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Conserved domains on  [gi|1958671442|ref|XP_038946275|]
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receptor-type tyrosine-protein phosphatase C isoform X3 [Rattus norvegicus]

Protein Classification

fibronectin type III domain-containing protein( domain architecture ID 13782767)

fibronectin type III (FN3) domain-containing protein may be involved in specific interactions with other molecules through its FN3 domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 520-720 3.14e-146

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: 436.18  E-value: 3.14e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  520 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCMEEGTRTFRDVVVTINDH 599
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  600 KRCPDYIIQKLSIAHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 679
Cdd:cd14557     81 KICPDYIIRKLNINNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIGI 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1958671442  680 DAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQ 720
Cdd:cd14557    161 DAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 830-1035 5.12e-118

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: 362.48  E-value: 5.12e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  830 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGEGKQTYGDMEVMLKDTNKS 909
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIEVELKDTEKS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  910 SAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSegmKYHKHASILVHCRDGSQQTG 989
Cdd:cd14558     81 PTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNS---KHGRSVPIVVHCSDGSSRTG 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1958671442  990 LFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYD 1035
Cdd:cd14558    158 IFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
CD45 pfam12567
Leukocyte receptor CD45; This family of proteins is found in eukaryotes. Proteins in this ...
 47-103 1.20e-19

Leukocyte receptor CD45; This family of proteins is found in eukaryotes. Proteins in this family are typically between 77 and 1130 amino acids in length. The family is found in association with pfam00041. CD45 plays a critical role in T-cell receptor (TCR)-mediated signaling. CD45 interacts with SKAP55 which is a transcriptional activator of IL-2.


:

Pssm-ID: 432641  Cd Length: 59  Bit Score: 83.57  E-value: 1.20e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958671442   47 VRYIYDDSSKNFNANLEGDKKPKCEYTDCEK-ELKNLPECSQKNVTLSNGSCT-PDKII 103
Cdd:pfam12567    1 VEYTYNSENKSFTAKLNVNDNVECENNDCENnELHNLQECEQINVSISHNSCTsPNKIL 59
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 210-275 5.54e-09

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 54.42  E-value: 5.54e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958671442  210 HVQCKNSTNSTTLVSWAEPA---SKHHGYILCYKKTPSE---KCENLANDVNSFEVKNLRPYTEYTVSLFAY 275
Cdd:cd00063      6 NLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGdwkEVEVTPGSETSYTLTGLKPGTEYEFRVRAV 77
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 298-378 5.07e-08

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 51.73  E-value: 5.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  298 PGKVNGMKTSRASDNSINVTCNSPYEINGPEARYILEVKSGGS----LVKTFNQSTCKFVVDNLYYSTDYEFLVYFYNGE 373
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSgdwkEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80


                   ....*
gi 1958671442  374 YLGDP 378
Cdd:cd00063     81 GESPP 85
Wzy_O6_O28 super family cl41481
oligosaccharide repeat unit polymerase; Members of this family are oligosaccharide repeat unit ...
 365-424 3.50e-04

oligosaccharide repeat unit polymerase; Members of this family are oligosaccharide repeat unit polymerases in a subfamily that includes the Wzy proteins for polymerization of the O-antigens O6, O28, O39, O59, and several others.


The actual alignment was detected with superfamily member NF033860:

Pssm-ID: 468211  Cd Length: 384  Bit Score: 44.14  E-value: 3.50e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  365 FLVYFYNGEYLGDpeikPQSTSYNSKALIIFLVFLIIVTSIALLVVLYKIYDLRKKRSSN 424
Cdd:NF033860    18 FIYFIITGELGGD----FSGVEINLSNILLLIILLLILLFFLFLYLLYKLFKKIKVKNKS 73
 
Name Accession Description Interval E-value
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 520-720 3.14e-146

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: 436.18  E-value: 3.14e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  520 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCMEEGTRTFRDVVVTINDH 599
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  600 KRCPDYIIQKLSIAHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 679
Cdd:cd14557     81 KICPDYIIRKLNINNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIGI 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1958671442  680 DAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQ 720
Cdd:cd14557    161 DAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 830-1035 5.12e-118

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: 362.48  E-value: 5.12e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  830 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGEGKQTYGDMEVMLKDTNKS 909
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIEVELKDTEKS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  910 SAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSegmKYHKHASILVHCRDGSQQTG 989
Cdd:cd14558     81 PTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNS---KHGRSVPIVVHCSDGSSRTG 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1958671442  990 LFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYD 1035
Cdd:cd14558    158 IFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
465-724 1.68e-110

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 344.64  E-value: 1.68e-110
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442   465 LFLAEFQSIPRVFS-KFPIKDARKSQNQNKNRYVDILPYDYNRVELSEINGDaGSTYINASYIDGFKEPRKYIAAQGPRD 543
Cdd:smart00194    1 GLEEEFEKLDRLKPdDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE-GSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442   544 ETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCMEEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKATgRE 623
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSET-RT 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442   624 VTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRR 703
Cdd:smart00194  159 VTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRS 238

                           250       260
                    ....*....|....*....|.
gi 1958671442   704 QRCLMVQVEAQYILIHQALVE 724
Cdd:smart00194  239 QRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
490-724 4.52e-106

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 331.90  E-value: 4.52e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  490 NQNKNRYVDILPYDYNRVELSEINGDagSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEE 569
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP--SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  570 GNRNKCAEYWPCMEEGTRTFRDVVVTI-NDHKRCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLR 648
Cdd:pfam00102   79 KGREKCAQYWPEEEGESLEYGDFTVTLkKEKEDEKDYTVRTLEVSNGGSEET-RTVKHFHYTGWPDHGVPESPNSLLDLL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958671442  649 RRVNAFSN-FFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 724
Cdd:pfam00102  158 RKVRKSSLdGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
757-1038 7.22e-89

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 286.48  E-value: 7.22e-89
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442   757 LEAEYQRLPSYRSW-RTQHIGNQEENKKKNRSSNVVPYDFNRVPLKHELEmskeseaesdessdedsdseETSKYINASF 835
Cdd:smart00194    2 LEEEFEKLDRLKPDdESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPG--------------------EGSDYINASY 61

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442   836 VMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW---GEGKQTYGDMEVMLKDTNKSSAY 912
Cdd:smart00194   62 IDGPNGPKAYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWpdeEGEPLTYGDITVTLKSVEKVDDY 141

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442   913 ILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPksgsegmkyHKHASILVHCRDGSQQTGLFC 992
Cdd:smart00194  142 TIRTLEVTNTGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQS---------TSTGPIVVHCSAGVGRTGTFI 212

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*.
gi 1958671442   993 ALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIMA 1038
Cdd:smart00194  213 AIDILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAIL 258
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
781-1038 2.88e-84

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 272.96  E-value: 2.88e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  781 NKKKNRSSNVVPYDFNRVPLKHElemskeseaesdessdedsdsEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFW 860
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGD---------------------PGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFW 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  861 QMIFQRKVKVIVMLTELMSGDQEVCAQYW---GEGKQTYGDMEVMLKDTNK-SSAYILRAFELRHSKRKEPRTVYQYQCT 936
Cdd:pfam00102   60 RMVWEEKVTIIVMLTELEEKGREKCAQYWpeeEGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYT 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  937 TWKGEELPAEPKDLVTLIQNIKQKLPKsgsegmkyHKHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSL 1016
Cdd:pfam00102  140 GWPDHGVPESPNSLLDLLRKVRKSSLD--------GRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKEL 211

                          250       260
                   ....*....|....*....|..
gi 1958671442 1017 RKARPGMVGSFEQYQFLYDIMA 1038
Cdd:pfam00102  212 RSQRPGMVQTLEQYIFLYDAIL 233
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 448-722 2.27e-49

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 178.30  E-value: 2.27e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  448 SDLLLETYKRKIADEGRLFLAEFQSIPrvfSKFPIKDARKSQNQNKNRYVDILPYDYNRVELSE---------------- 511
Cdd:PHA02746    12 FDFFDKTNHAKFCEFVLLEHAEVMDIP---IRGTTNHFLKKENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkk 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  512 ---INGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRnKCAEYWPCMEEGTRT 588
Cdd:PHA02746    89 ievTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDDDE-KCFELWTKEEDSELA 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  589 FRDVVVTINDHKRCPDYIIQKLSIAHKKEKaTGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA----------FSNFF 658
Cdd:PHA02746   168 FGRFVAKILDIIEELSFTKTRLMITDKISD-TSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEeqaelikqadNDPQT 246

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958671442  659 SGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQAL 722
Cdd:PHA02746   247 LGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
483-718 5.42e-41

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 152.55  E-value: 5.42e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  483 KDARKSQNQN---KNRYVDILPYDYNRVElseINGdagsTYINASYIDGfKEPRKYIAAQGPRDETVDDFWKMIWEQKAT 559
Cdd:COG5599     32 NDPQYLQNINgspLNRFRDIQPYKETALR---ANL----GYLNANYIQV-IGNHRYIATQYPLEEQLEDFFQMLFDNNTP 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  560 VIVMVTRCEEG--NRNKCAEYWPcmEEGTRTFRDVVVTINDHKRCPDYI---IQKLSIAHKKEKatGREVTHIQFTSWPD 634
Cdd:COG5599    104 VLVVLASDDEIskPKVKMPVYFR--QDGEYGKYEVSSELTESIQLRDGIearTYVLTIKGTGQK--KIEIPVLHVKNWPD 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  635 HGVP--EDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEG--KVDVYGYVVNLRRQR-CLMV 709
Cdd:COG5599    180 HGAIsaEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMV 259


                   ....*....
gi 1958671442  710 QVEAQYILI 718
Cdd:COG5599    260 QTSEQLDVL 268
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 780-1033 1.03e-32

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 129.74  E-value: 1.03e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  780 ENKKKNRSSNVVPYDFNRVPLKhelemskeseaesdessdedSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDF 859
Cdd:PHA02747    50 ENQPKNRYWDIPCWDHNRVILD--------------------SGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADF 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  860 WQMIFQRKVKVIVML--TELMSGdQEVCAQYWGEGKQTYGDMEVMLKDTNKSSA---YILRAFELRHSKRKEPRTVYQYQ 934
Cdd:PHA02747   110 WKAVWQEHCSIIVMLtpTKGTNG-EEKCYQYWCLNEDGNIDMEDFRIETLKTSVrakYILTLIEITDKILKDSRKISHFQ 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  935 CTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSE-GMKYHKHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVV 1013
Cdd:PHA02747   189 CSEWFEDETPSDHPDFIKFIKIIDINRKKSGKLfNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTA 268

                          250       260
                   ....*....|....*....|
gi 1958671442 1014 KSLRKARPGMVGSFEQYQFL 1033
Cdd:PHA02747   269 EKIREQRHAGIMNFDDYLFI 288
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
772-1040 2.06e-23

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 101.71  E-value: 2.06e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  772 TQHIGNQEeNKKKNRSSNVVPYDFNRVplkhelemskeseaesdessdedsdsEETSKYINASFVMSYwKPEMMIAAQGP 851
Cdd:COG5599     34 PQYLQNIN-GSPLNRFRDIQPYKETAL--------------------------RANLGYLNANYIQVI-GNHRYIATQYP 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  852 LKETIGDFWQMIFQRKVKVIVMLT--ELMSGDQEVCAQYWGEgKQTYGDMEVMLKDTNK---SSAYILRAFEL-RHSKRK 925
Cdd:COG5599     86 LEEQLEDFFQMLFDNNTPVLVVLAsdDEISKPKVKMPVYFRQ-DGEYGKYEVSSELTESiqlRDGIEARTYVLtIKGTGQ 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  926 EPRTVYQYQCTTWK-GEELPAEP-KDLVTLIqnIKQKLPKSGSEGmkyhkhaSILVHCRDGSQQTGLFCALFNLLES--A 1001
Cdd:COG5599    165 KKIEIPVLHVKNWPdHGAISAEAlKNLADLI--DKKEKIKDPDKL-------LPVVHCRAGVGRTGTLIACLALSKSinA 235

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1958671442 1002 ETEDVVDVFQVVKSLRKAR-PGMVGSFEQYQFLYDIMASI 1040
Cdd:COG5599    236 LVQITLSVEEIVIDMRTSRnGGMVQTSEQLDVLVKLAEQQ 275
CD45 pfam12567
Leukocyte receptor CD45; This family of proteins is found in eukaryotes. Proteins in this ...
 47-103 1.20e-19

Leukocyte receptor CD45; This family of proteins is found in eukaryotes. Proteins in this family are typically between 77 and 1130 amino acids in length. The family is found in association with pfam00041. CD45 plays a critical role in T-cell receptor (TCR)-mediated signaling. CD45 interacts with SKAP55 which is a transcriptional activator of IL-2.


Pssm-ID: 432641  Cd Length: 59  Bit Score: 83.57  E-value: 1.20e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958671442   47 VRYIYDDSSKNFNANLEGDKKPKCEYTDCEK-ELKNLPECSQKNVTLSNGSCT-PDKII 103
Cdd:pfam12567    1 VEYTYNSENKSFTAKLNVNDNVECENNDCENnELHNLQECEQINVSISHNSCTsPNKIL 59
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 210-275 5.54e-09

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 54.42  E-value: 5.54e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958671442  210 HVQCKNSTNSTTLVSWAEPA---SKHHGYILCYKKTPSE---KCENLANDVNSFEVKNLRPYTEYTVSLFAY 275
Cdd:cd00063      6 NLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGdwkEVEVTPGSETSYTLTGLKPGTEYEFRVRAV 77
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 298-378 5.07e-08

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 51.73  E-value: 5.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  298 PGKVNGMKTSRASDNSINVTCNSPYEINGPEARYILEVKSGGS----LVKTFNQSTCKFVVDNLYYSTDYEFLVYFYNGE 373
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSgdwkEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80


                   ....*
gi 1958671442  374 YLGDP 378
Cdd:cd00063     81 GESPP 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 209-275 2.49e-07

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 49.54  E-value: 2.49e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958671442   209 PHVQCKNSTNSTTLVSWAEPASKHH-GYILCYK-----KTPSEKCENLANDVNSFEVKNLRPYTEYTVSLFAY 275
Cdd:smart00060    5 SNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRveyreEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77
fn3 pfam00041
Fibronectin type III domain;
211-275 5.01e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 48.57  E-value: 5.01e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958671442  211 VQCKNSTNSTTLVSWAEPASKH---HGYILCYKKTPSEKCE---NLANDVNSFEVKNLRPYTEYTVSLFAY 275
Cdd:pfam00041    6 LTVTDVTSTSLTVSWTPPPDGNgpiTGYEVEYRPKNSGEPWneiTVPGTTTSVTLTGLKPGTEYEVRVQAV 76
Wzy_O6_O28 NF033860
oligosaccharide repeat unit polymerase; Members of this family are oligosaccharide repeat unit ...
 365-424 3.50e-04

oligosaccharide repeat unit polymerase; Members of this family are oligosaccharide repeat unit polymerases in a subfamily that includes the Wzy proteins for polymerization of the O-antigens O6, O28, O39, O59, and several others.


