY-TDGHPPVYMSMS-GCGRAGTFALF 422
Cdd:cd14542  79 KEKRVGPDFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYqGSEDVPICVHCSaGCGRTGTICAI 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 17539216 423 ETAHMSLHNEQ--PSLNMVKCLENVRNGRLHSVQNLSQFSVVY 463
Cdd:cd14542 159 DYVWNLLKTGKipEEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 223-470 2.21e-17

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: 82.39  E-value: 2.21e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 223 EFEKVSGYL--PPHISKNHFVSNMDKNRFVDVICMDHSRVKL------TDSSYIHAN-WVDLNSSKKA-ILTQLPLSHTA 292
Cdd:cd14609  20 EWQALCAYQaePNTCSTAQGEANVKKNRNPDFVPYDHARIKLkaesnpSRSDYINASpIIEHDPRMPAyIATQGPLSHTI 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 293 SDFWQMIIDQkiKCVLLIM-----TDGE--------------FNKFGGNSVfpqnQDFLKFEDRFIRVGEFKQVElgkgw 353
Cdd:cd14609 100 ADFWQMVWEN--GCTVIVMltplvEDGVkqcdrywpdegsslYHIYEVNLV----SEHIWCEDFLVRSFYLKNVQ----- 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 354 nlkvlSVSNGTYKTFihvhHYKNWPHGSIPSDVKQIWQVQSYLRKYTDGH--PPVYMSMSGCGRAGTFALFETAHMSLHN 431
Cdd:cd14609 169 -----TQETRTLTQF----HFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRscPIIVHCSDGAGRTGTYILIDMVLNRMAK 239

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 17539216 432 EQPSLNMVKCLENVRNGRLHSVQNLSQFSVVYTLIAEHV 470
Cdd:cd14609 240 GVKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAEEV 278
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 243-470 1.04e-16

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: 79.68  E-value: 1.04e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 243 NMDKNRFVDVICMDHSRVKLTD-------SSYIHANWV------DLNSSK---KAILTQLPLSHTASDFWQMIIDQKIKc 306
Cdd:cd14605   2 NKNKNRYKNILPFDHTRVVLHDgdpnepvSDYINANIImpefetKCNNSKpkkSYIATQGCLQNTVNDFWRMVFQENSR- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 307 vLLIMTDGEFNKFGGNSVFPQNQDFLKFEDRFIRVGEFKQVELGKGW--NLKVLSVSNGTYKTFIHVHHYKNWPHGSIPS 384
Cdd:cd14605  81 -VIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYIlrELKLSKVGQGNTERTVWQYHFRTWPDHGVPS 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 385 D----VKQIWQVQSYLRKYTDGHPPVYMSMSGCGRAGTFALFETAhMSLHNEQP---SLNMVKCLENVRNGRLHSVQNLS 457
Cdd:cd14605 160 DpggvLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDIL-IDIIREKGvdcDIDVPKTIQMVRSQRSGMVQTEA 238

                       250
                ....*....|...
gi 17539216 458 QFSVVYTLIAEHV 470
Cdd:cd14605 239 QYRFIYMAVQHYI 251
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 243-462 1.05e-16

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 80.82  E-value: 1.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216  243 NMDKNRFVDVICMDHSRVKL-----TDSSYIHANWVD-LNSSKKAILTQLPLSHTASDFWQMIIDQkiKCVLLIMTDGEF 316
Cdd:PHA02747  51 NQPKNRYWDIPCWDHNRVILdsgggSTSDYIHANWIDgFEDDKKFIATQGPFAETCADFWKAVWQE--HCSIIVMLTPTK 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216  317 NKFGGNSVFpqnQDFLKFEDRFIRVGEFK----QVELGKGWNLKVLSVSNGTYKTFIHVHHYK--NWPHGSIPSD----- 385
Cdd:PHA02747 129 GTNGEEKCY---QYWCLNEDGNIDMEDFRietlKTSVRAKYILTLIEITDKILKDSRKISHFQcsEWFEDETPSDhpdfi 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216  386 --VKQIWQV-QSYLRKYTDGH----PPVYMSMSGCGRAGTFALFETAHMSLhNEQPSLNMVKCLENVRNGRLHSVQNLSQ 458
Cdd:PHA02747 206 kfIKIIDINrKKSGKLFNPKDallcPIVVHCSDGVGKTGIFCAVDICLNQL-VKRKAICLAKTAEKIREQRHAGIMNFDD 284


                 ....
gi 17539216  459 FSVV 462
Cdd:PHA02747 285 YLFI 288
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 247-466 2.19e-16

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type tyrosine-protein phosphatase V (PTPRV or R-PTP-V), also known as embryonic stem cell protein-tyrosine phosphatase (ES cell phosphatase) or osteotesticular protein-tyrosine phosphatase (OST-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRV is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. In rodents, it may play a role in the maintenance of pluripotency and may function in signaling pathways during bone remodeling. It is the only PTP whose function has been lost between rodent and human. The human OST-PTP gene is a pseudogene.


Pssm-ID: 350466 [Multi-domain]  Cd Length: 230  Bit Score: 78.45  E-value: 2.19e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 247 NRFVDVICMDHSRVKLTD------SSYIHANWV-DLNSSKKAILTQLPLSHTASDFWQMIIDQKIkCVLLIMTDG-EFNK 318
Cdd:cd14618   1 NRYPHVLPYDHSRVRLSQlggephSDYINANFIpGYTSPQEFIATQGPLKKTIEDFWRLVWEQQV-CNIIMLTVGmENGR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 319 FGGNSVFPQNQDFLKFEDrfIRVGEFKQvELGKGWNLKVLSVSNGTYKTFIHVH--HYKNWPHGSIPSDVKQIWQVQSYL 396
Cdd:cd14618  80 VLCDHYWPSESTPVSYGH--ITVHLLAQ-SSEDEWTRREFKLWHEDLRKERRVKhlHYTAWPDHGIPESTSSLMAFRELV 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17539216 397 R---KYTDGHPPVYMSMS-GCGRAGTFALFETAHMSLHNEQpSLNMVKCLENVRNGRLHSVQNLSQFSVVYTLI 466
Cdd:cd14618 157 RehvQATKGKGPTLVHCSaGVGRSGTFIALDRLLRQLKEEK-VVDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 233-459 1.24e-15

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: 76.47  E-value: 1.24e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 233 PHISKNhFVSNMDKNRFVDVICMDHSRVKLTD------SSYIHANWV-DLNSSKKAILTQLPLSHTASDFWQMIIDQKIK 305
Cdd:cd14614   3 PHFAAD-LPVNRCKNRYTNILPYDFSRVKLVSmheeegSDYINANYIpGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQ 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 306 CVLLIMTDGEFNKFGGNSVFPQNQDFLKFEDRFIR-VGEFKQVElgkgWNLKVLSVSNGTYKTFIHVHHYKNWPHGSIPS 384
Cdd:cd14614  82 IIVMLTQCNEKRRVKCDHYWPFTEEPVAYGDITVEmLSEEEQPD----WAIREFRVSYADEVQDVMHFNYTAWPDHGVPT 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17539216 385 --DVKQIWQ-VQSYLRKYTDGHPPVYMSMS-GCGRAGTFALFETAHMSLHnEQPSLNMVKCLENVRNGRLHSVQNLSQF 459
Cdd:cd14614 158 anAAESILQfVQMVRQQAVKSKGPMIIHCSaGVGRTGTFIALDRLLQHIR-DHEFVDILGLVSEMRSYRMSMVQTEEQY 235
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 243-470 1.58e-15

