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Conserved domains on  [gi|281360500|ref|NP_722672|]
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IA-2 protein tyrosine phosphatase, isoform D [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 929-1212 3.41e-156

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.


The actual alignment was detected with superfamily member cd14610:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 283  Bit Score: 470.31  E-value: 3.41e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  929 TGHMVLSYMEDHLRNKGRLQREWEALCRYEAEPSAREAASQPQCAGLNRPGAPLPYDHSRVVLNHLANAEGLDYVNASTI 1008
Cdd:cd14610     1 TGHMILSYMEDHLKNKNRLEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1009 TDHDPRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVACARYWPEEGAEVYHIYEVHLVSEHIWCDDYL 1088
Cdd:cd14610    81 MDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIWCEDFL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1089 VRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVNKSYRGrRSCPIVVHGSAGAGRTGVYILLDLVLERM 1168
Cdd:cd14610   161 VRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRG-RSCPIIVHCSDGAGRSGTYILIDMVLNKM 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 281360500 1169 NKGAREIDIAATLEHLRDQRAGVVATRQQFEFVLMAVAEEVHAI 1212
Cdd:cd14610   240 AKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVNAI 283
Receptor_IA-2 super family cl13063
Protein-tyrosine phosphatase receptor IA-2; IA-2 is a protein-tyrosine phosphatase receptor ...
 692-782 5.29e-30

Protein-tyrosine phosphatase receptor IA-2; IA-2 is a protein-tyrosine phosphatase receptor that upon exocytosis, the cytoplasmic domain is cleaved and moves to the nucleus where it enhances transcription of the insulin gene. The mature exodomain of IA-2 participates in adhesion to the extracellular matrix and is self-proteolyzed in vitro by reactive oxygen species which may be a new shedding mechanism.


The actual alignment was detected with superfamily member pfam11548:

Pssm-ID: 463293  Cd Length: 89  Bit Score: 114.25  E-value: 5.29e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500   692 TEYVHVFVKNPIDSWNDGQRIMKELEQILHMQ-GYFSYLTVQQHEVSFRVNSnNPERKTAGDVARTINENrgvKNNIQRR 770
Cdd:pfam11548    1 EEYGYIVTDNDPLSWEEGLRLMEKVAELLHLPmSSFADIRVLGPAVTFKVRA-NNKNLTAADVAKAAVDI---KDKLEKE 76

                           90
                   ....*....|..
gi 281360500   771 VGFYVLHAGVGD 782
Cdd:pfam11548   77 TGLKILQAGVGD 88
 
Name Accession Description Interval E-value
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 929-1212 3.41e-156

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: 470.31  E-value: 3.41e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  929 TGHMVLSYMEDHLRNKGRLQREWEALCRYEAEPSAREAASQPQCAGLNRPGAPLPYDHSRVVLNHLANAEGLDYVNASTI 1008
Cdd:cd14610     1 TGHMILSYMEDHLKNKNRLEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1009 TDHDPRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVACARYWPEEGAEVYHIYEVHLVSEHIWCDDYL 1088
Cdd:cd14610    81 MDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIWCEDFL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1089 VRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVNKSYRGrRSCPIVVHGSAGAGRTGVYILLDLVLERM 1168
Cdd:cd14610   161 VRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRG-RSCPIIVHCSDGAGRSGTYILIDMVLNKM 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 281360500 1169 NKGAREIDIAATLEHLRDQRAGVVATRQQFEFVLMAVAEEVHAI 1212
Cdd:cd14610   240 AKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVNAI 283
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
947-1207 3.42e-87

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 283.78  E-value: 3.42e-87
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500    947 LQREWEALCRYEAEPSAREAASQPQCAGLNRPGAPLPYDHSRVVLNHLaNAEGLDYVNASTITDHDPRaPAYVAAQGPLP 1026
Cdd:smart00194    2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPP-PGEGSDYINASYIDGPNGP-KAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500   1027 STLAHFWQMIWEQGAVVIVALCRLQENGEVACARYWPEEG--AEVYHIYEVHLVSEHIwCDDYLVRSFYLKNLRTSETRT 1104
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgePLTYGDITVTLKSVEK-VDDYTIRTLEVTNTGCSETRT 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500   1105 VTQFHFLSWPHMGVPAQAKALLDFRRKVNKSYrGRRSCPIVVHGSAGAGRTGVYILLDLVLERMNKGaREIDIAATLEHL 1184
Cdd:smart00194  159 VTHYHYTNWPDHGVPESPESILDLIRAVRKSQ-STSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAG-KEVDIFEIVKEL 236

                           250       260
                    ....*....|....*....|...
gi 281360500   1185 RDQRAGVVATRQQFEFVLMAVAE 1207
Cdd:smart00194  237 RSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
976-1207 3.69e-87

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 282.59  E-value: 3.69e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500   976 NRPGAPLPYDHSRVVLNHLANAEglDYVNASTITDHdPRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGE 1055
Cdd:pfam00102    5 NRYKDVLPYDHTRVKLTGDPGPS--DYINASYIDGY-KKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKGR 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  1056 VACARYWPE--EGAEVYHIYEVHLVSEHIWCDDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVN 1133
Cdd:pfam00102   82 EKCAQYWPEeeGESLEYGDFTVTLKKEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRKVR 161

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281360500  1134 KSYRGRRSCPIVVHGSAGAGRTGVYILLDLVLERMNKGaREIDIAATLEHLRDQRAGVVATRQQFEFVLMAVAE 1207
Cdd:pfam00102  162 KSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAE-GEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
Receptor_IA-2 pfam11548
Protein-tyrosine phosphatase receptor IA-2; IA-2 is a protein-tyrosine phosphatase receptor ...
 692-782 5.29e-30

Protein-tyrosine phosphatase receptor IA-2; IA-2 is a protein-tyrosine phosphatase receptor that upon exocytosis, the cytoplasmic domain is cleaved and moves to the nucleus where it enhances transcription of the insulin gene. The mature exodomain of IA-2 participates in adhesion to the extracellular matrix and is self-proteolyzed in vitro by reactive oxygen species which may be a new shedding mechanism.


Pssm-ID: 463293  Cd Length: 89  Bit Score: 114.25  E-value: 5.29e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500   692 TEYVHVFVKNPIDSWNDGQRIMKELEQILHMQ-GYFSYLTVQQHEVSFRVNSnNPERKTAGDVARTINENrgvKNNIQRR 770
Cdd:pfam11548    1 EEYGYIVTDNDPLSWEEGLRLMEKVAELLHLPmSSFADIRVLGPAVTFKVRA-NNKNLTAADVAKAAVDI---KDKLEKE 76

                           90
                   ....*....|..
gi 281360500   771 VGFYVLHAGVGD 782
Cdd:pfam11548   77 TGLKILQAGVGD 88
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 978-1205 2.57e-28

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 116.64  E-value: 2.57e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  978 PGAPLpYDHSRVVLNhlANAEGLDYVNASTITDHDPRApAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVA 1057
Cdd:PHA02742   59 PDAPC-FDRNRVILK--IEDGGDDFINASYVDGHNAKG-RFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEA 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1058 CARYW-PEEGAEVYHiYEVHLVSEHIWC-DDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKV--- 1132
Cdd:PHA02742  135 CYPYWmPHERGKATH-GEFKIKTKKIKSfRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLAVrea 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1133 -------NKSYRGRRSCPIVVHGSAGAGRTGVYILLDLVLERMNKGArEIDIAATLEHLRDQRAGVVATRQQFEFVLMAV 1205
Cdd:PHA02742  214 dlkadvdIKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERA-IIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIV 292
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
930-1213 1.04e-25

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 108.64  E-value: 1.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  930 GHMVLSYMEDHLRNkgRLQREWEALcRYEAEPSAREaaSQPQCAGLNRPGAPLPYDHSRVVLNhlanaegLDYVNASTIT 1009
Cdd:COG5599     5 NPIAIKSEEEKINS--RLSTLTNEL-APSHNDPQYL--QNINGSPLNRFRDIQPYKETALRAN-------LGYLNANYIQ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1010 DHDPRApaYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQE--NGEVACARYWPEEGAevYHIYEVHL-VSEHIWC-D 1085
Cdd:COG5599    73 VIGNHR--YIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEisKPKVKMPVYFRQDGE--YGKYEVSSeLTESIQLrD 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1086 DYLVRSFYLKNLRTS-ETRTVTQFHFLSWP-HMGVPAQA-KALLDFRRKVNKSYRGRRScPIVVHGSAGAGRTGVYILLd 1162
Cdd:COG5599   149 GIEARTYVLTIKGTGqKKIEIPVLHVKNWPdHGAISAEAlKNLADLIDKKEKIKDPDKL-LPVVHCRAGVGRTGTLIAC- 226

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 281360500 1163 LVLERMNKGAREIDIAA--TLEHLRDQRA-GVVATRQQFEfVLMAVAEEVHAIL 1213
Cdd:COG5599   227 LALSKSINALVQITLSVeeIVIDMRTSRNgGMVQTSEQLD-VLVKLAEQQIRPL 279
 
Name Accession Description Interval E-value
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 929-1212 3.41e-156

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: 470.31  E-value: 3.41e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  929 TGHMVLSYMEDHLRNKGRLQREWEALCRYEAEPSAREAASQPQCAGLNRPGAPLPYDHSRVVLNHLANAEGLDYVNASTI 1008
Cdd:cd14610     1 TGHMILSYMEDHLKNKNRLEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1009 TDHDPRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVACARYWPEEGAEVYHIYEVHLVSEHIWCDDYL 1088
Cdd:cd14610    81 MDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIWCEDFL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1089 VRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVNKSYRGrRSCPIVVHGSAGAGRTGVYILLDLVLERM 1168
Cdd:cd14610   161 VRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRG-RSCPIIVHCSDGAGRSGTYILIDMVLNKM 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 281360500 1169 NKGAREIDIAATLEHLRDQRAGVVATRQQFEFVLMAVAEEVHAI 1212
Cdd:cd14610   240 AKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVNAI 283
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 931-1212 7.33e-147

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: 445.64  E-value: 7.33e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  931 HMVLSYMEDHLRNKGRLQREWEALCRYEAEPSAREAASQPQCAGLNRPGAPLPYDHSRVVLNHLANAEGLDYVNASTITD 1010
Cdd:cd14609     1 HMILAYMEDHLRNRDRLAKEWQALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1011 HDPRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVACARYWPEEGAEVYHIYEVHLVSEHIWCDDYLVR 1090
Cdd:cd14609    81 HDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIWCEDFLVR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1091 SFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVNKSYRGrRSCPIVVHGSAGAGRTGVYILLDLVLERMNK 1170
Cdd:cd14609   161 SFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRG-RSCPIIVHCSDGAGRTGTYILIDMVLNRMAK 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 281360500 1171 GAREIDIAATLEHLRDQRAGVVATRQQFEFVLMAVAEEVHAI 1212
Cdd:cd14609   240 GVKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAEEVNAI 281
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 1002-1210 1.15e-146

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: 441.88  E-value: 1.15e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1002 YVNASTITDHDPRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVACARYWPEEGAEVYHIYEVHLVSEH 1081
Cdd:cd14546     1 YINASTIYDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEVHLVSEH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1082 IWCDDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVNKSYRGrRSCPIVVHGSAGAGRTGVYILL 1161
Cdd:cd14546    81 IWCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRG-RSCPIVVHCSDGAGRTGTYILI 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 281360500 1162 DLVLERMNKGAREIDIAATLEHLRDQRAGVVATRQQFEFVLMAVAEEVH 1210
Cdd:cd14546   160 DMVLNRMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAEEVN 208
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
947-1207 3.42e-87