Pssm-ID: 468211  Cd Length: 384  Bit Score: 44.14  E-value: 3.50e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  365 FLVYFYNGEYLGDpeikPQSTSYNSKALIIFLVFLIIVTSIALLVVLYKIYDLRKKRSSN 424
Cdd:NF033860    18 FIYFIITGELGGD----FSGVEINLSNILLLIILLLILLFFLFLYLLYKLFKKIKVKNKS 73
fn3 pfam00041
Fibronectin type III domain;
299-378 5.73e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 39.71  E-value: 5.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  299 GKVNGMKTSRASDNSINVTCNSPYEINGPEARYILEVKS--GGSLVKTFN--QSTCKFVVDNLYYSTDYEFLVYFYNGEY 374
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPknSGEPWNEITvpGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....
gi 1958671442  375 LGDP 378
Cdd:pfam00041   81 EGPP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 298-368 1.77e-03

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 38.36  E-value: 1.77e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958671442   298 PGKVNGMKTSRASDNSINVTCNSPYE--INGPEARYILEVKSGGSLVKTFN--QSTCKFVVDNLYYSTDYEFLVY 368
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDdgITGYIVGYRVEYREEGSEWKEVNvtPSSTSYTLTGLKPGTEYEFRVR 75
 
Name Accession Description Interval E-value
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 520-720 3.14e-146

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: 436.18  E-value: 3.14e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  520 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCMEEGTRTFRDVVVTINDH 599
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  600 KRCPDYIIQKLSIAHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 679
Cdd:cd14557     81 KICPDYIIRKLNINNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIGI 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1958671442  680 DAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQ 720
Cdd:cd14557    161 DAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 830-1035 5.12e-118

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: 362.48  E-value: 5.12e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  830 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGEGKQTYGDMEVMLKDTNKS 909
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIEVELKDTEKS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  910 SAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSegmKYHKHASILVHCRDGSQQTG 989
Cdd:cd14558     81 PTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNS---KHGRSVPIVVHCSDGSSRTG 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1958671442  990 LFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYD 1035
Cdd:cd14558    158 IFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
465-724 1.68e-110

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 344.64  E-value: 1.68e-110
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442   465 LFLAEFQSIPRVFS-KFPIKDARKSQNQNKNRYVDILPYDYNRVELSEINGDaGSTYINASYIDGFKEPRKYIAAQGPRD 543
Cdd:smart00194    1 GLEEEFEKLDRLKPdDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE-GSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442   544 ETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCMEEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKATgRE 623
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSET-RT 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442   624 VTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRR 703
Cdd:smart00194  159 VTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRS 238

                           250       260
                    ....*....|....*....|.
gi 1958671442   704 QRCLMVQVEAQYILIHQALVE 724
Cdd:smart00194  239 QRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
490-724 4.52e-106

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 331.90  E-value: 4.52e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  490 NQNKNRYVDILPYDYNRVELSEINGDagSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEE 569
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP--SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  570 GNRNKCAEYWPCMEEGTRTFRDVVVTI-NDHKRCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLR 648
Cdd:pfam00102   79 KGREKCAQYWPEEEGESLEYGDFTVTLkKEKEDEKDYTVRTLEVSNGGSEET-RTVKHFHYTGWPDHGVPESPNSLLDLL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958671442  649 RRVNAFSN-FFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 724
Cdd:pfam00102  158 RKVRKSSLdGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 490-724 3.33e-98

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: 310.87  E-value: 3.33e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  490 NQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEE 569
Cdd:cd14553      3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  570 GNRNKCAEYWPcmEEGTRTFRDVVVTINDHKRCPDYIIQKLSIaHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRR 649
Cdd:cd14553     83 RSRVKCDQYWP--TRGTETYGLIQVTLLDTVELATYTVRTFAL-HKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLR 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958671442  650 RVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 724
Cdd:cd14553    160 RVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 520-720 3.91e-94

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: 298.43  E-value: 3.91e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  520 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCMEEGTRTFRDVVVTINDH 599
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  600 KRCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 679
Cdd:cd00047     81 EELSDYTIRTLELSPKGCSES-REVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAI 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1958671442  680 DAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQ 720
Cdd:cd00047    160 DILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 495-720 1.27e-92

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: 295.42  E-value: 1.27e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  495 RYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNK 574
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  575 CAEYWPCMEEGTrTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAF 654
Cdd:cd14548     81 CDHYWPFDQDPV-YYGDITVTMLSESVLPDWTIREFKLERGDEV---RSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDY 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958671442  655 SNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQ 720
Cdd:cd14548    157 IKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 445-733 1.48e-89

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: 290.00  E-value: 1.48e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  445 PIHSDLLLETYKRKIADEGRLFLAEFQSIPRVFSKFPIKDARKSQNQNKNRYVDILPYDYNRVELSEINGDAGSTYINAS 524
Cdd:cd14621      7 PLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINAS 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  525 YIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPcmEEGTRTFRDVVVTINDHKRCPD 604
Cdd:cd14621     87 FINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWP--DQGCWTYGNIRVSVEDVTVLVD 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  605 YIIQKLSIAHKKE---KATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDA 681
Cdd:cd14621    165 YTVRKFCIQQVGDvtnKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDA 244

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958671442  682 MLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVEYNQFGETEV 733
Cdd:cd14621    245 MLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
757-1038 7.22e-89

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 286.48  E-value: 7.22e-89
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442   757 LEAEYQRLPSYRSW-RTQHIGNQEENKKKNRSSNVVPYDFNRVPLKHELEmskeseaesdessdedsdseETSKYINASF 835
Cdd:smart00194    2 LEEEFEKLDRLKPDdESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPG--------------------EGSDYINASY 61

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442   836 VMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW---GEGKQTYGDMEVMLKDTNKSSAY 912
Cdd:smart00194   62 IDGPNGPKAYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWpdeEGEPLTYGDITVTLKSVEKVDDY 141

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442   913 ILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPksgsegmkyHKHASILVHCRDGSQQTGLFC 992
Cdd:smart00194  142 TIRTLEVTNTGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQS---------TSTGPIVVHCSAGVGRTGTFI 212

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*.
gi 1958671442   993 ALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIMA 1038
Cdd:smart00194  213 AIDILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAIL 258
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 520-719 1.48e-84

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: 272.69  E-value: 1.48e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  520 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPcmEEGTRTFRDVVVTINDH 599
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWP--KEGTETYGNIQVTLLST 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  600 KRCPDYIIQKLSIAHKKEK-----ATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTG 674
Cdd:cd14549     79 EVLATYTVRTFSLKNLKLKkvkgrSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTG 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1958671442  675 TYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIH 719
Cdd:cd14549    159 TYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
781-1038 2.88e-84

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 272.96  E-value: 2.88e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  781 NKKKNRSSNVVPYDFNRVPLKHElemskeseaesdessdedsdsEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFW 860
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGD---------------------PGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFW 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  861 QMIFQRKVKVIVMLTELMSGDQEVCAQYW---GEGKQTYGDMEVMLKDTNK-SSAYILRAFELRHSKRKEPRTVYQYQCT 936
Cdd:pfam00102   60 RMVWEEKVTIIVMLTELEEKGREKCAQYWpeeEGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYT 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  937 TWKGEELPAEPKDLVTLIQNIKQKLPKsgsegmkyHKHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSL 1016
Cdd:pfam00102  140 GWPDHGVPESPNSLLDLLRKVRKSSLD--------GRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKEL 211

                          250       260
                   ....*....|....*....|..
gi 1958671442 1017 RKARPGMVGSFEQYQFLYDIMA 1038
Cdd:pfam00102  212 RSQRPGMVQTLEQYIFLYDAIL 233
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 451-724 1.06e-83

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: 273.06  E-value: 1.06e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  451 LLETYKRKIADEGRLFLAEFQSI-PRvfSKFPIKDARKSQNQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGF 529
Cdd:cd14626      3 LADNIERLKANDGLKFSQEYESIdPG--QQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  530 KEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCmeEGTRTFRDVVVTINDHKRCPDYIIQK 609
Cdd:cd14626     81 RKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPI--RGTETYGMIQVTLLDTVELATYSVRT 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  610 LSIaHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAE 689
Cdd:cd14626    159 FAL-YKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHE 237

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1958671442  690 GKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 724
Cdd:cd14626    238 KTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 496-724 1.61e-81

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: 265.27  E-value: 1.61e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  496 YVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKC 575
Cdd:cd14620      1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  576 AEYWPcmEEGTRTFRDVVVTINDHKRCPDYIIQKLSIA---HKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVN 652
Cdd:cd14620     81 YQYWP--DQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQpqlPDGCKAP-RLVTQLHFTSWPDFGVPFTPIGMLKFLKKVK 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958671442  653 AFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 724
Cdd:cd14620    158 SVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 485-719 1.06e-78

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: 259.22  E-value: 1.06e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  485 ARKSQNQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMV 564
Cdd:cd14543     24 SLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMT 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  565 TRCEEGNRNKCAEYWPCMEEGTRTFRDVVVT---INDHKrcpDYIIQKLSIaHKKEKATGREVTHIQFTSWPDHGVPEDP 641
Cdd:cd14543    104 TRVVERGRVKCGQYWPLEEGSSLRYGDLTVTnlsVENKE---HYKKTTLEI-HNTETDESRQVTHFQFTSWPDFGVPSSA 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  642 HLLL--------KLRRRVNAFSNFFSG-----PIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLM 708
Cdd:cd14543    180 AALLdflgevrqQQALAVKAMGDRWKGhppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQRAFS 259

                          250
                   ....*....|.
gi 1958671442  709 VQVEAQYILIH 719
Cdd:cd14543    260 IQTPDQYYFCY 270
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 494-725 1.71e-77

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: 254.43  E-value: 1.71e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  494 NRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRN 573
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  574 KCAEYWPcMEEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA 653
Cdd:cd14619     81 KCEHYWP-LDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKT-LSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQ 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958671442  654 F--SNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVEY 725
Cdd:cd14619    159 WldQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDF 232
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 520-720 2.37e-76

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: 250.21  E-value: 2.37e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  520 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPcmEEGTRTFRDVVVTINDH 599
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWP--DQGCWTYGNLRVRVEDT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  600 KRCPDYIIQKLSIaHKKEKATG----REVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGT 675
Cdd:cd14551     79 VVLVDYTTRKFCI-QKVNRGIGekrvRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGT 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1958671442  676 YIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQ 720
Cdd:cd14551    158 FIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 830-1035 1.01e-75

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: 248.35  E-value: 1.01e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  830 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW---GEGKQTYGDMEVMLKDT 906
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWpeeGGKPLEYGDITVTLVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  907 NKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSgsegmkyhkHASILVHCRDGSQ 986
Cdd:cd00047     81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKP---------NGPIVVHCSAGVG 151

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958671442  987 QTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYD 1035
Cdd:cd00047    152 RTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 445-724 4.14e-75

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


Pssm-ID: 350473 [Multi-domain]  Cd Length: 282  Bit Score: 249.62  E-value: 4.14e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  445 PIHSDLLLETYKRKIADEGRLFLAEFQSIPRvFSKFPIKDARKSQNQNKNRYVDILPYDYNRVELSEINGDAGSTYINAS 524
Cdd:cd14625      3 PIPISELAEHTERLKANDNLKLSQEYESIDP-GQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINAN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  525 YIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPcmEEGTRTFRDVVVTINDHKRCPD 604
Cdd:cd14625     82 YIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWP--SRGTETYGMIQVTLLDTIELAT 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  605 YIIQKLSIaHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLE 684
Cdd:cd14625    160 FCVRTFSL-HKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLE 238

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1958671442  685 SLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 724
Cdd:cd14625    239 RIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 494-720 1.20e-74

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: 246.15  E-value: 1.20e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  494 NRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFK-EPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNR 572
Cdd:cd14547      1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  573 nKCAEYWPcMEEGTRtFRDVVVTINDHKRCPDYIIQKLSIAHKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVN 652
Cdd:cd14547     81 -KCAQYWP-EEENET-YGDFEVTVQSVKETDGYTVRKLTLKYGGEK---RYLKHYWYTSWPDHKTPEAAQPLLSLVQEVE 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  653 --AFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQ 720
Cdd:cd14547    155 eaRQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 494-720 4.06e-74

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: 244.73  E-value: 4.06e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  494 NRYVDILPYDYNRVELSeINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRN 573
Cdd:cd14615      1 NRYNNVLPYDISRVKLS-VQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  574 KCAEYWPcmEEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEkATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA 653
Cdd:cd14615     80 KCEEYWP--SKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQT-NESRTVRHFHFTSWPDHGVPETTDLLINFRHLVRE 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958671442  654 FS--NFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQ 720
Cdd:cd14615    157 YMkqNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 225
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 445-724 8.40e-74

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: 246.18  E-value: 8.40e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  445 PIHSDLLLETYKRKIADEGRLFLAEFQSIPRvFSKFPIKDARKSQNQNKNRYVDILPYDYNRVELSEINGDAGSTYINAS 524
Cdd:cd14624      3 PIPILELADHIERLKANDNLKFSQEYESIDP-GQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINAN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  525 YIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPcmEEGTRTFRDVVVTINDHKRCPD 604
Cdd:cd14624     82 YIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWP--SRGTETYGLIQVTLLDTVELAT 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  605 YIIQKLSIaHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLE 684
Cdd:cd14624    160 YCVRTFAL-YKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLE 238

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1958671442  685 SLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 724
Cdd:cd14624    239 RIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 494-720 2.75e-73

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: 242.52  E-value: 2.75e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  494 NRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRN 573
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  574 KCAEYWPcMEEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA 653
Cdd:cd14617     81 KCDHYWP-ADQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRD 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958671442  654 FSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQ 720
Cdd:cd14617    160 YINRTpgSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 489-724 1.46e-70

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: 235.30  E-value: 1.46e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  489 QNQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCE 568
Cdd:cd14630      2 ENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  569 EGNRNKCAEYWPcmeEGTRTFRDVVVTINDHKRCPDYIIQKLSIaHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLR 648
Cdd:cd14630     82 EVGRVKCVRYWP---DDTEVYGDIKVTLIETEPLAEYVIRTFTV-QKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFV 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958671442  649 RRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 724
Cdd:cd14630    158 RQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 473-720 2.72e-70

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: 234.78  E-value: 2.72e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  473 IPRVFSKFPIkdarksqNQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKM 552
Cdd:cd14614      2 IPHFAADLPV-------NRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKM 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  553 IWEQKATVIVMVTRCEEGNRNKCAEYWPCMEEGTrTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKatgREVTHIQFTSW 632
Cdd:cd14614     75 VLQQKSQIIVMLTQCNEKRRVKCDHYWPFTEEPV-AYGDITVEMLSEEEQPDWAIREFRVSYADEV---QDVMHFNYTAW 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  633 PDHGVP--EDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQ 710
Cdd:cd14614    151 PDHGVPtaNAAESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQ 230

                          250
                   ....*....|
gi 1958671442  711 VEAQYILIHQ 720
Cdd:cd14614    231 TEEQYIFIHQ 240
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 466-724 1.62e-69

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: 233.77  E-value: 1.62e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  466 FLAEFQSIPRVFSKFPI--KDARKSQNQNKNRYVDILPYDYNRVELSEINGDAG--STYINASYIDGFKEPRKYIAAQGP 541
Cdd:cd17667      1 FSEDFEEVQRCTADMNItaEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIATQGP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  542 RDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPcmEEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEK--- 618
Cdd:cd17667     81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWP--TENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKkgq 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  619 ---ATGRE----VTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGK 691
Cdd:cd17667    159 kgnPKGRQnertVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKST 238

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1958671442  692 VDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 724
Cdd:cd17667    239 VNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 271
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 449-724 1.93e-69

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: 233.78  E-value: 1.93e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  449 DLLLETYKRKIAdEGRLFLAEFQSIPRVFSKfPIKDARKSQNQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDG 528
Cdd:cd14633      1 DLLQHITQMKCA-EGYGFKEEYESFFEGQSA-PWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  529 FKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPcmeEGTRTFRDVVVTINDHKRCPDYIIQ 608
Cdd:cd14633     79 YHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWP---DDTEIYKDIKVTLIETELLAEYVIR 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  609 KLSIaHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEA 688
Cdd:cd14633    156 TFAV-EKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAER 234

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1958671442  689 EGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 724
Cdd:cd14633    235 EGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 490-725 2.92e-67

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: 226.58  E-value: 2.92e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  490 NQNKNRYVDILPYDYNRVELSEINGD-AGSTYINASYI-------DGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVI 561
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDRDPNvPGSDYINANYIrnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  562 VMVTRCEEGNRNKCAEYWPcmEEG-TRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKATGREVTHIQFTSWPDHGVPED 640
Cdd:cd14544     81 VMTTKEVERGKNKCVRYWP--DEGmQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPIREIWHYQYLSWPDHGVPSD 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  641 PHLLLKLRRRVNAFSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLESLEAEG---KVDVYGYVVNLRRQRCLMVQVEAQY 715
Cdd:cd14544    159 PGGVLNFLEDVNQRQESLphAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMVQTEAQY 238