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: 76.35  E-value: 1.58e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 243 NMDKNRFVDVICMDHSRVKLTD-------SSYIHANWVDLNSS--------KKAILTQLPLSHTASDFWQMIIDQ----- 302
Cdd:cd14544   1 NKGKNRYKNILPFDHTRVILKDrdpnvpgSDYINANYIRNENEgpttdenaKTYIATQGCLENTVSDFWSMVWQEnsrvi 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 303 ----------KIKCVLLIMTDGEFNKFGGNSVfpQNQDFLKFEDRFIRvgefkqvelgkgwNLKVLSVSNGTYKTFIHVH 372
Cdd:cd14544  81 vmttkevergKNKCVRYWPDEGMQKQYGPYRV--QNVSEHDTTDYTLR-------------ELQVSKLDQGDPIREIWHY 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 373 HYKNWPHGSIPSD-------VKQIWQVQSYLrkyTDGHPPVYMSMSGCGRAGTFALFEtAHMSLHNEQP---SLNMVKCL 442
Cdd:cd14544 146 QYLSWPDHGVPSDpggvlnfLEDVNQRQESL---PHAGPIVVHCSAGIGRTGTFIVID-MLLDQIKRKGldcDIDIQKTI 221

                       250       260
                ....*....|....*....|....*...
gi 17539216 443 ENVRNGRLHSVQNLSQFSVVYTLIAEHV 470
Cdd:cd14544 222 QMVRSQRSGMVQTEAQYKFIYVAVAQYI 249
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 247-419 1.66e-15

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: 75.51  E-value: 1.66e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 247 NRFVDVICMDHSRVKLT------DSSYIHANWV---DlNSSKKAILTQLPLSHTASDFWQMIIDQKIKCVLLImTDGEFN 317
Cdd:cd14547   1 NRYKTILPNEHSRVCLPsvdddpLSSYINANYIrgyD-GEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMI-TNLTEA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 318 KFGGNSVFPQNQDfLKFEDRFIRVGEFKQVElgkGWNLKVLSVSNGTYKtfIHVHHY--KNWPHGSIPSDVKQIWQVQS- 394
Cdd:cd14547  79 KEKCAQYWPEEEN-ETYGDFEVTVQSVKETD---GYTVRKLTLKYGGEK--RYLKHYwyTSWPDHKTPEAAQPLLSLVQe 152

                       170       180
                ....*....|....*....|....*...
gi 17539216 395 --YLRKYTDGHPPVYMSMS-GCGRAGTF 419
Cdd:cd14547 153 veEARQTEPHRGPIVVHCSaGIGRTGCF 180
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 231-466 5.48e-15

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 75.84  E-value: 5.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216  231 LPPHISKNHFV--SNMDKNRFVDVICMDHSRVKL-------------------------TDSSYIHANWVD-LNSSKKAI 282
Cdd:PHA02746  37 IPIRGTTNHFLkkENLKKNRFHDIPCWDHSRVVInaheslkmfdvgdsdgkkievtsedNAENYIHANFVDgFKEANKFI 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216  283 LTQLPLSHTASDFWQMIIDQKIKCVL-LIMTDGEFNKFGGNSVFPQNQDfLKFEDRFIRVGEFKQVELGKGWNLKVLSVS 361
Cdd:PHA02746 117 CAQGPKEDTSEDFFKLISEHESQVIVsLTDIDDDDEKCFELWTKEEDSE-LAFGRFVAKILDIIEELSFTKTRLMITDKI 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216  362 NGTYKTfIHVHHYKNWPHGSIPSDVKQIW-------QVQSYLRKYTDGHP----PVYMSMS-GCGRAGTFALFETAHMSL 429
Cdd:PHA02746 196 SDTSRE-IHHFWFPDWPDNGIPTGMAEFLelinkvnEEQAELIKQADNDPqtlgPIVVHCSaGIGRAGTFCAIDNALEQL 274

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 17539216  430 HNEQpSLNMVKCLENVRNGRLHSVQNLSQFSVVYTLI 466
Cdd:PHA02746 275 EKEK-EVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 248-468 7.08e-15

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: 73.93  E-value: 7.08e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 248 RFVDVICMDHSRVKL------TDSSYIHANWVDLNSSKKA-ILTQLPLSHTASDFWQMIIDQKiKCVLLIMTDGEFNKFG 320
Cdd:cd14623   1 RVLQIIPYEFNRVIIpvkrgeENTDYVNASFIDGYRQKDSyIASQGPLQHTIEDFWRMIWEWK-SCSIVMLTELEERGQE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 321 GNSVFPQNQDFLKFEDRFIrvgEFKQVELGKGWNLKVLSVSNG--TYKTFIHVHHYKNWPHGSIPSDVKQIWQVQSYLRK 398
Cdd:cd14623  80 KCAQYWPSDGSVSYGDITI---ELKKEEECESYTVRDLLVTNTreNKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQK 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17539216 399 ---YTDGHPPVYMSMSGCGRAGTFALFETAHMSLHNEQpSLNMVKCLENVRNGRLHSVQNLSQFSVVYTLIAE 468
Cdd:cd14623 157 qqqQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEG-ILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 267-462 1.09e-14

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: 73.13  E-value: 1.09e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 267 YIHANWVDLNSSK-----KAILTQLPLSHTASDFWQMIIDQkiKCVLLIM--TDGEFNKFGGNSVFPQnqdflkfedrfi 339
Cdd:cd14541   2 YINANYVNMEIPGsgivnRYIAAQGPLPNTCADFWQMVWEQ--KSTLIVMltTLVERGRVKCHQYWPD------------ 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 340 rvgEFKQVELGkgwNLKVLSVSNGTYKTFI---------------HVHH--YKNWP-HGsIPSDVKQIWQVQSYLRKYTD 401
Cdd:cd14541  68 ---LGETMQFG---NLQITCVSEEVTPSFAfrefiltntntgeerHITQmqYLAWPdHG-VPDDSSDFLDFVKRVRQNRV 140

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17539216 402 G--HPPVYMSMSGCGRAGTFALFETAHMSLHNEQP--SLNMVKcleNVRNGRLHSVQNLSQFSVV 462
Cdd:cd14541 141 GmvEPTVVHCSAGIGRTGVLITMETAMCLIEANEPvyPLDIVR---TMRDQRAMLIQTPSQYRFV 202
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 243-471 1.15e-14

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: 73.52  E-value: 1.15e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 243 NMDKNRFVDVICMDHSRVKLT------DSSYIHANWVD-LNSSKKAILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGE 315
Cdd:cd14630   3 NRNKNRYGNIISYDHSRVRLQlldgdpHSDYINANYIDgYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 316 FNKFGGNSVFPQNQDFlkFEDrfIRVGEFKQVELGKgWNLKVLSVSNGTYKTF--IHVHHYKNWPHGSIPSDVKQIWqvq 393
Cdd:cd14630  83 VGRVKCVRYWPDDTEV--YGD--IKVTLIETEPLAE-YVIRTFTVQKKGYHEIreIRQFHFTSWPDHGVPCYATGLL--- 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 394 SYLRKYTDGHPP-----VYMSMSGCGRAGTFALFETAhMSLHNEQPSLNMVKCLENVRNGRLHSVQNLSQFSVVYTLIAE 468
Cdd:cd14630 155 GFVRQVKFLNPPdagpiVVHCSAGAGRTGCFIAIDIM-LDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233


                ...
gi 17539216 469 HVL 471
Cdd:cd14630 234 ACL 236
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 243-468 1.30e-14

