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Conserved domains on  [gi|13677220|ref|NP_109595|]
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receptor-type tyrosine-protein phosphatase O isoform d [Homo sapiens]

Protein Classification

protein-tyrosine phosphatase family protein; phosphatase PAP2/dual specificity phosphatase family protein( domain architecture ID 12998700)

cys-based protein-tyrosine phosphatase (PTP) family protein may be a PTP or a dual-specificity phosphatase (DUSP or DSP), and may catalyze the dephosphorylation of target phosphoproteins at tyrosine or tyrosine and serine/threonine residues, respectively| bifunctional phosphatase PAP2/dual specificity phosphatase (DSP) family protein containing a C-terminal DSP domain that may dephosphorylate phosphotyrosine, phosphoserine, and phosphothreonine residues in target proteins, and an N-terminal phosphatase PAP2 domain that may be a histidine phosphatase that catalyzes the dephosphorylation of phospholipids

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
112-356 0e+00

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: 556.04  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 112 DIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 191
Cdd:cd14614   1 DIPHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 192 QIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMISEEEQDDWACRHFRINYADEMQDVMHFNYTAWPDHGVPTANA 271
Cdd:cd14614  81 QIIVMLTQCNEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPTANA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 272 AESILQFVHMVRQQATKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 351
Cdd:cd14614 161 AESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240

                ....*
gi 13677220 352 CVQLM 356
Cdd:cd14614 241 CVQLM 245
 
Name Accession Description Interval E-value
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
112-356 0e+00

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: 556.04  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 112 DIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 191
Cdd:cd14614   1 DIPHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 192 QIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMISEEEQDDWACRHFRINYADEMQDVMHFNYTAWPDHGVPTANA 271
Cdd:cd14614  81 QIIVMLTQCNEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPTANA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 272 AESILQFVHMVRQQATKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 351
Cdd:cd14614 161 AESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240

                ....*
gi 13677220 352 CVQLM 356
Cdd:cd14614 241 CVQLM 245
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
98-353 1.94e-120

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 348.88  E-value: 1.94e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220     98 KFSLQFEELKLIGLDIPHFA-ADLPLNRCKNRYTNILPYDFSRVRLvSMNEEEGADYINANYIPGYNSPQEYIATQGPLP 176
Cdd:smart00194   1 GLEEEFEKLDRLKPDDESCTvAAFPENRDKNRYKDVLPYDHTRVKL-KPPPGEGSDYINASYIDGPNGPKAYIATQGPLP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220    177 ETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPFTE-EPIAYGDITVEMISEEEQDDWACRHFRINYAD--EMQDV 253
Cdd:smart00194  80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGcsETRTV 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220    254 MHFNYTAWPDHGVPtaNAAESILQFVHMVRQQATKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMR 333
Cdd:smart00194 160 THYHYTNWPDHGVP--ESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELR 237
                          250       260
                   ....*....|....*....|
gi 13677220    334 SYRMSMVQTEEQYIFIHQCV 353
Cdd:smart00194 238 SQRPGMVQTEEQYIFLYRAI 257
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
123-353 1.11e-110

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 323.04  E-value: 1.11e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220   123 NRCKNRYTNILPYDFSRVRLvsMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNE 202
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKL--TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220   203 KRRVKCDHYWPFT-EEPIAYGDITVEMISEEEQ-DDWACRHFRINYADEMQD--VMHFNYTAWPDHGVPTANAaeSILQF 278
Cdd:pfam00102  79 KGREKCAQYWPEEeGESLEYGDFTVTLKKEKEDeKDYTVRTLEVSNGGSEETrtVKHFHYTGWPDHGVPESPN--SLLDL 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13677220   279 VHMVRQ-QATKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 353
Cdd:pfam00102 157 LRKVRKsSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
122-349 2.20e-54

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 180.67  E-value: 2.20e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 122 LNRCK-NRYTNILPYDFSRVRlvsmneeEGADYINANYIPGYNsPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQC 200
Cdd:COG5599  40 INGSPlNRFRDIQPYKETALR-------ANLGYLNANYIQVIG-NHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASD 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 201 NE--KRRVKCDHYWPFTEEPIAYgDITVEMISEEE-QDDWACRHFRINYAD---EMQDVMHFNYTAWPDHGVPTANAAES 274
Cdd:COG5599 112 DEisKPKVKMPVYFRQDGEYGKY-EVSSELTESIQlRDGIEARTYVLTIKGtgqKKIEIPVLHVKNWPDHGAISAEALKN 190
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13677220 275 ILQFVHMVRQQATKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHE--FVDILGLVSEMRSYR-MSMVQTEEQYIFI 349
Cdd:COG5599 191 LADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMVQTSEQLDVL 268
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
123-353 4.66e-42

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 149.38  E-value: 4.66e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220  123 NRCKNRYTNILPYDFSRVRLVSmnEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNE 202
Cdd:PHA02742  52 NMKKCRYPDAPCFDRNRVILKI--EDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220  203 KRRVKCDHYW-PFTEEPIAYGDITVEMISEEEQDDWACRHFRINYAD--EMQDVMHFNYTAWPDHGVPTanAAESILQFV 279
Cdd:PHA02742 130 DGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNtgASLDIKHFAYEDWPHGGLPR--DPNKFLDFV 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220  280 HMVRQQATKS-----------KGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 348
Cdd:PHA02742 208 LAVREADLKAdvdikgenivkEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIF 287

                 ....*
gi 13677220  349 IHQCV 353
Cdd:PHA02742 288 CYFIV 292
 
Name Accession Description Interval E-value
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
112-356 0e+00

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: 556.04  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 112 DIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 191
Cdd:cd14614   1 DIPHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 192 QIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMISEEEQDDWACRHFRINYADEMQDVMHFNYTAWPDHGVPTANA 271
Cdd:cd14614  81 QIIVMLTQCNEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPTANA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 272 AESILQFVHMVRQQATKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 351
Cdd:cd14614 161 AESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240

                ....*
gi 13677220 352 CVQLM 356
Cdd:cd14614 241 CVQLM 245
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
128-351 6.88e-149

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: 419.45  E-value: 6.88e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 128 RYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVK 207
Cdd:cd14548   1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 208 CDHYWPFTEEPIAYGDITVEMISEEEQDDWACRHFRINYADEMQDVMHFNYTAWPDHGVPtaNAAESILQFVHMVRQQAT 287
Cdd:cd14548  81 CDHYWPFDQDPVYYGDITVTMLSESVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVP--EAPDSLLRFVRLVRDYIK 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13677220 288 KSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 351
Cdd:cd14548 159 QEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
98-353 1.94e-120

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 348.88  E-value: 1.94e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220     98 KFSLQFEELKLIGLDIPHFA-ADLPLNRCKNRYTNILPYDFSRVRLvSMNEEEGADYINANYIPGYNSPQEYIATQGPLP 176
Cdd:smart00194   1 GLEEEFEKLDRLKPDDESCTvAAFPENRDKNRYKDVLPYDHTRVKL-KPPPGEGSDYINASYIDGPNGPKAYIATQGPLP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220    177 ETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPFTE-EPIAYGDITVEMISEEEQDDWACRHFRINYAD--EMQDV 253
Cdd:smart00194  80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGcsETRTV 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220    254 MHFNYTAWPDHGVPtaNAAESILQFVHMVRQQATKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMR 333
Cdd:smart00194 160 THYHYTNWPDHGVP--ESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELR 237
                          250       260
                   ....*....|....*....|
gi 13677220    334 SYRMSMVQTEEQYIFIHQCV 353
Cdd:smart00194 238 SQRPGMVQTEEQYIFLYRAI 257
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
123-353 1.11e-110

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 323.04  E-value: 1.11e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220   123 NRCKNRYTNILPYDFSRVRLvsMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNE 202
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKL--TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220   203 KRRVKCDHYWPFT-EEPIAYGDITVEMISEEEQ-DDWACRHFRINYADEMQD--VMHFNYTAWPDHGVPTANAaeSILQF 278
Cdd:pfam00102  79 KGREKCAQYWPEEeGESLEYGDFTVTLKKEKEDeKDYTVRTLEVSNGGSEETrtVKHFHYTGWPDHGVPESPN--SLLDL 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13677220   279 VHMVRQ-QATKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 353
Cdd:pfam00102 157 LRKVRKsSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
127-351 3.07e-102

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: 301.45  E-value: 3.07e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 127 NRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRV 206
Cdd:cd14617   1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 207 KCDHYWPFTEEPIAYGDITVEMISEEEQDDWACRHFRINYADEMQD---VMHFNYTAWPDHGVPtaNAAESILQFVHMVR 283
Cdd:cd14617  81 KCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQLDAprlVRHFHYTVWPDHGVP--ETTQSLIQFVRTVR 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 284 Q--QATKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 351
Cdd:cd14617 159 DyiNRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
127-353 3.39e-101

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: 299.11  E-value: 3.39e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 127 NRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRV 206
Cdd:cd14619   1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 207 KCDHYWPFTEEPIAYGDITVEMISEEEQDDWACRHFRINYADEMQD--VMHFNYTAWPDHGVPTanAAESILQFVHMVRQ 284
Cdd:cd14619  81 KCEHYWPLDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTlsVRHFHFTAWPDHGVPS--STDTLLAFRRLLRQ 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13677220 285 --QATKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 353
Cdd:cd14619 159 wlDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCI 229
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
127-353 2.54e-99

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: 294.16  E-value: 2.54e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 127 NRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRV 206
Cdd:cd14618   1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 207 KCDHYWPFTEEPIAYGDITVEMISEEEQDDWACRHFRINYADEMQD--VMHFNYTAWPDHGVPTANAaeSILQFVHMVRQ 284
Cdd:cd14618  81 LCDHYWPSESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKErrVKHLHYTAWPDHGIPESTS--SLMAFRELVRE 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13677220 285 --QATKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 353
Cdd:cd14618 159 hvQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
121-353 3.85e-97