                          250
                   ....*....|
gi 1958671442  716 ILIHQALVEY 725
Cdd:cd14544    239 KFIYVAVAQY 248
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 490-721 2.96e-67

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: 226.25  E-value: 2.96e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  490 NQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEE 569
Cdd:cd14554      6 NKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLRE 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  570 GNRNKCAEYWPcMEEGTRTFRDVVVTINDHKRcPDYIIQKLSIAHKKEKaTGREVTHIQFTSWPDHGVPEDPHLLLKLRR 649
Cdd:cd14554     86 MGREKCHQYWP-AERSARYQYFVVDPMAEYNM-PQYILREFKVTDARDG-QSRTVRQFQFTDWPEQGVPKSGEGFIDFIG 162

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958671442  650 RV-NAFSNF-FSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQA 721
Cdd:cd14554    163 QVhKTKEQFgQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 520-720 1.43e-66

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: 223.28  E-value: 1.43e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  520 YINASYID-GFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCMEEGTRTFrDVVVTIND 598
Cdd:cd18533      1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYG-DLTVELVS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  599 HKRCPD--YIIQKLSIAHKKEKAtgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA--FSNFFSGPIVVHCSAGVGRTG 674
Cdd:cd18533     80 EEENDDggFIVREFELSKEDGKV--KKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRElnDSASLDPPIIVHCSAGVGRTG 157

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958671442  675 TYIGIDAMLESLEA--------EGKVD-VYGYVVNLRRQRCLMVQVEAQYILIHQ 720
Cdd:cd18533    158 TFIALDSLLDELKRglsdsqdlEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 494-723 1.04e-65

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: 221.36  E-value: 1.04e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  494 NRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRN 573
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  574 KCAEYWPcMEEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA 653
Cdd:cd14618     81 LCDHYWP-SESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKE-RRVKHLHYTAWPDHGIPESTSSLMAFRELVRE 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958671442  654 F--SNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALV 723
Cdd:cd14618    159 HvqATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 520-724 6.38e-64

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: 215.55  E-value: 6.38e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  520 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPcmeEGTRTFRDVVVTINDH 599
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP---DDTEVYGDIKVTLVET 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  600 KRCPDYIIQKLSIaHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 679
Cdd:cd14555     78 EPLAEYVVRTFAL-ERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVI 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1958671442  680 DAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 724
Cdd:cd14555    157 DIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 520-723 2.27e-63

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: 214.07  E-value: 2.27e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  520 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCmeEGTRTFRDVVVTINDH 599
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPA--DGSEEYGNFLVTQKSV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  600 KRCPDYIIQ-------KLSIAHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGR 672
Cdd:cd17668     79 QVLAYYTVRnftlrntKIKKGSQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGR 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958671442  673 TGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALV 723
Cdd:cd17668    159 TGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 494-720 2.30e-62

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: 211.69  E-value: 2.30e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  494 NRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRN 573
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  574 KCAEYWPCMEEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKATgreVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA 653
Cdd:cd14616     81 RCHQYWPEDNKPVTVFGDIVITKLMEDVQIDWTIRDLKIERHGDYMM---VRQCNFTSWPEHGVPESSAPLIHFVKLVRA 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958671442  654 FSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQ 720
Cdd:cd14616    158 SRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 493-725 1.14e-60

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: 207.77  E-value: 1.14e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  493 KNRYVDILPYDYNRVEL-SEINGDAGSTYINASYIDGFK-EPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEG 570
Cdd:cd14612     18 KDRYKTILPNPQSRVCLrRAGSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKEK 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  571 NRnKCAEYWPCMEEgtrTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKL--- 647
Cdd:cd14612     98 KE-KCVHYWPEKEG---TYGRFEIRVQDMKECDGYTIRDLTIQLEEES---RSVKHYWFSSWPDHQTPESAGPLLRLvae 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  648 --RRRVNAFSnffSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVEY 725
Cdd:cd14612    171 veESRQTAAS---PGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLHHTLALY 247
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 506-724 1.35e-60

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: 206.41  E-value: 1.35e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  506 RVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPcmeEG 585
Cdd:cd14631      1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP---DD 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  586 TRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVH 665
Cdd:cd14631     78 TEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEI-REVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVH 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958671442  666 CSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 724
Cdd:cd14631    157 CSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 483-725 5.93e-60

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: 206.65  E-value: 5.93e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  483 KDARKSQNQNKNRYVDILPYDYNRVELSeiNGDA---GSTYINASYID----GFKEPRK-YIAAQGPRDETVDDFWKMIW 554
Cdd:cd14606     11 LEGQRPENKSKNRYKNILPFDHSRVILQ--GRDSnipGSDYINANYVKnqllGPDENAKtYIASQGCLEATVNDFWQMAW 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  555 EQKATVIVMVTRCEEGNRNKCAEYWPCMeEGTRTFRDVVVTINDHKRCPDYIIQ--KLSIAHKKEKAtgREVTHIQFTSW 632
Cdd:cd14606     89 QENSRVIVMTTREVEKGRNKCVPYWPEV-GMQRAYGPYSVTNCGEHDTTEYKLRtlQVSPLDNGELI--REIWHYQYLSW 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  633 PDHGVPEDPHLLLKLRRRVNAFSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLESLEAEG---KVDVYGYVVNLRRQRCL 707
Cdd:cd14606    166 PDHGVPSEPGGVLSFLDQINQRQESLphAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGldcDIDIQKTIQMVRAQRSG 245

                          250
                   ....*....|....*...
gi 1958671442  708 MVQVEAQYILIHQALVEY 725
Cdd:cd14606    246 MVQTEAQYKFIYVAIAQF 263
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 490-725 6.59e-60

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: 207.28  E-value: 6.59e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  490 NQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEE 569
Cdd:cd14627     53 NKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLRE 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  570 GNRNKCAEYWPCmeEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEkATGREVTHIQFTSWPDHGVPEDPHLLLKLRR 649
Cdd:cd14627    133 MGREKCHQYWPA--ERSARYQYFVVDPMAEYNMPQYILREFKVTDARD-GQSRTVRQFQFTDWPEQGVPKSGEGFIDFIG 209

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958671442  650 RVNAFSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVEY 725
Cdd:cd14627    210 QVHKTKEQFgqDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEY 287
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 490-725 6.89e-60

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: 207.27  E-value: 6.89e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  490 NQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEE 569
Cdd:cd14629     53 NKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLRE 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  570 GNRNKCAEYWPCmeEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEkATGREVTHIQFTSWPDHGVPEDPHLLLKLRR 649
Cdd:cd14629    133 MGREKCHQYWPA--ERSARYQYFVVDPMAEYNMPQYILREFKVTDARD-GQSRTIRQFQFTDWPEQGVPKTGEGFIDFIG 209

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958671442  650 RVNAFSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVEY 725
Cdd:cd14629    210 QVHKTKEQFgqDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEY 287
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 490-725 9.94e-60

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: 206.89  E-value: 9.94e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  490 NQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEE 569
Cdd:cd14628     52 NKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLRE 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  570 GNRNKCAEYWPCmeEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEkATGREVTHIQFTSWPDHGVPEDPHLLLKLRR 649
Cdd:cd14628    132 MGREKCHQYWPA--ERSARYQYFVVDPMAEYNMPQYILREFKVTDARD-GQSRTVRQFQFTDWPEQGVPKSGEGFIDFIG 208

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958671442  650 RVNAFSNFF--SGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVEY 725
Cdd:cd14628    209 QVHKTKEQFgqDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEY 286
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 520-724 2.51e-59

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) and type 13 (PTPN13, also known as PTPL1) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization. Human PTPN13 is an important regulator of tumor aggressiveness.


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 202.60  E-value: 2.51e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  520 YINASYI--DGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWP------CMEEGTRTFRD 591
Cdd:cd14538      1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdslnkpLICGGRLEVSL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  592 VVVTINDhkrcpDYIIQKLSIAHKkEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNffSGPIVVHCSAGVG 671
Cdd:cd14538     81 EKYQSLQ-----DFVIRRISLRDK-ETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHN--SGPIVVHCSAGIG 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958671442  672 RTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 724
Cdd:cd14538    153 RTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 520-724 5.71e-59

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


Pssm-ID: 350480 [Multi-domain]  Cd Length: 205  Bit Score: 201.43  E-value: 5.71e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  520 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPcmeEGTRTFRDVVVTINDH 599
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP---DDSDTYGDIKITLLKT 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  600 KRCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGI 679
Cdd:cd14632     78 ETLAEYSVRTFALERRGYSAR-HEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVL 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1958671442  680 DAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 724
Cdd:cd14632    157 DVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 489-723 1.63e-57

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: 198.52  E-value: 1.63e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  489 QNQNKNRYVDILPYDYNRVELSEINGdagstYINASYID---GfKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVT 565
Cdd:cd14597      2 ENRKKNRYKNILPYDTTRVPLGDEGG-----YINASFIKmpvG-DEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMT 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  566 RCEEGNRNKCAEYWP-CMEEGTRTFRDVVVTINDHKRCPDYIIQKLSIaHKKEKATGREVTHIQFTSWPDHGVPEDPHLL 644
Cdd:cd14597     76 QEVEGGKIKCQRYWPeILGKTTMVDNRLQLTLVRMQQLKNFVIRVLEL-EDIQTREVRHITHLNFTAWPDHDTPSQPEQL 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  645 LKL---RRRVNAfsnffSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQA 721
Cdd:cd14597    155 LTFisyMRHIHK-----SGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQV 229


                   ..
gi 1958671442  722 LV 723
Cdd:cd14597    230 IL 231
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 520-715 4.41e-57

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: 196.07  E-value: 4.41e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  520 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPcmeEGTRTFRDVVVTINDH 599
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWG---DEKKTYGDIEVELKDT 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  600 KRCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRV------NAFSNFFSGPIVVHCSAGVGRT 673
Cdd:cd14558     78 EKSPTYTVRVFEITHLKRKDS-RTVYQYQYHKWKGEELPEKPKDLVDMIKSIkqklpyKNSKHGRSVPIVVHCSDGSSRT 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1958671442  674 GTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQY 715
Cdd:cd14558    157 GIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQY 198
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 489-725 7.05e-57

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


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 197.16  E-value: 7.05e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  489 QNQNKNRYVDILPYDYNRVELSEinGDA---GSTYINASYI--------DGFKEPRKYIAAQGPRDETVDDFWKMIWEQK 557
Cdd:cd14605      1 ENKNKNRYKNILPFDHTRVVLHD--GDPnepVSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQEN 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  558 ATVIVMVTRCEEGNRNKCAEYWP----CMEEGTRTFRDVvvtindhKRCP--DYIIQKLSIAHKKEKATGREVTHIQFTS 631
Cdd:cd14605     79 SRVIVMTTKEVERGKSKCVKYWPdeyaLKEYGVMRVRNV-------KESAahDYILRELKLSKVGQGNTERTVWQYHFRT 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  632 WPDHGVPEDPHLLLKLRRRVNAFSNFFS--GPIVVHCSAGVGRTGTYIGIDAMLESLEAEG---KVDVYGYVVNLRRQRC 706
Cdd:cd14605    152 WPDHGVPSDPGGVLDFLEEVHHKQESIMdaGPVVVHCSAGIGRTGTFIVIDILIDIIREKGvdcDIDVPKTIQMVRSQRS 231

                          250
                   ....*....|....*....
gi 1958671442  707 LMVQVEAQYILIHQALVEY 725
Cdd:cd14605    232 GMVQTEAQYRFIYMAVQHY 250
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 520-725 9.28e-57

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: 195.75  E-value: 9.28e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  520 YINASYID---GFKEpRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCM--EEGTRTFRDVVV 594
Cdd:cd14540      1 YINASHITatvGGKQ-RFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLggEHDALTFGEYKV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  595 TINDHKRCPDYIIQKLSIAHKKEKaTGREVTHIQFTSWPDHGVPEDPHLLL-------KLRRRVNAFS--NFFSGPIVVH 665
Cdd:cd14540     80 STKFSVSSGCYTTTGLRVKHTLSG-QSRTVWHLQYTDWPDHGCPEDVSGFLdfleeinSVRRHTNQDVagHNRNPPTLVH 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  666 CSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVEY 725
Cdd:cd14540    159 CSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQY 218
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 489-724 4.02e-56

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: 195.43  E-value: 4.02e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  489 QNQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCE 568
Cdd:cd14603     29 ENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACREI 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  569 EGNRNKCAEYWPCMEEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKLR 648
Cdd:cd14603    109 EMGKKKCERYWAQEQEPLQTGPFTITLVKEKRLNEEVILRTLKVTFQKES---RSVSHFQYMAWPDHGIPDSPDCMLAMI 185

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958671442  649 RRVNAFSNFFSGPIVVHCSAGVGRTGTYIGID---AMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 724
Cdd:cd14603    186 ELARRLQGSGPEPLCVHCSAGCGRTGVICTVDyvrQLLLTQRIPPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 453-725 1.14e-55

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: 195.22  E-value: 1.14e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  453 ETYKRKIaDEGRLFlAEFQSIPRVFSKFPIKDARKSQNQNKNRYVDILPYDYNRVELSEiNGDAGSTYINASYIDGF--K 530
Cdd:cd14599      3 KTLERKL-EEGMVF-TEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVP-TKENNTGYINASHIKVTvgG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  531 EPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCM--EEGTRTFRDVVVTINDHKRCPDYIIQ 608
Cdd:cd14599     80 EEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLgsKHSSATYGKFKVTTKFRTDSGCYATT 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  609 KLSIAHKkekATGREVT--HIQFTSWPDHGVPEDPHLLLK-------LRRRVNAF---SNFFSGPIVVHCSAGVGRTGTY 676
Cdd:cd14599    160 GLKVKHL---LSGQERTvwHLQYTDWPDHGCPEEVQGFLSyleeiqsVRRHTNSMldsTKNCNPPIVVHCSAGVGRTGVV 236

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1958671442  677 IGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVEY 725
Cdd:cd14599    237 ILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQF 285
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 493-714 1.43e-55

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: 192.61  E-value: 1.43e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  493 KNRYVDILPYDYNRVELSEINGDagSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNR 572
Cdd:cd14545      1 LNRYRDRDPYDHDRSRVKLKQGD--NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  573 NKCAEYWPCMEEGTRTFRDVV--VTINDHKRCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDHGVPEDP----HLLLK 646
Cdd:cd14545     79 IKCAQYWPQGEGNAMIFEDTGlkVTLLSEEDKSYYTVRTLELENLKTQET-REVLHFHYTTWPDFGVPESPaaflNFLQK 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  647 LRRRVNAFSNFfsGPIVVHCSAGVGRTGTYIGIDAMLESLEAEG--KVDVYGYVVNLRRQRCLMVQVEAQ 714
Cdd:cd14545    158 VRESGSLSSDV--GPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKYRMGLIQTPDQ 225
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 520-723 1.52e-55

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: 191.33  E-value: 1.52e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  520 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPcmEEGTRTFRDVVVTINDH 599
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWP--EDGSVSSGDITVELKDQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  600 KRCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDHGVPEDP----HLLLKLRRRVNAFSNffsGPIVVHCSAGVGRTGT 675
Cdd:cd14552     79 TDYEDYTLRDFLVTKGKGGST-RTVRQFHFHGWPEVGIPDNGkgmiDLIAAVQKQQQQSGN---HPITVHCSAGAGRTGT 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1958671442  676 YIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALV 723
Cdd:cd14552    155 FCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVVQ 202
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 520-720 6.23e-55