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: 73.92  E-value: 1.30e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 243 NMDKNRFVDVICMDHSRVKLTD------SSYIHANWVDLNSSKKA-ILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGE 315
Cdd:cd14626  41 NKPKNRYANVIAYDHSRVILTSvdgvpgSDYINANYIDGYRKQNAyIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEE 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 316 FNKFGGNSVFPqnqdfLKFEDRF--IRVGEFKQVELGKgWNLKVLSV-SNGTY-KTFIHVHHYKNWPHGSIPSDVKQIWq 391
Cdd:cd14626 121 KSRVKCDQYWP-----IRGTETYgmIQVTLLDTVELAT-YSVRTFALyKNGSSeKREVRQFQFMAWPDHGVPEYPTPIL- 193

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 392 vqSYLRKYTDGHPP-----VYMSMSGCGRAGTFALFETAHMSLHNEQPS--LNMVKCLENVRNgrlHSVQNLSQFSVVYT 464
Cdd:cd14626 194 --AFLRRVKACNPPdagpmVVHCSAGVGRTGCFIVIDAMLERMKHEKTVdiYGHVTCMRSQRN---YMVQTEDQYIFIHE 268


                ....
gi 17539216 465 LIAE 468
Cdd:cd14626 269 ALLE 272
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 267-466 1.37e-14

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: 72.70  E-value: 1.37e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 267 YIHANWVDLNSSKKA---ILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEFNKFGGNSVFPQnqdfLKFEDRFIRVGE 343
Cdd:cd14598   1 YINASHIKVTVGGKEwdyIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPR----LGSRHNTVTYGR 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 344 FK-----QVELG--KGWNLKVLSVSNGTYKTFIHVhHYKNWPHGSIPSDVK----QIWQVQSyLRKYTDG-------HPP 405
Cdd:cd14598  77 FKittrfRTDSGcyATTGLKIKHLLTGQERTVWHL-QYTDWPEHGCPEDLKgflsYLEEIQS-VRRHTNStidpkspNPP 154

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17539216 406 VYMSMS-GCGRAGTFALFETAHMSL-HNEQpsLNMVKCLENVRNGRLHSVQNLSQFSVVYTLI 466
Cdd:cd14598 155 VLVHCSaGVGRTGVVILSEIMIACLeHNEM--LDIPRVLDMLRQQRMMMVQTLSQYTFVYKVL 215
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 247-459 1.61e-14

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: 72.93  E-value: 1.61e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 247 NRFVDVICMDHSRVKLTDSS-----YIHANWV-DLNSSKKAILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEFNKFG 320
Cdd:cd14615   1 NRYNNVLPYDISRVKLSVQShstddYINANYMpGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRTK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 321 GNSVFPQNQDfLKFEDRFIRVG-EFKQVElgkgWNLKVLSVSN---GTYKTFIHVhHYKNWPHGSIPSDVKQIWQVQSYL 396
Cdd:cd14615  81 CEEYWPSKQK-KDYGDITVTMTsEIVLPE----WTIRDFTVKNaqtNESRTVRHF-HFTSWPDHGVPETTDLLINFRHLV 154

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17539216 397 RKYTDGHPP-----VYMSmSGCGRAGTFALFETAHMSLHNEqpslNMVKCLENVRNGRLHS---VQNLSQF 459
Cdd:cd14615 155 REYMKQNPPnspilVHCS-AGVGRTGTFIAIDRLIYQIENE----NVVDVYGIVYDLRMHRplmVQTEDQY 220
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 243-466 1.76e-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: 72.94  E-value: 1.76e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 243 NMDKNRFVDVICMDHSRVKL-TDSSYIHANWVDL---NSSKKAILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEFNK 318
Cdd:cd14597   3 NRKKNRYKNILPYDTTRVPLgDEGGYINASFIKMpvgDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEVEGGK 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 319 FGGNSVFPQNQDFLKFEDRFIRVGEFKQVELgKGWNLKVLSVSNGTYKTFIHVHH--YKNWPHGSIPSDVKQIWQVQSYL 396
Cdd:cd14597  83 IKCQRYWPEILGKTTMVDNRLQLTLVRMQQL-KNFVIRVLELEDIQTREVRHITHlnFTAWPDHDTPSQPEQLLTFISYM 161

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17539216 397 RKYTDGHPPVYMSMSGCGRAGTFALFET--AHMSLHNEQPSLNMVKCLENVRNGRlhsVQNLSQFSVVYTLI 466
Cdd:cd14597 162 RHIHKSGPIITHCSAGIGRSGTLICIDVvlGLISKDLDFDISDIVRTMRLQRHGM---VQTEDQYIFCYQVI 230
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 267-466 1.98e-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: 1.98e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 267 YIHANWVDLNSSKKA-ILTQLPLSHTASDFWQMIIDQKiKCVLLIMTDGEFNKfggnsvfpQNQDFLKF-EDRFIRVGEF 344
Cdd:cd14552   1 YINASFIDGYRQKDAyIATQGPLDHTVEDFWRMIWEWK-SCSIVMLTEIKERS--------QNKCAQYWpEDGSVSSGDI 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 345 ----KQVELGKGWNLKVLSVSNGTYKTF--IHVHHYKNWPHGSIPSDVKQ----IWQVQSYlRKYTDGHPPVYMSMSGCG 414
Cdd:cd14552  72 tvelKDQTDYEDYTLRDFLVTKGKGGSTrtVRQFHFHGWPEVGIPDNGKGmidlIAAVQKQ-QQQSGNHPITVHCSAGAG 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 17539216 415 RAGTFALFETAHMSLHNEQpSLNMVKCLENVRNGRLHSVQNLSQFSVVYTLI 466
Cdd:cd14552 151 RTGTFCALSTVLERVKAEG-VLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 243-470 2.95e-14

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: 72.99  E-value: 2.95e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 243 NMDKNRFVDVICMDHSRVKLTD-------SSYIHAN------WVDLNSSKKAILTQLPLSHTASDFWQMIIDQKIKcvLL 309
Cdd:cd14606  18 NKSKNRYKNILPFDHSRVILQGrdsnipgSDYINANyvknqlLGPDENAKTYIASQGCLEATVNDFWQMAWQENSR--VI 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 310 IMTDGEFNKfGGNSVFP------QNQDFLKFEDRFirVGEFKQVElgkgWNLKVLSVS---NGTYKTFIHVHHYKNWPHG 380
Cdd:cd14606  96 VMTTREVEK-GRNKCVPywpevgMQRAYGPYSVTN--CGEHDTTE----YKLRTLQVSpldNGELIREIWHYQYLSWPDH 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 381 SIPSD-------VKQIWQVQSYLRKytdGHPPVYMSMSGCGRAGTFALFE--TAHMSLHNEQPSLNMVKCLENVRNGRLH 451
Cdd:cd14606 169 GVPSEpggvlsfLDQINQRQESLPH---AGPIIVHCSAGIGRTGTIIVIDmlMENISTKGLDCDIDIQKTIQMVRAQRSG 245

                       250
                ....*....|....*....
gi 17539216 452 SVQNLSQFSVVYTLIAEHV 470
Cdd:cd14606 246 MVQTEAQYKFIYVAIAQFI 264
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 243-470 3.33e-14