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: 288.91  E-value: 3.85e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 121 PLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQC 200
Cdd:cd14553   1 EVNKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 201 NEKRRVKCDHYWPfTEEPIAYGDITVEMISEEEQDDWACRHFRI--NYADEMQDVMHFNYTAWPDHGVPtaNAAESILQF 278
Cdd:cd14553  81 EERSRVKCDQYWP-TRGTETYGLIQVTLLDTVELATYTVRTFALhkNGSSEKREVRQFQFTAWPDHGVP--EHPTPFLAF 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13677220 279 VHMVRQQATKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 353
Cdd:cd14553 158 LRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDAL 232
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
127-353 1.93e-95

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: 284.02  E-value: 1.93e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 127 NRYTNILPYDFSRVRLVSMNEEEgADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRV 206
Cdd:cd14615   1 NRYNNVLPYDISRVKLSVQSHST-DDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 207 KCDHYWPfTEEPIAYGDITVEMISEEEQDDWACRHFRINYADEMQD--VMHFNYTAWPDHGVPtaNAAESILQFVHMVRQ 284
Cdd:cd14615  80 KCEEYWP-SKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESrtVRHFHFTSWPDHGVP--ETTDLLINFRHLVRE 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13677220 285 QATKS--KGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 353
Cdd:cd14615 157 YMKQNppNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCA 227
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
127-351 7.18e-95

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: 282.57  E-value: 7.18e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 127 NRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRV 206
Cdd:cd14616   1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 207 KCDHYWPFTEEPIA-YGDITVEMISEEEQDDWACRHFRINYADEMQDVMHFNYTAWPDHGVPTANAaeSILQFVHMVRQQ 285
Cdd:cd14616  81 RCHQYWPEDNKPVTvFGDIVITKLMEDVQIDWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSA--PLIHFVKLVRAS 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13677220 286 ATKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 351
Cdd:cd14616 159 RAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
153-351 2.81e-93

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: 277.63  E-value: 2.81e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 153 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWP-FTEEPIAYGDITVEMISE 231
Cdd:cd00047   1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPeEGGKPLEYGDITVTLVSE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 232 EEQDDWACRHFRINYAD--EMQDVMHFNYTAWPDHGVPTanAAESILQFVHMVRQQATKSKGPMIIHCSAGVGRTGTFIA 309
Cdd:cd00047  81 EELSDYTIRTLELSPKGcsESREVTHLHYTGWPDHGVPS--SPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIA 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 13677220 310 LDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 351
Cdd:cd00047 159 IDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
117-350 6.54e-87

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: 263.84  E-value: 6.54e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 117 AADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVM 196
Cdd:cd14543  23 CSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVM 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 197 LTQCNEKRRVKCDHYWPFTEEPIA-YGDITVEMISEEEQDDWACRHFRINYA--DEMQDVMHFNYTAWPDHGVPTanAAE 273
Cdd:cd14543 103 TTRVVERGRVKCGQYWPLEEGSSLrYGDLTVTNLSVENKEHYKKTTLEIHNTetDESRQVTHFQFTSWPDFGVPS--SAA 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 274 SILQFVHMVRQQ---ATKSKG----------PMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMV 340
Cdd:cd14543 181 ALLDFLGEVRQQqalAVKAMGdrwkghppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQRAFSI 260
                       250
                ....*....|
gi 13677220 341 QTEEQYIFIH 350
Cdd:cd14543 261 QTPDQYYFCY 270
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
127-351 2.54e-84

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: 255.78  E-value: 2.54e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 127 NRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQE-YIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRr 205
Cdd:cd14547   1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEEKaYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAK- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 206 VKCDHYWPFtEEPIAYGDITVEMISEEEQDDWACRHFRINYADEMQDVMHFNYTAWPDHGVPtaNAAESILQFVHMVRQ- 284
Cdd:cd14547  80 EKCAQYWPE-EENETYGDFEVTVQSVKETDGYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTP--EAAQPLLSLVQEVEEa 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13677220 285 -QATKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 351
Cdd:cd14547 157 rQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
153-350 2.24e-83

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: 252.66  E-value: 2.24e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 153 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMISEE 232
Cdd:cd14549   1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWP-KEGTETYGNIQVTLLSTE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 233 EQDDWACRHF--------RINYADEMQDVMHFNYTAWPDHGVPtanaaESILQFVHMVRQQATKSK---GPMIIHCSAGV 301
Cdd:cd14549  80 VLATYTVRTFslknlklkKVKGRSSERVVYQYHYTQWPDHGVP-----DYTLPVLSFVRKSSAANPpgaGPIVVHCSAGV 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 13677220 302 GRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIH 350
Cdd:cd14549 155 GRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
83-353 3.84e-82

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: 251.88  E-value: 3.84e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220  83 DFDAYIKDMAKDSDYKFSLQFEELKlIGLDIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGY 162
Cdd:cd14626   2 DLADNIERLKANDGLKFSQEYESID-PGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 163 NSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPF--TEepiAYGDITVEMISEEEQDDWACR 240
Cdd:cd14626  81 RKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIrgTE---TYGMIQVTLLDTVELATYSVR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 241 HFRI--NYADEMQDVMHFNYTAWPDHGVPtaNAAESILQFVHMVRQQATKSKGPMIIHCSAGVGRTGTFIALDRLLQHIR 318
Cdd:cd14626 158 TFALykNGSSEKREVRQFQFMAWPDHGVP--EYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMK 235
                       250       260       270
                ....*....|....*....|....*....|....*
gi 13677220 319 DHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 353
Cdd:cd14626 236 HEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEAL 270
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
99-350 5.19e-77

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: 238.78  E-value: 5.19e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220  99 FSLQFEELKLIGLDIPHFA--ADLPLNRCKNRYTNILPYDFSRVRLVSM--NEEEGADYINANYIPGYNSPQEYIATQGP 174
Cdd:cd17667   1 FSEDFEEVQRCTADMNITAehSNHPDNKHKNRYINILAYDHSRVKLRPLpgKDSKHSDYINANYVDGYNKAKAYIATQGP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 175 LPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMISEEEQDDWACRHFRI-NYADEM--- 250
Cdd:cd17667  81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWP-TENSEEYGNIIVTLKSTKIHACYTVRRFSIrNTKVKKgqk 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 251 ---------QDVMHFNYTAWPDHGVPtaNAAESILQFVHMVRQQATKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHE 321
Cdd:cd17667 160 gnpkgrqneRTVIQYHYTQWPDMGVP--EYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKS 237
                       250       260
                ....*....|....*....|....*....
gi 13677220 322 FVDILGLVSEMRSYRMSMVQTEEQYIFIH 350
Cdd:cd17667 238 TVNVLGFLKHIRTQRNYLVQTEEQYIFIH 266
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
111-355 5.05e-75

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: 232.80  E-value: 5.05e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 111 LDIPHFAAdlplnrcKNRYTNILPYDFSRVRLVS-MNEEEGADYINANYIPGYN-SPQEYIATQGPLPETRNDFWKMVLQ 188
Cdd:cd14612  10 LDIPGHAS-------KDRYKTILPNPQSRVCLRRaGSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 189 QKSQIIVMLTQCNEKRRvKCDHYWPFTEEpiAYGDITVEMISEEEQDDWACRHFRINYADEMQDVMHFNYTAWPDHGVPt 268
Cdd:cd14612  83 EECPIIVMITKLKEKKE-KCVHYWPEKEG--TYGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTP- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 269 aNAAESILQFVHMV--RQQATKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQY 346
Cdd:cd14612 159 -ESAGPLLRLVAEVeeSRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQY 237

                ....*....
gi 13677220 347 IFIHQCVQL 355
Cdd:cd14612 238 QFLHHTLAL 246
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
78-353 6.15e-75

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: 233.83  E-value: 6.15e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220  78 PVQLDDFDAYIKDMAKDSDYKFSLQFEELKlIGLDIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINAN 157
Cdd:cd14625   3 PIPISELAEHTERLKANDNLKLSQEYESID-PGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINAN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 158 YIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMISEEEQDDW 237
Cdd:cd14625  82 YIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWP-SRGTETYGMIQVTLLDTIELATF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 238 ACRHFRI--NYADEMQDVMHFNYTAWPDHGVPtaNAAESILQFVHMVRQQATKSKGPMIIHCSAGVGRTGTFIALDRLLQ 315
Cdd:cd14625 161 CVRTFSLhkNGSSEKREVRQFQFTAWPDHGVP--EYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLE 238
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 13677220 316 HIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 353
Cdd:cd14625 239 RIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDAL 276
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
78-353 7.17e-75

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: 233.86  E-value: 7.17e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220  78 PVQLDDFDAYIKDMAKDSDYKFSLQFEELKlIGLDIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINAN 157
Cdd:cd14624   3 PIPILELADHIERLKANDNLKFSQEYESID-PGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINAN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 158 YIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMISEEEQDDW 237
Cdd:cd14624  82 YIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWP-SRGTETYGLIQVTLLDTVELATY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 238 ACRHFRI--NYADEMQDVMHFNYTAWPDHGVPtaNAAESILQFVHMVRQQATKSKGPMIIHCSAGVGRTGTFIALDRLLQ 315
Cdd:cd14624 161 CVRTFALykNGSSEKREVRQFQFTAWPDHGVP--EHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLE 238
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 13677220 316 HIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 353
Cdd:cd14624 239 RIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDAL 276
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
153-351 1.18e-74

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: 230.60  E-value: 1.18e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 153 YINANYI-PGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMISE 231
Cdd:cd18533   1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYGDLTVELVSE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 232 EEQDDWAC--RHFRINYAD-EMQDVMHFNYTAWPDHGVPtaNAAESILQFVHMVR--QQATKSKGPMIIHCSAGVGRTGT 306
Cdd:cd18533  81 EENDDGGFivREFELSKEDgKVKKVYHIQYKSWPDFGVP--DSPEDLLTLIKLKRelNDSASLDPPIIVHCSAGVGRTGT 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 13677220 307 FIALDRLLQHIRDHEFVD---------ILGLVSEMRSYRMSMVQTEEQYIFIHQ 351
Cdd:cd18533 159 FIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
117-357 2.17e-74