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: 189.56  E-value: 6.23e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  520 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCMEEGTRTFRDVVVTINDH 599
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKISLEKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  600 KR-CPDYIIQKLSIAHKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIG 678
Cdd:cd14542     81 KRvGPDFLIRTLKVTFQKES---RTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICA 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1958671442  679 IDAMLESLEAEGKVD---VYGYVVNLRRQRCLMVQVEAQYILIHQ 720
Cdd:cd14542    158 IDYVWNLLKTGKIPEefsLFDLVREMRKQRPAMVQTKEQYELVYR 202
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 495-724 7.39e-55

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: 190.64  E-value: 7.39e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  495 RYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNK 574
Cdd:cd14623      1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  575 CAEYWPcmEEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDHGVPEDP----HLLLKLRRR 650
Cdd:cd14623     81 CAQYWP--SDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENKS-RQIRQFHFHGWPEVGIPSDGkgmiNIIAAVQKQ 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958671442  651 VNAFSNFfsgPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 724
Cdd:cd14623    158 QQQSGNH---PITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 466-724 1.71e-54

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: 192.07  E-value: 1.71e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  466 FLAEFQSIPRVFSKF------PIKDARKSQNQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQ 539
Cdd:cd14604     27 FASDFMRLRRLSTKYrtekiyPTATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQ 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  540 GPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCMEEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKa 619
Cdd:cd14604    107 GPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNET- 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  620 tgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAeGKV----DVY 695
Cdd:cd14604    186 --RRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKA-GKIpeefNVF 262

                          250       260
                   ....*....|....*....|....*....
gi 1958671442  696 GYVVNLRRQRCLMVQVEAQYILIHQALVE 724
Cdd:cd14604    263 NLIQEMRTQRHSAVQTKEQYELVHRAIAQ 291
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 830-1037 1.77e-54

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: 188.63  E-value: 1.77e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  830 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW-GEGKQTYGDMEVMLKDTNK 908
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWpEDGSVSSGDITVELKDQTD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  909 SSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSEgmkyhkhaSILVHCRDGSQQT 988
Cdd:cd14552     81 YEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGNH--------PITVHCSAGAGRT 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958671442  989 GLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIM 1037
Cdd:cd14552    153 GTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 520-715 3.20e-53

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: 185.23  E-value: 3.20e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  520 YINASYID----GFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCMEEgTRTFRDVVVT 595
Cdd:cd14541      2 YINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGE-TMQFGNLQIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  596 INDHKRCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGT 675
Cdd:cd14541     81 CVSEEVTPSFAFREFILTNTNTGEE-RHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTGV 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1958671442  676 YIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQY 715
Cdd:cd14541    160 LITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQY 199
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 493-720 6.48e-53

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: 184.74  E-value: 6.48e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  493 KNRYVDILPYDYNRVELSEIN-GDAGSTYINASYIDGFK-EPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEG 570
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPKNsNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  571 NRnKCAEYWPcmeEGTRTFRDVVVTINDHKRCPDYIIQKLSIahkKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRR 650
Cdd:cd14611     82 NE-KCVLYWP---EKRGIYGKVEVLVNSVKECDNYTIRNLTL---KQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLD 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958671442  651 V--NAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQ 720
Cdd:cd14611    155 VeeDRLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 493-725 2.80e-52

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: 184.30  E-value: 2.80e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  493 KNRYVDILPYDYNRVEL-SEINGDAGSTYINASYIDGF-KEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEG 570
Cdd:cd14613     28 KNRYKTILPNPHSRVCLtSPDQDDPLSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  571 NRnKCAEYWPcmeEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKLRRR 650
Cdd:cd14613    108 NE-KCTEYWP---EEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEE---RGLKHYWYTSWPDQKTPDNAPPLLQLVQE 180

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958671442  651 VNAF---SNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVEY 725
Cdd:cd14613    181 VEEArqqAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVLSLY 258
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 485-724 5.05e-52

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: 184.49  E-value: 5.05e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  485 ARKSQNQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGfKEPRK--YIAAQGPRDETVDDFWKMIWEQKATVIV 562
Cdd:cd14610     39 AQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMD-HDPRNpaYIATQGPLPATVADFWQMVWESGCVVIV 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  563 MVTRCEEGNRNKCAEYWPcmEEGTRTFRDVVVT-INDHKRCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDHGVPEDP 641
Cdd:cd14610    118 MLTPLAENGVKQCYHYWP--DEGSNLYHIYEVNlVSEHIWCEDFLVRSFYLKNLQTNET-RTVTQFHFLSWNDQGVPAST 194

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  642 HLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGK-VDVYGYVVNLRRQRCLMVQVEAQYILIHQ 720
Cdd:cd14610    195 RSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKGAKeIDIAATLEHLRDQRPGMVQTKEQFEFALT 274


                   ....
gi 1958671442  721 ALVE 724
Cdd:cd14610    275 AVAE 278
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 493-724 5.44e-52

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: 182.73  E-value: 5.44e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  493 KNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNR 572
Cdd:cd14602      1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  573 NKCAEYWPCMEEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKatgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVN 652
Cdd:cd14602     81 KKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSET---RTIYQFHYKNWPDHDVPSSIDPILELIWDVR 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958671442  653 AFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEaEGKV----DVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 724
Cdd:cd14602    158 CYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 470-733 6.38e-52

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: 184.07  E-value: 6.38e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  470 FQSIPRVFSKFPIKDARKSQNQNKNRYVDILPYDYNRVELSEINGDagstYINASYIDGFKEPRKYIAAQGPRDETVDDF 549
Cdd:cd14608      5 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDND----YINASLIKMEEAQRSYILTQGPLPNTCGHF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  550 WKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCMEEGTRTFRD--VVVTINDHKRCPDYIIQKLSIAHKKEKATgREVTHI 627
Cdd:cd14608     81 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDtnLKLTLISEDIKSYYTVRQLELENLTTQET-REILHF 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  628 QFTSWPDHGVPEDP----HLLLKLRRrvNAFSNFFSGPIVVHCSAGVGRTGTYIGIDA---MLESLEAEGKVDVYGYVVN 700
Cdd:cd14608    160 HYTTWPDFGVPESPasflNFLFKVRE--SGSLSPEHGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLE 237

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1958671442  701 LRRQRCLMVQVEAQYILIHQALVEYNQF--GETEV 733
Cdd:cd14608    238 MRKFRMGLIQTADQLRFSYLAVIEGAKFimGDSSV 272
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 520-734 2.57e-51

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: 179.56  E-value: 2.57e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  520 YINASYIDGfKEPRK--YIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPcmEEGTRTFRDVVVT-I 596
Cdd:cd14546      1 YINASTIYD-HDPRNpaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWP--EEGSEVYHIYEVHlV 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  597 NDHKRCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTY 676
Cdd:cd14546     78 SEHIWCDDYLVRSFYLKNLQTSET-RTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGTY 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958671442  677 IGIDAMLESLEAEGK-VDVYGYVVNLRRQRCLMVQVEAQYILIHQALVEynqfgetEVN 734
Cdd:cd14546    157 ILIDMVLNRMAKGAKeIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE-------EVN 208
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 786-1034 3.90e-51

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: 179.47  E-value: 3.90e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  786 RSSNVVPYDFNRVPLKhelemskeseaesdessdeDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQ 865
Cdd:cd14548      1 RYTNILPYDHSRVKLI-------------------PINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWE 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  866 RKVKVIVMLTELMSGDQEVCAQYWGEGKQ--TYGDMEVMLKDTNKSSAYILRAFELRHskRKEPRTVYQYQCTTWKGEEL 943
Cdd:cd14548     62 QNSHTIVMLTQCMEKGRVKCDHYWPFDQDpvYYGDITVTMLSESVLPDWTIREFKLER--GDEVRSVRQFHFTAWPDHGV 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  944 PAEPKDLVTLIQNIKQKLPKSGSegmkyhkhaSILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGM 1023
Cdd:cd14548    140 PEAPDSLLRFVRLVRDYIKQEKG---------PTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLM 210

                          250
                   ....*....|.
gi 1958671442 1024 VGSFEQYQFLY 1034
Cdd:cd14548    211 VQTEAQYIFLH 221
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 786-1037 6.30e-51

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: 179.47  E-value: 6.30e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  786 RSSNVVPYDFNRV--PLKHELEmskeseaesdessdedsdseeTSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMI 863
Cdd:cd14623      1 RVLQIIPYEFNRViiPVKRGEE---------------------NTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMI 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  864 FQRKVKVIVMLTELMSGDQEVCAQYW-GEGKQTYGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEE 942
Cdd:cd14623     60 WEWKSCSIVMLTELEERGQEKCAQYWpSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVG 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  943 LPAEPKDLVTLIQNIKQKLPKSGSEgmkyhkhaSILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPG 1022
Cdd:cd14623    140 IPSDGKGMINIIAAVQKQQQQSGNH--------PITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPH 211

                          250
                   ....*....|....*
gi 1958671442 1023 MVGSFEQYQFLYDIM 1037
Cdd:cd14623    212 MVQTLEQYEFCYKVV 226
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 467-723 6.55e-51

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: 180.82  E-value: 6.55e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  467 LAEFQSIPRVFSKFPIKDARKSQNQNKNRYVDILPYDYNRVELSEingdaGSTYINASYID----GFKEPRKYIAAQGPR 542
Cdd:cd14600     17 LIQFEQLYRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVLQG-----NEDYINASYVNmeipSANIVNKYIATQGPL 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  543 DETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWP----CMEEGtrTFRdvvVTINDHKRCPDYIIQKLSIAhKKEK 618
Cdd:cd14600     92 PHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPdppdVMEYG--GFR---VQCHSEDCTIAYVFREMLLT-NTQT 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  619 ATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAfSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYV 698
Cdd:cd14600    166 GEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRS-KRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIV 244

                          250       260
                   ....*....|....*....|....*
gi 1958671442  699 VNLRRQRCLMVQVEAQYILIHQALV 723
Cdd:cd14600    245 RKMRDQRAMMVQTSSQYKFVCEAIL 269
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 830-1035 2.47e-50

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: 177.06  E-value: 2.47e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  830 YINASFV-MSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW--GEGKQTYGD--MEVMLK 904
Cdd:cd18533      1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWpsGEYEGEYGDltVELVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  905 DTNKSSAYILRAFELRHSKrKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQnIKQKLPKSGSEGmkyhkhASILVHCRDG 984
Cdd:cd18533     81 EENDDGGFIVREFELSKED-GKVKKVYHIQYKSWPDFGVPDSPEDLLTLIK-LKRELNDSASLD------PPIIVHCSAG 152

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  985 SQQTGLFCALFNLL--------ESAETEDVVD-VFQVVKSLRKARPGMVGSFEQYQFLYD 1035
Cdd:cd18533    153 VGRTGTFIALDSLLdelkrglsDSQDLEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 830-1037 5.53e-50

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: 175.58  E-value: 5.53e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  830 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW-GEGKQTYGDMEVMLKDTNK 908
Cdd:cd14622      2 YINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWpSEGSVTHGEITIEIKNDTL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  909 SSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSEgmkyhkhaSILVHCRDGSQQT 988
Cdd:cd14622     82 LETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNH--------PIVVHCSAGAGRT 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958671442  989 GLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIM 1037
Cdd:cd14622    154 GTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 467-724 1.08e-49

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type tyrosine-protein phosphatase-like N (PTPRN or R-PTP-N), also called islet cell antigen 512 (ICA512) or PTP IA-2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. PTPRN is located in secretory granules of neuroendocrine cells and is involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. It is a major autoantigen in type 1 diabetes and is involved in the regulation of insulin secretion.


Pssm-ID: 350457 [Multi-domain]  Cd Length: 281  Bit Score: 177.92  E-value: 1.08e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  467 LAEFQSIPRVFSKfpikdARKSQNQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGfKEPR--KYIAAQGPRDE 544
Cdd:cd14609     24 LCAYQAEPNTCST-----AQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIE-HDPRmpAYIATQGPLSH 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  545 TVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPcmEEGTRTFRDVVVT-INDHKRCPDYIIQKLSIAHKKEKATgRE 623
Cdd:cd14609     98 TIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWP--DEGSSLYHIYEVNlVSEHIWCEDFLVRSFYLKNVQTQET-RT 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  624 VTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLeAEG--KVDVYGYVVNL 701
Cdd:cd14609    175 LTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRM-AKGvkEIDIAATLEHV 253

                          250       260
                   ....*....|....*....|...
gi 1958671442  702 RRQRCLMVQVEAQYILIHQALVE 724
Cdd:cd14609    254 RDQRPGMVRTKDQFEFALTAVAE 276
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 448-722 2.27e-49

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 178.30  E-value: 2.27e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  448 SDLLLETYKRKIADEGRLFLAEFQSIPrvfSKFPIKDARKSQNQNKNRYVDILPYDYNRVELSE---------------- 511
Cdd:PHA02746    12 FDFFDKTNHAKFCEFVLLEHAEVMDIP---IRGTTNHFLKKENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkk 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  512 ---INGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRnKCAEYWPCMEEGTRT 588
Cdd:PHA02746    89 ievTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDDDE-KCFELWTKEEDSELA 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  589 FRDVVVTINDHKRCPDYIIQKLSIAHKKEKaTGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA----------FSNFF 658
Cdd:PHA02746   168 FGRFVAKILDIIEELSFTKTRLMITDKISD-TSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEeqaelikqadNDPQT 246

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958671442  659 SGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQAL 722
Cdd:PHA02746   247 LGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 781-1034 4.12e-49

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: 174.63  E-value: 4.12e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  781 NKKKNRSSNVVPYDFNRVPLKhelemskeseaesdessdeDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFW 860
Cdd:cd14554      6 NKFKNRLVNILPYESTRVCLQ-------------------PIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFW 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  861 QMIFQRKVKVIVMLTELMSGDQEVCAQYW-GEGKQTYGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWK 939
Cdd:cd14554     67 RMLWEHNSTIIVMLTKLREMGREKCHQYWpAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWP 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  940 GEELPAEPKDLVTLIQNIKQKLPKSGSEGmkyhkhaSILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKA 1019
Cdd:cd14554    147 EQGVPKSGEGFIDFIGQVHKTKEQFGQEG-------PITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQ 219

                          250
                   ....*....|....*
gi 1958671442 1020 RPGMVGSFEQYQFLY 1034
Cdd:cd14554    220 RPAMVQTEDQYQFCY 234
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 520-725 1.53e-48

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: 171.73  E-value: 1.53e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  520 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPcmEEGTRTFRDVVVTINDH 599
Cdd:cd14622      2 YINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWP--SEGSVTHGEITIEIKND 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  600 KRCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDHGVPEDPH----LLLKLRRRVNAFSNffsGPIVVHCSAGVGRTGT 675
Cdd:cd14622     80 TLLETISIRDFLVTYNQEKQT-RLVRQFHFHGWPEIGIPAEGKgmidLIAAVQKQQQQTGN---HPIVVHCSAGAGRTGT 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958671442  676 YIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVEY 725
Cdd:cd14622    156 FIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 779-1035 2.01e-48

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: 172.58  E-value: 2.01e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  779 EENKKKNRSSNVVPYDFNRVPLKhelemskeseaesdessdeDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGD 858
Cdd:cd14553      1 EVNKPKNRYANVIAYDHSRVILQ-------------------PIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGD 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  859 FWQMIFQRKVKVIVMLTELMSGDQEVCAQYW-GEGKQTYGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTT 937
Cdd:cd14553     62 FWRMVWEQRSATIVMMTKLEERSRVKCDQYWpTRGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTA 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  938 WKGEELPAEPKDLVTLIQNIKQ-KLPKSGsegmkyhkhaSILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSL 1016
Cdd:cd14553    142 WPDHGVPEHPTPFLAFLRRVKAcNPPDAG----------PIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCL 211

                          250
                   ....*....|....*....
gi 1958671442 1017 RKARPGMVGSFEQYQFLYD 1035
Cdd:cd14553    212 RAQRNYMVQTEDQYIFIHD 230
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 830-1035 2.40e-48

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: 170.99  E-value: 2.40e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  830 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW-GEGKQTYGDMEVMLKDTNK 908
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWpKEGTETYGNIQVTLLSTEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  909 SSAYILRAFELRHSK------RKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNikqklpksgSEGMKYHKHASILVHCR 982
Cdd:cd14549     81 LATYTVRTFSLKNLKlkkvkgRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRK---------SSAANPPGAGPIVVHCS 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958671442  983 DGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYD 1035
Cdd:cd14549    152 AGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 520-719 8.61e-48

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis thaliana protein tyrosine phosphatase 1 (AtPTP1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. AtPTP1 dephosphorylates and inhibits MAP kinase 6 (MPK6) in non-oxidative stress conditions. Together with MAP kinase phosphatase 1 (MKP1) it expresses salicylic acid (SA) and camalexin biosynthesis, and therefore, modulating defense response.