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: 72.04  E-value: 3.33e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 243 NMDKNRFVDVICMDHSRVKLT------DSSYIHANWVDLNSSKKA-ILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGE 315
Cdd:cd14553   3 NKPKNRYANVIAYDHSRVILQpiegvpGSDYINANYCDGYRKQNAyIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 316 FNKFGGNSVFPqNQDFLKFEDrfIRVGEFKQVELGKgWNLKVLSVSNGTYKTFIHVHH--YKNWPHGSIPSDVKQIWQvq 393
Cdd:cd14553  83 RSRVKCDQYWP-TRGTETYGL--IQVTLLDTVELAT-YTVRTFALHKNGSSEKREVRQfqFTAWPDHGVPEHPTPFLA-- 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 394 sYLRKYTDGHPP------VYMSmSGCGRAGTFALFETAHMSLHNEQpSLNM---VKCLENVRNgrlHSVQNLSQFSVVYT 464
Cdd:cd14553 157 -FLRRVKACNPPdagpivVHCS-AGVGRTGCFIVIDSMLERIKHEK-TVDIyghVTCLRAQRN---YMVQTEDQYIFIHD 230


                ....*.
gi 17539216 465 LIAEHV 470
Cdd:cd14553 231 ALLEAV 236
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 243-471 3.89e-14

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: 73.13  E-value: 3.89e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 243 NMDKNRFVDVICMDHSRVKLT------DSSYIHANWVDLNSSK-KAILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGE 315
Cdd:cd14621  52 NKEKNRYVNILPYDHSRVHLTpvegvpDSDYINASFINGYQEKnKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKE 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 316 FNKFGGNSVFPQN------------QDFLKFEDRFIRVGEFKQVElgkgwnlkvlSVSNGTYKTFIHVHHYKNWPHGSIP 383
Cdd:cd14621 132 RKECKCAQYWPDQgcwtygnirvsvEDVTVLVDYTVRKFCIQQVG----------DVTNKKPQRLITQFHFTSWPDFGVP 201

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 384 SDVKQIWQvqsYLRKYTDGHPP-----VYMSMSGCGRAGTFALFETAHMSLHNEQpSLNMVKCLENVRNGRLHSVQNLSQ 458
Cdd:cd14621 202 FTPIGMLK---FLKKVKNCNPQyagaiVVHCSAGVGRTGTFIVIDAMLDMMHAER-KVDVYGFVSRIRAQRCQMVQTDMQ 277

                       250
                ....*....|...
gi 17539216 459 FSVVYTLIAEHVL 471
Cdd:cd14621 278 YVFIYQALLEHYL 290
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 267-466 6.52e-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: 70.95  E-value: 6.52e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 267 YIHANWVDL---NSSKKAILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEFNKFGGNSVFPQ---NQDFLKFEDrfIR 340
Cdd:cd14540   1 YINASHITAtvgGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTlggEHDALTFGE--YK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 341 VGEFKQVELGKGW--NLKVLSVSNGTYKTFIHVhHYKNWPHGSIPSDVKQ----IWQVQSyLRKYTDG-------HPPVY 407
Cdd:cd14540  79 VSTKFSVSSGCYTttGLRVKHTLSGQSRTVWHL-QYTDWPDHGCPEDVSGfldfLEEINS-VRRHTNQdvaghnrNPPTL 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17539216 408 MSMS-GCGRAGTFALFETAHMSL-HNEQPSLNMVkcLENVRNGRLHSVQNLSQFSVVY-TLI 466
Cdd:cd14540 157 VHCSaGVGRTGVVILADLMLYCLdHNEELDIPRV--LALLRHQRMLLVQTLAQYKFVYnVLI 216
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 267-470 1.22e-13

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: 69.78  E-value: 1.22e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 267 YIHANWV-DLNSSKKA-ILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEFNKFGGNSVFPQ--NQDFLKFEDRFIRVG 342
Cdd:cd14546   1 YINASTIyDHDPRNPAyIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEegSEVYHIYEVHLVSEH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 343 EFKQVELGKGWNLKvlSVSNGTYKTfIHVHHYKNWPHGSIPSDVKQIWQVQSYLRKYTDGH--PPVYMSMSGCGRAGTFA 420
Cdd:cd14546  81 IWCDDYLVRSFYLK--NLQTSETRT-VTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRscPIVVHCSDGAGRTGTYI 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 17539216 421 LFETAHMSLHNEQPSLNMVKCLENVRNGRLHSVQNLSQFSVVYTLIAEHV 470
Cdd:cd14546 158 LIDMVLNRMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAEEV 207
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 243-470 1.82e-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: 70.89  E-value: 1.82e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 243 NMDKNRFVDVICMDHSRVKL------TDSSYIHANWVDLNSSKKA-ILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGE 315
Cdd:cd14625  47 NKPKNRYANVIAYDHSRVILqpiegiMGSDYINANYIDGYRKQNAyIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEE 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 316 FNKFGGNSVFPqNQDFLKFEdrFIRVGEFKQVELGKgWNLKVLSV-SNGTY-KTFIHVHHYKNWPHGSIPSDVKQIWqvq 393
Cdd:cd14625 127 KSRIKCDQYWP-SRGTETYG--MIQVTLLDTIELAT-FCVRTFSLhKNGSSeKREVRQFQFTAWPDHGVPEYPTPFL--- 199

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 394 SYLRKYTDGHPP-----VYMSMSGCGRAGTFALFETAHMSLHNEQpSLNMVKCLENVRNGRLHSVQNLSQFSVVYTLIAE 468
Cdd:cd14625 200 AFLRRVKTCNPPdagpiVVHCSAGVGRTGCFIVIDAMLERIKHEK-TVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278


                ..
gi 17539216 469 HV 470
Cdd:cd14625 279 AV 280
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 243-470 2.01e-13

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: 70.47  E-value: 2.01e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 243 NMDKNRFVDVICMDHSRVKL------TDSSYIHANWV-DLNSSKKA-ILTQLPLSHTASDFWQMIIDQkiKCVLLIMtdg 314
Cdd:cd14610  44 NVQKNRSLAVLPYDHSRIILkaenshSHSDYINASPImDHDPRNPAyIATQGPLPATVADFWQMVWES--GCVVIVM--- 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 315 eFNKFGGNSV------FPQNQDFLKFEDRFIRVGEFKQVE--LGKGWNLKVLSVSNG-TYKTFihvhHYKNWPHGSIPSD 385
Cdd:cd14610 119 -LTPLAENGVkqcyhyWPDEGSNLYHIYEVNLVSEHIWCEdfLVRSFYLKNLQTNETrTVTQF----HFLSWNDQGVPAS 193

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 386 VKQIWQVQSYLRKYTDGH--PPVYMSMSGCGRAGTFALFETAHMSLHNEQPSLNMVKCLENVRNGRLHSVQNLSQFSVVY 463
Cdd:cd14610 194 TRSLLDFRRKVNKCYRGRscPIIVHCSDGAGRSGTYILIDMVLNKMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFAL 273


                ....*..
gi 17539216 464 TLIAEHV 470
Cdd:cd14610 274 TAVAEEV 280
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 267-463 2.76e-13

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: 68.65  E-value: 2.76e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 267 YIHANWVDLNSSK---KAILTQLPLSHTASDFWQMIIDQkiKCVLLIMtdgeFNKFGGNSVFPQNQDFLKFEDRFIRV-G 342
Cdd:cd17658   1 YINASLVETPASEslpKFIATQGPLPHTFEDFWEMVIQQ--RCPVIIM----LTRLVDNYSTAKCADYFPAEENESREfG 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 343 EFkqVELGKGWN-------LKVLSVS-NGTYKTFIHVHH--YKNWPHGSIPSDVKQIWQVqsYLRKYT---DGHPPVYMS 409
Cdd:cd17658  75 RI--SVTNKKLKhsqhsitLRVLEVQyIESEEPPLSVLHiqYPEWPDHGVPKDTRSVREL--LKRLYGippSAGPIVVHC 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17539216 410 MSGCGRAGTF-ALFETAHMSLHNEQPSLNMVKCLENVRNGRLHSVQNLSQFSVVY 463
Cdd:cd17658 151 SAGIGRTGAYcTIHNTIRRILEGDMSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 267-468 3.52e-13