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 283.78  E-value: 3.42e-87
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500    947 LQREWEALCRYEAEPSAREAASQPQCAGLNRPGAPLPYDHSRVVLNHLaNAEGLDYVNASTITDHDPRaPAYVAAQGPLP 1026
Cdd:smart00194    2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPP-PGEGSDYINASYIDGPNGP-KAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500   1027 STLAHFWQMIWEQGAVVIVALCRLQENGEVACARYWPEEG--AEVYHIYEVHLVSEHIwCDDYLVRSFYLKNLRTSETRT 1104
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgePLTYGDITVTLKSVEK-VDDYTIRTLEVTNTGCSETRT 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500   1105 VTQFHFLSWPHMGVPAQAKALLDFRRKVNKSYrGRRSCPIVVHGSAGAGRTGVYILLDLVLERMNKGaREIDIAATLEHL 1184
Cdd:smart00194  159 VTHYHYTNWPDHGVPESPESILDLIRAVRKSQ-STSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAG-KEVDIFEIVKEL 236

                           250       260
                    ....*....|....*....|...
gi 281360500   1185 RDQRAGVVATRQQFEFVLMAVAE 1207
Cdd:smart00194  237 RSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
976-1207 3.69e-87

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 282.59  E-value: 3.69e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500   976 NRPGAPLPYDHSRVVLNHLANAEglDYVNASTITDHdPRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGE 1055
Cdd:pfam00102    5 NRYKDVLPYDHTRVKLTGDPGPS--DYINASYIDGY-KKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKGR 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  1056 VACARYWPE--EGAEVYHIYEVHLVSEHIWCDDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVN 1133
Cdd:pfam00102   82 EKCAQYWPEeeGESLEYGDFTVTLKKEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRKVR 161

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281360500  1134 KSYRGRRSCPIVVHGSAGAGRTGVYILLDLVLERMNKGaREIDIAATLEHLRDQRAGVVATRQQFEFVLMAVAE 1207
Cdd:pfam00102  162 KSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAE-GEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1002-1201 3.32e-73

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: 242.19  E-value: 3.32e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1002 YVNASTITDHDPRaPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVACARYWPEEGAE--VYHIYEVHLVS 1079
Cdd:cd00047     1 YINASYIDGYRGP-KEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKplEYGDITVTLVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1080 EHIwCDDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVNKSYRGRRScPIVVHGSAGAGRTGVYI 1159
Cdd:cd00047    80 EEE-LSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNG-PIVVHCSAGVGRTGTFI 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 281360500 1160 LLDLVLERMNKGaREIDIAATLEHLRDQRAGVVATRQQFEFV 1201
Cdd:cd00047   158 AIDILLERLEAE-GEVDVFEIVKALRKQRPGMVQTLEQYEFI 198
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 976-1209 2.00e-63

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: 215.72  E-value: 2.00e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  976 NRPGAPLPYDHSRVVLNHLANAEGLDYVNASTITDHDpRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGE 1055
Cdd:cd14553     7 NRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYR-KQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEERSR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1056 VACARYWPEEGAEVYHIYEVHLVsEHIWCDDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVnKS 1135
Cdd:cd14553    86 VKCDQYWPTRGTETYGLIQVTLL-DTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRV-KA 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281360500 1136 YRGRRSCPIVVHGSAGAGRTGVYILLDLVLERMnKGAREIDIAATLEHLRDQRAGVVATRQQFEFVLMAVAEEV 1209
Cdd:cd14553   164 CNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERI-KHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEAV 236
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 949-1200 9.57e-63

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: 214.92  E-value: 9.57e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  949 REWEALcRYEAEPSAREAASQPQCAGLNRPGAPLPYDHSRVVLNHLANAEGLDYVNAStITDHDPRAPAYVAAQGPLPST 1028
Cdd:cd14543     7 EEYEDI-RREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINAN-FMDGYKQKNAYIATQGPLPKT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1029 LAHFWQMIWEQGAVVIVALCRLQENGEVACARYWPEEGAEVYHIYEVHLVSEHIWC-DDYLVRSFYLKNLRTSETRTVTQ 1107
Cdd:cd14543    85 YSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENkEHYKKTTLEIHNTETDESRQVTH 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1108 FHFLSWPHMGVPAQAKALLDFRRKVnKSYRgRRSC--------------PIVVHGSAGAGRTGVYILLDLVLERMNKgAR 1173
Cdd:cd14543   165 FQFTSWPDFGVPSSAAALLDFLGEV-RQQQ-ALAVkamgdrwkghppgpPIVVHCSAGIGRTGTFCTLDICLSQLED-VG 241

                         250       260
                  ....*....|....*....|....*..
gi 281360500 1174 EIDIAATLEHLRDQRAGVVATRQQFEF 1200
Cdd:cd14543   242 TLNVMQTVRRMRTQRAFSIQTPDQYYF 268
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 976-1204 4.21e-58

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: 200.44  E-value: 4.21e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  976 NRPGAPLPYDHSRVVLNHLANAEGLDYVNASTITDHDPRApAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGE 1055
Cdd:cd14554    10 NRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRG-AYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLREMGR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1056 VACARYWPEEGAEVYHIYEVHLVSEHIWcDDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVNKS 1135
Cdd:cd14554    89 EKCHQYWPAERSARYQYFVVDPMAEYNM-PQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKT 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1136 Y-RGRRSCPIVVHGSAGAGRTGVYILLDLVLERMnKGAREIDIAATLEHLRDQRAGVVATRQQFEFVLMA 1204
Cdd:cd14554   168 KeQFGQEGPITVHCSAGVGRTGVFITLSIVLERM-RYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 982-1201 6.56e-58

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: 199.50  E-value: 6.56e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  982 LPYDHSRVVLNHLANAEGLDYVNASTITD-HDPRApaYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVACAR 1060
Cdd:cd14548     6 LPYDHSRVKLIPINEEEGSDYINANYIPGyNSPRE--FIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVKCDH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1061 YWPEEGAEVYH--IyEVHLVSEHIwCDDYLVRSFYLKnlRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVnKSYRG 1138
Cdd:cd14548    84 YWPFDQDPVYYgdI-TVTMLSESV-LPDWTIREFKLE--RGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLV-RDYIK 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281360500 1139 RRSCPIVVHGSAGAGRTGVYILLDLVLERMNKgAREIDIAATLEHLRDQRAGVVATRQQFEFV 1201
Cdd:cd14548   159 QEKGPTIVHCSAGVGRTGTFIALDRLLQQIES-EDYVDIFGIVYDLRKHRPLMVQTEAQYIFL 220
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 976-1206 1.53e-56

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: 196.53  E-value: 1.53e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  976 NRPGAPLPYDHSRVVLNHLANAE-GLDYVNASTI------TDHDPRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALC 1048
Cdd:cd14544     5 NRYKNILPFDHTRVILKDRDPNVpGSDYINANYIrnenegPTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVIVMTT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1049 RLQENGEVACARYWPEEGA-EVYHIYEVHLVSEHIwCDDYLVRSFYLKNL-RTSETRTVTQFHFLSWPHMGVPAQAKALL 1126
Cdd:cd14544    85 KEVERGKNKCVRYWPDEGMqKQYGPYRVQNVSEHD-TTDYTLRELQVSKLdQGDPIREIWHYQYLSWPDHGVPSDPGGVL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1127 DFRRKVNKSYRGR-RSCPIVVHGSAGAGRTGVYILLDLVLERMNKG--AREIDIAATLEHLRDQRAGVVATRQQFEFVLM 1203
Cdd:cd14544   164 NFLEDVNQRQESLpHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKglDCDIDIQKTIQMVRSQRSGMVQTEAQYKFIYV 243


                  ...
gi 281360500 1204 AVA 1206
Cdd:cd14544   244 AVA 246
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1002-1201 6.92e-56

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: 192.95  E-value: 6.92e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1002 YVNASTItDHDPRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVACARYWPEEGAEVYHIYEVHLVSEH 1081
Cdd:cd14549     1 YINANYV-DGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1082 IWCdDYLVRSFYLKNLR------TSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVNkSYRGRRSCPIVVHGSAGAGRT 1155
Cdd:cd14549    80 VLA-TYTVRTFSLKNLKlkkvkgRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSS-AANPPGAGPIVVHCSAGVGRT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 281360500 1156 GVYILLDLVLERMnKGAREIDIAATLEHLRDQRAGVVATRQQFEFV 1201
Cdd:cd14549   158 GTYIVIDSMLQQI-QDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFI 202
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 976-1209 6.59e-54

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: 189.86  E-value: 6.59e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  976 NRPGAPLPYDHSRVVLNHLANAEGLDYVNASTItDHDPRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGE 1055
Cdd:cd14626    45 NRYANVIAYDHSRVILTSVDGVPGSDYINANYI-DGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSR 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1056 VACARYWPEEGAEVYHIYEVHLVsEHIWCDDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVnKS 1135
Cdd:cd14626   124 VKCDQYWPIRGTETYGMIQVTLL-DTVELATYSVRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRV-KA 201

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281360500 1136 YRGRRSCPIVVHGSAGAGRTGVYILLDLVLERMnKGAREIDIAATLEHLRDQRAGVVATRQQFEFVLMAVAEEV 1209
Cdd:cd14626   202 CNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERM-KHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAA 274
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 975-1200 4.27e-53

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: 185.67  E-value: 4.27e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  975 LNRPGAPLPYDHSRVVLnHLANaEGLDYVNASTItdHDPRAP-AYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQEN 1053
Cdd:cd14545     1 LNRYRDRDPYDHDRSRV-KLKQ-GDNDYINASLV--EVEEAKrSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1054 GEVACARYWPEEGAEVYHI----YEVHLVSEHIWcDDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFR 1129
Cdd:cd14545    77 GQIKCAQYWPQGEGNAMIFedtgLKVTLLSEEDK-SYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281360500 1130 RKVNKSyrGRRSC---PIVVHGSAGAGRTGVYILLDLVLERMNKG-AREIDIAATLEHLRDQRAGVVATRQQFEF 1200
Cdd:cd14545   156 QKVRES--GSLSSdvgPPVVHCSAGIGRSGTFCLVDTCLVLIEKGnPSSVDVKKVLLEMRKYRMGLIQTPDQLRF 228
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1002-1201 2.20e-52

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: 183.22  E-value: 2.20e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1002 YVNASTITDHDPRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVACARYWPEEGAEVYH-IYEVHLVSE 1080
Cdd:cd18533     1 YINASYITLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYgDLTVELVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1081 H-IWCDDYLVRSFYLKNlRTSETRTVTQFHFLSWPHMGVPAQAKALL---DFRRKVNKSyrGRRSCPIVVHGSAGAGRTG 1156
Cdd:cd18533    81 EeNDDGGFIVREFELSK-EDGKVKKVYHIQYKSWPDFGVPDSPEDLLtliKLKRELNDS--ASLDPPIIVHCSAGVGRTG 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 281360500 1157 VYILLDLVLERMNKGAREID--------IAATLEHLRDQRAGVVATRQQFEFV 1201
Cdd:cd18533   158 TFIALDSLLDELKRGLSDSQdledsedpVYEIVNQLRKQRMSMVQTLRQYIFL 210
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1001-1215 1.60e-51