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 169.57  E-value: 8.61e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  520 YINASYI--DGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNR-NKCAEYWPCMEEGTRTFRDVVVTI 596
Cdd:cd17658      1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPAEENESREFGRISVTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  597 NDHKrCPDYIIQK--LSIAHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFsGPIVVHCSAGVGRTG 674
Cdd:cd17658     81 KKLK-HSQHSITLrvLEVQYIESEEPPLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGIPPSA-GPIVVHCSAGIGRTG 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958671442  675 TYIGIDAMLE-----SLEAegkVDVYGYVVNLRRQRCLMVQVEAQYILIH 719
Cdd:cd17658    159 AYCTIHNTIRrilegDMSA---VDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 478-714 1.47e-47

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein phosphatase non-receptor type 2 (PTPN2), also called T-cell protein-tyrosine phosphatase (TCPTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN2, a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner. It is deleted in 6% of all T-cell acute lymphoblastic leukemias and is associated with constitutive JAK1/STAT5 signaling and tumorigenesis.


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 170.53  E-value: 1.47e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  478 SKFPIKDARKSQNQNKNRYVDILPYDYNRVELSEINGDagstYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQK 557
Cdd:cd14607     12 HDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTEND----YINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQK 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  558 ATVIVMVTRCEEGNRNKCAEYWPCMEEGTRTFRDV--VVTINDHKRCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDH 635
Cdd:cd14607     88 TKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKETgfSVKLLSEDVKSYYTVHLLQLENINSGET-RTISHFHYTTWPDF 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  636 GVPEDP----HLLLKLRRrvNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEG--KVDVYGYVVNLRRQRCLMV 709
Cdd:cd14607    167 GVPESPasflNFLFKVRE--SGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGLI 244


                   ....*
gi 1958671442  710 QVEAQ 714
Cdd:cd14607    245 QTPDQ 249
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 520-724 6.06e-47

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: 167.23  E-value: 6.06e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  520 YINASYID---GFKEpRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCMEEGTRTFRDVVVTI 596
Cdd:cd14596      1 YINASYITmpvGEEE-LFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  597 NDHKRCPDYIIQKLSIAhKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNffSGPIVVHCSAGVGRTGTY 676
Cdd:cd14596     80 ENYQALQYFIIRIIKLV-EKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHN--TGPIVVHCSAGIGRAGVL 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1958671442  677 IGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 724
Cdd:cd14596    157 ICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLE 204
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 785-1037 8.93e-47

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: 167.76  E-value: 8.93e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  785 NRSSNVVPYDFNRVPLKhelemskeseaesdessdeDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIF 864
Cdd:cd14619      1 NRFRNVLPYDWSRVPLK-------------------PIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIW 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  865 QRKVKVIVMLTELMSGDQEVCAQYWGEGKQ--TYGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEE 942
Cdd:cd14619     62 EQQSSTIVMLTNCMEAGRVKCEHYWPLDYTpcTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHG 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  943 LPAEPKDLVTLIQNIKQKLPKSGSEGmkyhkhaSILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPG 1022
Cdd:cd14619    142 VPSSTDTLLAFRRLLRQWLDQTMSGG-------PTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPL 214

                          250
                   ....*....|....*
gi 1958671442 1023 MVGSFEQYQFLYDIM 1037
Cdd:cd14619    215 MVQTESQYVFLHQCI 229
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 731-1034 1.10e-45

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


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 166.45  E-value: 1.10e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  731 TEVNLSELHSCLQNLKKRDPPSDPSPLEAEYQRLPSYRSWRTQHI-GNQEENKKKNRSSNVVPYDFNRVPLKhelemske 809
Cdd:cd14627      2 TEVPARNLYSYIQKLAQVEVGEHVTGMELEFKRLANSKAHTSRFIsANLPCNKFKNRLVNIMPYETTRVCLQ-------- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  810 seaesdessdeDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW 889
Cdd:cd14627     74 -----------PIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYW 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  890 -GEGKQTYGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSEG 968
Cdd:cd14627    143 pAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDG 222

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958671442  969 mkyhkhaSILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLY 1034
Cdd:cd14627    223 -------PISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCY 281
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 482-719 1.10e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 167.10  E-value: 1.10e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  482 IKDARKSQNQNKNRYVDILPYDYNRVELsEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVI 561
Cdd:PHA02747    43 IANFEKPENQPKNRYWDIPCWDHNRVIL-DSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSII 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  562 VMVTRCEEGN-RNKCAEYWPCMEEGTRTFRDVVV-TINDHKRcPDYIIQKLSIAHKKEKaTGREVTHIQFTSWPDHGVPE 639
Cdd:PHA02747   122 VMLTPTKGTNgEEKCYQYWCLNEDGNIDMEDFRIeTLKTSVR-AKYILTLIEITDKILK-DSRKISHFQCSEWFEDETPS 199

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  640 DPHLLLKL-----RRRVNAFSNFFS-----GPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMV 709
Cdd:PHA02747   200 DHPDFIKFikiidINRKKSGKLFNPkdallCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGI 279

                          250
                   ....*....|
gi 1958671442  710 QVEAQYILIH 719
Cdd:PHA02747   280 MNFDDYLFIQ 289
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 731-1034 1.21e-45

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: 166.45  E-value: 1.21e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  731 TEVNLSELHSCLQNLKKRDPPSDPSPLEAEYQRLPSYRSWRTQHI-GNQEENKKKNRSSNVVPYDFNRVPLKhelemske 809
Cdd:cd14628      1 TEVPARNLYAYIQKLTQIETGENVTGMELEFKRLASSKAHTSRFIsANLPCNKFKNRLVNIMPYESTRVCLQ-------- 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  810 seaesdessdeDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW 889
Cdd:cd14628     73 -----------PIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYW 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  890 -GEGKQTYGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSEG 968
Cdd:cd14628    142 pAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDG 221

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958671442  969 mkyhkhaSILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLY 1034
Cdd:cd14628    222 -------PISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCY 280
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 781-1034 1.36e-45

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: 165.62  E-value: 1.36e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  781 NKKKNRSSNVVPYDFNRVPLKHELEmskeseaesdessdedsdsEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFW 860
Cdd:cd14543     29 NQEKNRYGDVLCLDQSRVKLPKRNG-------------------DERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFW 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  861 QMIFQRKVKVIVMLTELMSGDQEVCAQYW---GEGKQTYGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTT 937
Cdd:cd14543     90 RMVWEQKVLVIVMTTRVVERGRVKCGQYWpleEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESRQVTHFQFTS 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  938 WKGEELPAEPKDLVTLIQNIKQKLPKSGSE-GMKYHKHAS---ILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVV 1013
Cdd:cd14543    170 WPDFGVPSSAAALLDFLGEVRQQQALAVKAmGDRWKGHPPgppIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTV 249

                          250       260
                   ....*....|....*....|.
gi 1958671442 1014 KSLRKARPGMVGSFEQYQFLY 1034
Cdd:cd14543    250 RRMRTQRAFSIQTPDQYYFCY 270
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 830-1035 1.25e-44

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: 160.27  E-value: 1.25e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  830 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEvCAQYWGE-GKQTYGDMEVMLKDTNK 908
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQS-CPQYWPDeGSGTYGPIQVEFVSTTI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  909 SSAYILRAFELRHSKRKEP--RTVYQYQCTTW-KGEELPAEPKDLVTLIQNIKQKLPKSGSEgmkyhkhaSILVHCRDGS 985
Cdd:cd14556     80 DEDVISRIFRLQNTTRPQEgyRMVQQFQFLGWpRDRDTPPSKRALLKLLSEVEKWQEQSGEG--------PIVVHCLNGV 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958671442  986 QQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYD 1035
Cdd:cd14556    152 GRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 731-1034 1.84e-44

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350477 [Multi-domain]  Cd Length: 291  Bit Score: 162.97  E-value: 1.84e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  731 TEVNLSELHSCLQNLKKRDPPSDPSPLEAEYQRLPSYRSWRTQHI-GNQEENKKKNRSSNVVPYDFNRVPLKhelemske 809
Cdd:cd14629      2 TEVPARNLYAHIQKLTQVPPGESVTAMELEFKLLANSKAHTSRFIsANLPCNKFKNRLVNIMPYELTRVCLQ-------- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  810 seaesdessdeDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW 889
Cdd:cd14629     74 -----------PIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYW 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  890 -GEGKQTYGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSEG 968
Cdd:cd14629    143 pAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEQFGQDG 222

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958671442  969 mkyhkhaSILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLY 1034
Cdd:cd14629    223 -------PITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCY 281
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 785-1033 3.14e-44

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: 159.98  E-value: 3.14e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  785 NRSSNVVPYDFNRVPLKHElemskeseaesdessdedsdSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIF 864
Cdd:cd14615      1 NRYNNVLPYDISRVKLSVQ--------------------SHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVW 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  865 QRKVKVIVMLTELMSGDQEVCAQYW-GEGKQTYGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEEL 943
Cdd:cd14615     61 EKNVYAIVMLTKCVEQGRTKCEEYWpSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGV 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  944 PaEPKDLVTLIQNIKQklpksgsEGMKYH-KHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPG 1022
Cdd:cd14615    141 P-ETTDLLINFRHLVR-------EYMKQNpPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPL 212

                          250
                   ....*....|.
gi 1958671442 1023 MVGSFEQYQFL 1033
Cdd:cd14615    213 MVQTEDQYVFL 223
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 779-1035 5.56e-44

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: 159.81  E-value: 5.56e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  779 EENKKKNRSSNVVPYDFNRVPLKhelemskeseaesdessdeDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGD 858
Cdd:cd14630      1 DENRNKNRYGNIISYDHSRVRLQ-------------------LLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKD 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  859 FWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGEGKQTYGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTW 938
Cdd:cd14630     62 FWRMIWQENSASVVMVTNLVEVGRVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSW 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  939 KGEELPAEPKDLVTLIQNIKQKLPKSGsegmkyhkhASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRK 1018
Cdd:cd14630    142 PDHGVPCYATGLLGFVRQVKFLNPPDA---------GPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRA 212

                          250
                   ....*....|....*..
gi 1958671442 1019 ARPGMVGSFEQYQFLYD 1035
Cdd:cd14630    213 QRVNMVQTEEQYVFVHD 229
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 785-1034 8.16e-44

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: 158.95  E-value: 8.16e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  785 NRSSNVVPYDFNRVPLKHelemskeseaesdessdedSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIF 864
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQ-------------------LGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVW 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  865 QRKVKVIVMLTELMSGDQEVCAQYWGEGKQ--TYGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEE 942
Cdd:cd14618     62 EQQVCNIIMLTVGMENGRVLCDHYWPSESTpvSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHG 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  943 LPAEPKDLVTLIQNIKQKLPKSGSEGmkyhkhaSILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPG 1022
Cdd:cd14618    142 IPESTSSLMAFRELVREHVQATKGKG-------PTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYL 214

                          250
                   ....*....|..
gi 1958671442 1023 MVGSFEQYQFLY 1034
Cdd:cd14618    215 MIQTLSQYIFLH 226
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 520-725 1.03e-43

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: 158.21  E-value: 1.03e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  520 YINASYID---GFKEpRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCM--EEGTRTFRDVVV 594
Cdd:cd14598      1 YINASHIKvtvGGKE-WDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLgsRHNTVTYGRFKI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  595 TINDHKRCPDYIIQKLSIAHkkeKATGREVT--HIQFTSWPDHGVPEDPHLLL-------KLRRRVNAFSNFFSG--PIV 663
Cdd:cd14598     80 TTRFRTDSGCYATTGLKIKH---LLTGQERTvwHLQYTDWPEHGCPEDLKGFLsyleeiqSVRRHTNSTIDPKSPnpPVL 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958671442  664 VHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVEY 725
Cdd:cd14598    157 VHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQF 218
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 520-724 2.07e-43

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: 157.03  E-value: 2.07e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  520 YINASYID----GFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPcMEEGTRTFRDVVVT 595
Cdd:cd14601      2 YINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWP-EPSGSSSYGGFQVT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  596 INDHKRCPDYIIQKLSIAHkKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGT 675
Cdd:cd14601     81 CHSEEGNPAYVFREMTLTN-LEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTGV 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958671442  676 YIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 724
Cdd:cd14601    160 LITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 520-720 2.73e-43

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: 156.39  E-value: 2.73e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  520 YINASYIDGFKE--PRkYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCMEEGTRTFRDVVVTIN 597
Cdd:cd14539      1 YINASLIEDLTPycPR-FIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAITVSLQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  598 DHKRCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSG---PIVVHCSAGVGRTG 674
Cdd:cd14539     80 SVRTTPTHVERIISIQHKDTRLS-RSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSlqtPIVVHCSSGVGRTG 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1958671442  675 TY-IGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQ 720
Cdd:cd14539    159 AFcLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 830-1035 8.49e-43

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: 155.07  E-value: 8.49e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  830 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGEGKQTYGDMEVMLKDTNKS 909
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEVYGDIKVTLVETEPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  910 SAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGsegmkyhkhASILVHCRDGSQQTG 989
Cdd:cd14555     81 AEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSA---------GPIVVHCSAGAGRTG 151

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1958671442  990 LFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYD 1035
Cdd:cd14555    152 CYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHD 197
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 733-1037 3.46e-42

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: 156.02  E-value: 3.46e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  733 VNLSELHSCLQNLKKrdppSDPSPLEAEYQRLPSYRSWRTQHiGNQEENKKKNRSSNVVPYDFNRVPLKhelemskesea 812
Cdd:cd14625      4 IPISELAEHTERLKA----NDNLKLSQEYESIDPGQQFTWEH-SNLEVNKPKNRYANVIAYDHSRVILQ----------- 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  813 esdessdeDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW-GE 891
Cdd:cd14625     68 --------PIEGIMGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWpSR 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  892 GKQTYGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGsegmky 971
Cdd:cd14625    140 GTETYGMIQVTLLDTIELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDA------ 213

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958671442  972 hkhASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIM 1037
Cdd:cd14625    214 ---GPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDAL 276
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 487-725 6.93e-42

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 155.93  E-value: 6.93e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  487 KSQNQNKNRYVDILPYDYNRVELSEINGdaGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTR 566
Cdd:PHA02742    49 ELKNMKKCRYPDAPCFDRNRVILKIEDG--GDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITK 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  567 CEEGNRNKCAEYWPCMEEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKeKATGREVTHIQFTSWPDHGVPEDP----- 641
Cdd:PHA02742   127 IMEDGKEACYPYWMPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTN-TGASLDIKHFAYEDWPHGGLPRDPnkfld 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  642 ------HLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQY 715
Cdd:PHA02742   206 fvlavrEADLKADVDIKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQY 285

                          250
                   ....*....|
gi 1958671442  716 ILIHQALVEY 725
Cdd:PHA02742   286 IFCYFIVLIF 295
PHA02738 PHA02738
hypothetical protein; Provisional
 489-733 7.56e-42