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: 231.64  E-value: 2.17e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 117 AADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVM 196
Cdd:cd14603  24 AGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILM 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 197 LTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMISEEE-QDDWACRHFRINYADEMQDVMHFNYTAWPDHGVPtaNAAESI 275
Cdd:cd14603 104 ACREIEMGKKKCERYWAQEQEPLQTGPFTITLVKEKRlNEEVILRTLKVTFQKESRSVSHFQYMAWPDHGIP--DSPDCM 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 276 LQFVHMVRQQATKSKGPMIIHCSAGVGRTGTFIALDR-----LLQHIRDHefVDILGLVSEMRSYRMSMVQTEEQYIFIH 350
Cdd:cd14603 182 LAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYvrqllLTQRIPPD--FSIFDVVLEMRKQRPAAVQTEEQYEFLY 259

                ....*..
gi 13677220 351 QCVQLMW 357
Cdd:cd14603 260 HTVAQMF 266
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
123-353 2.66e-73

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: 227.99  E-value: 2.66e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 123 NRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNE 202
Cdd:cd14630   3 NRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 203 KRRVKCDHYWPftEEPIAYGDITVEMISEEEQDDWACRHFRINY--ADEMQDVMHFNYTAWPDHGVPTanAAESILQFVH 280
Cdd:cd14630  83 VGRVKCVRYWP--DDTEVYGDIKVTLIETEPLAEYVIRTFTVQKkgYHEIREIRQFHFTSWPDHGVPC--YATGLLGFVR 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13677220 281 MVRQQATKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 353
Cdd:cd14630 159 QVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAI 231
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
118-351 1.95e-72

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: 225.87  E-value: 1.95e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 118 ADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVML 197
Cdd:cd14554   1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 198 TQCNEKRRVKCDHYWPfTEEPIAYGDITVEMISEEEQDDWACRHFRINYA--DEMQDVMHFNYTAWPDHGVPtaNAAESI 275
Cdd:cd14554  81 TKLREMGREKCHQYWP-AERSARYQYFVVDPMAEYNMPQYILREFKVTDArdGQSRTVRQFQFTDWPEQGVP--KSGEGF 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13677220 276 LQF---VHMVRQQATKSkGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 351
Cdd:cd14554 158 IDFigqVHKTKEQFGQE-GPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYR 235
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
83-353 9.75e-72

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: 225.31  E-value: 9.75e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220  83 DFDAYIKDMAKDSDYKFSLQFEELkLIGLDIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGY 162
Cdd:cd14633   1 DLLQHITQMKCAEGYGFKEEYESF-FEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 163 NSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPFTEEpiAYGDITVEMISEEEQDDWACRHF 242
Cdd:cd14633  80 HRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTE--IYKDIKVTLIETELLAEYVIRTF 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 243 RINY--ADEMQDVMHFNYTAWPDHGVPTanAAESILQFVHMVRQQATKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDH 320
Cdd:cd14633 158 AVEKrgVHEIREIRQFHFTGWPDHGVPY--HATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAERE 235
                       250       260       270
                ....*....|....*....|....*....|...
gi 13677220 321 EFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 353
Cdd:cd14633 236 GVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAI 268
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
123-354 4.30e-70

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: 220.03  E-value: 4.30e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 123 NRCKNRYTNILPYDFSRVRLVSM-NEEEGADYINANYIPGYNSP-------QEYIATQGPLPETRNDFWKMVLQQKSQII 194
Cdd:cd14544   1 NKGKNRYKNILPFDHTRVILKDRdPNVPGSDYINANYIRNENEGpttdenaKTYIATQGCLENTVSDFWSMVWQENSRVI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 195 VMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMISEEEQDDWACRHFRINYADEMQD---VMHFNYTAWPDHGVPTANA 271
Cdd:cd14544  81 VMTTKEVERGKNKCVRYWPDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPireIWHYQYLSWPDHGVPSDPG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 272 AesILQFVHMV--RQQATKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEF---VDILGLVSEMRSYRMSMVQTEEQY 346
Cdd:cd14544 161 G--VLNFLEDVnqRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTEAQY 238

                ....*...
gi 13677220 347 IFIHQCVQ 354
Cdd:cd14544 239 KFIYVAVA 246
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
152-353 1.77e-67

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: 212.19  E-value: 1.77e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 152 DYINANY----IPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVE 227
Cdd:cd14541   1 DYINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFGNLQIT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 228 MISEEEQDDWACRHFRIN--YADEMQDVMHFNYTAWPDHGVPtaNAAESILQFVHMVRQQATKSKGPMIIHCSAGVGRTG 305
Cdd:cd14541  81 CVSEEVTPSFAFREFILTntNTGEERHITQMQYLAWPDHGVP--DDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTG 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 13677220 306 TFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 353
Cdd:cd14541 159 VLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAI 206
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
99-355 9.71e-66

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: 209.33  E-value: 9.71e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220  99 FSLQ--FEELKLIGLDIPHFaaDLPLNRCKNRYTNILPYDFSRVRLVSMNEEEG-ADYINANYIPGYNSPQE-YIATQGP 174
Cdd:cd14613   1 FLLQaeFFEIPMNFVDPKEY--DIPGLVRKNRYKTILPNPHSRVCLTSPDQDDPlSSYINANYIRGYGGEEKvYIATQGP 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 175 LPETRNDFWKMVLQQKSQIIVMLTQCNEKRRvKCDHYWPftEEPIAYGDITVEMISEEEQDDWACRHFRINYADEMQDVM 254
Cdd:cd14613  79 TVNTVGDFWRMVWQERSPIIVMITNIEEMNE-KCTEYWP--EEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEERGLK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 255 HFNYTAWPDHGVPtaNAAESILQFVHMV---RQQATKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSE 331
Cdd:cd14613 156 HYWYTSWPDQKTP--DNAPPLLQLVQEVeeaRQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQ 233
                       250       260
                ....*....|....*....|....
gi 13677220 332 MRSYRMSMVQTEEQYIFIHQCVQL 355
Cdd:cd14613 234 LRLDRGGMIQTCEQYQFVHHVLSL 257
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
153-351 2.94e-65

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: 206.22  E-value: 2.94e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 153 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWP-FTEEPIAYGDITVEMISE 231
Cdd:cd14557   1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsMEEGSRAFGDVVVKINEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 232 EEQDDWACRHFRINYADEM---QDVMHFNYTAWPDHGVPtaNAAESILQFVHMVRQQATKSKGPMIIHCSAGVGRTGTFI 308
Cdd:cd14557  81 KICPDYIIRKLNINNKKEKgsgREVTHIQFTSWPDHGVP--EDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYI 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 13677220 309 ALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 351
Cdd:cd14557 159 GIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
153-353 3.50e-65

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The type II (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350403 [Multi-domain]  Cd Length: 204  Bit Score: 205.92  E-value: 3.50e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 153 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPftEEPIAYGDITVEMISEE 232
Cdd:cd14555   1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP--DDTEVYGDIKVTLVETE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 233 EQDDWACRHFRINYA--DEMQDVMHFNYTAWPDHGVPTanAAESILQFVHMVRQQATKSKGPMIIHCSAGVGRTGTFIAL 310
Cdd:cd14555  79 PLAEYVVRTFALERRgyHEIREVRQFHFTGWPDHGVPY--HATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVI 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 13677220 311 DRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 353
Cdd:cd14555 157 DIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAI 199
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
123-360 4.43e-65

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: 209.02  E-value: 4.43e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 123 NRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNE 202
Cdd:cd14604  57 NVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFE 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 203 KRRVKCDHYWP-FTEEPIAYGDITVEMISEEEQDDWACRHFRINYADEMQDVMHFNYTAWPDHGVPTanAAESILQFVHM 281
Cdd:cd14604 137 MGRKKCERYWPlYGEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPDHDVPS--SFDSILDMISL 214
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 282 VRQQATKSKGPMIIHCSAGVGRTGTFIALD---RLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCVQLMWM 358
Cdd:cd14604 215 MRKYQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFE 294

                ..
gi 13677220 359 KK 360
Cdd:cd14604 295 KQ 296
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
123-353 5.86e-65

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein phosphatase non-receptor type 13 (PTPN13, also known as PTPL1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN13 is an important regulator of tumor aggressiveness. It regulates breast cancer cell aggressiveness through direct inactivation of Src kinase. In hepatocellular carcinoma, PTPN13 is a tumor suppressor. PTPN13 contains a FERM domain, five PDZ domains, and a C-terminal catalytic PTP domain. With its PDZ domains, PTPN13 has numerous interacting partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated substrates. Its FERM domain is necessary for localization to the membrane.


Pssm-ID: 350445 [Multi-domain]  Cd Length: 234  Bit Score: 206.60  E-value: 5.86e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 123 NRCKNRYTNILPYDFSRVRLvsmnEEEGaDYINANYI--PGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQC 200
Cdd:cd14597   3 NRKKNRYKNILPYDTTRVPL----GDEG-GYINASFIkmPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 201 NEKRRVKCDHYWPFT-EEPIAYGD-ITVEMISEEEQDDWACRHFRIN--YADEMQDVMHFNYTAWPDHGVPtaNAAESIL 276
Cdd:cd14597  78 VEGGKIKCQRYWPEIlGKTTMVDNrLQLTLVRMQQLKNFVIRVLELEdiQTREVRHITHLNFTAWPDHDTP--SQPEQLL 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13677220 277 QFVHMVRQqaTKSKGPMIIHCSAGVGRTGTFIALDRLLQHI-RDHEFvDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 353
Cdd:cd14597 156 TFISYMRH--IHKSGPIITHCSAGIGRSGTLICIDVVLGLIsKDLDF-DISDIVRTMRLQRHGMVQTEDQYIFCYQVI 230
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
121-353 2.39e-64

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: 205.88  E-value: 2.39e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 121 PLNRCKNRYTNILPYDFSRVRLVSM-NEEEGADYINANYI------PGyNSPQEYIATQGPLPETRNDFWKMVLQQKSQI 193
Cdd:cd14606  16 PENKSKNRYKNILPFDHSRVILQGRdSNIPGSDYINANYVknqllgPD-ENAKTYIASQGCLEATVNDFWQMAWQENSRV 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 194 IVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMISEEEQDDWACRHFR---INYADEMQDVMHFNYTAWPDHGVPTAN 270
Cdd:cd14606  95 IVMTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQvspLDNGELIREIWHYQYLSWPDHGVPSEP 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 271 AAesILQFVHMV--RQQATKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEF---VDILGLVSEMRSYRMSMVQTEEQ 345
Cdd:cd14606 175 GG--VLSFLDQInqRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGMVQTEAQ 252