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: 180.60  E-value: 1.60e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1001 DYVNASTITDHDPRAPA---YVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVACARYWPEEGAEVYH-IYEVH 1076
Cdd:cd14541     1 DYINANYVNMEIPGSGIvnrYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFgNLQIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1077 LVSEHIwCDDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVNKsYRGRRSCPIVVHGSAGAGRTG 1156
Cdd:cd14541    81 CVSEEV-TPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQ-NRVGMVEPTVVHCSAGIGRTG 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281360500 1157 VYILLD--LVLERMNKGAREIDIaatLEHLRDQRAGVVATRQQFEFVLmavaeevHAILKA 1215
Cdd:cd14541   159 VLITMEtaMCLIEANEPVYPLDI---VRTMRDQRAMLIQTPSQYRFVC-------EAILRV 209
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1002-1201 1.71e-51

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: 180.31  E-value: 1.71e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1002 YVNASTITDHDpRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVACARYWPEEGAEV--YHIYEVHLVS 1079
Cdd:cd14542     1 YINANFIKGVS-GSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQlqFGPFKISLEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1080 EHIWCDDYLVRSfyLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVnKSYRGRRSCPIVVHGSAGAGRTGVYI 1159
Cdd:cd14542    80 EKRVGPDFLIRT--LKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLV-RDYQGSEDVPICVHCSAGCGRTGTIC 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 281360500 1160 LLDLV--LERMNKGAREIDIAATLEHLRDQRAGVVATRQQFEFV 1201
Cdd:cd14542   157 AIDYVwnLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELV 200
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 976-1201 3.60e-51

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: 180.47  E-value: 3.60e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  976 NRPGAPLPYDHSRVVLNHLANAEGLDYVNASTITDH-DPRApaYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENG 1054
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYwSSQE--FIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1055 EVACARYWPEEGAE-VYHIYEVHLVSEHIwCDDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVN 1133
Cdd:cd14619    79 RVKCEHYWPLDYTPcTYGHLRVTVVSEEV-MENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLR 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281360500 1134 KSYRGRRSC-PIVVHGSAGAGRTGVYILLDLVLERMNKGAReIDIAATLEHLRDQRAGVVATRQQFEFV 1201
Cdd:cd14619   158 QWLDQTMSGgPTVVHCSAGVGRTGTLIALDVLLQQLQSEGL-LGPFSFVQKMRENRPLMVQTESQYVFL 225
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 982-1207 4.15e-51

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: 180.14  E-value: 4.15e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  982 LPYDHSRVVLNHLANAEGLDYVNASTITDHDPRApAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVACARY 1061
Cdd:cd14620     5 LPYDHSRVILSQLDGIPCSDYINASYIDGYKEKN-KFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKCYQY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1062 WPEEGAEVYHIYEVhLVSEHIWCDDYLVRSFYLKNLRTSET---RTVTQFHFLSWPHMGVPAQAKALLDFRRKVnKSYRG 1138
Cdd:cd14620    84 WPDQGCWTYGNIRV-AVEDCVVLVDYTIRKFCIQPQLPDGCkapRLVTQLHFTSWPDFGVPFTPIGMLKFLKKV-KSVNP 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281360500 1139 RRSCPIVVHGSAGAGRTGVYILLDLVLERMNKGAReIDIAATLEHLRDQRAGVVATRQQFEFVLMAVAE 1207
Cdd:cd14620   162 VHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQK-VDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 956-1213 6.84e-51

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: 181.38  E-value: 6.84e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  956 RYEAEPSAREAASQPQCAGLNRPGAPLPYDHSRVVLNHLANaeglDYVNASTITDHDPRApAYVAAQGPLPSTLAHFWQM 1035
Cdd:cd14608     9 RHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDN----DYINASLIKMEEAQR-SYILTQGPLPNTCGHFWEM 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1036 IWEQGAVVIVALCRLQENGEVACARYWP--EEGAEVYHI--YEVHLVSEHIWcDDYLVRSFYLKNLRTSETRTVTQFHFL 1111
Cdd:cd14608    84 VWEQKSRGVVMLNRVMEKGSLKCAQYWPqkEEKEMIFEDtnLKLTLISEDIK-SYYTVRQLELENLTTQETREILHFHYT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1112 SWPHMGVPAQAKALLDFRRKVNKSyrGRRS---CPIVVHGSAGAGRTGVYILLDLVLERMN--KGAREIDIAATLEHLRD 1186
Cdd:cd14608   163 TWPDFGVPESPASFLNFLFKVRES--GSLSpehGPVVVHCSAGIGRSGTFCLADTCLLLMDkrKDPSSVDIKKVLLEMRK 240

                         250       260
                  ....*....|....*....|....*..
gi 281360500 1187 QRAGVVATRQQFEFVLMAVAEEVHAIL 1213
Cdd:cd14608   241 FRMGLIQTADQLRFSYLAVIEGAKFIM 267
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 976-1201 3.15e-50

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: 177.70  E-value: 3.15e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  976 NRPGAPLPYDHSRV---VLNHLANaeglDYVNASTITDHDpRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQE 1052
Cdd:cd14615     1 NRYNNVLPYDISRVklsVQSHSTD----DYINANYMPGYN-SKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1053 NGEVACARYWPEEGAEVYHIYEVHLVSEhIWCDDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKV 1132
Cdd:cd14615    76 QGRTKCEEYWPSKQKKDYGDITVTMTSE-IVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLV 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1133 NK-SYRGRRSCPIVVHGSAGAGRTGVYILLDLVLERMNKgAREIDIAATLEHLRDQRAGVVATRQQFEFV 1201
Cdd:cd14615   155 REyMKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIEN-ENVVDVYGIVYDLRMHRPLMVQTEDQYVFL 223
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1002-1205 5.46e-50

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: 175.92  E-value: 5.46e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1002 YVNASTITDHDPRaPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVACARYWPEEGAEVYHIYEVHLVSEH 1081
Cdd:cd14552     1 YINASFIDGYRQK-DAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1082 IwCDDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVNKSYRGRRSCPIVVHGSAGAGRTGVYILL 1161
Cdd:cd14552    80 D-YEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGNHPITVHCSAGAGRTGTFCAL 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 281360500 1162 DLVLERMnKGAREIDIAATLEHLRDQRAGVVATRQQFEFVLMAV 1205
Cdd:cd14552   159 STVLERV-KAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1002-1207 1.60e-49

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: 174.48  E-value: 1.60e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1002 YVNASTItdhdpRAPA------YVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVACARYWPEEGAE---VYHI 1072
Cdd:cd14538     1 YINASHI-----RIPVggdtyhYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKpliCGGR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1073 YEVHLVSEHIWcDDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVNKSYrgrRSCPIVVHGSAGA 1152
Cdd:cd14538    76 LEVSLEKYQSL-QDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIH---NSGPIVVHCSAGI 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 281360500 1153 GRTGVYILLDLVLERMNKGaREIDIAATLEHLRDQRAGVVATRQQFEFVLMAVAE 1207
Cdd:cd14538   152 GRTGVLITIDVALGLIERD-LPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 976-1201 1.69e-49

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; The kinase interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes tyrosine-protein phosphatases non-receptor type 7 (PTPN7) and non-receptor type 5 (PTPN5), and protein-tyrosine phosphatase receptor type R (PTPRR). PTPN7 is also called hematopoietic protein-tyrosine phosphatase (HePTP) while PTPN5 is also called striatal-enriched protein-tyrosine phosphatase (STEP). They belong to the family of classical tyrosine-specific PTPs (EC 3.1.3.48) that catalyze the dephosphorylation of phosphotyrosine peptides. KIM-PTPs are characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. They are highly specific to the MAPKs ERK1/2 (extracellular-signal-regulated kinase 1/2) and p38, over JNK (c-Jun N-terminal kinase); they dephosphorylate these kinases and thereby critically modulate cell proliferation and differentiation.


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 175.28  E-value: 1.69e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  976 NRPGAPLPYDHSRVVLNHLANAEGLDYVNASTITDHDPRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGE 1055
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1056 vACARYWPEEGAEVYHIYEVhLVSEHIWCDDYLVRSFYLKNlrTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVNKS 1135
Cdd:cd14547    81 -KCAQYWPEEENETYGDFEV-TVQSVKETDGYTVRKLTLKY--GGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEA 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281360500 1136 YRGRRSC-PIVVHGSAGAGRTGVYILLDLVLERMnKGAREIDIAATLEHLRDQRAGVVATRQQFEFV 1201
Cdd:cd14547   157 RQTEPHRgPIVVHCSAGIGRTGCFIATSIGCQQL-REEGVVDVLGIVCQLRLDRGGMVQTAEQYEFV 222
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 950-1210 1.81e-49

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: 177.15  E-value: 1.81e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  950 EWEALCRYEAEPS-AREAASQPQCAGLNRPGAPLPYDHSRVVLNHLA--NAEGLDYVNASTITDHDpRAPAYVAAQGPLP 1026
Cdd:cd17667     4 DFEEVQRCTADMNiTAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPgkDSKHSDYINANYVDGYN-KAKAYIATQGPLK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1027 STLAHFWQMIWEQGAVVIVALCRLQENGEVACARYWPEEGAEVYHIYEVHLVSEHIW-CddYLVRSFYLKNLRTSE---- 1101
Cdd:cd17667    83 STFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHaC--YTVRRFSIRNTKVKKgqkg 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1102 -------TRTVTQFHFLSWPHMGVPAQAKALLDFRRKvNKSYRGRRSCPIVVHGSAGAGRTGVYILLDLVLERMnKGARE 1174
Cdd:cd17667   161 npkgrqnERTVIQYHYTQWPDMGVPEYALPVLTFVRR-SSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQI-KDKST 238

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 281360500 1175 IDIAATLEHLRDQRAGVVATRQQFEFVLMAVAEEVH 1210
Cdd:cd17667   239 VNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 964-1207 1.93e-49

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein phosphatase non-receptor type 6 (PTPN6), also called SH2 domain-containing protein-tyrosine phosphatase 1 (SHP1 or SHP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN6 expression is restricted mainly to hematopoietic and epithelial cells. It is an important regulator of hematopoietic cells, downregulating pathways that promote cell growth, survival, adhesion, and activation. It regulates glucose homeostasis by modulating insulin signalling in the liver and muscle, and it also negatively regulates bone resorption, affecting both the formation and the function of osteoclasts. PTPN6 contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350454 [Multi-domain]  Cd Length: 266  Bit Score: 176.61  E-value: 1.93e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  964 REAASQPQCAGLNRPGAPLPYDHSRVVL-NHLANAEGLDYVNASTITDH----DPRAPAYVAAQGPLPSTLAHFWQMIWE 1038
Cdd:cd14606    10 RLEGQRPENKSKNRYKNILPFDHSRVILqGRDSNIPGSDYINANYVKNQllgpDENAKTYIASQGCLEATVNDFWQMAWQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1039 QGAVVIVALCRLQENGEVACARYWPEEGAE-VYHIYEVHLVSEHIwCDDYLVRSFYLKNLRTSET-RTVTQFHFLSWPHM 1116
Cdd:cd14606    90 ENSRVIVMTTREVEKGRNKCVPYWPEVGMQrAYGPYSVTNCGEHD-TTEYKLRTLQVSPLDNGELiREIWHYQYLSWPDH 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1117 GVPAQAKALLDFRRKVN-KSYRGRRSCPIVVHGSAGAGRTGVYILLDLVLERMN-KGAR-EIDIAATLEHLRDQRAGVVA 1193
Cdd:cd14606   169 GVPSEPGGVLSFLDQINqRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENIStKGLDcDIDIQKTIQMVRAQRSGMVQ 248

                         250
                  ....*....|....
gi 281360500 1194 TRQQFEFVLMAVAE 1207
Cdd:cd14606   249 TEAQYKFIYVAIAQ 262
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 956-1205 2.03e-49