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: 68.55  E-value: 3.52e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 267 YIHANWVDLNSSKKA---ILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEFNKFGGNSVFPQN-QDFLKFEDRFiRVG 342
Cdd:cd14538   1 YINASHIRIPVGGDTyhyIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSlNKPLICGGRL-EVS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 343 EFKQVELgKGWNLKVLSVSNGTYKTFIHVHH--YKNWPHGSIPSDVKQIWQVQSYLRKYTDGHPPVYMSMSGCGRAGTFA 420
Cdd:cd14538  80 LEKYQSL-QDFVIRRISLRDKETGEVHHITHlnFTTWPDHGTPQSADPLLRFIRYMRRIHNSGPIVVHCSAGIGRTGVLI 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 17539216 421 LFETAHMSLHNEQP--SLNMVKCLENVRNGRlhsVQNLSQFSVVYTLIAE 468
Cdd:cd14538 159 TIDVALGLIERDLPfdIQDIVKDLREQRQGM---IQTKDQYIFCYKACLE 205
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 267-463 5.23e-13

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: 67.79  E-value: 5.23e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 267 YIHANWVD--LNSSKKAILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEFNKFGGNSVFPQNQ-DFLKFEDrfIRVgE 343
Cdd:cd14539   1 YINASLIEdlTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERgQALVYGA--ITV-S 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 344 FKQVELGKGWNLKVLSVSNGTYK---TFIHVhHYKNWPHGSIPSDVKQ----IWQVQSYLRKYTDGHPPVYMSMS-GCGR 415
Cdd:cd14539  78 LQSVRTTPTHVERIISIQHKDTRlsrSVVHL-QFTTWPELGLPDSPNPllrfIEEVHSHYLQQRSLQTPIVVHCSsGVGR 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 17539216 416 AGTFALFETAHMSLHNEQPSLNMVKCLENVRNGRLHSVQNLSQFSVVY 463
Cdd:cd14539 157 TGAFCLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 243-471 6.04e-13

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 68.92  E-value: 6.04e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 243 NMDKNRFVDVICMDHSRVKL------TDSSYIHANWVD-LNSSKKAILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGE 315
Cdd:cd14633  40 NRMKNRYGNIIAYDHSRVRLqpiegeTSSDYINGNYIDgYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVE 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 316 FNKFGGNSVFPQNQDFLkfedRFIRVgEFKQVELGKGWNLKVLSVSN-GTYKTF-IHVHHYKNWPHGSIPSDVKQIWqvq 393
Cdd:cd14633 120 VGRVKCCKYWPDDTEIY----KDIKV-TLIETELLAEYVIRTFAVEKrGVHEIReIRQFHFTGWPDHGVPYHATGLL--- 191

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 394 SYLRKYTDGHPP-----VYMSMSGCGRAGTFALFETAhMSLHNEQPSLNMVKCLENVRNGRLHSVQNLSQFSVVYTLIAE 468
Cdd:cd14633 192 GFVRQVKSKSPPnagplVVHCSAGAGRTGCFIVIDIM-LDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270


                ...
gi 17539216 469 HVL 471
Cdd:cd14633 271 ACL 273
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 267-459 6.66e-13

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: 67.38  E-value: 6.66e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 267 YIHANWVD-LNSSKKAILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEFNKFGGNSVFPQN--QDFlkfedRFIRVgE 343
Cdd:cd14549   1 YINANYVDgYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEgtETY-----GNIQV-T 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 344 FKQVELGKGWNLKVLSVSNGTYKTFIHVH--------HYKNWP-HGsIPSDVkqiWQVQSYLRKYTDGHPP------VYM 408
Cdd:cd14549  75 LLSTEVLATYTVRTFSLKNLKLKKVKGRSservvyqyHYTQWPdHG-VPDYT---LPVLSFVRKSSAANPPgagpivVHC 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 17539216 409 SmSGCGRAGTFALFETAHMSLHNEQpSLNMVKCLENVRNGRLHSVQNLSQF 459
Cdd:cd14549 151 S-AGVGRTGTYIVIDSMLQQIQDKG-TVNVFGFLKHIRTQRNYLVQTEEQY 199
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 267-468 1.65e-12

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: 66.57  E-value: 1.65e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 267 YIHANWVDLNSSKKA-ILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEFNKFGGNSVFPqNQDFLKFEDRFIrvgEFK 345
Cdd:cd14622   2 YINASFIDGYRQKDYfIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWP-SEGSVTHGEITI---EIK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 346 QVELGKGWNLK--VLSVSNGTYKTFIHVHHYKNWPHGSIPSDVKQIWQVQSYLRKY---TDGHPPVYMSMSGCGRAGTFA 420
Cdd:cd14622  78 NDTLLETISIRdfLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQqqqTGNHPIVVHCSAGAGRTGTFI 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 17539216 421 LFETAHMSLHNEQpSLNMVKCLENVRNGRLHSVQNLSQFSVVYTLIAE 468
Cdd:cd14622 158 ALSNILERVKAEG-LLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQD 204
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 267-433 1.67e-12

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: 66.19  E-value: 1.67e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 267 YIHANWVD-LNSSKKAILTQLPLSHTASDFWQMIIDQKIKCVLLImTDGEfnkfggnsvfpQNQDFLKF---EDRFIRVG 342
Cdd:cd14550   1 YINASYLQgYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVML-TDNE-----------LNEDEPIYwptKEKPLECE 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 343 EFKqVELGKGWNLKVLSVSNGTYKTFI----------HVHHYK--NWPH--GSIPSDVKQIWQVQSyLRKYTDGhPPVYM 408
Cdd:cd14550  69 TFK-VTLSGEDHSCLSNEIRLIVRDFIlestqddyvlEVRQFQcpSWPNpcSPIHTVFELINTVQE-WAQQRDG-PIVVH 145

                       170       180
                ....*....|....*....|....*
gi 17539216 409 SMSGCGRAGTFALFETAHMSLHNEQ 433
Cdd:cd14550 146 DRYGGVQAATFCALTTLHQQLEHES 170
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 243-470 1.29e-11

catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type tyrosine-protein phosphatase D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 65.14  E-value: 1.29e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 243 NMDKNRFVDVICMDHSRVKLT------DSSYIHANWVDLNSSKKA-ILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGE 315
Cdd:cd14624  47 NKPKNRYANVIAYDHSRVLLSaiegipGSDYINANYIDGYRKQNAyIATQGALPETFGDFWRMIWEQRSATVVMMTKLEE 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 316 FNKFGGNSVFPQNQdflKFEDRFIRVGEFKQVELGKGWNLKVLSVSNGTY-KTFIHVHHYKNWPHGSIPSDVKQIWqvqS 394
Cdd:cd14624 127 RSRVKCDQYWPSRG---TETYGLIQVTLLDTVELATYCVRTFALYKNGSSeKREVRQFQFTAWPDHGVPEHPTPFL---A 200

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 395 YLRKYTDGHPP-----VYMSMSGCGRAGTFALFETAHMSLHNEQpSLNMVKCLENVRNGRLHSVQNLSQFSVVYTLIAEH 469
Cdd:cd14624 201 FLRRVKTCNPPdagpmVVHCSAGVGRTGCFIVIDAMLERIKHEK-TVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEA 279


                .
gi 17539216 470 V 470
Cdd:cd14624 280 V 280
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 247-459 2.24e-11