                ....*...
gi 13677220 346 YIFIHQCV 353
Cdd:cd14606 253 YKFIYVAI 260
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
153-353 8.35e-64

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: 202.60  E-value: 8.35e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 153 YINANYI--PGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWP-FTEEP-IAYGDITVEM 228
Cdd:cd14538   1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdSLNKPlICGGRLEVSL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 229 ISEEEQDDWACRHFRI--NYADEMQDVMHFNYTAWPDHGVPTanAAESILQFVHMVRQQATksKGPMIIHCSAGVGRTGT 306
Cdd:cd14538  81 EKYQSLQDFVIRRISLrdKETGEVHHITHLNFTTWPDHGTPQ--SADPLLRFIRYMRRIHN--SGPIVVHCSAGIGRTGV 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 13677220 307 FIALDRLLQHI-RDHEFvDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 353
Cdd:cd14538 157 LITIDVALGLIeRDLPF-DIQDIVKDLREQRQGMIQTKDQYIFCYKAC 203
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
126-348 1.04e-63

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: 203.01  E-value: 1.04e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 126 KNRYTNILPYDFSRVRLVSMNEEegADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRR 205
Cdd:cd14545   1 LNRYRDRDPYDHDRSRVKLKQGD--NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 206 VKCDHYWPFTEEP---IAYGDITVEMISEEEQDDWACRHFRIN--YADEMQDVMHFNYTAWPDHGVPTANAAesILQFVH 280
Cdd:cd14545  79 IKCAQYWPQGEGNamiFEDTGLKVTLLSEEDKSYYTVRTLELEnlKTQETREVLHFHYTTWPDFGVPESPAA--FLNFLQ 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13677220 281 MVRQQATKS--KGPMIIHCSAGVGRTGTFIALDRLLQHI--RDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 348
Cdd:cd14545 157 KVRESGSLSsdVGPPVVHCSAGIGRSGTFCLVDTCLVLIekGNPSSVDVKKVLLEMRKYRMGLIQTPDQLRF 228
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
101-349 1.27e-63

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: 204.31  E-value: 1.27e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 101 LQFEEL--KLIGLDIPhfAADLPLNRCKNRYTNILPYDFSRVRLvsmneEEGADYINANY----IPGYNSPQEYIATQGP 174
Cdd:cd14600  18 IQFEQLyrKKPGLAIT--CAKLPQNMDKNRYKDVLPYDATRVVL-----QGNEDYINASYvnmeIPSANIVNKYIATQGP 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 175 LPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMISEEEQDDWACRHFRINYAD--EMQD 252
Cdd:cd14600  91 LPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVFREMLLTNTQtgEERT 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 253 VMHFNYTAWPDHGVPtaNAAESILQFVHMVRQQATKSKgPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEM 332
Cdd:cd14600 171 VTHLQYVAWPDHGVP--DDSSDFLEFVNYVRSKRVENE-PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKM 247
                       250
                ....*....|....*..
gi 13677220 333 RSYRMSMVQTEEQYIFI 349
Cdd:cd14600 248 RDQRAMMVQTSSQYKFV 264
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
103-348 7.20e-63

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: 202.56  E-value: 7.20e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 103 FEELKLIGLDIPHFAADLPLNRCKNRYTNILPYDFSRVRLvsmnEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDF 182
Cdd:cd14608   5 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKL----HQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 183 WKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPFTEE-PIAYGD--ITVEMISEEEQDDWACRHFRIN--YADEMQDVMHFN 257
Cdd:cd14608  81 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEkEMIFEDtnLKLTLISEDIKSYYTVRQLELEnlTTQETREILHFH 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 258 YTAWPDHGVPTANAaeSILQFVHMVRQQATKSK--GPMIIHCSAGVGRTGTFIALDR---LLQHIRDHEFVDILGLVSEM 332
Cdd:cd14608 161 YTTWPDFGVPESPA--SFLNFLFKVRESGSLSPehGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEM 238
                       250
                ....*....|....*.
gi 13677220 333 RSYRMSMVQTEEQYIF 348
Cdd:cd14608 239 RKFRMGLIQTADQLRF 254
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
86-351 1.09e-62

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: 202.66  E-value: 1.09e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220  86 AYIKDMAK----DSDYKFSLQFEELKLIGLDIPHF-AADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIP 160
Cdd:cd14627  11 SYIQKLAQvevgEHVTGMELEFKRLANSKAHTSRFiSANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFID 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 161 GYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMISEEEQDDWACR 240
Cdd:cd14627  91 GYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWP-AERSARYQYFVVDPMAEYNMPQYILR 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 241 HFRINYADEMQD--VMHFNYTAWPDHGVPtaNAAESILQF---VHMVRQQATKSkGPMIIHCSAGVGRTGTFIALDRLLQ 315
Cdd:cd14627 170 EFKVTDARDGQSrtVRQFQFTDWPEQGVP--KSGEGFIDFigqVHKTKEQFGQD-GPISVHCSAGVGRTGVFITLSIVLE 246
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 13677220 316 HIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 351
Cdd:cd14627 247 RMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQ 282
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
139-353 2.76e-62

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: 199.09  E-value: 2.76e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 139 RVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPftEEP 218
Cdd:cd14631   1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP--DDT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 219 IAYGDITVEMISEEEQDDWACRHFRINYA--DEMQDVMHFNYTAWPDHGVPTanAAESILQFVHMVRQQATKSKGPMIIH 296
Cdd:cd14631  79 EVYGDFKVTCVEMEPLAEYVVRTFTLERRgyNEIREVKQFHFTGWPDHGVPY--HATGLLSFIRRVKLSNPPSAGPIVVH 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 13677220 297 CSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 353
Cdd:cd14631 157 CSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 213
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
86-351 3.95e-62

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: 201.11  E-value: 3.95e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220  86 AYIKDMAK----DSDYKFSLQFEELKLIGLDIPHF-AADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIP 160
Cdd:cd14628  10 AYIQKLTQietgENVTGMELEFKRLASSKAHTSRFiSANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFID 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 161 GYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMISEEEQDDWACR 240
Cdd:cd14628  90 GYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWP-AERSARYQYFVVDPMAEYNMPQYILR 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 241 HFRINYADEMQD--VMHFNYTAWPDHGVPtaNAAESILQF---VHMVRQQATKSkGPMIIHCSAGVGRTGTFIALDRLLQ 315
Cdd:cd14628 169 EFKVTDARDGQSrtVRQFQFTDWPEQGVP--KSGEGFIDFigqVHKTKEQFGQD-GPISVHCSAGVGRTGVFITLSIVLE 245
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 13677220 316 HIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 351
Cdd:cd14628 246 RMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYR 281
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
126-351 5.38e-62

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: 198.60  E-value: 5.38e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 126 KNRYTNILPYDFSRVRLVSMNEEEG-ADYINANYIPGYNSPQE-YIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEK 203
Cdd:cd14611   2 KNRYKTILPNPHSRVCLKPKNSNDSlSTYINANYIRGYGGKEKaFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 204 RRvKCDHYWPftEEPIAYGDITVEMISEEEQDDWACRHFRINYADEMQDVMHFNYTAWPDHGVPtaNAAESILQFVHMVR 283
Cdd:cd14611  82 NE-KCVLYWP--EKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTP--DSAQPLLQLMLDVE 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 284 Q--QATKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 351
Cdd:cd14611 157 EdrLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
78-353 6.32e-62

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: 200.64  E-value: 6.32e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220  78 PVQLDDFDAYIKDMAKDSDYKFSLQFEELKLIGLDIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINAN 157
Cdd:cd14621   7 PLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINAS 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 158 YIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMISEEEQDDW 237
Cdd:cd14621  87 FINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWP-DQGCWTYGNIRVSVEDVTVLVDY 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 238 ACRHFRINYADEMQD------VMHFNYTAWPDHGVPTANAAesILQFVHMVRQQATKSKGPMIIHCSAGVGRTGTFIALD 311
Cdd:cd14621 166 TVRKFCIQQVGDVTNkkpqrlITQFHFTSWPDFGVPFTPIG--MLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVID 243
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 13677220 312 RLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 353
Cdd:cd14621 244 AMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQAL 285
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
129-351 1.88e-61

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: 197.09  E-value: 1.88e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 129 YTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKC 208
Cdd:cd14620   1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 209 DHYWPfTEEPIAYGDITVEMISEEEQDDWACRHFRINYadEMQD-------VMHFNYTAWPDHGVPTANAAesILQFVHM 281
Cdd:cd14620  81 YQYWP-DQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQP--QLPDgckaprlVTQLHFTSWPDFGVPFTPIG--MLKFLKK 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 282 VRQQATKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 351
Cdd:cd14620 156 VKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQ 225
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
123-354 2.40e-61

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: 197.93  E-value: 2.40e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 123 NRCKNRYTNILPYDFSRVRLVSMN-EEEGADYINANYI-PGYNS-------PQEYIATQGPLPETRNDFWKMVLQQKSQI 193
Cdd:cd14605   2 NKNKNRYKNILPFDHTRVVLHDGDpNEPVSDYINANIImPEFETkcnnskpKKSYIATQGCLQNTVNDFWRMVFQENSRV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 194 IVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMISEEEQDDWACRHFR---INYADEMQDVMHFNYTAWPDHGVPTAN 270
Cdd:cd14605  82 IVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYILRELKlskVGQGNTERTVWQYHFRTWPDHGVPSDP 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 271 AAesILQFVHMV--RQQATKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEF---VDILGLVSEMRSYRMSMVQTEEQ 345
Cdd:cd14605 162 GG--VLDFLEEVhhKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTEAQ 239

                ....*....
gi 13677220 346 YIFIHQCVQ 354
Cdd:cd14605 240 YRFIYMAVQ 248
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
105-346 2.46e-61