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: 176.31  E-value: 2.03e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  956 RYEAEPSAREAASQPQCAGLNRPGAPLPYDHSRVVLNHLANaeglDYVNASTITDHDPRApAYVAAQGPLPSTLAHFWQM 1035
Cdd:cd14607     8 RNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTEN----DYINASLVVIEEAQR-SYILTQGPLPNTCCHFWLM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1036 IWEQGAVVIVALCRLQENGEVACARYWPEEGAEVYHIYE----VHLVSEHIWcDDYLVRSFYLKNLRTSETRTVTQFHFL 1111
Cdd:cd14607    83 VWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKEtgfsVKLLSEDVK-SYYTVHLLQLENINSGETRTISHFHYT 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1112 SWPHMGVPAQAKALLDFRRKVNKSYR-GRRSCPIVVHGSAGAGRTGVYILLDLVLERMNKG-AREIDIAATLEHLRDQRA 1189
Cdd:cd14607   162 TWPDFGVPESPASFLNFLFKVRESGSlSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKdPDSVDIKQVLLDMRKYRM 241

                         250
                  ....*....|....*.
gi 281360500 1190 GVVATRQQFEFVLMAV 1205
Cdd:cd14607   242 GLIQTPDQLRFSYMAV 257
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 976-1209 3.37e-49

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: 176.44  E-value: 3.37e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  976 NRPGAPLPYDHSRVVLNHLANAEGLDYVNASTItDHDPRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGE 1055
Cdd:cd14625    51 NRYANVIAYDHSRVILQPIEGIMGSDYINANYI-DGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSR 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1056 VACARYWPEEGAEVYHIYEVHLVsEHIWCDDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVnKS 1135
Cdd:cd14625   130 IKCDQYWPSRGTETYGMIQVTLL-DTIELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRV-KT 207

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281360500 1136 YRGRRSCPIVVHGSAGAGRTGVYILLDLVLERMnKGAREIDIAATLEHLRDQRAGVVATRQQFEFVLMAVAEEV 1209
Cdd:cd14625   208 CNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERI-KHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAV 280
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 982-1207 5.77e-49

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: 174.08  E-value: 5.77e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  982 LPYDHSRVVLNHLANAEGLDYVNASTItDHDPRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVACARY 1061
Cdd:cd14623     6 IPYEFNRVIIPVKRGEENTDYVNASFI-DGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEKCAQY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1062 WPEEGAEVYHIYEVHLVSEHiWCDDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVNKSYRGRRS 1141
Cdd:cd14623    85 WPSDGSVSYGDITIELKKEE-ECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQQSGN 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281360500 1142 CPIVVHGSAGAGRTGVYILLDLVLERMnKGAREIDIAATLEHLRDQRAGVVATRQQFEFVLMAVAE 1207
Cdd:cd14623   164 HPITVHCSAGAGRTGTFCALSTVLERV-KAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 947-1207 7.54e-49

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: 176.08  E-value: 7.54e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  947 LQREWEALCRYEAEPSAREAASQPQCAGLNRPGAPLPYDHSRVVLNHLANAEGLDYVNASTItDHDPRAPAYVAAQGPLP 1026
Cdd:cd14628    27 MELEFKRLASSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFI-DGYRQQKAYIATQGPLA 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1027 STLAHFWQMIWEQGAVVIVALCRLQENGEVACARYWPEEGAEVYHIYEVHLVSEHIwCDDYLVRSFYLKNLRTSETRTVT 1106
Cdd:cd14628   106 ETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYN-MPQYILREFKVTDARDGQSRTVR 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1107 QFHFLSWPHMGVPAQAKALLDFRRKVNKSYRG-RRSCPIVVHGSAGAGRTGVYILLDLVLERMN-KGAreIDIAATLEHL 1184
Cdd:cd14628   185 QFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQfGQDGPISVHCSAGVGRTGVFITLSIVLERMRyEGV--VDIFQTVKML 262

                         250       260
                  ....*....|....*....|...
gi 281360500 1185 RDQRAGVVATRQQFEFVLMAVAE 1207
Cdd:cd14628   263 RTQRPAMVQTEDQYQFCYRAALE 285
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 947-1207 1.74e-48

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: 174.92  E-value: 1.74e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  947 LQREWEALCRYEAEPSAREAASQPQCAGLNRPGAPLPYDHSRVVLNHLANAEGLDYVNASTItDHDPRAPAYVAAQGPLP 1026
Cdd:cd14627    28 MELEFKRLANSKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFI-DGYRQQKAYIATQGPLA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1027 STLAHFWQMIWEQGAVVIVALCRLQENGEVACARYWPEEGAEVYHIYEVHLVSEHIwCDDYLVRSFYLKNLRTSETRTVT 1106
Cdd:cd14627   107 ETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYN-MPQYILREFKVTDARDGQSRTVR 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1107 QFHFLSWPHMGVPAQAKALLDFRRKVNKSYRG-RRSCPIVVHGSAGAGRTGVYILLDLVLERMN-KGAreIDIAATLEHL 1184
Cdd:cd14627   186 QFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQfGQDGPISVHCSAGVGRTGVFITLSIVLERMRyEGV--VDIFQTVKML 263

                         250       260
                  ....*....|....*....|...
gi 281360500 1185 RDQRAGVVATRQQFEFVLMAVAE 1207
Cdd:cd14627   264 RTQRPAMVQTEDEYQFCYQAALE 286
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 976-1205 6.58e-48

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11), also called SH2 domain-containing tyrosine phosphatase 2 (SHP-2 or SHP2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 promotes the activation of the RAS/Mitogen-Activated Protein Kinases (MAPK) Extracellular-Regulated Kinases 1/2 (ERK1/2) pathway, a canonical signaling cascade that plays key roles in various cellular processes, including proliferation, survival, differentiation, migration, or metabolism. It also regulates the phosphoinositide 3-kinase (PI3K)/AKT pathway, a fundamental cascade that functions in cell survival, proliferation, migration, morphogenesis, and metabolism. PTPN11 dysregulation is associated with several developmental diseases and malignancies, such as Noonan syndrome and juvenile myelomonocytic leukemia. It contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 171.74  E-value: 6.58e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  976 NRPGAPLPYDHSRVVLNH-LANAEGLDYVNASTI-----TDHDPRAP--AYVAAQGPLPSTLAHFWQMIWEQGAVVIVAL 1047
Cdd:cd14605     6 NRYKNILPFDHTRVVLHDgDPNEPVSDYINANIImpefeTKCNNSKPkkSYIATQGCLQNTVNDFWRMVFQENSRVIVMT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1048 CRLQENGEVACARYWPEEGA-EVYHIYEVHLVSEHIwCDDYLVRSFYLKNLRTSET-RTVTQFHFLSWPHMGVPAQAKAL 1125
Cdd:cd14605    86 TKEVERGKSKCVKYWPDEYAlKEYGVMRVRNVKESA-AHDYILRELKLSKVGQGNTeRTVWQYHFRTWPDHGVPSDPGGV 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1126 LDFRRKVNKSYRG-RRSCPIVVHGSAGAGRTGVYILLDLVLERM-NKGAR-EIDIAATLEHLRDQRAGVVATRQQFEFVL 1202
Cdd:cd14605   165 LDFLEEVHHKQESiMDAGPVVVHCSAGIGRTGTFIVIDILIDIIrEKGVDcDIDVPKTIQMVRSQRSGMVQTEAQYRFIY 244


                  ...
gi 281360500 1203 MAV 1205
Cdd:cd14605   245 MAV 247
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 976-1207 1.15e-47

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: 170.59  E-value: 1.15e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  976 NRPGAPLPYDHSRVVLNHLANAEGLDYVNASTITD-HDPRApaYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENG 1054
Cdd:cd14630     7 NRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGyHRPRH--YIATQGPMQETVKDFWRMIWQENSASVVMVTNLVEVG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1055 EVACARYWPEEgAEVYHIYEVHLVSEHIWCdDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVnK 1134
Cdd:cd14630    85 RVKCVRYWPDD-TEVYGDIKVTLIETEPLA-EYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQV-K 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281360500 1135 SYRGRRSCPIVVHGSAGAGRTGVYILLDLVLErMNKGAREIDIAATLEHLRDQRAGVVATRQQFEFVLMAVAE 1207
Cdd:cd14630   162 FLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLD-MAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 965-1207 1.73e-47

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: 171.16  E-value: 1.73e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  965 EAASQPQCAGLNRPGAPLPYDHSRVVLNHLANAEGLDYVNASTITDHDpRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVI 1044
Cdd:cd14603    23 VAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVD-GSRAYIATQGPLSHTVLDFWRMIWQYGVKVI 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1045 VALCRLQENGEVACARYWPEEGAEV-YHIYEVHLVSEHIWCDDYLVRSFYLKnlRTSETRTVTQFHFLSWPHMGVPAQAK 1123
Cdd:cd14603   102 LMACREIEMGKKKCERYWAQEQEPLqTGPFTITLVKEKRLNEEVILRTLKVT--FQKESRSVSHFQYMAWPDHGIPDSPD 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1124 ALLDFRRKVNKsYRGRRSCPIVVHGSAGAGRTGVYILLD-----LVLERMNKGAREIDIaaTLEhLRDQRAGVVATRQQF 1198
Cdd:cd14603   180 CMLAMIELARR-LQGSGPEPLCVHCSAGCGRTGVICTVDyvrqlLLTQRIPPDFSIFDV--VLE-MRKQRPAAVQTEEQY 255


                  ....*....
gi 281360500 1199 EFVLMAVAE 1207
Cdd:cd14603   256 EFLYHTVAQ 264
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 976-1209 2.57e-47

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: 171.07  E-value: 2.57e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  976 NRPGAPLPYDHSRVVLNHLANAEGLDYVNASTItDHDPRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGE 1055
Cdd:cd14624    51 NRYANVIAYDHSRVLLSAIEGIPGSDYINANYI-DGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSR 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1056 VACARYWPEEGAEVYHIYEVHLVsEHIWCDDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVnKS 1135
Cdd:cd14624   130 VKCDQYWPSRGTETYGLIQVTLL-DTVELATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRV-KT 207

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281360500 1136 YRGRRSCPIVVHGSAGAGRTGVYILLDLVLERMnKGAREIDIAATLEHLRDQRAGVVATRQQFEFVLMAVAEEV 1209
Cdd:cd14624   208 CNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERI-KHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAV 280
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 965-1207 7.65e-47

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: 170.20  E-value: 7.65e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  965 EAASQPQCAGLNRPGAPLPYDHSRVvlnHLANAEGL---DYVNASTITDHDPRApAYVAAQGPLPSTLAHFWQMIWEQGA 1041
Cdd:cd14621    45 EAASKEENKEKNRYVNILPYDHSRV---HLTPVEGVpdsDYINASFINGYQEKN-KFIAAQGPKEETVNDFWRMIWEQNT 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1042 VVIVALCRLQENGEVACARYWPEEGAEVYHIYEVHlVSEHIWCDDYLVRSFYLKNL----RTSETRTVTQFHFLSWPHMG 1117
Cdd:cd14621   121 ATIVMVTNLKERKECKCAQYWPDQGCWTYGNIRVS-VEDVTVLVDYTVRKFCIQQVgdvtNKKPQRLITQFHFTSWPDFG 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1118 VPAQAKALLDFRRKV---NKSYRGrrscPIVVHGSAGAGRTGVYILLDLVLERMNkGAREIDIAATLEHLRDQRAGVVAT 1194
Cdd:cd14621   200 VPFTPIGMLKFLKKVkncNPQYAG----AIVVHCSAGVGRTGTFIVIDAMLDMMH-AERKVDVYGFVSRIRAQRCQMVQT 274