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 156.24  E-value: 7.56e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  489 QNQNKNRYVDILPYDYNRVEL-SEIN-GDagstYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTR 566
Cdd:PHA02738    48 KNRKLNRYLDAVCFDHSRVILpAERNrGD----YINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCK 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  567 CEEGNRNKCAEYWPCMEEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEkATgREVTHIQFTSWPDHGVPEDPHLLLK 646
Cdd:PHA02738   124 KKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDGTS-AT-QTVTHFNFTAWPDHDVPKNTSEFLN 201

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  647 LRRRV---------NAFSN----FFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEA 713
Cdd:PHA02738   202 FVLEVrqcqkelaqESLQIghnrLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPF 281

                          250       260
                   ....*....|....*....|
gi 1958671442  714 QYILIHQALVEYNQFGETEV 733
Cdd:PHA02738   282 QYFFCYRAVKRYVNLTVNKV 301
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 828-1034 4.29e-41

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: 151.01  E-value: 4.29e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  828 SKYINASFVMSY-WKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEvCAQYWGEGK-QTYGDMEVMLKD 905
Cdd:cd14547     25 SSYINANYIRGYdGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKEK-CAQYWPEEEnETYGDFEVTVQS 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  906 TNKSSAYILRAFELRHskRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQkLPKSGSEgmkyhkHASILVHCRDGS 985
Cdd:cd14547    104 VKETDGYTVRKLTLKY--GGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEE-ARQTEPH------RGPIVVHCSAGI 174

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958671442  986 QQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLY 1034
Cdd:cd14547    175 GRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 736-1037 4.80e-41

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: 152.50  E-value: 4.80e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  736 SELHSCLQNLKKrdppSDPSPLEAEYQRLPSYRSWrTQHIGNQEENKKKNRSSNVVPYDFNRVPLkhelemskeseaesd 815
Cdd:cd14626      1 SDLADNIERLKA----NDGLKFSQEYESIDPGQQF-TWENSNLEVNKPKNRYANVIAYDHSRVIL--------------- 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  816 essdEDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW-GEGKQ 894
Cdd:cd14626     61 ----TSVDGVPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWpIRGTE 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  895 TYGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGsegmkyhkh 974
Cdd:cd14626    137 TYGMIQVTLLDTVELATYSVRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDA--------- 207

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958671442  975 ASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIM 1037
Cdd:cd14626    208 GPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEAL 270
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
483-718 5.42e-41

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 152.55  E-value: 5.42e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  483 KDARKSQNQN---KNRYVDILPYDYNRVElseINGdagsTYINASYIDGfKEPRKYIAAQGPRDETVDDFWKMIWEQKAT 559
Cdd:COG5599     32 NDPQYLQNINgspLNRFRDIQPYKETALR---ANL----GYLNANYIQV-IGNHRYIATQYPLEEQLEDFFQMLFDNNTP 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  560 VIVMVTRCEEG--NRNKCAEYWPcmEEGTRTFRDVVVTINDHKRCPDYI---IQKLSIAHKKEKatGREVTHIQFTSWPD 634
Cdd:COG5599    104 VLVVLASDDEIskPKVKMPVYFR--QDGEYGKYEVSSELTESIQLRDGIearTYVLTIKGTGQK--KIEIPVLHVKNWPD 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  635 HGVP--EDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEG--KVDVYGYVVNLRRQR-CLMV 709
Cdd:COG5599    180 HGAIsaEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMV 259


                   ....*....
gi 1958671442  710 QVEAQYILI 718
Cdd:COG5599    260 QTSEQLDVL 268
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 830-1038 6.25e-41

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: 149.90  E-value: 6.25e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  830 YINASFVMSYwKPE--MMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW-GEGKQTYGDMEVML-KD 905
Cdd:cd14546      1 YINASTIYDH-DPRnpAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWpEEGSEVYHIYEVHLvSE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  906 TNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVtliqNIKQKLPKSgsegmkYHKHAS-ILVHCRDG 984
Cdd:cd14546     80 HIWCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLL----EFRRKVNKS------YRGRSCpIVVHCSDG 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958671442  985 SQQTGLFCALFNLLES-AETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIMA 1038
Cdd:cd14546    150 AGRTGTYILIDMVLNRmAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVA 204
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 760-1037 6.30e-41

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: 152.11  E-value: 6.30e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  760 EYQRLPSYRSWRTQHiGNQEENKKKNRSSNVVPYDFNRVPLKhelemskeseaesdessDEDSDSEETSKYINASFVMSY 839
Cdd:cd17667      7 EVQRCTADMNITAEH-SNHPDNKHKNRYINILAYDHSRVKLR-----------------PLPGKDSKHSDYINANYVDGY 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  840 WKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW-GEGKQTYGDMEVMLKDTNKSSAYILRAFE 918
Cdd:cd17667     69 NKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWpTENSEEYGNIIVTLKSTKIHACYTVRRFS 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  919 LRHSK-----------RKEPRTVYQYQCTTWKGEELPAEPKDLVTLI-QNIKQKLPKSGsegmkyhkhaSILVHCRDGSQ 986
Cdd:cd17667    149 IRNTKvkkgqkgnpkgRQNERTVIQYHYTQWPDMGVPEYALPVLTFVrRSSAARTPEMG----------PVLVHCSAGVG 218

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958671442  987 QTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIM 1037
Cdd:cd17667    219 RTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDAL 269
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 778-1035 7.69e-41

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: 151.73  E-value: 7.69e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  778 QEENKKKNRSSNVVPYDFNRVPLKhelemskeseaesdessdeDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIG 857
Cdd:cd14633     37 KDENRMKNRYGNIIAYDHSRVRLQ-------------------PIEGETSSDYINGNYIDGYHRPNHYIATQGPMQETIY 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  858 DFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGEGKQTYGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTT 937
Cdd:cd14633     98 DFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTG 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  938 WKGEELPAEPKDLVTLIQNIKQKLPKSGsegmkyhkhASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLR 1017
Cdd:cd14633    178 WPDHGVPYHATGLLGFVRQVKSKSPPNA---------GPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELR 248

                          250
                   ....*....|....*...
gi 1958671442 1018 KARPGMVGSFEQYQFLYD 1035
Cdd:cd14633    249 SRRVNMVQTEEQYVFIHD 266
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 827-1035 4.06e-40

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: 147.86  E-value: 4.06e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  827 TSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGEGKQTYGDMEVMLKDT 906
Cdd:cd14631     12 SSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEVYGDFKVTCVEM 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  907 NKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGsegmkyhkhASILVHCRDGSQ 986
Cdd:cd14631     92 EPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSA---------GPIVVHCSAGAG 162

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958671442  987 QTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYD 1035
Cdd:cd14631    163 RTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHD 211
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 735-1032 2.71e-39

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: 147.90  E-value: 2.71e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  735 LSELHSCLQNlKKRdppsdpspLEAEYQRLPSYRSW-RTQHIGNQEENKKKNRSSNVVPYDFNRVPLKHElemskeseae 813
Cdd:cd14610      6 LSYMEDHLKN-KNR--------LEKEWEALCAYQAEpNATNVAQREENVQKNRSLAVLPYDHSRIILKAE---------- 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  814 sdessdedsDSEETSKYINASFVMSYwKPE--MMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW-G 890
Cdd:cd14610     67 ---------NSHSHSDYINASPIMDH-DPRnpAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWpD 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  891 EGKQTYGDMEVMLKDTNK-SSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVtliqNIKQKLPKSgsegm 969
Cdd:cd14610    137 EGSNLYHIYEVNLVSEHIwCEDFLVRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLL----DFRRKVNKC----- 207

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958671442  970 kYH-KHASILVHCRDGSQQTGLFCALFNLLES-AETEDVVDVFQVVKSLRKARPGMVGSFEQYQF 1032
Cdd:cd14610    208 -YRgRSCPIIVHCSDGAGRSGTYILIDMVLNKmAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 271
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 830-1035 5.16e-39

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: 144.42  E-value: 5.16e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  830 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGEGKQTYGDMEVMLKDTNKS 909
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDIKITLLKTETL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  910 SAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGsegmkyhkhASILVHCRDGSQQTG 989
Cdd:cd14632     81 AEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDA---------GPVVVHCSAGAGRTG 151

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1958671442  990 LFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYD 1035
Cdd:cd14632    152 CYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHD 197
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 747-1037 6.83e-39

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: 146.80  E-value: 6.83e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  747 KRDPPSDPSPLEAEYQRLPSYRSWRTQHiGNQEENKKKNRSSNVVPYDFNRVPLKhelemskeseaesdessdeDSDSEE 826
Cdd:cd14624     14 ERLKANDNLKFSQEYESIDPGQQFTWEH-SNLEVNKPKNRYANVIAYDHSRVLLS-------------------AIEGIP 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  827 TSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW-GEGKQTYGDMEVMLKD 905
Cdd:cd14624     74 GSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWpSRGTETYGLIQVTLLD 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  906 TNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGsegmkyhkhASILVHCRDGS 985
Cdd:cd14624    154 TVELATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDA---------GPMVVHCSAGV 224

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958671442  986 QQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIM 1037
Cdd:cd14624    225 GRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDAL 276
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 830-1037 6.98e-39

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


Pssm-ID: 350506 [Multi-domain]  Cd Length: 209  Bit Score: 143.97  E-value: 6.98e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  830 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW-GEGKQTYGDMEVMLKDTNK 908
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWpADGSEEYGNFLVTQKSVQV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  909 SSAYILRAFELRHSK--------RKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNikqklpksgSEGMKYHKHASILVH 980
Cdd:cd17668     81 LAYYTVRNFTLRNTKikkgsqkgRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRK---------ASYAKRHAVGPVVVH 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958671442  981 CRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIM 1037
Cdd:cd17668    152 CSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDAL 208
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 830-1034 3.07e-38

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: 141.97  E-value: 3.07e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  830 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW-GEGKQTYGDMEVMLKDTNK 908
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWpDQGCWTYGNLRVRVEDTVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  909 SSAYILRAFELRH----SKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKsgsegmkyhKHASILVHCRDG 984
Cdd:cd14551     81 LVDYTTRKFCIQKvnrgIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPP---------RAGPIVVHCSAG 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958671442  985 SQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLY 1034
Cdd:cd14551    152 VGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 830-1034 6.16e-38

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: 141.12  E-value: 6.16e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  830 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW---GEGKQTYGDMEVMLKDT 906
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWpsmEEGSRAFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  907 NKSSAYILRAFELRHSKRK-EPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIkQKLPKSGSegmkyhkhASILVHCRDGS 985
Cdd:cd14557     81 KICPDYIIRKLNINNKKEKgSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRV-NAFNNFFS--------GPIVVHCSAGV 151

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958671442  986 QQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLY 1034
Cdd:cd14557    152 GRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 781-1034 8.47e-38

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: 142.22  E-value: 8.47e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  781 NKKKNRSSNVVPYDFNRVPLKhelemskeseaesdessdEDSDSEETSKYINASFVMSYW--KPEMM-----IAAQGPLK 853
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILK------------------DRDPNVPGSDYINANYIRNENegPTTDEnaktyIATQGCLE 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  854 ETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW---GEGKQtYGDMEVMLKDTNKSSAYILRAFEL-RHSKRKEPRT 929
Cdd:cd14544     63 NTVSDFWSMVWQENSRVIVMTTKEVERGKNKCVRYWpdeGMQKQ-YGPYRVQNVSEHDTTDYTLRELQVsKLDQGDPIRE 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  930 VYQYQCTTWKGEELPAEPKDLVTLIQNIKQK---LPKSGsegmkyhkhaSILVHCRDGSQQTGLFCALFNLLESAETEDV 1006
Cdd:cd14544    142 IWHYQYLSWPDHGVPSDPGGVLNFLEDVNQRqesLPHAG----------PIVVHCSAGIGRTGTFIVIDMLLDQIKRKGL 211

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1958671442 1007 ---VDVFQVVKSLRKARPGMVGSFEQYQFLY 1034
Cdd:cd14544    212 dcdIDIQKTIQMVRSQRSGMVQTEAQYKFIY 242
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 742-1041 9.57e-38

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: 143.63  E-value: 9.57e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  742 LQNLKKRDPPSDPSPLEAEYQRLPSYRSWRTQHIGNQEENKKKNRSSNVVPYDFNRVPLkhelemskeseaesdessdED 821
Cdd:cd14621     13 LEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHL-------------------TP 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  822 SDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW-GEGKQTYGDME 900
Cdd:cd14621     74 VEGVPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWpDQGCWTYGNIR 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  901 VMLKDTNKSSAYILRAFELRH----SKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGsegmkyhkhAS 976
Cdd:cd14621    154 VSVEDVTVLVDYTVRKFCIQQvgdvTNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYA---------GA 224

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958671442  977 ILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIMASIY 1041
Cdd:cd14621    225 IVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHY 289
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 623-724 1.05e-37

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: 136.72  E-value: 1.05e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442   623 EVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNF--FSGPIVVHCSAGVGRTGTYIGIDAMLESLEAE-GKVDVYGYVV 699
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQseSSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1958671442   700 NLRRQRCLMVQVEAQYILIHQALVE 724
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
623-724 1.05e-37

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 136.72  E-value: 1.05e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442   623 EVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNF--FSGPIVVHCSAGVGRTGTYIGIDAMLESLEAE-GKVDVYGYVV 699
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQseSSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1958671442   700 NLRRQRCLMVQVEAQYILIHQALVE 724
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 779-1037 1.16e-37

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: 141.51  E-value: 1.16e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  779 EENKKKNRSSNVVPYDFNRVPLKHElemskeseaesdessdedsdseetSKYINASFV-MSYWKPEMM-IAAQGPLKETI 856
Cdd:cd14597      1 KENRKKNRYKNILPYDTTRVPLGDE------------------------GGYINASFIkMPVGDEEFVyIACQGPLPTTV 56

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  857 GDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGE--GKQTYGD--MEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQ 932
Cdd:cd14597     57 ADFWQMVWEQKSTVIAMMTQEVEGGKIKCQRYWPEilGKTTMVDnrLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITH 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  933 YQCTTWKGEELPAEPKDLVTLIQNIKQklpksgsegmkYHKHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQV 1012
Cdd:cd14597    137 LNFTAWPDHDTPSQPEQLLTFISYMRH-----------IHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDI 205

                          250       260
                   ....*....|....*....|....*
gi 1958671442 1013 VKSLRKARPGMVGSFEQYQFLYDIM 1037
Cdd:cd14597    206 VRTMRLQRHGMVQTEDQYIFCYQVI 230
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 789-1034 3.14e-37

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: 140.08  E-value: 3.14e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  789 NVVPYDFNRVPLKHelemskeseaesdessdedSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKV 868
Cdd:cd14620      3 NILPYDHSRVILSQ-------------------LDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKS 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  869 KVIVMLTELMSGDQEVCAQYWGE-GKQTYGDMEVMLKDTNKSSAYILRAFELR---HSKRKEPRTVYQYQCTTWKGEELP 944
Cdd:cd14620     64 ATIVMLTNLKERKEEKCYQYWPDqGCWTYGNIRVAVEDCVVLVDYTIRKFCIQpqlPDGCKAPRLVTQLHFTSWPDFGVP 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  945 AEPKDLVTLIQNIKQKLPksgsegmkyhKHAS-ILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGM 1023
Cdd:cd14620    144 FTPIGMLKFLKKVKSVNP----------VHAGpIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQM 213

                          250
                   ....*....|.
gi 1958671442 1024 VGSFEQYQFLY 1034
Cdd:cd14620    214 VQTDMQYSFIY 224
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 781-1034 1.27e-36