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: 199.18  E-value: 2.46e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 105 ELKLIGLDIPH----FAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRN 180
Cdd:cd14629  31 EFKLLANSKAHtsrfISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTE 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 181 DFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMISEEEQDDWACRHFRINYADEMQD--VMHFNY 258
Cdd:cd14629 111 DFWRMLWEHNSTIVVMLTKLREMGREKCHQYWP-AERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSrtIRQFQF 189
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 259 TAWPDHGVPtaNAAESILQF---VHMVRQQATKSkGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSY 335
Cdd:cd14629 190 TDWPEQGVP--KTGEGFIDFigqVHKTKEQFGQD-GPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQ 266
                       250
                ....*....|.
gi 13677220 336 RMSMVQTEEQY 346
Cdd:cd14629 267 RPAMVQTEDQY 277
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
126-353 2.54e-61

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


Pssm-ID: 350450 [Multi-domain]  Cd Length: 234  Bit Score: 196.98  E-value: 2.54e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 126 KNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRR 205
Cdd:cd14602   1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 206 VKCDHYWPFT-EEPIAYGDITVEMISEEEQDDWACRHFRINYADEMQDVMHFNYTAWPDHGVPTanAAESILQFVHMVRQ 284
Cdd:cd14602  81 KKCERYWAEPgEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPS--SIDPILELIWDVRC 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13677220 285 QATKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDH---EFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 353
Cdd:cd14602 159 YQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGiipENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAV 230
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
153-350 9.91e-61

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


Pssm-ID: 350506 [Multi-domain]  Cd Length: 209  Bit Score: 194.81  E-value: 9.91e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 153 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMISEE 232
Cdd:cd17668   1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP-ADGSEEYGNFLVTQKSVQ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 233 EQDDWACRHFRINYAD----------EMQDVMHFNYTAWPDHGVPTANAaeSILQFVHMVRQQATKSKGPMIIHCSAGVG 302
Cdd:cd17668  80 VLAYYTVRNFTLRNTKikkgsqkgrpSGRVVTQYHYTQWPDMGVPEYTL--PVLTFVRKASYAKRHAVGPVVVHCSAGVG 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 13677220 303 RTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIH 350
Cdd:cd17668 158 RTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 205
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
153-351 1.94e-60

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: 193.79  E-value: 1.94e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 153 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMltQCNEKR--RVKCDHYWP-FTEEPIAYGDITVEMI 229
Cdd:cd14542   1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVM--ACREFEmgKKKCERYWPeEGEEQLQFGPFKISLE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 230 SEEEQ-DDWACRHFRINYADEMQDVMHFNYTAWPDHGVPTanAAESILQFVHMVRQQATKSKGPMIIHCSAGVGRTGTFI 308
Cdd:cd14542  79 KEKRVgPDFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPS--SVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTIC 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 13677220 309 ALD---RLLQ-HIRDHEFvDILGLVSEMRSYRMSMVQTEEQYIFIHQ 351
Cdd:cd14542 157 AIDyvwNLLKtGKIPEEF-SLFDLVREMRKQRPAMVQTKEQYELVYR 202
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
153-353 1.32e-59

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


Pssm-ID: 350480 [Multi-domain]  Cd Length: 205  Bit Score: 191.80  E-value: 1.32e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 153 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPftEEPIAYGDITVEMISEE 232
Cdd:cd14632   1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP--DDSDTYGDIKITLLKTE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 233 EQDDWACRHF---RINYADEmQDVMHFNYTAWPDHGVPTanAAESILQFVHMVRQQATKSKGPMIIHCSAGVGRTGTFIA 309
Cdd:cd14632  79 TLAEYSVRTFaleRRGYSAR-HEVKQFHFTSWPEHGVPY--HATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIV 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 13677220 310 LDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 353
Cdd:cd14632 156 LDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAI 199
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
112-353 2.67e-59

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: 192.87  E-value: 2.67e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 112 DIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEeegaDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 191
Cdd:cd14607  13 DYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTEN----DYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKT 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 192 QIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDIT---VEMISEEEQDDWACRHFRINYAD--EMQDVMHFNYTAWPDHGV 266
Cdd:cd14607  89 KAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKETgfsVKLLSEDVKSYYTVHLLQLENINsgETRTISHFHYTTWPDFGV 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 267 PTANAaeSILQFVHMVRQQATKS--KGPMIIHCSAGVGRTGTFIALDR--LLQHIRDHEFVDILGLVSEMRSYRMSMVQT 342
Cdd:cd14607 169 PESPA--SFLNFLFKVRESGSLSpeHGPAVVHCSAGIGRSGTFSLVDTclVLMEKKDPDSVDIKQVLLDMRKYRMGLIQT 246
                       250
                ....*....|.
gi 13677220 343 EEQYIFIHQCV 353
Cdd:cd14607 247 PDQLRFSYMAV 257
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
153-354 2.55e-57

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: 185.55  E-value: 2.55e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 153 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMISEE 232
Cdd:cd14552   1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWP-EDGSVSSGDITVELKDQT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 233 EQDDWACRHFRI--NYADEMQDVMHFNYTAWPDHGVPtANAAESILQFVHMVRQQATKSKGPMIIHCSAGVGRTGTFIAL 310
Cdd:cd14552  80 DYEDYTLRDFLVtkGKGGSTRTVRQFHFHGWPEVGIP-DNGKGMIDLIAAVQKQQQQSGNHPITVHCSAGAGRTGTFCAL 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 13677220 311 DRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCVQ 354
Cdd:cd14552 159 STVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVVQ 202
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
128-354 6.95e-57

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: 185.63  E-value: 6.95e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 128 RYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVK 207
Cdd:cd14623   1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 208 CDHYWPfTEEPIAYGDITVEMISEEEQDDWACRHFRI--NYADEMQDVMHFNYTAWPDHGVPTanAAESILQFVHMVRQQ 285
Cdd:cd14623  81 CAQYWP-SDGSVSYGDITIELKKEEECESYTVRDLLVtnTRENKSRQIRQFHFHGWPEVGIPS--DGKGMINIIAAVQKQ 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 286 ATKSKG-PMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCVQ 354
Cdd:cd14623 158 QQQSGNhPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQ 227
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
152-354 5.65e-55

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: 179.82  E-value: 5.65e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 152 DYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMISE 231
Cdd:cd14622   1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWP-SEGSVTHGEITIEIKND 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 232 EEQDDWACRHFRINYADEMQD--VMHFNYTAWPDHGVPtANAAESILQFVHMVRQQATKSKGPMIIHCSAGVGRTGTFIA 309
Cdd:cd14622  80 TLLETISIRDFLVTYNQEKQTrlVRQFHFHGWPEIGIP-AEGKGMIDLIAAVQKQQQQTGNHPIVVHCSAGAGRTGTFIA 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 13677220 310 LDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCVQ 354
Cdd:cd14622 159 LSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQ 203
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
122-349 2.20e-54

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 180.67  E-value: 2.20e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 122 LNRCK-NRYTNILPYDFSRVRlvsmneeEGADYINANYIPGYNsPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQC 200
Cdd:COG5599  40 INGSPlNRFRDIQPYKETALR-------ANLGYLNANYIQVIG-NHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASD 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 201 NE--KRRVKCDHYWPFTEEPIAYgDITVEMISEEE-QDDWACRHFRINYAD---EMQDVMHFNYTAWPDHGVPTANAAES 274
Cdd:COG5599 112 DEisKPKVKMPVYFRQDGEYGKY-EVSSELTESIQlRDGIEARTYVLTIKGtgqKKIEIPVLHVKNWPDHGAISAEALKN 190
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13677220 275 ILQFVHMVRQQATKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHE--FVDILGLVSEMRSYR-MSMVQTEEQYIFI 349
Cdd:COG5599 191 LADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMVQTSEQLDVL 268
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
153-351 3.20e-53

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: 175.10  E-value: 3.20e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 153 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPFTEEPiAYGDITVEMISEE 232
Cdd:cd14551   1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCW-TYGNLRVRVEDTV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 233 EQDDWACRHFRINYADE------MQDVMHFNYTAWPDHGVPTANAAesILQFVHMVRQQATKSKGPMIIHCSAGVGRTGT 306
Cdd:cd14551  80 VLVDYTTRKFCIQKVNRgigekrVRLVTQFHFTSWPDFGVPFTPIG--MLKFLKKVKSANPPRAGPIVVHCSAGVGRTGT 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 13677220 307 FIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 351
Cdd:cd14551 158 FIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
153-350 3.12e-52

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: 172.58  E-value: 3.12e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 153 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPftEEPIAYGDITVEMISEE 232
Cdd:cd14558   1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWG--DEKKTYGDIEVELKDTE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 233 EQDDWACRHFRINY--ADEMQDVMHFNYTAWPDHGVPT-----ANAAESILQFVHMVRQQATKSKgPMIIHCSAGVGRTG 305
Cdd:cd14558  79 KSPTYTVRVFEITHlkRKDSRTVYQYQYHKWKGEELPEkpkdlVDMIKSIKQKLPYKNSKHGRSV-PIVVHCSDGSSRTG 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 13677220 306 TFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIH 350
Cdd:cd14558 158 IFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
153-350 3.36e-51

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: 169.95  E-value: 3.36e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 153 YINANYI--PGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQ-CNEKRRVKCDHYWPFTE-EPIAYGDITVEM 228
Cdd:cd17658   1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRlVDNYSTAKCADYFPAEEnESREFGRISVTN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 229 ISEE-EQDDWACRHFRINYAdEMQD----VMHFNYTAWPDHGVP-TANAAESILQFVHMVrqqaTKSKGPMIIHCSAGVG 302
Cdd:cd17658  81 KKLKhSQHSITLRVLEVQYI-ESEEpplsVLHIQYPEWPDHGVPkDTRSVRELLKRLYGI----PPSAGPIVVHCSAGIG 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 13677220 303 RTGTFIALDRLLQHIR--DHEFVDILGLVSEMRSYRMSMVQTEEQYIFIH 350
Cdd:cd17658 156 RTGAYCTIHNTIRRILegDMSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
152-349 4.22e-50