                         250
                  ....*....|...
gi 281360500 1195 RQQFEFVLMAVAE 1207
Cdd:cd14621   275 DMQYVFIYQALLE 287
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1002-1201 1.22e-46

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: 166.69  E-value: 1.22e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1002 YVNASTITDHDpRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVACARYWPEEGAEVYHIYEVHLVSEH 1081
Cdd:cd17668     1 YINANYVDGYN-KPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1082 IWCdDYLVRSFYLKNLRT--------SETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVNKSYRGRRScPIVVHGSAGAG 1153
Cdd:cd17668    80 VLA-YYTVRNFTLRNTKIkkgsqkgrPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVG-PVVVHCSAGVG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 281360500 1154 RTGVYILLDLVLERMnKGAREIDIAATLEHLRDQRAGVVATRQQFEFV 1201
Cdd:cd17668   158 RTGTYIVLDSMLQQI-QHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFI 204
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 947-1207 1.69e-46

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: 169.14  E-value: 1.69e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  947 LQREWEALCRYEAEPSAREAASQPQCAGLNRPGAPLPYDHSRVVLNHLANAEGLDYVNASTItDHDPRAPAYVAAQGPLP 1026
Cdd:cd14629    28 MELEFKLLANSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFI-DGYRQQKAYIATQGPLA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1027 STLAHFWQMIWEQGAVVIVALCRLQENGEVACARYWPEEGAEVYHIYEVHLVSEHIwCDDYLVRSFYLKNLRTSETRTVT 1106
Cdd:cd14629   107 ETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYN-MPQYILREFKVTDARDGQSRTIR 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1107 QFHFLSWPHMGVPAQAKALLDFRRKVNKSYRG-RRSCPIVVHGSAGAGRTGVYILLDLVLERMN-KGAreIDIAATLEHL 1184
Cdd:cd14629   186 QFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEQfGQDGPITVHCSAGVGRTGVFITLSIVLERMRyEGV--VDMFQTVKTL 263

                         250       260
                  ....*....|....*....|...
gi 281360500 1185 RDQRAGVVATRQQFEFVLMAVAE 1207
Cdd:cd14629   264 RTQRPAMVQTEDQYQLCYRAALE 286
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1002-1202 2.64e-46

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: 166.09  E-value: 2.64e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1002 YVNASTIT-DHDPRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVACARYWP----EEGAEVYHIYEVH 1076
Cdd:cd14540     1 YINASHITaTVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPtlggEHDALTFGEYKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1077 LVSEHIwCDDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDF-------RRKVNKSYRGR-RSCPIVVHG 1148
Cdd:cd14540    81 TKFSVS-SGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFleeinsvRRHTNQDVAGHnRNPPTLVHC 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 281360500 1149 SAGAGRTGVYILLDLVLERMNKGaREIDIAATLEHLRDQRAGVVATRQQFEFVL 1202
Cdd:cd14540   160 SAGVGRTGVVILADLMLYCLDHN-EELDIPRVLALLRHQRMLLVQTLAQYKFVY 212
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 967-1205 3.97e-46

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: 167.33  E-value: 3.97e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  967 ASQPQCAGLNRPGAPLPYDHSRVVLNhlanaEGLDYVNASTITDHDPRAP---AYVAAQGPLPSTLAHFWQMIWEQGAVV 1043
Cdd:cd14600    35 AKLPQNMDKNRYKDVLPYDATRVVLQ-----GNEDYINASYVNMEIPSANivnKYIATQGPLPHTCAQFWQVVWEQKLSL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1044 IVALCRLQENGEVACARYWPEEgAEV--YHIYEVHLVSEHiwCD-DYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPA 1120
Cdd:cd14600   110 IVMLTTLTERGRTKCHQYWPDP-PDVmeYGGFRVQCHSED--CTiAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPD 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1121 QAKALLDFRRKVnksyRGRR--SCPIVVHGSAGAGRTGVYILLD--LVLERMNKGAREIDIAATlehLRDQRAGVVATRQ 1196
Cdd:cd14600   187 DSSDFLEFVNYV----RSKRveNEPVLVHCSAGIGRTGVLVTMEtaMCLTERNQPVYPLDIVRK---MRDQRAMMVQTSS 259


                  ....*....
gi 281360500 1197 QFEFVLMAV 1205
Cdd:cd14600   260 QYKFVCEAI 268
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 976-1207 5.40e-46

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: 165.40  E-value: 5.40e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  976 NRPGAPLPYDHSRVVLNHLANAEGLDYVNASTITD-HDPRApaYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENG 1054
Cdd:cd14602     2 NRYKDILPYDHSRVELSLITSDEDSDYINANFIKGvYGPRA--YIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1055 EVACARYWPEEGAEVYHIYEVHLVsehiwCD------DYLVRSfyLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDF 1128
Cdd:cd14602    80 KKKCERYWAEPGEMQLEFGPFSVT-----CEaekrksDYIIRT--LKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILEL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1129 RRKVnKSYRGRRSCPIVVHGSAGAGRTGVYILLDLVLERMNKG--AREIDIAATLEHLRDQRAGVVATRQQFEFVLMAVA 1206
Cdd:cd14602   153 IWDV-RCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGiiPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVI 231


                  .
gi 281360500 1207 E 1207
Cdd:cd14602   232 E 232
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1002-1201 1.73e-45

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 1.


Pssm-ID: 350405 [Multi-domain]  Cd Length: 201  Bit Score: 163.07  E-value: 1.73e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1002 YVNASTITDH-DPRApaYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVACARYWP--EEGAEVYHIYEVHLV 1078
Cdd:cd14557     1 YINASYIDGFkEPRK--YIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsmEEGSRAFGDVVVKIN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1079 SEHIwCDDYLVRSFYLKNLRTSET-RTVTQFHFLSWPHMGVPAQAKALLDFRRKVNkSYRGRRSCPIVVHGSAGAGRTGV 1157
Cdd:cd14557    79 EEKI-CPDYIIRKLNINNKKEKGSgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVN-AFNNFFSGPIVVHCSAGVGRTGT 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 281360500 1158 YILLDLVLERMNKGAReIDIAATLEHLRDQRAGVVATRQQFEFV 1201
Cdd:cd14557   157 YIGIDAMLEGLEAEGR-VDVYGYVVKLRRQRCLMVQVEAQYILI 199
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1001-1207 1.83e-45

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 162.87  E-value: 1.83e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1001 DYVNASTItDHDPRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVACARYWPEEGAEVYHIYEVHLVSE 1080
Cdd:cd14622     1 DYINASFI-DGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKND 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1081 HIwCDDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVNKSYRGRRSCPIVVHGSAGAGRTGVYIL 1160
Cdd:cd14622    80 TL-LETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNHPIVVHCSAGAGRTGTFIA 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 281360500 1161 LDLVLERMnKGAREIDIAATLEHLRDQRAGVVATRQQFEFVLMAVAE 1207
Cdd:cd14622   159 LSNILERV-KAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQD 204
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 947-1207 1.85e-45

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


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 165.60  E-value: 1.85e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  947 LQREWEALcrYEAEPSAREAASQPQCAGLNRPGAPLPYDHSRVVLNHLANAEGLDYVNASTItDHDPRAPAYVAAQGPLP 1026
Cdd:cd14633    17 FKEEYESF--FEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYI-DGYHRPNHYIATQGPMQ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1027 STLAHFWQMIWEQGAVVIVALCRLQENGEVACARYWPEEgAEVYHIYEVHLVSEHIwCDDYLVRSFYLKNLRTSETRTVT 1106
Cdd:cd14633    94 ETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD-TEIYKDIKVTLIETEL-LAEYVIRTFAVEKRGVHEIREIR 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1107 QFHFLSWPHMGVPAQAKALLDFRRKVnKSYRGRRSCPIVVHGSAGAGRTGVYILLDLVLErMNKGAREIDIAATLEHLRD 1186
Cdd:cd14633   172 QFHFTGWPDHGVPYHATGLLGFVRQV-KSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLD-MAEREGVVDIYNCVRELRS 249

                         250       260
                  ....*....|....*....|.
gi 281360500 1187 QRAGVVATRQQFEFVLMAVAE 1207
Cdd:cd14633   250 RRVNMVQTEEQYVFIHDAILE 270
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1002-1207 2.54e-45

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: 162.39  E-value: 2.54e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1002 YVNASTItDHDPRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVACARYWPEEgAEVYHIYEVHLVSEH 1081
Cdd:cd14555     1 YINANYI-DGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDD-TEVYGDIKVTLVETE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1082 IWCdDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVnKSYRGRRSCPIVVHGSAGAGRTGVYILL 1161
Cdd:cd14555    79 PLA-EYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRV-KASNPPSAGPIVVHCSAGAGRTGCYIVI 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 281360500 1162 DLVLErMNKGAREIDIAATLEHLRDQRAGVVATRQQFEFVLMAVAE 1207
Cdd:cd14555   157 DIMLD-MAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 976-1207 2.83e-45

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: 165.88  E-value: 2.83e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  976 NRPGAPLPYDHSRVVLNHLANAEGLDYVNASTITD-HDPRApaYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENG 1054
Cdd:cd14604    61 NRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGvYGPKA--YIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMG 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1055 EVACARYWPEEGAEvyhiyEVHLVSEHIWCD------DYLVRSFYLKnlRTSETRTVTQFHFLSWPHMGVPAQAKALLDF 1128
Cdd:cd14604   139 RKKCERYWPLYGEE-----PMTFGPFRISCEaeqartDYFIRTLLLE--FQNETRRLYQFHYVNWPDHDVPSSFDSILDM 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1129 rRKVNKSYRGRRSCPIVVHGSAGAGRTGVYILLDLV--LERMNKGAREIDIAATLEHLRDQRAGVVATRQQFEFVLMAVA 1206
Cdd:cd14604   212 -ISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTwnLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIA 290


                  .
gi 281360500 1207 E 1207
Cdd:cd14604   291 Q 291
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1002-1200 6.97e-45

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: 161.02  E-value: 6.97e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1002 YVNASTITD-HDPRApaYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVACARYWPEEGaEVYHIYEVHLVSE 1080
Cdd:cd14558     1 YINASFIDGyWGPKS--LIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEK-KTYGDIEVELKDT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1081 HIwCDDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKV-----NKSYRGRRSCPIVVHGSAGAGRT 1155
Cdd:cd14558    78 EK-SPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIkqklpYKNSKHGRSVPIVVHCSDGSSRT 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 281360500 1156 GVYILLDLVLE--RMNKgarEIDIAATLEHLRDQRAGVVATRQQFEF 1200
Cdd:cd14558   157 GIFCALWNLLEsaETEK---VVDVFQVVKALRKQRPGMVSTLEQYQF 200
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1001-1205 3.26e-44

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: 159.73  E-value: 3.26e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1001 DYVNASTITDHDPRAP---AYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVACARYWPE-EGAEVYHIYEVH 1076
Cdd:cd14601     1 DYINANYINMEIPSSSiinRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEpSGSSSYGGFQVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1077 LVSEHiWCDDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVnKSYRGRRSCPIVVHGSAGAGRTG 1156
Cdd:cd14601    81 CHSEE-GNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLV-RNKRAGKDEPVVVHCSAGIGRTG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 281360500 1157 VYILLD--LVLERMNKGAREIDIAATlehLRDQRAGVVATRQQFEFVLMAV 1205
Cdd:cd14601   159 VLITMEtaMCLIECNQPVYPLDIVRT---MRDQRAMMIQTPSQYRFVCEAI 206
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 988-1207 6.94e-44