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: 138.87  E-value: 1.27e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  781 NKKKNRSSNVVPYDFNRVPL--KHELEmskeseaesdessdedsdseeTSKYINASFVMSYWKPEMMIAAQGPLKETIGD 858
Cdd:cd14614     12 NRCKNRYTNILPYDFSRVKLvsMHEEE---------------------GSDYINANYIPGYNSPQEYIATQGPLPETRND 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  859 FWQMIFQRKVKVIVMLTELMSGDQEVCAQYW--GEGKQTYGDMEVMLKDTNKSSAYILRAFELRHSkrKEPRTVYQYQCT 936
Cdd:cd14614     71 FWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWpfTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYA--DEVQDVMHFNYT 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  937 TWKGEELPA--EPKDLVTLIQNIKQKLPKSgsegmkyhkHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVK 1014
Cdd:cd14614    149 AWPDHGVPTanAAESILQFVQMVRQQAVKS---------KGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVS 219

                          250       260
                   ....*....|....*....|
gi 1958671442 1015 SLRKARPGMVGSFEQYQFLY 1034
Cdd:cd14614    220 EMRSYRMSMVQTEEQYIFIH 239
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 744-1032 1.63e-36

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: 139.79  E-value: 1.63e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  744 NLKKRDPpsdpspLEAEYQRLPSYRSW-RTQHIGNQEENKKKNRSSNVVPYDFNRVPLKHELEmskeseaesdessdeds 822
Cdd:cd14609     10 HLRNRDR------LAKEWQALCAYQAEpNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESN----------------- 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  823 dsEETSKYINASFVMSYwKPEM--MIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW-GEGKQTYGDM 899
Cdd:cd14609     67 --PSRSDYINASPIIEH-DPRMpaYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWpDEGSSLYHIY 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  900 EVMLKDTNK-SSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVtliqNIKQKLPKSgsegmkYH-KHASI 977
Cdd:cd14609    144 EVNLVSEHIwCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLL----DFRRKVNKC------YRgRSCPI 213

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958671442  978 LVHCRDGSQQTGLFCALFNLLES-AETEDVVDVFQVVKSLRKARPGMVGSFEQYQF 1032
Cdd:cd14609    214 IVHCSDGAGRTGTYILIDMVLNRmAKGVKEIDIAATLEHVRDQRPGMVRTKDQFEF 269
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 742-1044 2.12e-36

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: 139.68  E-value: 2.12e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  742 LQNLKKRDPPSDPSpLEAEYQRLPSYRS-WRTQHI-----GNQEENKKKNRSSNVVPYDFNRVPLKHELEmskeseaesd 815
Cdd:cd14604     13 VQAMKSTDHNGEDN-FASDFMRLRRLSTkYRTEKIyptatGEKEENVKKNRYKDILPFDHSRVKLTLKTS---------- 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  816 essdedsdsEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW---GEG 892
Cdd:cd14604     82 ---------SQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWplyGEE 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  893 KQTYGDMEVMLKDTNKSSAYILRAFELRHskRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQklpksgsegMKYH 972
Cdd:cd14604    153 PMTFGPFRISCEAEQARTDYFIRTLLLEF--QNETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRK---------YQEH 221

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958671442  973 KHASILVHCRDGSQQTGLFCAL---FNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIMASIYPTQ 1044
Cdd:cd14604    222 EDVPICIHCSAGCGRTGAICAIdytWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEKQ 296
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 827-1038 4.18e-36

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: 137.27  E-value: 4.18e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  827 TSKYINASFVMSY-WKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGdQEVCAQYWGEGKQTYGDMEVMLKD 905
Cdd:cd14612     43 EGSYINANYIRGYdGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKEK-KEKCVHYWPEKEGTYGRFEIRVQD 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  906 TNKSSAYILRAFELRHSkrKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSEGmkyhkhaSILVHCRDGS 985
Cdd:cd14612    122 MKECDGYTIRDLTIQLE--EESRSVKHYWFSSWPDHQTPESAGPLLRLVAEVEESRQTAASPG-------PIVVHCSAGI 192

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958671442  986 QQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIMA 1038
Cdd:cd14612    193 GRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLHHTLA 245
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 520-720 8.05e-36

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: 134.84  E-value: 8.05e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  520 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNkCAEYWPcmEEGTRTFRDVVVTINDH 599
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQS-CPQYWP--DEGSGTYGPIQVEFVST 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  600 KRCPDYIIQKLSIAHKKEKATG-REVTHIQFTSWPDHG-VPEDPHLLLKLRRRVNA-FSNFFSGPIVVHCSAGVGRTGTY 676
Cdd:cd14556     78 TIDEDVISRIFRLQNTTRPQEGyRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKwQEQSGEGPIVVHCLNGVGRSGVF 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1958671442  677 IGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQ 720
Cdd:cd14556    158 CAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 780-1034 1.23e-35

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: 136.30  E-value: 1.23e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  780 ENKKKNRSSNVVPYDFNRVPLkHELEMSKEseaesdessdedsdseeTSKYINASFVMSYW-------KPEM-MIAAQGP 851
Cdd:cd14605      1 ENKNKNRYKNILPFDHTRVVL-HDGDPNEP-----------------VSDYINANIIMPEFetkcnnsKPKKsYIATQGC 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  852 LKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGE--GKQTYGDMEVMLKDTNKSSAYILRafELRHSKRKE--- 926
Cdd:cd14605     63 LQNTVNDFWRMVFQENSRVIVMTTKEVERGKSKCVKYWPDeyALKEYGVMRVRNVKESAAHDYILR--ELKLSKVGQgnt 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  927 PRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKlpksgSEGMKyhKHASILVHCRDGSQQTGLFCALFNLLESAETEDV 1006
Cdd:cd14605    141 ERTVWQYHFRTWPDHGVPSDPGGVLDFLEEVHHK-----QESIM--DAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGV 213

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1958671442 1007 ---VDVFQVVKSLRKARPGMVGSFEQYQFLY 1034
Cdd:cd14605    214 dcdIDVPKTIQMVRSQRSGMVQTEAQYRFIY 244
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 830-1034 5.92e-35

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: 132.55  E-value: 5.92e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  830 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVML-TELMSGDQEvCAQYW---GEGKQTYGDMEVML-K 904
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMAcREFEMGKKK-CERYWpeeGEEQLQFGPFKISLeK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  905 DTNKSSAYILRAFELRHSkrKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKqKLPKSGSEgmkyhkhaSILVHCRDG 984
Cdd:cd14542     80 EKRVGPDFLIRTLKVTFQ--KESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVR-DYQGSEDV--------PICVHCSAG 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958671442  985 SQQTGLFCAL---FNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLY 1034
Cdd:cd14542    149 CGRTGTICAIdyvWNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 830-1036 9.72e-35

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: 132.11  E-value: 9.72e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  830 YINASFV--------MSYwkpemmIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGEGKQT----YG 897
Cdd:cd14538      1 YINASHIripvggdtYHY------IACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKplicGG 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  898 DMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKqklpksgsegmKYHKHASI 977
Cdd:cd14538     75 RLEVSLEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMR-----------RIHNSGPI 143

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958671442  978 LVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDI 1036
Cdd:cd14538    144 VVHCSAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKA 202
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 772-1041 1.94e-34

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: 133.03  E-value: 1.94e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  772 TQHIGNQEENKKKNRSSNVVPYDFNRV---PLKHELEmskeseaesdessdedsdseetSKYINASFVMSYWKPEMMIAA 848
Cdd:cd14603     21 STVAGGRKENVKKNRYKDILPYDQTRVilsLLQEEGH----------------------SDYINANFIKGVDGSRAYIAT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  849 QGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGEGKQT--YGDMEV-MLKDTNKSSAYILRAfeLRHSKRK 925
Cdd:cd14603     79 QGPLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEPlqTGPFTItLVKEKRLNEEVILRT--LKVTFQK 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  926 EPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQklpKSGSEgmkyhkHASILVHCRDGSQQTGLFCAL---FNLLESAE 1002
Cdd:cd14603    157 ESRSVSHFQYMAWPDHGIPDSPDCMLAMIELARR---LQGSG------PEPLCVHCSAGCGRTGVICTVdyvRQLLLTQR 227

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1958671442 1003 TEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIMASIY 1041
Cdd:cd14603    228 IPPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQMF 266
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 783-1041 2.41e-34

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: 132.68  E-value: 2.41e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  783 KKNRSSNVVPYDFNRVPLKHELEmskeseaesdessdedsdSEETSKYINASFVMSYWKPE-MMIAAQGPLKETIGDFWQ 861
Cdd:cd14613     27 RKNRYKTILPNPHSRVCLTSPDQ------------------DDPLSSYINANYIRGYGGEEkVYIATQGPTVNTVGDFWR 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  862 MIFQRKVKVIVMLTELMSGDqEVCAQYWGEGKQTYGDMEVMLKDTNKSSAYILRAFELRhsKRKEPRTVYQYQCTTWKGE 941
Cdd:cd14613     89 MVWQERSPIIVMITNIEEMN-EKCTEYWPEEQVTYEGIEITVKQVIHADDYRLRLITLK--SGGEERGLKHYWYTSWPDQ 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  942 ELPAEPKDLVTLIQNIKQKLPKSGSegmkyhKHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARP 1021
Cdd:cd14613    166 KTPDNAPPLLQLVQEVEEARQQAEP------NCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRG 239

                          250       260
                   ....*....|....*....|
gi 1958671442 1022 GMVGSFEQYQFLYDIMaSIY 1041
Cdd:cd14613    240 GMIQTCEQYQFVHHVL-SLY 258
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 785-1034 3.15e-34

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: 131.18  E-value: 3.15e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  785 NRSSNVVPYDFNRVPLKHElemskeseaesdessdedsDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIF 864
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIAD-------------------AGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVW 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  865 QRKVKVIVMLTELMSGDQEVCAQYWGEGKQ---TYGDMEVMLKDTNKSSAYILRafELRHSKRKEPRTVYQYQCTTWKGE 941
Cdd:cd14616     62 ETRAKTIVMLTQCFEKGRIRCHQYWPEDNKpvtVFGDIVITKLMEDVQIDWTIR--DLKIERHGDYMMVRQCNFTSWPEH 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  942 ELPAEPKDLVTLIQNIKQKLPksgsegmkyHKHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARP 1021
Cdd:cd14616    140 GVPESSAPLIHFVKLVRASRA---------HDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERM 210

                          250
                   ....*....|...
gi 1958671442 1022 GMVGSFEQYQFLY 1034
Cdd:cd14616    211 CMVQNLAQYIFLH 223
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 773-1034 3.86e-34

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: 132.31  E-value: 3.86e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  773 QHIGNQEENKKKNRSSNVVPYDFNRVPLKhelemskeseaesdessdEDSDSEETSKYINASFVMSYW-----KPEMMIA 847
Cdd:cd14606     10 RLEGQRPENKSKNRYKNILPFDHSRVILQ------------------GRDSNIPGSDYINANYVKNQLlgpdeNAKTYIA 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  848 AQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGE--GKQTYGDMEVMLKDTNKSSAYILRAFELRHSKRK 925
Cdd:cd14606     72 SQGCLEATVNDFWQMAWQENSRVIVMTTREVEKGRNKCVPYWPEvgMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNG 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  926 E-PRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQK---LPKSGsegmkyhkhaSILVHCRDGSQQTGLFCALFNLLESA 1001
Cdd:cd14606    152 ElIREIWHYQYLSWPDHGVPSEPGGVLSFLDQINQRqesLPHAG----------PIIVHCSAGIGRTGTIIVIDMLMENI 221

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1958671442 1002 ETEDV---VDVFQVVKSLRKARPGMVGSFEQYQFLY 1034
Cdd:cd14606    222 STKGLdcdIDIQKTIQMVRAQRSGMVQTEAQYKFIY 257
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 830-1037 5.10e-34

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: 130.27  E-value: 5.10e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  830 YINASFV-MSYWKPEMM-IAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW-----GEGKQTYGDMEVM 902
Cdd:cd14540      1 YINASHItATVGGKQRFyIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWptlggEHDALTFGEYKVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  903 LKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSEGMKYHKHASILVHCR 982
Cdd:cd14540     81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRRHTNQDVAGHNRNPPTLVHCS 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958671442  983 DGSQQTG--LFCALfnLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIM 1037
Cdd:cd14540    161 AGVGRTGvvILADL--MLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVL 215
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 784-1034 1.43e-33

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: 129.43  E-value: 1.43e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  784 KNRSSNVVPYDFNRVPLKHELEmskeseaesdessdedsdseeTSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMI 863
Cdd:cd14545      1 LNRYRDRDPYDHDRSRVKLKQG---------------------DNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMV 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  864 FQRKVKVIVMLTELMSGDQEVCAQYWGEGKQTYGDME-----VMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTW 938
Cdd:cd14545     60 WEQNSKAVIMLNKLMEKGQIKCAQYWPQGEGNAMIFEdtglkVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTW 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  939 KGEELPAEPKDLVTLIQNIKQklpkSGSEGmkyHKHASILVHCRDGSQQTGLFCALFNLLESAETEDV--VDVFQVVKSL 1016
Cdd:cd14545    140 PDFGVPESPAAFLNFLQKVRE----SGSLS---SDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEM 212

                          250
                   ....*....|....*...
gi 1958671442 1017 RKARPGMVGSFEQYQFLY 1034
Cdd:cd14545    213 RKYRMGLIQTPDQLRFSY 230
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 784-1034 1.54e-33

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: 129.27  E-value: 1.54e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  784 KNRSSNVVPYDFNRVPLKHElemskeseaesdessdedSDSEETSKYINASFVMSYW-KPEMMIAAQGPLKETIGDFWQM 862
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPK------------------NSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQM 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  863 IFQRKVKVIVMLTELMSGDqEVCAQYWGEGKQTYGDMEVMLKDTNKSSAYILRAFELRHSKRKepRTVYQYQCTTWKGEE 942
Cdd:cd14611     64 VWQEDSPVIVMITKLKEKN-EKCVLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQS--RSVKHYWYTSWPDHK 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  943 LPAEPKDLVTLIQNIKQKLPKSGSEGmkyhkhaSILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPG 1022
Cdd:cd14611    141 TPDSAQPLLQLMLDVEEDRLASPGRG-------PVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGG 213

                          250
                   ....*....|..
gi 1958671442 1023 MVGSFEQYQFLY 1034
Cdd:cd14611    214 MVQTSEQYEFVH 225
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 830-1035 2.69e-33

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: 127.89  E-value: 2.69e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  830 YINASFV--MSYWKPEMmIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGEGK---QTYGDMEVMLK 904
Cdd:cd14539      1 YINASLIedLTPYCPRF-IATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERgqaLVYGAITVSLQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  905 DTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSEgmkyhkHASILVHCRDG 984
Cdd:cd14539     80 SVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSL------QTPIVVHCSSG 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958671442  985 SQQTGLFCALFN-LLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYD 1035
Cdd:cd14539    154 VGRTGAFCLLYAaVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 780-1033 1.03e-32

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 129.74  E-value: 1.03e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  780 ENKKKNRSSNVVPYDFNRVPLKhelemskeseaesdessdedSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDF 859
Cdd:PHA02747    50 ENQPKNRYWDIPCWDHNRVILD--------------------SGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADF 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  860 WQMIFQRKVKVIVML--TELMSGdQEVCAQYWGEGKQTYGDMEVMLKDTNKSSA---YILRAFELRHSKRKEPRTVYQYQ 934
Cdd:PHA02747   110 WKAVWQEHCSIIVMLtpTKGTNG-EEKCYQYWCLNEDGNIDMEDFRIETLKTSVrakYILTLIEITDKILKDSRKISHFQ 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  935 CTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSE-GMKYHKHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVV 1013
Cdd:PHA02747   189 CSEWFEDETPSDHPDFIKFIKIIDINRKKSGKLfNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTA 268

                          250       260
                   ....*....|....*....|
gi 1958671442 1014 KSLRKARPGMVGSFEQYQFL 1033
Cdd:PHA02747   269 EKIREQRHAGIMNFDDYLFI 288
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 784-1035 1.03e-32