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: 167.43  E-value: 4.22e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 152 DYINANYI----PGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVE 227
Cdd:cd14601   1 DYINANYInmeiPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYGGFQVT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 228 MISEEEQDDWACRHFRINY--ADEMQDVMHFNYTAWPDHGVPtaNAAESILQFVHMVRQQATKSKGPMIIHCSAGVGRTG 305
Cdd:cd14601  81 CHSEEGNPAYVFREMTLTNleKNESRPLTQIQYIAWPDHGVP--DDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTG 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 13677220 306 TFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFI 349
Cdd:cd14601 159 VLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFV 202
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
153-353 1.10e-49

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: 166.08  E-value: 1.10e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 153 YINANYIPGYNSPQE--YIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPFT-EEPIAYGDITVEMI 229
Cdd:cd14596   1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETlQEPMELENYQLRLE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 230 SEEEQDDWACRHFRI--NYADEMQDVMHFNYTAWPDHGVPtaNAAESILQFVHMVRqqATKSKGPMIIHCSAGVGRTGTF 307
Cdd:cd14596  81 NYQALQYFIIRIIKLveKETGENRLIKHLQFTTWPDHGTP--QSSDQLVKFICYMR--KVHNTGPIVVHCSAGIGRAGVL 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 13677220 308 IALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 353
Cdd:cd14596 157 ICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVV 202
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
153-351 2.16e-49

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: 165.25  E-value: 2.16e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 153 YINANYIPGY-NSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPfTE--EPIAYGDITVEMI 229
Cdd:cd14539   1 YINASLIEDLtPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWP-TErgQALVYGAITVSLQ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 230 SEEEQDDWACRHFRINYAD--EMQDVMHFNYTAWPDHGVPTA-NAAESILQFVHMVRQQATKSKGPMIIHCSAGVGRTGT 306
Cdd:cd14539  80 SVRTTPTHVERIISIQHKDtrLSRSVVHLQFTTWPELGLPDSpNPLLRFIEEVHSHYLQQRSLQTPIVVHCSSGVGRTGA 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 13677220 307 FIALDRLLQHIR-DHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 351
Cdd:cd14539 160 FCLLYAAVQEIEaGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
153-351 1.30e-48

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: 162.96  E-value: 1.30e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 153 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRvKCDHYWPfTEEPIAYGDITVEMISEE 232
Cdd:cd14556   1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQ-SCPQYWP-DEGSGTYGPIQVEFVSTT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 233 EQDDWACRHFRINYADEMQD----VMHFNYTAWPDHGvPTANAAESILQFVHMVRQ-QATKSKGPMIIHCSAGVGRTGTF 307
Cdd:cd14556  79 IDEDVISRIFRLQNTTRPQEgyrmVQQFQFLGWPRDR-DTPPSKRALLKLLSEVEKwQEQSGEGPIVVHCLNGVGRSGVF 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 13677220 308 IALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 351
Cdd:cd14556 158 CAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
153-351 2.06e-48

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: 163.01  E-value: 2.06e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 153 YINANYIPGY--NSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPFT---EEPIAYGDITVE 227
Cdd:cd14540   1 YINASHITATvgGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLggeHDALTFGEYKVS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 228 MISEEEQDDWACRHFRINY--ADEMQDVMHFNYTAWPDHGVP-TANAAESILQFVHMVRQQATKSKG------PMIIHCS 298
Cdd:cd14540  81 TKFSVSSGCYTTTGLRVKHtlSGQSRTVWHLQYTDWPDHGCPeDVSGFLDFLEEINSVRRHTNQDVAghnrnpPTLVHCS 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 13677220 299 AGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 351
Cdd:cd14540 161 AGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYN 213
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
118-351 5.52e-46

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: 159.01  E-value: 5.52e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 118 ADLPLNRCKNRYTNILPYDFSRVRLVSmNEEEGADYINANYIPGYNSPQE--YIATQGPLPETRNDFWKMVLQQKSQIIV 195
Cdd:cd14599  33 ATLPENAERNRIREVVPYEENRVELVP-TKENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVIA 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 196 MLTQCNEKRRVKCDHYWP---FTEEPIAYGDITVEMISEEEQDDWACRHFRINY--ADEMQDVMHFNYTAWPDHGVPT-A 269
Cdd:cd14599 112 MVTAEEEGGRSKSHRYWPklgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHllSGQERTVWHLQYTDWPDHGCPEeV 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 270 NAAESILQFVHMVRQQ------ATKSKGP-MIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQT 342
Cdd:cd14599 192 QGFLSYLEEIQSVRRHtnsmldSTKNCNPpIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQT 271

                ....*....
gi 13677220 343 EEQYIFIHQ 351
Cdd:cd14599 272 IAQYKFVYQ 280
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
123-348 8.44e-46

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: 158.30  E-value: 8.44e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 123 NRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNsPQE--YIATQGPLPETRNDFWKMVLQQKSQIIVMLTQC 200
Cdd:cd14610  44 NVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMDHD-PRNpaYIATQGPLPATVADFWQMVWESGCVVIVMLTPL 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 201 NEKRRVKCDHYWPfTEEPIAYGDITVEMISEEEQ-DDWACRHFRIN--YADEMQDVMHFNYTAWPDHGVPTanAAESILQ 277
Cdd:cd14610 123 AENGVKQCYHYWP-DEGSNLYHIYEVNLVSEHIWcEDFLVRSFYLKnlQTNETRTVTQFHFLSWNDQGVPA--STRSLLD 199
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13677220 278 FVHMVRQQATKSKGPMIIHCSAGVGRTGTFIALDRLLQHI-RDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 348
Cdd:cd14610 200 FRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 271
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
153-353 1.76e-42

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


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 147.21  E-value: 1.76e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 153 YINANYIPGYNSPQE-YIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMISE 231
Cdd:cd14546   1 YINASTIYDHDPRNPaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWP-EEGSEVYHIYEVHLVSE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 232 EE-QDDWACRHFRIN--YADEMQDVMHFNYTAWPDHGVPTanAAESILQFVHMVRQQATKSKGPMIIHCSAGVGRTGTFI 308
Cdd:cd14546  80 HIwCDDYLVRSFYLKnlQTSETRTVTQFHFLSWPDEGIPA--SAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGTYI 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 13677220 309 ALD----RLLQHIRDhefVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 353
Cdd:cd14546 158 LIDmvlnRMAKGAKE---IDIAATLEHLRDQRPGMVKTKDQFEFVLTAV 203
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
123-348 1.97e-42

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: 149.42  E-value: 1.97e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 123 NRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNsPQ--EYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQC 200
Cdd:cd14609  42 NVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIEHD-PRmpAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPL 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 201 NEKRRVKCDHYWPfTEEPIAYGDITVEMISEEEQ-DDWACRHFRIN--YADEMQDVMHFNYTAWPDHGVPTanAAESILQ 277
Cdd:cd14609 121 VEDGVKQCDRYWP-DEGSSLYHIYEVNLVSEHIWcEDFLVRSFYLKnvQTQETRTLTQFHFLSWPAEGIPS--STRPLLD 197
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13677220 278 FVHMVRQQATKSKGPMIIHCSAGVGRTGTFIALDRLLQHI-RDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 348
Cdd:cd14609 198 FRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGMVRTKDQFEF 269
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
123-353 4.66e-42

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 149.38  E-value: 4.66e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220  123 NRCKNRYTNILPYDFSRVRLVSmnEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNE 202
Cdd:PHA02742  52 NMKKCRYPDAPCFDRNRVILKI--EDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220  203 KRRVKCDHYW-PFTEEPIAYGDITVEMISEEEQDDWACRHFRINYAD--EMQDVMHFNYTAWPDHGVPTanAAESILQFV 279
Cdd:PHA02742 130 DGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNtgASLDIKHFAYEDWPHGGLPR--DPNKFLDFV 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220  280 HMVRQQATKS-----------KGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 348
Cdd:PHA02742 208 LAVREADLKAdvdikgenivkEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIF 287

                 ....*
gi 13677220  349 IHQCV 353
Cdd:PHA02742 288 CYFIV 292
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
121-354 8.39e-42

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 149.02  E-value: 8.39e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220  121 PLNRCKNRYTNILPYDFSRV-------------------RLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRND 181
Cdd:PHA02746  49 KENLKKNRFHDIPCWDHSRVvinaheslkmfdvgdsdgkKIEVTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSED 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220  182 FWKMVLQQKSQIIVMLTQCNEKRRvKCDHYWPFTEE-PIAYGDITVEMISEEEQDDWACRHFRIN--YADEMQDVMHFNY 258
Cdd:PHA02746 129 FFKLISEHESQVIVSLTDIDDDDE-KCFELWTKEEDsELAFGRFVAKILDIIEELSFTKTRLMITdkISDTSREIHHFWF 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220  259 TAWPDHGVPTaNAAEsILQFVHMVRQQATKSK----------GPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGL 328
Cdd:PHA02746 208 PDWPDNGIPT-GMAE-FLELINKVNEEQAELIkqadndpqtlGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEI 285
                        250       260
                 ....*....|....*....|....*.
gi 13677220  329 VSEMRSYRMSMVQTEEQYIFIHQCVQ 354
Cdd:PHA02746 286 VLKIRKQRHSSVFLPEQYAFCYKALK 311
PHA02738 PHA02738
hypothetical protein; Provisional
123-355 2.09e-41

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 147.76  E-value: 2.09e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220  123 NRCKNRYTNILPYDFSRVRLVSmnEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNE 202
Cdd:PHA02738  49 NRKLNRYLDAVCFDHSRVILPA--ERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKE 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220  203 KRRVKCDHYWPFTEE-PIAYGDITVEMISEEEQDDWACRHFRINYADE-MQDVMHFNYTAWPDHGVPtaNAAESILQFVH 280
Cdd:PHA02738 127 NGREKCFPYWSDVEQgSIRFGKFKITTTQVETHPHYVKSTLLLTDGTSaTQTVTHFNFTAWPDHDVP--KNTSEFLNFVL 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220  281 MVRQ------QATKSKG-------PMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYI 347
Cdd:PHA02738 205 EVRQcqkelaQESLQIGhnrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYF 284