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: 63.39  E-value: 2.24e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 247 NRFVDVICMDHSRVKLTD------SSYIHANWVD-LNSSKKAILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEFNKF 319
Cdd:cd14616   1 NRFPNIKPYNNNRVKLIAdagvpgSDYINASYISgYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 320 GGNSVFPQ-NQDFLKFEDRFI-RVGEFKQVElgkgWNLKVLSVS-NGTYKTFIHVhHYKNWPHGSIPSDVKQIWQVQSYL 396
Cdd:cd14616  81 RCHQYWPEdNKPVTVFGDIVItKLMEDVQID----WTIRDLKIErHGDYMMVRQC-NFTSWPEHGVPESSAPLIHFVKLV 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17539216 397 R--KYTDGHPPVYMSMSGCGRAGTFALFEtaHMSLH-NEQPSLNMVKCLENVRNGRLHSVQNLSQF 459
Cdd:cd14616 156 RasRAHDNTPMIVHCSAGVGRTGVFIALD--HLTQHiNDHDFVDIYGLVAELRSERMCMVQNLAQY 219
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 246-471 4.80e-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: 4.80e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 246 KNRFVDVICMDHSRVKLTD-------SSYIHANWVDL--NSSKKAILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEF 316
Cdd:cd14613  28 KNRYKTILPNPHSRVCLTSpdqddplSSYINANYIRGygGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 317 NKfGGNSVFPQNQdfLKFEDRFIRVgefKQVELGKGWNLKVLSVSNGTYKTFIHVHHYKNWPHGSIPSDVKQIWQ----V 392
Cdd:cd14613 108 NE-KCTEYWPEEQ--VTYEGIEITV---KQVIHADDYRLRLITLKSGGEERGLKHYWYTSWPDQKTPDNAPPLLQlvqeV 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 393 QSYLRKYTDGHPPVYMSMS-GCGRAGTFALFETAHMSLHNEQpSLNMVKCLENVRNGRLHSVQNLSQFSVVYtliaeHVL 471
Cdd:cd14613 182 EEARQQAEPNCGPVIVHCSaGIGRTGCFIATSICCKQLRNEG-VVDILRTTCQLRLDRGGMIQTCEQYQFVH-----HVL 255
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 265-471 5.74e-11

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: 62.35  E-value: 5.74e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 265 SSYIHANWVD-LNSSKKAILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEFNKFGGNSVFPQNQDFLkfedrfirvGE 343
Cdd:cd14631  13 SDYINANYIDgYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEVY---------GD 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 344 FK----QVELGKGWNLKVLSVSNGTYKTFIHVH--HYKNWPHGSIPSDVKQIWqvqSYLRKYTDGHPP-----VYMSMSG 412
Cdd:cd14631  84 FKvtcvEMEPLAEYVVRTFTLERRGYNEIREVKqfHFTGWPDHGVPYHATGLL---SFIRRVKLSNPPsagpiVVHCSAG 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17539216 413 CGRAGTFALFETAhMSLHNEQPSLNMVKCLENVRNGRLHSVQNLSQFSVVYTLIAEHVL 471
Cdd:cd14631 161 AGRTGCYIVIDIM-LDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 218
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 267-462 9.72e-11

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: 61.50  E-value: 9.72e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 267 YIHANWVDLNSSKKAILTQL-----PLSHTASDFWQMIIDQKIKCVLLIMTDGEFNKFGGNSVFPQNQDFLKFedrfirv 341
Cdd:cd14601   2 YINANYINMEIPSSSIINRYiacqgPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSY------- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 342 GEFK---QVELGKGW----NLKVLSVSNGTYKTFIHVhHYKNWPHGSIPSDVKQIWQVQSYLRKYTDGHP-PVYMSMS-G 412
Cdd:cd14601  75 GGFQvtcHSEEGNPAyvfrEMTLTNLEKNESRPLTQI-QYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDePVVVHCSaG 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 17539216 413 CGRAGTFALFETAHMSLHNEQP--SLNMVKCLenvRNGRLHSVQNLSQFSVV 462
Cdd:cd14601 154 IGRTGVLITMETAMCLIECNQPvyPLDIVRTM---RDQRAMMIQTPSQYRFV 202
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 247-459 2.14e-10

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. YopH is an essential virulence determinant of the pathogenic bacterium by dephosphorylating several focal adhesion proteins including p130Cas in human epithelial cells, resulting in the disruption of focal adhesions and cell detachment from the extracellular matrix. It contains an N-terminal domain that contains signals required for TTSS-mediated delivery of YopH into host cells and a C-terminal catalytic PTP domain.


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 60.49  E-value: 2.14e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 247 NRFVDVicmdHSRVKLTDSSYIHANWVDLNSSKKAILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEFNKFGGNSVFP 326
Cdd:cd14559   1 NRFTNI----QTRVSTPVGKNLNANRVQIGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYFR 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 327 QNQDF--LKFEDRFIRVGEFKQVELGKGWNLKvLSVSNGTYKtfIHVHHYKNWP-HGSIPSDV----------------K 387
Cdd:cd14559  77 QSGTYgsVTVKSKKTGKDELVDGLKADMYNLK-ITDGNKTIT--IPVVHVTNWPdHTAISSEGlkeladlvnksaeekrN 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17539216 388 QIWQVQSYLRKYTDGHPPVYMSMSGCGRAGTFAlfetAHMSLHNEQPSLN---MVKCLENVRNGrlHSVQNLSQF 459
Cdd:cd14559 154 FYKSKGSSAINDKNKLLPVIHCRAGVGRTGQLA----AAMELNKSPNNLSvedIVSDMRTSRNG--KMVQKDEQL 222
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 249-468 2.74e-10

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: 60.34  E-value: 2.74e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 249 FVDVICMDHSRVKLTD------SSYIHANWVDLNSSK-KAILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEFNKFGG 321
Cdd:cd14620   1 YPNILPYDHSRVILSQldgipcSDYINASYIDGYKEKnKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 322 NSVFPQN------------QDFLKFEDRFIRvgEF-KQVELGKGWNLKVLsvsngtyktfIHVHHYKNWPHGSIP-SDVK 387
Cdd:cd14620  81 YQYWPDQgcwtygnirvavEDCVVLVDYTIR--KFcIQPQLPDGCKAPRL----------VTQLHFTSWPDFGVPfTPIG 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 388 QIwqvqSYLRKYTDGHP----PVYMSMS-GCGRAGTFALFEtAHMSLHNEQPSLNMVKCLENVRNGRLHSVQNLSQFSVV 462
Cdd:cd14620 149 ML----KFLKKVKSVNPvhagPIVVHCSaGVGRTGTFIVID-AMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFI 223


                ....*.
gi 17539216 463 YTLIAE 468
Cdd:cd14620 224 YQALLE 229
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 267-463 3.37e-10

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: 59.73  E-value: 3.37e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 267 YIHANWVDLNSSKKA-ILTQLPLSHTASDFWQMIIDQkiKCVLLIMTdgefnkfggNSVFPQNQDFLKF--EDRFIRVGE 343
Cdd:cd14556   1 YINAALLDSYKQPAAfIVTQHPLPNTVTDFWRLVYDY--GCTSIVML---------NQLDPKDQSCPQYwpDEGSGTYGP 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 344 FkQVEL-----GKGWNLKVLSVSNGTY----KTFIHVHHYKNWP-HGSIPSDVKQIWQVQSYLRKY---TDGHPPVYMSM 410
Cdd:cd14556  70 I-QVEFvsttiDEDVISRIFRLQNTTRpqegYRMVQQFQFLGWPrDRDTPPSKRALLKLLSEVEKWqeqSGEGPIVVHCL 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17539216 411 SGCGRAGTFAlfeTAHMSLH--NEQPSLNMVKCLENVRNGRLHSVQNLSQFSVVY 463
Cdd:cd14556 149 NGVGRSGVFC---AISSVCEriKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 243-463 1.30e-09