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350479 [Multi-domain]  Cd Length: 218  Bit Score: 159.03  E-value: 6.94e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  988 RVVLNHLANAEGLDYVNASTItDHDPRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVACARYWPEEgA 1067
Cdd:cd14631     1 RVILQPVEDDPSSDYINANYI-DGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD-T 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1068 EVYHIYEVHLVS-EHIwcDDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVNKSyRGRRSCPIVV 1146
Cdd:cd14631    79 EVYGDFKVTCVEmEPL--AEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLS-NPPSAGPIVV 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281360500 1147 HGSAGAGRTGVYILLDLVLErMNKGAREIDIAATLEHLRDQRAGVVATRQQFEFVLMAVAE 1207
Cdd:cd14631   156 HCSAGAGRTGCYIVIDIMLD-MAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 976-1200 2.86e-43

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: 157.68  E-value: 2.86e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  976 NRPGAPLPYDHSRVVLNhlanAEGlDYVNASTItdhdpRAPA------YVAAQGPLPSTLAHFWQMIWEQGAVVIVALCR 1049
Cdd:cd14597     7 NRYKNILPYDTTRVPLG----DEG-GYINASFI-----KMPVgdeefvYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1050 LQENGEVACARYWPEEGAEVYHIYE---VHLVS-EHIwcDDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKAL 1125
Cdd:cd14597    77 EVEGGKIKCQRYWPEILGKTTMVDNrlqLTLVRmQQL--KNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQL 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281360500 1126 LDFRRKVNKSYrgrRSCPIVVHGSAGAGRTGVYILLDLVLERMNKGArEIDIAATLEHLRDQRAGVVATRQQFEF 1200
Cdd:cd14597   155 LTFISYMRHIH---KSGPIITHCSAGIGRSGTLICIDVVLGLISKDL-DFDISDIVRTMRLQRHGMVQTEDQYIF 225
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1002-1201 5.57e-43

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


Pssm-ID: 350399 [Multi-domain]  Cd Length: 202  Bit Score: 155.84  E-value: 5.57e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1002 YVNASTITDHDPRApAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVACARYWPEEGAEVYHIYEVHlVSEH 1081
Cdd:cd14551     1 YINASYIDGYQEKN-KFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVR-VEDT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1082 IWCDDYLVRSFYLK----NLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVnKSYRGRRSCPIVVHGSAGAGRTGV 1157
Cdd:cd14551    79 VVLVDYTTRKFCIQkvnrGIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKV-KSANPPRAGPIVVHCSAGVGRTGT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 281360500 1158 YILLDLVLErMNKGAREIDIAATLEHLRDQRAGVVATRQQFEFV 1201
Cdd:cd14551   158 FIVIDAMLD-MMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFI 200
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1002-1200 1.71e-42

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: 154.46  E-value: 1.71e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1002 YVNASTITDHDPRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVACARYWPEE--GAEVYHIYEVHLVS 1079
Cdd:cd14539     1 YINASLIEDLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErgQALVYGAITVSLQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1080 EHIwCDDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVNKSYRGRRS--CPIVVHGSAGAGRTGV 1157
Cdd:cd14539    81 VRT-TPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSlqTPIVVHCSSGVGRTGA 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 281360500 1158 YILLDLVLERMNKGAREIDIAATLEHLRDQRAGVVATRQQFEF 1200
Cdd:cd14539   160 FCLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKF 202
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1002-1207 2.29e-42

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: 154.13  E-value: 2.29e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1002 YVNASTIT------DHdprapAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVACARYWPEEGAEVYHI--Y 1073
Cdd:cd14596     1 YINASYITmpvgeeEL-----FYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELenY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1074 EVHLVSEHIwCDDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVNKSYrgrRSCPIVVHGSAGAG 1153
Cdd:cd14596    76 QLRLENYQA-LQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVH---NTGPIVVHCSAGIG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 281360500 1154 RTGVYILLDLVLERMNKGArEIDIAATLEHLRDQRAGVVATRQQFEFVLMAVAE 1207
Cdd:cd14596   152 RAGVLICVDVLLSLIEKDL-SFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLE 204
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1002-1207 7.58e-42

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: 152.51  E-value: 7.58e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1002 YVNASTItDHDPRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVACARYWPEEgAEVYHIYEVHLVSEH 1081
Cdd:cd14632     1 YINANYI-DGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDD-SDTYGDIKITLLKTE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1082 IWCdDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVnKSYRGRRSCPIVVHGSAGAGRTGVYILL 1161
Cdd:cd14632    79 TLA-EYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRV-KASTPPDAGPVVVHCSAGAGRTGCYIVL 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 281360500 1162 DLVLErMNKGAREIDIAATLEHLRDQRAGVVATRQQFEFVLMAVAE 1207
Cdd:cd14632   157 DVMLD-MAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 976-1201 2.12e-41

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: 152.40  E-value: 2.12e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  976 NRPGAPLPYDHSRVVLNHLANAEGLDYVNASTITDHDpRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGE 1055
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYT-SPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1056 VACARYWPEEGAEVYHIY-EVHLVSEHIwCDDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVNK 1134
Cdd:cd14618    80 VLCDHYWPSESTPVSYGHiTVHLLAQSS-EDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVRE 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281360500 1135 SYRGRR-SCPIVVHGSAGAGRTGVYILLDLVLERMnKGAREIDIAATLEHLRDQRAGVVATRQQFEFV 1201
Cdd:cd14618   159 HVQATKgKGPTLVHCSAGVGRSGTFIALDRLLRQL-KEEKVVDVFNTVYILRMHRYLMIQTLSQYIFL 225
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 976-1201 4.31e-41

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: 151.22  E-value: 4.31e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  976 NRPGAPLPYDHSRVVLNHLANAEGLDYVNASTITDHDPRApAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGE 1055
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRR-EYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1056 VACARYWPEEGAEVYH-IYEVHLVSEHIWcDDYLVRSFYLKNL-RTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVn 1133
Cdd:cd14617    80 VKCDHYWPADQDSLYYgDLIVQMLSESVL-PEWTIREFKICSEeQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTV- 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1134 KSY--RGRRSCPIVVHGSAGAGRTGVYILLDLVLERMNKgAREIDIAATLEHLRDQRAGVVATRQQFEFV 1201
Cdd:cd14617   158 RDYinRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDS-KDSVDIYGAVHDLRLHRVHMVQTECQYVYL 226
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 983-1202 8.86e-40

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: 147.36  E-value: 8.86e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  983 PYDHSRVVLNHLANAEGLDYVNASTITDHdpRAP-AYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVACARY 1061
Cdd:cd14616     8 PYNNNRVKLIADAGVPGSDYINASYISGY--LCPnEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRIRCHQY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1062 WPEEG--AEVYHIYEVHLVSEHIWcDDYLVRSfyLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVnKSYRGR 1139
Cdd:cd14616    86 WPEDNkpVTVFGDIVITKLMEDVQ-IDWTIRD--LKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLV-RASRAH 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281360500 1140 RSCPIVVHGSAGAGRTGVYILLDLVLERMNKgAREIDIAATLEHLRDQRAGVVATRQQFEFVL 1202
Cdd:cd14616   162 DNTPMIVHCSAGVGRTGVFIALDHLTQHIND-HDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 965-1201 1.21e-39

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: 147.73  E-value: 1.21e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  965 EAASQPQCAGLNRPGAPLPYDHSRVVLNHLANAEGLDYVNASTITDHD-PRApaYVAAQGPLPSTLAHFWQMIWEQGAVV 1043
Cdd:cd14614     5 FAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNsPQE--YIATQGPLPETRNDFWKMVLQQKSQI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1044 IVALCRLQENGEVACARYWP-EEGAEVYHIYEVHLVSEHiWCDDYLVRSFYLKnlRTSETRTVTQFHFLSWPHMGVPA-- 1120
Cdd:cd14614    83 IVMLTQCNEKRRVKCDHYWPfTEEPVAYGDITVEMLSEE-EQPDWAIREFRVS--YADEVQDVMHFNYTAWPDHGVPTan 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1121 QAKALLDFRRKVNKSyRGRRSCPIVVHGSAGAGRTGVYILLDLVLERMnKGAREIDIAATLEHLRDQRAGVVATRQQFEF 1200
Cdd:cd14614   160 AAESILQFVQMVRQQ-AVKSKGPMIIHCSAGVGRTGTFIALDRLLQHI-RDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 237


                  .
gi 281360500 1201 V 1201
Cdd:cd14614   238 I 238
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 970-1206 2.62e-38

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: 143.82  E-value: 2.62e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  970 PQCAGLNRPGAPLPYDHSRVVLNHLANAEGLD-YVNASTITDHDPRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALC 1048
Cdd:cd14612    13 PGHASKDRYKTILPNPQSRVCLRRAGSQEEEGsYINANYIRGYDGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMIT 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1049 RLQENGEvACARYWPEEgAEVYHIYEVHlVSEHIWCDDYLVRSFYLKnlRTSETRTVTQFHFLSWPHMGVPAQAKALLDF 1128
Cdd:cd14612    93 KLKEKKE-KCVHYWPEK-EGTYGRFEIR-VQDMKECDGYTIRDLTIQ--LEEESRSVKHYWFSSWPDHQTPESAGPLLRL 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281360500 1129 RRKVNKSYRGRRS-CPIVVHGSAGAGRTGVYILLDLVLERMnKGAREIDIAATLEHLRDQRAGVVATRQQFEFVLMAVA 1206
Cdd:cd14612   168 VAEVEESRQTAASpGPIVVHCSAGIGRTGCFIATSIGCQQL-KDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLHHTLA 245
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 967-1201 1.03e-36

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: 140.52  E-value: 1.03e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  967 ASQPQCAGLNRPGAPLPYDHSRVVLnhLANAEG-LDYVNAS----TITDHDPRapaYVAAQGPLPSTLAHFWQMIWEQGA 1041
Cdd:cd14599    33 ATLPENAERNRIREVVPYEENRVEL--VPTKENnTGYINAShikvTVGGEEWH---YIATQGPLPHTCHDFWQMVWEQGV 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1042 VVIVALCRLQENGEVACARYWPEEGAEvyHIYEVH---LVSEHIWCDD--YLVRSFYLKNLRTSETRTVTQFHFLSWPHM 1116
Cdd:cd14599   108 NVIAMVTAEEEGGRSKSHRYWPKLGSK--HSSATYgkfKVTTKFRTDSgcYATTGLKVKHLLSGQERTVWHLQYTDWPDH 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1117 GVPAQAKALLDF-------RRKVNKSYRGRRSC--PIVVHGSAGAGRTGVYILLDLVLERMNKGAReIDIAATLEHLRDQ 1187
Cdd:cd14599   186 GCPEEVQGFLSYleeiqsvRRHTNSMLDSTKNCnpPIVVHCSAGVGRTGVVILTELMIGCLEHNEK-VEVPVMLRHLREQ 264

                         250
                  ....*....|....
gi 281360500 1188 RAGVVATRQQFEFV 1201
Cdd:cd14599   265 RMFMIQTIAQYKFV 278
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 976-1201 1.08e-36

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: 139.61  E-value: 1.08e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  976 NRPGAPLPYDHSRVVLNHLANAEGLD-YVNASTITDHDPRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENG 1054
Cdd:cd14613    29 NRYKTILPNPHSRVCLTSPDQDDPLSsYINANYIRGYGGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEMN 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1055 EvACARYWPEEGAeVYHIYEVhLVSEHIWCDDYLVRSFYLKNlrTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVNK 1134
Cdd:cd14613   109 E-KCTEYWPEEQV-TYEGIEI-TVKQVIHADDYRLRLITLKS--GGEERGLKHYWYTSWPDQKTPDNAPPLLQLVQEVEE 183