                 ....*...
gi 13677220  348 FIHQCVQL 355
Cdd:PHA02738 285 FCYRAVKR 292
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
253-353 6.88e-39

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 134.41  E-value: 6.88e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220    253 VMHFNYTAWPDHGVPTAnaAESILQFVHMVR--QQATKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRD-HEFVDILGLV 329
Cdd:smart00404   2 VKHYHYTGWPDHGVPES--PDSILELLRAVKknLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEVDIFDTV 79
                           90       100
                   ....*....|....*....|....
gi 13677220    330 SEMRSYRMSMVQTEEQYIFIHQCV 353
Cdd:smart00404  80 KELRSQRPGMVQTEEQYLFLYRAL 103
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
253-353 6.88e-39

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: 134.41  E-value: 6.88e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220    253 VMHFNYTAWPDHGVPTAnaAESILQFVHMVR--QQATKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRD-HEFVDILGLV 329
Cdd:smart00012   2 VKHYHYTGWPDHGVPES--PDSILELLRAVKknLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEVDIFDTV 79
                           90       100
                   ....*....|....*....|....
gi 13677220    330 SEMRSYRMSMVQTEEQYIFIHQCV 353
Cdd:smart00012  80 KELRSQRPGMVQTEEQYLFLYRAL 103
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
121-350 2.52e-37

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 137.06  E-value: 2.52e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220  121 PLNRCKNRYTNILPYDFSRVRLVSmNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQC 200
Cdd:PHA02747  49 PENQPKNRYWDIPCWDHNRVILDS-GGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPT 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220  201 NEKR-RVKCDHYWPFTEE-PIAYGDITVEMISEEEQDDWACRHFRIN--YADEMQDVMHFNYTAWPDHGVPTANAaeSIL 276
Cdd:PHA02747 128 KGTNgEEKCYQYWCLNEDgNIDMEDFRIETLKTSVRAKYILTLIEITdkILKDSRKISHFQCSEWFEDETPSDHP--DFI 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220  277 QFVHM---VRQQATKSKG-------PMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQY 346
Cdd:PHA02747 206 KFIKIidiNRKKSGKLFNpkdallcPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDY 285

                 ....
gi 13677220  347 IFIH 350
Cdd:PHA02747 286 LFIQ 289
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
153-351 6.64e-36

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: 130.48  E-value: 6.64e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 153 YINANYIPGYNSPQE--YIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPF---TEEPIAYGDITVE 227
Cdd:cd14598   1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRlgsRHNTVTYGRFKIT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 228 MISEEEQDDWACRHFRINYADEMQD--VMHFNYTAWPDHGVPT-ANAAESILQFVHMVRQQATKS------KGPMIIHCS 298
Cdd:cd14598  81 TRFRTDSGCYATTGLKIKHLLTGQErtVWHLQYTDWPEHGCPEdLKGFLSYLEEIQSVRRHTNSTidpkspNPPVLVHCS 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 13677220 299 AGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 351
Cdd:cd14598 161 AGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYK 213
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
153-351 7.16e-35

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


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 127.44  E-value: 7.16e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 153 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRvkCDHYWPfTEEPIAYGDITVEMISEE 232
Cdd:cd14634   1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAAQL--CMQYWP-EKTSCCYGPIQVEFVSAD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 233 EQDDWACRHFRINYADEMQD----VMHFNYTAWPDHGvPTANAAESILQFVHMV---RQQATKSKGPMIIHCSAGVGRTG 305
Cdd:cd14634  78 IDEDIISRIFRICNMARPQDgyriVQHLQYIGWPAYR-DTPPSKRSILKVVRRLekwQEQYDGREGRTVVHCLNGGGRSG 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 13677220 306 TFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 351
Cdd:cd14634 157 TFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYE 202
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
153-353 4.46e-32

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


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 120.01  E-value: 4.46e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 153 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRV-KCDHYWPfteEP--IAYGDITVEMI 229
Cdd:cd14637   1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWP---EPglQQYGPMEVEFV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 230 SEEEQDDWACRHFRINYADEMQD----VMHFNYTAWPDHGvPTANAAESILQFVHMVRQ-QATKSKGPMIIHCSAGVGRT 304
Cdd:cd14637  78 SGSADEDIVTRLFRVQNITRLQEghlmVRHFQFLRWSAYR-DTPDSKKAFLHLLASVEKwQRESGEGRTVVHCLNGGGRS 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 13677220 305 GTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 353
Cdd:cd14637 157 GTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIA 205
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
153-351 7.90e-32

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: 118.96  E-value: 7.90e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 153 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCdhYWPFTEEPIAYGDITVEMISEE 232
Cdd:cd14550   1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPI--YWPTKEKPLECETFKVTLSGED 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 233 EQ-----DDWACRHFRI--NYADEMQDVMHFNYTAWPDhgvpTANAAESILQFVHMVRQQATKSKGPMIIHCSAGVGRTG 305
Cdd:cd14550  79 HSclsneIRLIVRDFILesTQDDYVLEVRQFQCPSWPN----PCSPIHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAA 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 13677220 306 TFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 351
Cdd:cd14550 155 TFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
153-353 4.91e-30

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: 114.39  E-value: 4.91e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 153 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQcNEKRRVKCDHYWPFTEEPIAYGDITVEMISE- 231
Cdd:cd17670   1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD-NQGLAEDEFVYWPSREESMNCEAFTVTLISKd 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 232 ------EEQ---DDWACRHFRINYADEmqdVMHFNYTAWPDHGVPTAnaaeSILQFVHMVRQQATKSKGPMIIHCSAGVG 302
Cdd:cd17670  80 rlclsnEEQiiiHDFILEATQDDYVLE---VRHFQCPKWPNPDAPIS----STFELINVIKEEALTRDGPTIVHDEFGAV 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 13677220 303 RTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 353
Cdd:cd17670 153 SAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
153-353 1.19e-29

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: 113.55  E-value: 1.19e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 153 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCdHYWPFTEEPIAYGDITVEMISEE 232
Cdd:cd17669   1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPNKDEPINCETFKVTLIAEE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 233 -----EQDDWACRHFRINYA--DEMQDVMHFNYTAWPDHGVPTANAAEsilqFVHMVRQQATKSKGPMIIHCSAGVGRTG 305
Cdd:cd17669  80 hkclsNEEKLIIQDFILEATqdDYVLEVRHFQCPKWPNPDSPISKTFE----LISIIKEEAANRDGPMIVHDEHGGVTAG 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 13677220 306 TFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 353
Cdd:cd17669 156 TFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
153-350 6.52e-29

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 111.66  E-value: 6.52e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 153 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRrvKCDHYWPfTEEPIAYGDITVEMISEE 232
Cdd:cd14636   1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQ--GCPQYWP-EEGMLRYGPIQVECMSCS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 233 EQDDWACRHFRINYADEMQD----VMHFNYTAWPDH-GVPTANaaESILQFVHMV---RQQATKSKGPMIIHCSAGVGRT 304
Cdd:cd14636  78 MDCDVISRIFRICNLTRPQEgylmVQQFQYLGWASHrEVPGSK--RSFLKLILQVekwQEECDEGEGRTIIHCLNGGGRS 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 13677220 305 GTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIH 350
Cdd:cd14636 156 GMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCY 201
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
153-351 3.16e-27

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: 107.08  E-value: 3.16e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 153 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRvkCDHYWPftEEPI-AYGDITVEMISE 231
Cdd:cd14635   1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQL--CPQYWP--ENGVhRHGPIQVEFVSA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 232 EEQDDWACRHFRINYADEMQD----VMHFNYTAWPDHGvPTANAAESILQFVHMV---RQQATKSKGPMIIHCSAGVGRT 304
Cdd:cd14635  77 DLEEDIISRIFRIYNAARPQDgyrmVQQFQFLGWPMYR-DTPVSKRSFLKLIRQVdkwQEEYNGGEGRTVVHCLNGGGRS 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 13677220 305 GTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 351
Cdd:cd14635 156 GTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYE 202
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
127-346 9.88e-20

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


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 87.07  E-value: 9.88e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 127 NRYTNIlpydfsrvrlVSMNEEEGADYINANYIPGYNSPQeYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRV 206
Cdd:cd14559   1 NRFTNI----------QTRVSTPVGKNLNANRVQIGNKNV-AIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRK 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 207 KCDHYWPFTEEpiaYGDITV--EMISEEEQ-DDWACRHFRINYADEMQD----VMHFnyTAWPDHGVPTANAAESILQFV 279
Cdd:cd14559  70 GLPPYFRQSGT---YGSVTVksKKTGKDELvDGLKADMYNLKITDGNKTitipVVHV--TNWPDHTAISSEGLKELADLV 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 280 HMVRQQ-------------ATKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDIlglVSEMRSYRMS-MVQTEEQ 345
Cdd:cd14559 145 NKSAEEkrnfykskgssaiNDKNKLLPVIHCRAGVGRTGQLAAAMELNKSPNNLSVEDI---VSDMRTSRNGkMVQKDEQ 221

                .
gi 13677220 346 Y 346
Cdd:cd14559 222 L 222
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
123-370 2.78e-14

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 72.69  E-value: 2.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220  123 NRCK--NRYTNILPYDFSRVRLVSMNEeegadYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQC 200
Cdd:PHA02740  51 NKAKdeNLALHITRLLHRRIKLFNDEK-----VLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRH 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220  201 NEKrrvKC-DHYWPFTEEPIAYGD----ITVEMISEEeqddwacrHFRI------NYADEMQDVMHFNYTAWPDHGVptA 269
Cdd:PHA02740 126 ADK---KCfNQFWSLKEGCVITSDkfqiETLEIIIKP--------HFNLtllsltDKFGQAQKISHFQYTAWPADGF--S 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220  270 NAAESILQF--------VHMVRQQATKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQ 341
Cdd:PHA02740 193 HDPDAFIDFfcniddlcADLEKHKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMN 272
                        250       260
                 ....*....|....*....|....*....
gi 13677220  342 TEEQYIFihqCVQLMWMKKKQQFCISDVI 370
Cdd:PHA02740 273 CLDDYVF---CYHLIAAYLKEKFDILKFI 298
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
228-351 1.61e-12