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: 58.69  E-value: 1.30e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 243 NMDKNRFVDVICMDHSRVKLT------DSSYIHANWVDLNSSKKA-ILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGE 315
Cdd:cd14554   6 NKFKNRLVNILPYESTRVCLQpirgveGSDYINASFIDGYRQRGAyIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLRE 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 316 FNKFGGNSVFPQnqdflkfeDRFIRVG----------EFKQVELGKgwnLKVLSVSNGTYKTfIHVHHYKNWPHGSIPSD 385
Cdd:cd14554  86 MGREKCHQYWPA--------ERSARYQyfvvdpmaeyNMPQYILRE---FKVTDARDGQSRT-VRQFQFTDWPEQGVPKS 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 386 ----VKQIWQVQSYLRKYTDGHPPVYMSMSGCGRAGTFALFETAHMSLHNEQpSLNMVKCLENVRNGRLHSVQNLSQFSV 461
Cdd:cd14554 154 gegfIDFIGQVHKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEG-VVDVFQTVKLLRTQRPAMVQTEDQYQF 232


                ..
gi 17539216 462 VY 463
Cdd:cd14554 233 CY 234
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 243-470 2.84e-09

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: 58.20  E-value: 2.84e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 243 NMDKNRFVDVICMDHSRVKLT------DSSYIHANWVDLNSSKKA-ILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGE 315
Cdd:cd14629  53 NKFKNRLVNIMPYELTRVCLQpirgveGSDYINASFIDGYRQQKAyIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLRE 132

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 316 FNKFGGNSVFPQnqdflkfeDRFIRVGEFkQVELGKGWNL--------KVLSVSNGTYKTfIHVHHYKNWPHGSIPSD-- 385
Cdd:cd14629 133 MGREKCHQYWPA--------ERSARYQYF-VVDPMAEYNMpqyilrefKVTDARDGQSRT-IRQFQFTDWPEQGVPKTge 202

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 386 --VKQIWQVQSYLRKYTDGHPPVYMSMSGCGRAGTFALFETAHMSLHNEQpSLNMVKCLENVRNGRLHSVQNLSQFSVVY 463
Cdd:cd14629 203 gfIDFIGQVHKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEG-VVDMFQTVKTLRTQRPAMVQTEDQYQLCY 281


                ....*..
gi 17539216 464 TLIAEHV 470
Cdd:cd14629 282 RAALEYL 288
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 223-470 6.18e-09

PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type tyrosine-protein phosphatase-like D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 57.05  E-value: 6.18e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 223 EFEKVSGYlPPHISKnhFVS-----NMDKNRFVDVICMDHSRVKLT------DSSYIHANWVDLNSSKKA-ILTQLPLSH 290
Cdd:cd14628  30 EFKRLASS-KAHTSR--FISanlpcNKFKNRLVNIMPYESTRVCLQpirgveGSDYINASFIDGYRQQKAyIATQGPLAE 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 291 TASDFWQMIIDQKIKCVLLIMTDGEFNKFGGNSVFPQnqdflkfeDRFIRVGEFkQVELGKGWNL--------KVLSVSN 362
Cdd:cd14628 107 TTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPA--------ERSARYQYF-VVDPMAEYNMpqyilrefKVTDARD 177

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 363 GTYKTfIHVHHYKNWPHGSIPSD----VKQIWQVQSYLRKYTDGHPPVYMSMSGCGRAGTFALFETAHMSLHNEQpSLNM 438
Cdd:cd14628 178 GQSRT-VRQFQFTDWPEQGVPKSgegfIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEG-VVDI 255

                       250       260       270
                ....*....|....*....|....*....|..
gi 17539216 439 VKCLENVRNGRLHSVQNLSQFSVVYTLIAEHV 470
Cdd:cd14628 256 FQTVKMLRTQRPAMVQTEDQYQFCYRAALEYL 287
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 267-464 9.95e-09

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: 55.22  E-value: 9.95e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 267 YIHANWVD-LNSSKKAILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEFNKFGGNSVFPQ-NQDFLKFEDRFIRVGEF 344
Cdd:cd14557   1 YINASYIDgFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSmEEGSRAFGDVVVKINEE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 345 KQVelgKGWNLKVLSVSNGTYKTFIH-VHH--YKNWPHGSIPSDVKQIWQVQSYLRKYTD--GHPPVYMSMSGCGRAGTF 419
Cdd:cd14557  81 KIC---PDYIIRKLNINNKKEKGSGReVTHiqFTSWPDHGVPEDPHLLLKLRRRVNAFNNffSGPIVVHCSAGVGRTGTY 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 17539216 420 ALFETAHMSLHNEQpSLNMVKCLENVRNGRLHSVQNLSQFSVVYT 464
Cdd:cd14557 158 IGIDAMLEGLEAEG-RVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 223-470 1.47e-08

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


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 55.89  E-value: 1.47e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 223 EFEKVSGYlPPHISKnhFVS-----NMDKNRFVDVICMDHSRVKLT------DSSYIHANWVDLNSSKKA-ILTQLPLSH 290
Cdd:cd14627  31 EFKRLANS-KAHTSR--FISanlpcNKFKNRLVNIMPYETTRVCLQpirgveGSDYINASFIDGYRQQKAyIATQGPLAE 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 291 TASDFWQMIIDQKIKCVLLIMTDGEFNKFGGNSVFPQnqdflkfeDRFIRVGEFkQVELGKGWNL--------KVLSVSN 362
Cdd:cd14627 108 TTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPA--------ERSARYQYF-VVDPMAEYNMpqyilrefKVTDARD 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 363 GTYKTfIHVHHYKNWPHGSIPSD----VKQIWQVQSYLRKYTDGHPPVYMSMSGCGRAGTFALFETAHMSLHNEQpSLNM 438
Cdd:cd14627 179 GQSRT-VRQFQFTDWPEQGVPKSgegfIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEG-VVDI 256

                       250       260       270
                ....*....|....*....|....*....|..
gi 17539216 439 VKCLENVRNGRLHSVQNLSQFSVVYTLIAEHV 470
Cdd:cd14627 257 FQTVKMLRTQRPAMVQTEDEYQFCYQAALEYL 288
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 267-468 2.96e-08

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: 53.98  E-value: 2.96e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 267 YIHANWVDL-NSSKKA--ILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEFNKFGGNSVFP-QNQDFLKFEDRFIRVG 342
Cdd:cd14596   1 YINASYITMpVGEEELfyIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPeTLQEPMELENYQLRLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 343 EFKQVELGKGWNLKVLSVSNGTYKTFIHVhHYKNWPHGSIPSDVKQIWQVQSYLRKYTDGHPPVYMSMSGCGRAGTFALF 422
Cdd:cd14596  81 NYQALQYFIIRIIKLVEKETGENRLIKHL-QFTTWPDHGTPQSSDQLVKFICYMRKVHNTGPIVVHCSAGIGRAGVLICV 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 17539216 423 ETAhMSLHNEQPSLNMVKCLENVRNGRLHSVQNLSQFSVVYTLIAE 468
Cdd:cd14596 160 DVL-LSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLE 204
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 246-419 5.90e-08