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281360500 1135 SYR--GRRSCPIVVHGSAGAGRTGVYILLDLVLERMNKGAReIDIAATLEHLRDQRAGVVATRQQFEFV 1201
Cdd:cd14613   184 ARQqaEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGV-VDILRTTCQLRLDRGGMIQTCEQYQFV 251
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 976-1201 3.13e-36

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: 137.36  E-value: 3.13e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  976 NRPGAPLPYDHSRVVLNHLANAEGLD-YVNASTITDHDPRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENG 1054
Cdd:cd14611     3 NRYKTILPNPHSRVCLKPKNSNDSLStYINANYIRGYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1055 EvACARYWPEEGAeVYHIYEVhLVSEHIWCDDYLVRSFYLKNlrTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVNK 1134
Cdd:cd14611    83 E-KCVLYWPEKRG-IYGKVEV-LVNSVKECDNYTIRNLTLKQ--GSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDVEE 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281360500 1135 SYRGRRS-CPIVVHGSAGAGRTGVYILLDLVLERM-NKGAreIDIAATLEHLRDQRAGVVATRQQFEFV 1201
Cdd:cd14611   158 DRLASPGrGPVVVHCSAGIGRTGCFIATTIGCQQLkEEGV--VDVLSIVCQLRVDRGGMVQTSEQYEFV 224
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1002-1201 7.61e-33

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


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 126.75  E-value: 7.61e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1002 YVNASTITDHDPRApAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEvACARYWPEEGAEVYHIYEVHLVSEH 1081
Cdd:cd14556     1 YINAALLDSYKQPA-AFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQ-SCPQYWPDEGSGTYGPIQVEFVSTT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1082 IWCdDYLVRSFYLKN-LRTSE-TRTVTQFHFLSWP-HMGVPAQAKALLDFRRKVNKSYRGRRSCPIVVHGSAGAGRTGVY 1158
Cdd:cd14556    79 IDE-DVISRIFRLQNtTRPQEgYRMVQQFQFLGWPrDRDTPPSKRALLKLLSEVEKWQEQSGEGPIVVHCLNGVGRSGVF 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 281360500 1159 ILLDLVLERMnKGAREIDIAATLEHLRDQRAGVVATRQQFEFV 1201
Cdd:cd14556   158 CAISSVCERI-KVENVVDVFQAVKTLRNHRPNMVETEEQYKFC 199
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1002-1200 1.65e-32

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: 125.65  E-value: 1.65e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1002 YVNASTI-TDHDPRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVA-CARYWPEEGAEVYHIYEVHLVS 1079
Cdd:cd17658     1 YINASLVeTPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTAkCADYFPAEENESREFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1080 EHIWCDDYLV--RSFYLKNLRTSET-RTVTQFHFLSWPHMGVPAQAKALldfRRKVNKSYRGRRSC-PIVVHGSAGAGRT 1155
Cdd:cd17658    81 KKLKHSQHSItlRVLEVQYIESEEPpLSVLHIQYPEWPDHGVPKDTRSV---RELLKRLYGIPPSAgPIVVHCSAGIGRT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 281360500 1156 GVYILLDLVLERMNKGARE-IDIAATLEHLRDQRAGVVATRQQFEF 1200
Cdd:cd17658   158 GAYCTIHNTIRRILEGDMSaVDLSKTVRKFRSQRIGMVQTQDQYIF 203
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1104-1207 5.46e-32

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: 120.54  E-value: 5.46e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500   1104 TVTQFHFLSWPHMGVPAQAKALLDFRRKVNKSYRGRRSC-PIVVHGSAGAGRTGVYILLDLVLERMNKGAREIDIAATLE 1182
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSgPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 281360500   1183 HLRDQRAGVVATRQQFEFVLMAVAE 1207
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1104-1207 5.46e-32

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 120.54  E-value: 5.46e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500   1104 TVTQFHFLSWPHMGVPAQAKALLDFRRKVNKSYRGRRSC-PIVVHGSAGAGRTGVYILLDLVLERMNKGAREIDIAATLE 1182
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSgPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 281360500   1183 HLRDQRAGVVATRQQFEFVLMAVAE 1207
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1002-1201 6.44e-31

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: 121.62  E-value: 6.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1002 YVNASTI-TDHDPRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVACARYWPEEGAEVYHI-YEVHLVS 1079
Cdd:cd14598     1 YINASHIkVTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRHNTVtYGRFKIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1080 EHIWCDD--YLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDF-------RRKVNKSYRGRRS-CPIVVHGS 1149
Cdd:cd14598    81 TRFRTDSgcYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYleeiqsvRRHTNSTIDPKSPnPPVLVHCS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 281360500 1150 AGAGRTGVYILLDLVLERMNKGAReIDIAATLEHLRDQRAGVVATRQQFEFV 1201
Cdd:cd14598   161 AGVGRTGVVILSEIMIACLEHNEM-LDIPRVLDMLRQQRMMMVQTLSQYTFV 211
Receptor_IA-2 pfam11548
Protein-tyrosine phosphatase receptor IA-2; IA-2 is a protein-tyrosine phosphatase receptor ...
 692-782 5.29e-30

Protein-tyrosine phosphatase receptor IA-2; IA-2 is a protein-tyrosine phosphatase receptor that upon exocytosis, the cytoplasmic domain is cleaved and moves to the nucleus where it enhances transcription of the insulin gene. The mature exodomain of IA-2 participates in adhesion to the extracellular matrix and is self-proteolyzed in vitro by reactive oxygen species which may be a new shedding mechanism.


Pssm-ID: 463293  Cd Length: 89  Bit Score: 114.25  E-value: 5.29e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500   692 TEYVHVFVKNPIDSWNDGQRIMKELEQILHMQ-GYFSYLTVQQHEVSFRVNSnNPERKTAGDVARTINENrgvKNNIQRR 770
Cdd:pfam11548    1 EEYGYIVTDNDPLSWEEGLRLMEKVAELLHLPmSSFADIRVLGPAVTFKVRA-NNKNLTAADVAKAAVDI---KDKLEKE 76

                           90
                   ....*....|..
gi 281360500   771 VGFYVLHAGVGD 782
Cdd:pfam11548   77 TGLKILQAGVGD 88
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 978-1205 2.57e-28

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 116.64  E-value: 2.57e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  978 PGAPLpYDHSRVVLNhlANAEGLDYVNASTITDHDPRApAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVA 1057
Cdd:PHA02742   59 PDAPC-FDRNRVILK--IEDGGDDFINASYVDGHNAKG-RFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEA 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1058 CARYW-PEEGAEVYHiYEVHLVSEHIWC-DDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKV--- 1132
Cdd:PHA02742  135 CYPYWmPHERGKATH-GEFKIKTKKIKSfRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLAVrea 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1133 -------NKSYRGRRSCPIVVHGSAGAGRTGVYILLDLVLERMNKGArEIDIAATLEHLRDQRAGVVATRQQFEFVLMAV 1205
Cdd:PHA02742  214 dlkadvdIKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERA-IIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIV 292
PHA02738 PHA02738
hypothetical protein; Provisional
 975-1205 2.43e-27

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 114.25  E-value: 2.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  975 LNRPGAPLPYDHSRVVLNHLANAEglDYVNASTItDHDPRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENG 1054
Cdd:PHA02738   52 LNRYLDAVCFDHSRVILPAERNRG--DYINANYV-DGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENG 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1055 EVACARYWP--EEGAEVYHIYEVHLVSehIWCDDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKV 1132
Cdd:PHA02738  129 REKCFPYWSdvEQGSIRFGKFKITTTQ--VETHPHYVKSTLLLTDGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEV 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1133 NKSYR---------GRRSC---PIVVHGSAGAGRTGVYILLDLVLERMNKGArEIDIAATLEHLRDQRAGVVATRQQFEF 1200
Cdd:PHA02738  207 RQCQKelaqeslqiGHNRLqppPIVVHCNAGLGRTPCYCVVDISISRFDACA-TVSIPSIVSSIRNQRYYSLFIPFQYFF 285


                  ....*
gi 281360500 1201 VLMAV 1205
Cdd:PHA02738  286 CYRAV 290
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
930-1213 1.04e-25

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 108.64  E-value: 1.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  930 GHMVLSYMEDHLRNkgRLQREWEALcRYEAEPSAREaaSQPQCAGLNRPGAPLPYDHSRVVLNhlanaegLDYVNASTIT 1009
Cdd:COG5599     5 NPIAIKSEEEKINS--RLSTLTNEL-APSHNDPQYL--QNINGSPLNRFRDIQPYKETALRAN-------LGYLNANYIQ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1010 DHDPRApaYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQE--NGEVACARYWPEEGAevYHIYEVHL-VSEHIWC-D 1085
Cdd:COG5599    73 VIGNHR--YIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEisKPKVKMPVYFRQDGE--YGKYEVSSeLTESIQLrD 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1086 DYLVRSFYLKNLRTS-ETRTVTQFHFLSWP-HMGVPAQA-KALLDFRRKVNKSYRGRRScPIVVHGSAGAGRTGVYILLd 1162
Cdd:COG5599   149 GIEARTYVLTIKGTGqKKIEIPVLHVKNWPdHGAISAEAlKNLADLIDKKEKIKDPDKL-LPVVHCRAGVGRTGTLIAC- 226

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 281360500 1163 LVLERMNKGAREIDIAA--TLEHLRDQRA-GVVATRQQFEfVLMAVAEEVHAIL 1213
Cdd:COG5599   227 LALSKSINALVQITLSVeeIVIDMRTSRNgGMVQTSEQLD-VLVKLAEQQIRPL 279
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 984-1205 1.47e-25

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 108.96  E-value: 1.47e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  984 YDHSRVVLNHLANAEGLD-------------------YVNASTItDHDPRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVI 1044
Cdd:PHA02746   63 WDHSRVVINAHESLKMFDvgdsdgkkievtsednaenYIHANFV-DGFKEANKFICAQGPKEDTSEDFFKLISEHESQVI 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1045 VALCRLQENGEVaCARYW-PEEGAEVYHIYEVHLVSEHIWCDDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAK 1123
Cdd:PHA02746  142 VSLTDIDDDDEK-CFELWtKEEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFWFPDWPDNGIPTGMA 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1124 ALLDFRRKVNKSYR---------GRRSCPIVVHGSAGAGRTGVYILLDLVLERMNKgAREIDIAATLEHLRDQRAGVVAT 1194
Cdd:PHA02746  221 EFLELINKVNEEQAelikqadndPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEK-EKEVCLGEIVLKIRKQRHSSVFL 299

                         250
                  ....*....|.
gi 281360500 1195 RQQFEFVLMAV 1205
Cdd:PHA02746  300 PEQYAFCYKAL 310
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1002-1201 1.99e-23

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: 99.71  E-value: 1.99e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1002 YVNASTITDHDPRApAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLqeNGEVACARYWPEEGAEVYHIYEVHLVSEH 1081
Cdd:cd14634     1 YINAALMDSHKQPA-AFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM--DAAQLCMQYWPEKTSCCYGPIQVEFVSAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1082 IwCDDYLVRSFYLKNLRTSET--RTVTQFHFLSWP-HMGVPAQAKALLDFRRKVNK---SYRGRRScPIVVHGSAGAGRT 1155
Cdd:cd14634    78 I-DEDIISRIFRICNMARPQDgyRIVQHLQYIGWPaYRDTPPSKRSILKVVRRLEKwqeQYDGREG-RTVVHCLNGGGRS 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 281360500 1156 GVYILLDLVLErMNKGAREIDIAATLEHLRDQRAGVVATRQQFEFV 1201
Cdd:cd14634   156 GTFCAICSVCE-MIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFV 200
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1002-1200 2.21e-23