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 64.22  E-value: 1.61e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 228 MISEEEQDDWACRHFRINYademqdvMHFNytaWPDHGVPTANAAESILQFVHmvrqQATKSKGPMIIHCSAGVGRTGTF 307
Cdd:COG2453  32 LTEEEELLLGLLEEAGLEY-------LHLP---IPDFGAPDDEQLQEAVDFID----EALREGKKVLVHCRGGIGRTGTV 97
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 13677220 308 IAldrLLQHIRDHEFVDILGLVSEMRSYRmsmVQTEEQYIFIHQ 351
Cdd:COG2453  98 AA---AYLVLLGLSAEEALARVRAARPGA---VETPAQRAFLER 135
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
270-351 9.23e-09

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


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 52.74  E-value: 9.23e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 270 NAAESILQFVHMVRQQATKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRdhefvDILGLVSEMRSYR-MSMVQTEEQYIF 348
Cdd:cd14494  36 DLTLAMVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGM-----SAEEAVRIVRLIRpGGIPQTIEQLDF 110

                ...
gi 13677220 349 IHQ 351
Cdd:cd14494 111 LIK 113
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
262-351 1.87e-07

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


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 49.97  E-value: 1.87e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 262 PDHGVPTAnaaESILQFVHMVRQQATKSKgPMIIHCSAGVGRTGTFIALdrllqHIRDHEFVDILGLVSEMRSYRMSMVQ 341
Cdd:cd14504  58 EDYTPPTL---EQIDEFLDIVEEANAKNE-AVLVHCLAGKGRTGTMLAC-----YLVKTGKISAVDAINEIRRIRPGSIE 128
                        90
                ....*....|
gi 13677220 342 TEEQYIFIHQ 351
Cdd:cd14504 129 TSEQEKFVIQ 138
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
262-351 9.36e-07

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 48.41  E-value: 9.36e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 262 PDHGVPTANAaesilQFVHMVRQ--QATKSKGPMIIHCSAGVGRTGTFIAldRLLQHIRDHEFVD-ILGLVsemRSYRMS 338
Cdd:cd14505  81 PDGGVPSDIA-----QWQELLEEllSALENGKKVLIHCKGGLGRTGLIAA--CLLLELGDTLDPEqAIAAV---RALRPG 150
                        90
                ....*....|...
gi 13677220 339 MVQTEEQYIFIHQ 351
Cdd:cd14505 151 AIQTPKQENFLHQ 163
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
253-357 3.99e-06

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


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 47.34  E-value: 3.99e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 253 VMHFNYtAWPDHGVPTANAAESILQfvhmVRQQATKSKGPMIIHCSAGVGRTGTFIALdRLLQHIRDHEFVDILGLvsem 332
Cdd:cd14506  77 IYFYNF-GWKDYGVPSLTTILDIVK----VMAFALQEGGKVAVHCHAGLGRTGVLIAC-YLVYALRMSADQAIRLV---- 146
                        90       100
                ....*....|....*....|....*
gi 13677220 333 RSYRMSMVQTEEQYIFIHQCVQLMW 357
Cdd:cd14506 147 RSKRPNSIQTRGQVLCVREFAQFLL 171
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
262-310 6.41e-05

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


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 43.21  E-value: 6.41e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 13677220 262 PDHGVPTanaaESILQ-FVHMVRqqatKSKGPMIIHCSAGVGRTGTFIAL 310
Cdd:cd14499  88 PDGSTPS----DDIVKkFLDICE----NEKGAIAVHCKAGLGRTGTLIAC 129
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
265-310 8.75e-04

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


Pssm-ID: 350378 [Multi-domain]  Cd Length: 158  Bit Score: 39.66  E-value: 8.75e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 13677220 265 GVPTANAAESILQFvhMVRQQAtksKGPMIIHCSAGVGRTGTFIAL 310
Cdd:cd14529  69 TRPTESDVQSFLLI--MDLKLA---PGPVLIHCKHGKDRTGLVSAL 109
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
262-308 1.39e-03

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


Pssm-ID: 350360 [Multi-domain]  Cd Length: 177  Bit Score: 39.27  E-value: 1.39e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 13677220 262 PDHGVPTAnaaESILQFVHMVRQQATK-SKGPMIIHCSAGVGRTGTFI 308
Cdd:cd14510  82 DDHNVPTL---DEMLSFTAEVREWMAAdPKNVVAIHCKGGKGRTGTMV 126
COG5350 COG5350
Predicted protein tyrosine phosphatase [General function prediction only];
262-318 1.40e-03

Predicted protein tyrosine phosphatase [General function prediction only];


Pssm-ID: 444131  Cd Length: 165  Bit Score: 39.07  E-value: 1.40e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13677220 262 PDHGVPTANAAESILQFVHMVRQQAtkskgPMIIHCSAGVGRT--GTFIAL---------DRLLQHIR 318
Cdd:COG5350  58 PGLILPTEEHVEALLAFGRDWDREA-----PLLVHCHAGISRStaAALIAAaalnpdrdeAELAQRLR 120
Y_phosphatase3 pfam13350
Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 ...
223-310 2.43e-03

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


Pssm-ID: 463853 [Multi-domain]  Cd Length: 243  Bit Score: 39.15  E-value: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220   223 DITVEMIS--EEEQDDWACRHFRINYADEMQDVMHFNYTAWPDHgvptanAAESILQFVHMVRQQAtkskGPMIIHCSAG 300
Cdd:pfam13350  70 DVRYVHLPvaDSEASSPELLARRALDPDDGEEFMAELYRDMVTS------ARAAYRALFEALADND----GPVLFHCTAG 139
                          90
                  ....*....|
gi 13677220   301 VGRTGTFIAL 310
Cdd:pfam13350 140 KDRTGVAAAL 149
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
245-310 2.88e-03

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 38.08  E-value: 2.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220  245 NYADEMQD--------VMHFNYTA------------WP--DHGVPTANAAESILQFVHMVRQQATKSKGPMIIHCSAGVG 302
Cdd:PTZ00242  31 LYIKELQRynvthlvrVCGPTYDAellekngievhdWPfdDGAPPPKAVIDNWLRLLDQEFAKQSTPPETIAVHCVAGLG 110

                 ....*...
gi 13677220  303 RTGTFIAL 310
Cdd:PTZ00242 111 RAPILVAL 118
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
255-309 3.84e-03

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 37.26  E-value: 3.84e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 13677220    255 HFNYTAWP---DHGVPTANAAESILQFVHmvrqQATKSKGPMIIHCSAGVGRTGTFIA 309
Cdd:smart00195  44 DFTYLGVPiddNTETKISPYFPEAVEFIE----DAESKGGKVLVHCQAGVSRSATLII 97
PTPlike_phytase pfam14566
Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in ...
214-314 4.75e-03

Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in abundance in seeds and acting as an inorganic phosphate reservoir. Phytases are phosphatases that hydrolyze phytate to less-phosphorylated myo-inositol derivatives and inorganic phosphate. The active-site sequence (HCXXGXGR) of the phytase identified from the gut micro-organizm Selenomonas ruminantium forms a loop (P loop) at the base of a substrate binding pocket that is characteriztic of protein tyrosine phosphatases (PTPs). The depth of this pocket is an important determinant of the substrate specificity of PTPs. In humans this enzyme is thought to aid bone mineralization and salvage the inositol moiety prior to apoptosis.


Pssm-ID: 464208 [Multi-domain]  Cd Length: 157  Bit Score: 37.29  E-value: 4.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220   214 FTEEPIAYGDI-TVEMISEEEQDD-WACRHFRInyademqdvmhfnytAWPDHGVPTANAAESILQFVhmvrqQATKSKG 291
Cdd:pfam14566  74 LTVVDVWESDVqTPEEVYERLKAEgPGVDYRRI---------------PITDEKAPLEEDFDALISIV-----KDAPEDT 133
                          90       100
                  ....*....|....*....|...
gi 13677220   292 PMIIHCSAGVGRTGTFIALDRLL 314
Cdd:pfam14566 134 ALVFNCQMGRGRTTTAMVIADLV 156
PTPLP-like cd14495
Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily ...
254-326 5.43e-03

Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily contains the tandem protein tyrosine phosphatase (PTP)-like domains of protein tyrosine phosphatase-like phytases (PTPLPs) and similar domains including the PTP domain of Pseudomonas syringae tyrosine-protein phosphatase hopPtoD2. PTPLPs, also known as cysteine phytases, are one of four known classes of phytases, enzymes that degrade phytate (inositol hexakisphosphate [InsP(6)]) to less-phosphorylated myo-inositol derivatives. Phytate is the most abundant cellular inositol phosphate and plays important roles in a broad scope of cellular processes, including DNA repair, RNA processing and export, development, apoptosis, and pathogenicity. PTPLPs adopt a PTP fold, including the active-site signature sequence (CX5R(S/T)) and utilize a classical PTP reaction mechanism. However, these enzymes display no catalytic activity against classical PTP substrates due to several unique structural features that confer specificity for myo-inositol polyphosphates.


Pssm-ID: 350345  Cd Length: 278  Bit Score: 38.12  E-value: 5.43e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13677220 254 MHFNYTAWPDHGVPTAnaaESILQFVHMVRQqaTKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDIL 326
Cdd:cd14495 155 AHYVRIAATDHVWPDD---EEIDAFVAFYRS--LPADAWLHFHCRAGKGRTTTFMVMYDMLKNPKDVSFDDII 222
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
241-309 8.55e-03

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


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 36.79  E-value: 8.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13677220 241 HFRI-NYADEMQD--------VMHFNytaWPDHGVPTANAAESILQfvHMvrqQATKSKGPM---IIHCSAGVGRTGTFI 308
Cdd:cd14497  42 HYMIfNLSEEEYDddskfegrVLHYG---FPDHHPPPLGLLLEIVD--DI---DSWLSEDPNnvaVVHCKAGKGRTGTVI 113

                .
gi 13677220 309 A 309
Cdd:cd14497 114 C 114
 
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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