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: 53.38  E-value: 5.90e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 246 KNRFVDVICMDHSRVKLTD-------SSYIHANWVD--LNSSKKAILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEF 316
Cdd:cd14611   2 KNRYKTILPNPHSRVCLKPknsndslSTYINANYIRgyGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 317 NKfggNSV--FPQNQD-FLKFEDRFIRVGEFKQvelgkgWNLKVLSVSNGTYKTFIHVHHYKNWPHGSIPSDVKQIWQ-- 391
Cdd:cd14611  82 NE---KCVlyWPEKRGiYGKVEVLVNSVKECDN------YTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQlm 152

                       170       180       190
                ....*....|....*....|....*....|
gi 17539216 392 --VQSYLRKYTDGHPPVYMSMSGCGRAGTF 419
Cdd:cd14611 153 ldVEEDRLASPGRGPVVVHCSAGIGRTGCF 182
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 246-419 1.13e-07

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: 52.92  E-value: 1.13e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 246 KNRFVDVICMDHSRVKL-------TDSSYIHANWV-DLNSSKKA-ILTQLPLSHTASDFWQMIIDQkiKCVLLIM-TDGE 315
Cdd:cd14612  18 KDRYKTILPNPQSRVCLrragsqeEEGSYINANYIrGYDGKEKAyIATQGPMLNTVSDFWEMVWQE--ECPIIVMiTKLK 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 316 FNKFGGNSVFPQNQD-FLKFEdrfIRVGEFKQVElgkGWNLKVLSVSNGTYKTfiHVHHY--KNWPHGSIPSDVKQ---- 388
Cdd:cd14612  96 EKKEKCVHYWPEKEGtYGRFE---IRVQDMKECD---GYTIRDLTIQLEEESR--SVKHYwfSSWPDHQTPESAGPllrl 167

                       170       180       190
                ....*....|....*....|....*....|.
gi 17539216 389 IWQVQSYLRKYTDGHPPVYMSMSGCGRAGTF 419
Cdd:cd14612 168 VAEVEESRQTAASPGPIVVHCSAGIGRTGCF 198
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 267-464 2.53e-07

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: 51.24  E-value: 2.53e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 267 YIHANWVD-LNSSKKAILTQLPLSHTASDFWQMIIDQKIKcVLLIMTDgefNKFGGnsvfpQNQDFLKFEDRFIRVG--- 342
Cdd:cd14558   1 YINASFIDgYWGPKSLIATQGPLPDTIADFWQMIFQKKVK-VIVMLTE---LKEGD-----QEQCAQYWGDEKKTYGdie 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 343 -EFKQVELGKGWNLKVLSVSNGTYKTFIHV--HHYKNWPHGSIPSD-------VKQIWQVQSYLRKYTDGHPPVYMSMS- 411
Cdd:cd14558  72 vELKDTEKSPTYTVRVFEITHLKRKDSRTVyqYQYHKWKGEELPEKpkdlvdmIKSIKQKLPYKNSKHGRSVPIVVHCSd 151

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 412 GCGRAGTFA----LFETAHMSlhneqpslNMVKCLENVRN---GRLHSVQNLSQFSVVYT 464
Cdd:cd14558 152 GSSRTGIFCalwnLLESAETE--------KVVDVFQVVKAlrkQRPGMVSTLEQYQFLYD 203
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 267-463 3.38e-07

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: 50.68  E-value: 3.38e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 267 YIHANWVDLNSSK-KAILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEFNKFGGNSVFPQN------------QDFLK 333
Cdd:cd14551   1 YINASYIDGYQEKnKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQgcwtygnlrvrvEDTVV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 334 FEDRFIRVGEFKQvelgkgwnlkVLSVSNGTYKTFIHVHHYKNWPHGSIPSD----VKQIWQVQSYLRKYtDGhPPVYMS 409
Cdd:cd14551  81 LVDYTTRKFCIQK----------VNRGIGEKRVRLVTQFHFTSWPDFGVPFTpigmLKFLKKVKSANPPR-AG-PIVVHC 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17539216 410 MSGCGRAGTFALFETAHMSLHNEQpSLNMVKCLENVRNGRLHSVQNLSQFSVVY 463
Cdd:cd14551 149 SAGVGRTGTFIVIDAMLDMMHAEG-KVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 267-468 1.23e-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: 46.22  E-value: 1.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 267 YIHANWVDLNSSKKA-ILTQLPLSHTASDFWQMIIDqkIKCVLLIMtdgeFNKFGGNSVFPQNQDflkfEDRFIRVG--- 342
Cdd:cd14635   1 YINAALMDSYKQPSAfIVTQHPLPNTVKDFWRLVLD--YHCTSIVM----LNDVDPAQLCPQYWP----ENGVHRHGpiq 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 343 -EFKQVELGKGWNLKVLSVSNGT-----YKtFIHVHHYKNWP-HGSIP----SDVKQIWQVQSYLRKYTDGH-PPVYMSM 410
Cdd:cd14635  71 vEFVSADLEEDIISRIFRIYNAArpqdgYR-MVQQFQFLGWPmYRDTPvskrSFLKLIRQVDKWQEEYNGGEgRTVVHCL 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17539216 411 SGCGRAGTF-ALFETAHMSLHneQPSLNMVKCLENVRNGRLHSVQNLSQFSVVYTLIAE 468
Cdd:cd14635 150 NGGGRSGTFcAISIVCEMLRH--QRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 267-466 3.76e-05

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: 44.60  E-value: 3.76e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 267 YIHANWV-DLNSSKKAILTQLPLSHTASDFWQMIIDQKIKCVLLI-----MTDGEFnkfggnSVFPQNQDFLKFEDRFIR 340
Cdd:cd17669   1 YINASYImGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLpdgqnMAEDEF------VYWPNKDEPINCETFKVT 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216 341 VGEFKQVELGKGWNLK----VLSVSNGTYktFIHVHHYK--NWPHGSIPsdVKQIWQVQSYLRKYT---DGhPPVYMSMS 411
Cdd:cd17669  75 LIAEEHKCLSNEEKLIiqdfILEATQDDY--VLEVRHFQcpKWPNPDSP--ISKTFELISIIKEEAanrDG-PMIVHDEH 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17539216 412 GCGRAGTFALFETAHMSLHNEQpSLNMVKCLENVRNGRLHSVQNLSQFSVVYTLI 466
Cdd:cd17669 150 GGVTAGTFCALTTLMHQLEKEN-SVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 267-316 4.42e-04

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: 41.59  E-value: 4.42e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17539216 267 YIHANWV-DLNSSKKAILTQLPLSHTASDFWQMIIDQKIKCVLLI-----MTDGEF 316
Cdd:cd17670   1 YINASYImGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdnqgLAEDEF 56
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 257-470 4.43e-03

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 39.18  E-value: 4.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216  257 HSRVKL-TDSSYIHANWVD-LNSSKKAILTQLPLSHTASDFWQMIIDQKIKCVLLIMTDGEFNKFggNSVFPQNQDFLKF 334
Cdd:PHA02740  67 HRRIKLfNDEKVLDARFVDgYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADKKCF--NQFWSLKEGCVIT 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539216  335 EDRFiRVGEFKQVeLGKGWNLKVLSVSN--GTYKTFIHvHHYKNWPHGSIPSDVK-------QIWQVQSYLRKY-TDGH- 403
Cdd:PHA02740 145 SDKF-QIETLEII-IKPHFNLTLLSLTDkfGQAQKISH-FQYTAWPADGFSHDPDafidffcNIDDLCADLEKHkADGKi 221

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17539216  404 -PPVYMSMSGCGRAGTFALFETAhMSLHNEQPSLNMVKCLENVRNGRLHSVQNLSQFSVVYTLIAEHV 470
Cdd:PHA02740 222 aPIIIDCIDGISSSAVFCVFDIC-ATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYL 288
 
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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