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: 99.60  E-value: 2.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1002 YVNAStITDHDPRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRL-QENGEVACARYWPEEGAEVYHIYEVHLVSE 1080
Cdd:cd14637     1 YINAA-LTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLnQSNSAWPCLQYWPEPGLQQYGPMEVEFVSG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1081 HIwCDDYLVRSFYLKNL-RTSETR-TVTQFHFLSW-PHMGVPAQAKALLDFRRKVNKSYRGRRSCPIVVHGSAGAGRTGV 1157
Cdd:cd14637    80 SA-DEDIVTRLFRVQNItRLQEGHlMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGGGRSGT 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 281360500 1158 YILLDLVLErMNKGAREIDIAATLEHLRDQRAGVVATRQQFEF 1200
Cdd:cd14637   159 YCASAMILE-MIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRF 200
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 965-1201 4.40e-23

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 101.62  E-value: 4.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  965 EAASQPQCAGLNRPGAPLPYDHSRVVLNHLANAEGlDYVNASTITD-HDPRApaYVAAQGPLPSTLAHFWQMIWEQGAVV 1043
Cdd:PHA02747   44 ANFEKPENQPKNRYWDIPCWDHNRVILDSGGGSTS-DYIHANWIDGfEDDKK--FIATQGPFAETCADFWKAVWQEHCSI 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1044 IVALCRLQE-NGEVACARYW--PEEGAEVYHIYEVHLVSEHIWCdDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPA 1120
Cdd:PHA02747  121 IVMLTPTKGtNGEEKCYQYWclNEDGNIDMEDFRIETLKTSVRA-KYILTLIEITDKILKDSRKISHFQCSEWFEDETPS 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1121 QAKALLDF-------RRKVNKSYRGRRS--CPIVVHGSAGAGRTGVYILLDLVLERMNKgAREIDIAATLEHLRDQRAGV 1191
Cdd:PHA02747  200 DHPDFIKFikiidinRKKSGKLFNPKDAllCPIVVHCSDGVGKTGIFCAVDICLNQLVK-RKAICLAKTAEKIREQRHAG 278

                         250
                  ....*....|
gi 281360500 1192 VATRQQFEFV 1201
Cdd:PHA02747  279 IMNFDDYLFI 288
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1002-1200 5.48e-23

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: 98.16  E-value: 5.48e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1002 YVNASTITDHDpRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVACarYWPEEGAEV-YHIYEVHLVSE 1080
Cdd:cd14550     1 YINASYLQGYR-RSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPI--YWPTKEKPLeCETFKVTLSGE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1081 HIWCD----DYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPaqAKALLDFRRKVNKSYRgRRSCPIVVHGSAGAGRTG 1156
Cdd:cd14550    78 DHSCLsneiRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSP--IHTVFELINTVQEWAQ-QRDGPIVVHDRYGGVQAA 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 281360500 1157 VYILLDLVLERM-NKGAREIDIAATLEHLRdqRAGVVATRQQFEF 1200
Cdd:cd14550   155 TFCALTTLHQQLeHESSVDVYQVAKLYHLM--RPGVFTSKEDYQF 197
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1002-1200 3.53e-21

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: 93.17  E-value: 3.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1002 YVNASTITDHdpRAPA-YVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLqeNGEVACARYWPEEGAEVYHIYEVHLVSE 1080
Cdd:cd14636     1 YINAALMDSY--RQPAaFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEV--DLAQGCPQYWPEEGMLRYGPIQVECMSC 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1081 HIWCdDYLVRSFYLKNL-RTSETR-TVTQFHFLSWP-HMGVPAQAKALLDFRRKVNK------SYRGRrscpIVVHGSAG 1151
Cdd:cd14636    77 SMDC-DVISRIFRICNLtRPQEGYlMVQQFQYLGWAsHREVPGSKRSFLKLILQVEKwqeecdEGEGR----TIIHCLNG 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 281360500 1152 AGRTGVYILLDLVLErMNKGAREIDIAATLEHLRDQRAGVVATRQQFEF 1200
Cdd:cd14636   152 GGRSGMFCAISIVCE-MIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRF 199
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1002-1200 8.77e-18

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: 83.20  E-value: 8.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1002 YVNAStITDHDPRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLqeNGEVACARYWPEEGAEVYHIYEVHLVSEH 1081
Cdd:cd14635     1 YINAA-LMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV--DPAQLCPQYWPENGVHRHGPIQVEFVSAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1082 IWcDDYLVRSFYLKNLRTSET--RTVTQFHFLSWP-HMGVPAQAKALLDFRRKVNK---SYRGRRScPIVVHGSAGAGRT 1155
Cdd:cd14635    78 LE-EDIISRIFRIYNAARPQDgyRMVQQFQFLGWPmYRDTPVSKRSFLKLIRQVDKwqeEYNGGEG-RTVVHCLNGGGRS 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 281360500 1156 GVYILLDLVLErMNKGAREIDIAATLEHLRDQRAGVVATRQQFEF 1200
Cdd:cd14635   156 GTFCAISIVCE-MLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKF 199
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1002-1205 5.64e-14

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


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 72.33  E-value: 5.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1002 YVNASTITDHDpRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVACArYWPEEGAEVY-HIYEVHLVSE 1080
Cdd:cd17669     1 YINASYIMGYY-QSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEPINcETFKVTLIAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1081 HIWC----DDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVP-AQAKALLDfrrkVNKSYRGRRSCPIVVHGSAGAGRT 1155
Cdd:cd17669    79 EHKClsneEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELIS----IIKEEAANRDGPMIVHDEHGGVTA 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 281360500 1156 GVYILLDLVLERMNKgAREIDIAATLEHLRDQRAGVVATRQQFEFVLMAV 1205
Cdd:cd17669   155 GTFCALTTLMHQLEK-ENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1002-1205 3.59e-12

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: 67.01  E-value: 3.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1002 YVNASTITDHdPRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVACArYWP-EEGAEVYHIYEVHLVSE 1080
Cdd:cd17670     1 YINASYIMGY-YRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFV-YWPsREESMNCEAFTVTLISK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1081 HIWC----DDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLdfrRKVNKSYRGRRSCPIVVHGSAGAGRTG 1156
Cdd:cd17670    79 DRLClsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFEL---INVIKEEALTRDGPTIVHDEFGAVSAG 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 281360500 1157 VYILLDLVLERMnKGAREIDIAATLEHLRDQRAGVVATRQQFEFVLMAV 1205
Cdd:cd17670   156 TLCALTTLSQQL-ENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 946-1190 2.00e-05

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 48.04  E-value: 2.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500  946 RLQREWEALCryeaePSAREAASQPQCAGLNRP-----GAPLP-YDHSRVVLNHLANAEGLDYVNAstiTDHDPRapaYV 1019
Cdd:PHA02740   26 CIIKEYRAIV-----PEHEDEANKACAQAENKAkdenlALHITrLLHRRIKLFNDEKVLDARFVDG---YDFEQK---FI 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1020 AAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVAcaRYWP--EEGAEVYHIYEVHLVSehIWCDDYLVRSFYLKNL 1097
Cdd:PHA02740   95 CIINLCEDACDKFLQALSDNKVQIIVLISRHADKKCFN--QFWSlkEGCVITSDKFQIETLE--IIIKPHFNLTLLSLTD 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1098 RTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVNKSYRGRRS-------CPIVVHGSAGAGRTGVYILLDLVLERMNK 1170
Cdd:PHA02740  171 KFGQAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLCADLEKhkadgkiAPIIIDCIDGISSSAVFCVFDICATEFDK 250

                         250       260
                  ....*....|....*....|
gi 281360500 1171 GAReIDIAATLEHLRDQRAG 1190
Cdd:PHA02740  251 TGM-LSIANALKKVRQKKYG 269
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 1107-1201 6.94e-04

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: 41.49  E-value: 6.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1107 QFHFLSWPHMGVPA--QAKALLDFRRKVNKSYRgrrscPIVVHGSAGAGRTGVYILLDLVLERMNKGAREIDIaatlehL 1184
Cdd:cd14504    51 RYHHIPIEDYTPPTleQIDEFLDIVEEANAKNE-----AVLVHCLAGKGRTGTMLACYLVKTGKISAVDAINE------I 119

                          90
                  ....*....|....*..
gi 281360500 1185 RDQRAGVVATRQQFEFV 1201
Cdd:cd14504   120 RRIRPGSIETSEQEKFV 136
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 1108-1226 1.51e-03

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: 41.57  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1108 FHFLSWPHMGVPAQAKAL-----LDFRRKVNKSyrgrrscpIVVHGSAGAGRTGVYILLDLV-LERMNKgareidiAATL 1181
Cdd:cd14506    79 FYNFGWKDYGVPSLTTILdivkvMAFALQEGGK--------VAVHCHAGLGRTGVLIACYLVyALRMSA-------DQAI 143

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 281360500 1182 EHLRDQRAGVVATRQQFEFVlmavaEEVHAILKALPANTSGEKRE 1226
Cdd:cd14506   144 RLVRSKRPNSIQTRGQVLCV-----REFAQFLLPLRNVFACPDPK 183
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1107-1201 2.23e-03

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 39.95  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1107 QFHFLSWPHMGVP--AQAKALLDFrrkVNKSYRGRRscPIVVHGSAGAGRTGVYILLDLVLermnkgaREIDIAATLEHL 1184
Cdd:COG2453    49 EYLHLPIPDFGAPddEQLQEAVDF---IDEALREGK--KVLVHCRGGIGRTGTVAAAYLVL-------LGLSAEEALARV 116

                          90
                  ....*....|....*..
gi 281360500 1185 RDQRAGVVATRQQFEFV 1201
Cdd:COG2453   117 RAARPGAVETPAQRAFL 133
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 1003-1199 2.27e-03

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: 41.23  E-value: 2.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1003 VNASTIT-DHDPRApayVAAQGPLPSTLAHFWQMIWEQGavvIVALCRLQENGEVACaRYWPEEGAEVYHIYEVHLVSEH 1081
Cdd:cd14559    18 LNANRVQiGNKNVA---IACQYPKNEQLEDHLKMLADNR---TPCLVVLASNKDIQR-KGLPPYFRQSGTYGSVTVKSKK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1082 IwCDDYLVRSF----YLKNLRTSETR-TVTQFHFLSWPHMGvPAQAKALLDFRRKVNKS-------YRGRRSCPI----- 1144
Cdd:cd14559    91 T-GKDELVDGLkadmYNLKITDGNKTiTIPVVHVTNWPDHT-AISSEGLKELADLVNKSaeekrnfYKSKGSSAIndknk 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 281360500 1145 ---VVHGSAGAGRTGVYIlldlVLERMNKGAREIDIAATLEHLRDQRAG-VVATRQQFE 1199
Cdd:cd14559   169 llpVIHCRAGVGRTGQLA----AAMELNKSPNNLSVEDIVSDMRTSRNGkMVQKDEQLD 223
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1119-1203 4.22e-03

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: 38.48  E-value: 4.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360500 1119 PAQAKALLDFRRKVNKsyrgrRSCPIVVHGSAGAGRTGVYILLDLVLERMNKGAREIDIaatlehLRDQRAGVVATR-QQ 1197
Cdd:cd14494    39 LAMVDRFLEVLDQAEK-----PGEPVLVHCKAGVGRTGTLVACYLVLLGGMSAEEAVRI------VRLIRPGGIPQTiEQ 107


                  ....*.
gi 281360500 1198 FEFVLM 1203
Cdd:cd14494   108 LDFLIK 113
 
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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