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: 127.26  E-value: 1.03e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  784 KNRSSNVVPYDFNRVPLKhelemskeseaesdessdeDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMI 863
Cdd:cd14602      1 KNRYKDILPYDHSRVELS-------------------LITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMI 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  864 FQRKVKVIVMLTELMSGDQEVCAQYW---GEGKQTYGDMEVMLKDTNKSSAYILRAfeLRHSKRKEPRTVYQYQCTTWKG 940
Cdd:cd14602     62 WEYSVLIIVMACMEFEMGKKKCERYWaepGEMQLEFGPFSVTCEAEKRKSDYIIRT--LKVKFNSETRTIYQFHYKNWPD 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  941 EELPAEPKDLVTLIQNIKQklpksgsegmkYHKHAS--ILVHCRDGSQQTGLFCAL---FNLLESAETEDVVDVFQVVKS 1015
Cdd:cd14602    140 HDVPSSIDPILELIWDVRC-----------YQEDDSvpICIHCSAGCGRTGVICAIdytWMLLKDGIIPENFSVFSLIQE 208

                          250       260
                   ....*....|....*....|
gi 1958671442 1016 LRKARPGMVGSFEQYQFLYD 1035
Cdd:cd14602    209 MRTQRPSLVQTKEQYELVYN 228
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 830-1036 5.48e-32

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: 123.98  E-value: 5.48e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  830 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTE--LMSGdqevCAQYW-GEGKQTYGDMEVMLKDT 906
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEvdLAQG----CPQYWpEEGMLRYGPIQVECMSC 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  907 NKSSAYILRAFELRHSKRKEP--RTVYQYQCTTWKGE-ELPAEPKDLVTLIQNIkQKLPKSGSEGmkyhkHASILVHCRD 983
Cdd:cd14636     77 SMDCDVISRIFRICNLTRPQEgyLMVQQFQYLGWASHrEVPGSKRSFLKLILQV-EKWQEECDEG-----EGRTIIHCLN 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958671442  984 GSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDI 1036
Cdd:cd14636    151 GGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDV 203
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 830-1036 7.00e-32

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: 123.98  E-value: 7.00e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  830 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGdqEVCAQYWGEGKQ-TYGDMEVMLKDTNK 908
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAA--QLCMQYWPEKTScCYGPIQVEFVSADI 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  909 SSAYILRAFELRHSKRKEP--RTVYQYQCTTWKG-EELPAEPKDLVTLIQNI-KQKLPKSGSEGmkyhkhaSILVHCRDG 984
Cdd:cd14634     79 DEDIISRIFRICNMARPQDgyRIVQHLQYIGWPAyRDTPPSKRSILKVVRRLeKWQEQYDGREG-------RTVVHCLNG 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958671442  985 SQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDI 1036
Cdd:cd14634    152 GGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEV 203
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 830-1034 2.00e-31

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: 122.57  E-value: 2.00e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  830 YINASFVM--SYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEV-CAQYW---GEGKQTYGDMEVML 903
Cdd:cd17658      1 YINASLVEtpASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTAkCADYFpaeENESREFGRISVTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  904 KDTNKSSAYI-LRAFELRHSKRKE-PRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGsegmkyhkhaSILVHC 981
Cdd:cd17658     81 KKLKHSQHSItLRVLEVQYIESEEpPLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGIPPSAG----------PIVVHC 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958671442  982 RDGSQQTGLFCALFNLLESAETEDV--VDVFQVVKSLRKARPGMVGSFEQYQFLY 1034
Cdd:cd17658    151 SAGIGRTGAYCTIHNTIRRILEGDMsaVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 830-1036 2.06e-31

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: 122.32  E-value: 2.06e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  830 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTEL-MSGDQEVCAQYWGE-GKQTYGDMEVMLKDTN 907
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLnQSNSAWPCLQYWPEpGLQQYGPMEVEFVSGS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  908 KSSAYILRAFELRHSKR--KEPRTVYQYQCTTWKG-EELPAEPKDLVTLIQNIKQKLPKSGsEGmkyhkhaSILVHCRDG 984
Cdd:cd14637     81 ADEDIVTRLFRVQNITRlqEGHLMVRHFQFLRWSAyRDTPDSKKAFLHLLASVEKWQRESG-EG-------RTVVHCLNG 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958671442  985 SQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDI 1036
Cdd:cd14637    153 GGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEI 204
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 780-1034 4.23e-31

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: 123.15  E-value: 4.23e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  780 ENKKKNRSSNVVPYDFNRVPLKHelemskeseaesdessdedsdseETSKYINASFVMSYWKPEMMIAAQGPLKETIGDF 859
Cdd:cd14607     23 ENRNRNRYRDVSPYDHSRVKLQN-----------------------TENDYINASLVVIEEAQRSYILTQGPLPNTCCHF 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  860 WQMIFQRKVKVIVMLTELMSGDQEVCAQYW---GEGKQTYGD--MEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQ 934
Cdd:cd14607     80 WLMVWQQKTKAVVMLNRIVEKDSVKCAQYWptdEEEVLSFKEtgFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFH 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  935 CTTWKGEELPAEPKDLVtliqNIKQKLPKSGSEGMkyhKHASILVHCRDGSQQTGLFCALFNLLESAETED--VVDVFQV 1012
Cdd:cd14607    160 YTTWPDFGVPESPASFL----NFLFKVRESGSLSP---EHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQV 232

                          250       260
                   ....*....|....*....|..
gi 1958671442 1013 VKSLRKARPGMVGSFEQYQFLY 1034
Cdd:cd14607    233 LLDMRKYRMGLIQTPDQLRFSY 254
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 830-1041 1.55e-30

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: 120.13  E-value: 1.55e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  830 YINASFV-MSYWKPEMM---IAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYW--GEGKQTYGDMEVML 903
Cdd:cd14541      2 YINANYVnMEIPGSGIVnryIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWpdLGETMQFGNLQITC 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  904 KDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKlpksgSEGMKYhkhaSILVHCRD 983
Cdd:cd14541     82 VSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQN-----RVGMVE----PTVVHCSA 152

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958671442  984 GSQQTGLFCAL---FNLLESAETedvVDVFQVVKSLRKARPGMVGSFEQYQFLYDIMASIY 1041
Cdd:cd14541    153 GIGRTGVLITMetaMCLIEANEP---VYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRVY 210
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 830-1034 2.08e-30

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: 119.35  E-value: 2.08e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  830 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTEL-MSGDqevCAQYW-GEGKqtygDME-----VM 902
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNeLNED---EPIYWpTKEK----PLEcetfkVT 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  903 LKDTNKSSA-----YILRAFELRHSKRKEPRTVYQYQCTTWKGEELPaePKDLVTLIQNIkQKLPKSgsegmkyhKHASI 977
Cdd:cd14550     74 LSGEDHSCLsneirLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSP--IHTVFELINTV-QEWAQQ--------RDGPI 142

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958671442  978 LVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLY 1034
Cdd:cd14550    143 VVHDRYGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLY 199
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 775-1034 3.69e-30

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: 121.29  E-value: 3.69e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  775 IGNQEENKKKNRSSNVVPYDFNRVPLKHElemskeseaesdessdedsdseeTSKYINASFVMSYWKPEMMIAAQGPLKE 854
Cdd:cd14608     19 VAKLPKNKNRNRYRDVSPFDHSRIKLHQE-----------------------DNDYINASLIKMEEAQRSYILTQGPLPN 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  855 TIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGEGKqtygDMEVMLKDTN---------KSSAYILRAFELRHSKRK 925
Cdd:cd14608     76 TCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKE----EKEMIFEDTNlkltlisedIKSYYTVRQLELENLTTQ 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  926 EPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQklpkSGSEGmkyHKHASILVHCRDGSQQTGLFC---ALFNLLESAE 1002
Cdd:cd14608    152 ETREILHFHYTTWPDFGVPESPASFLNFLFKVRE----SGSLS---PEHGPVVVHCSAGIGRSGTFCladTCLLLMDKRK 224

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1958671442 1003 TEDVVDVFQVVKSLRKARPGMVGSFEQYQFLY 1034
Cdd:cd14608    225 DPSSVDIKKVLLEMRKFRMGLIQTADQLRFSY 256
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 778-1037 1.00e-29

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 121.29  E-value: 1.00e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  778 QEENKKKNRSSNVVPYDFNRVPLKHELEMSKESEAESDESSDEDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIG 857
Cdd:PHA02746    48 KKENLKKNRFHDIPCWDHSRVVINAHESLKMFDVGDSDGKKIEVTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSE 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  858 DFWQMIFQRKVKVIVMLTELmSGDQEVCAQYWGEGKQ---TYGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQ 934
Cdd:PHA02746   128 DFFKLISEHESQVIVSLTDI-DDDDEKCFELWTKEEDselAFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFW 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  935 CTTWKGEELPAEPKDLVTLIQ--NIKQKLPKSGSEGmKYHKHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQV 1012
Cdd:PHA02746   207 FPDWPDNGIPTGMAEFLELINkvNEEQAELIKQADN-DPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEI 285

                          250       260
                   ....*....|....*....|....*
gi 1958671442 1013 VKSLRKARPGMVGSFEQYQFLYDIM 1037
Cdd:PHA02746   286 VLKIRKQRHSSVFLPEQYAFCYKAL 310
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 785-1034 3.14e-29

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: 116.94  E-value: 3.14e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  785 NRSSNVVPYDFNRVPLKHelemskeseaesdessdedSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIF 864
Cdd:cd14617      1 NRYNNILPYDSTRVKLSN-------------------VDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVW 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  865 QRKVKVIVMLTELMSGDQEVCAQYWGEGKQT--YGDMEVMLKDTNKSSAYILRAFEL-RHSKRKEPRTVYQYQCTTWKGE 941
Cdd:cd14617     62 EQNVHNIVMVTQCVEKGRVKCDHYWPADQDSlyYGDLIVQMLSESVLPEWTIREFKIcSEEQLDAPRLVRHFHYTVWPDH 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  942 ELPAEPKDLVTLIQNIKQKLPKSGSEGMKyhkhasiLVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARP 1021
Cdd:cd14617    142 GVPETTQSLIQFVRTVRDYINRTPGSGPT-------VVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRV 214

                          250
                   ....*....|...
gi 1958671442 1022 GMVGSFEQYQFLY 1034
Cdd:cd14617    215 HMVQTECQYVYLH 227
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 520-706 6.06e-29

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: 115.11  E-value: 6.06e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  520 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEgnRNKCAEYWPCMEE--GTRTFRdVVVTIN 597
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNEL--NEDEPIYWPTKEKplECETFK-VTLSGE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  598 DHK---RCPDYIIQKLSIAHKKEKATgREVTHIQFTSWPDHGVPedPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTG 674
Cdd:cd14550     78 DHSclsNEIRLIVRDFILESTQDDYV-LEVRQFQCPSWPNPCSP--IHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAA 154

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1958671442  675 TYIGIDAMLESLEAEGKVDVYGYVV--NLRRQRC 706
Cdd:cd14550    155 TFCALTTLHQQLEHESSVDVYQVAKlyHLMRPGV 188
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 778-1041 8.28e-29

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: 117.26  E-value: 8.28e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  778 QEENKKKNRSSNVVPYDFNRVPLKHElemskeseaesdessdedsdseetSKYINASFV-MSYWKPEMM---IAAQGPLK 853
Cdd:cd14600     37 LPQNMDKNRYKDVLPYDATRVVLQGN------------------------EDYINASYVnMEIPSANIVnkyIATQGPLP 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  854 ETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGEGKQT--YGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVY 931
Cdd:cd14600     93 HTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVmeYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVT 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  932 QYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSgsegmkyhkhASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQ 1011
Cdd:cd14600    173 HLQYVAWPDHGVPDDSSDFLEFVNYVRSKRVEN----------EPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLD 242

                          250       260       270
                   ....*....|....*....|....*....|
gi 1958671442 1012 VVKSLRKARPGMVGSFEQYQFLYDIMASIY 1041
Cdd:cd14600    243 IVRKMRDQRAMMVQTSSQYKFVCEAILRVY 272
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 760-1037 1.85e-28

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: 116.64  E-value: 1.85e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  760 EYQRLPSYRSWRTQHIGNQEENKKKNRSSNVVPYDFNRVPLKHELEmskeseaesdessdedsdseETSKYINASF--VM 837
Cdd:cd14599     17 EYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKE--------------------NNTGYINASHikVT 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  838 SYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGE-----GKQTYGDMEVMLKDTNKSSAY 912
Cdd:cd14599     77 VGGEEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCY 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  913 ILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIK--QKLPKSGSEGMKyHKHASILVHCRDGSQQTGL 990
Cdd:cd14599    157 ATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQsvRRHTNSMLDSTK-NCNPPIVVHCSAGVGRTGV 235

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1958671442  991 FCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIM 1037
Cdd:cd14599    236 VILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVL 282
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 780-1034 2.43e-28

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 116.64  E-value: 2.43e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  780 ENKKKNRSSNVVPYDFNRVPLKHElemskeseaesdessdedsdsEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDF 859
Cdd:PHA02742    51 KNMKKCRYPDAPCFDRNRVILKIE---------------------DGGDDFINASYVDGHNAKGRFICTQAPLEETALDF 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  860 WQMIFQRKVKVIVMLTELMSGDQEVCAQYWG---EGKQTYGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCT 936
Cdd:PHA02742   110 WQAIFQDQVRVIVMITKIMEDGKEACYPYWMpheRGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYE 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  937 TWKGEELPAEPKDLVTLIQNIKQKLPKS--GSEGMKYHKHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVK 1014
Cdd:PHA02742   190 DWPHGGLPRDPNKFLDFVLAVREADLKAdvDIKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVR 269

                          250       260
                   ....*....|....*....|
gi 1958671442 1015 SLRKARPGMVGSFEQYQFLY 1034
Cdd:PHA02742   270 DLRKQRHNCLSLPQQYIFCY 289
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 830-1037 2.50e-28

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


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 113.55  E-value: 2.50e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  830 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAqYWGEGKQTYG----DMEVMLKD 905
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEPINcetfKVTLIAEE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  906 ---TNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKdlVTLIQNIKQKLPksgsegmkyHKHASILVHCR 982
Cdd:cd17669     80 hkcLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEEAA---------NRDGPMIVHDE 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958671442  983 DGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIM 1037
Cdd:cd17669    149 HGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 830-1037 4.00e-28

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: 112.92  E-value: 4.00e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  830 YINASFVMSYWKPE--MMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGEGKQT---YGDMEVMLK 904
Cdd:cd14596      1 YINASYITMPVGEEelFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEpmeLENYQLRLE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  905 DTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKqklpksgsegmKYHKHASILVHCRDG 984
Cdd:cd14596     81 NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMR-----------KVHNTGPIVVHCSAG 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958671442  985 SQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIM 1037
Cdd:cd14596    150 IGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVV 202
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 830-1036 1.02e-27

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


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 111.70  E-value: 1.02e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  830 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELmsGDQEVCAQYWGE-GKQTYGDMEVMLKDTNK 908
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV--DPAQLCPQYWPEnGVHRHGPIQVEFVSADL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  909 SSAYILRAFELRHSKRKEP--RTVYQYQCTTWKG-EELPAEPKDLVTLIQNI-KQKLPKSGSEGmkyhkhaSILVHCRDG 984
Cdd:cd14635     79 EEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMyRDTPVSKRSFLKLIRQVdKWQEEYNGGEG-------RTVVHCLNG 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958671442  985 SQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDI 1036
Cdd:cd14635    152 GGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEV 203
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
929-1039 1.03e-27

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 108.22  E-value: 1.03e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442   929 TVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSegmkyhkHASILVHCRDGSQQTGLFCALFNLLESAETE-DVV 1007
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSES-------SGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEV 73

                            90       100       110
                    ....*....|....*....|....*....|..
gi 1958671442  1008 DVFQVVKSLRKARPGMVGSFEQYQFLYDIMAS 1039
Cdd:smart00404   74 DIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 929-1039 1.03e-27

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: 108.22  E-value: 1.03e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442   929 TVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSegmkyhkHASILVHCRDGSQQTGLFCALFNLLESAETE-DVV 1007
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSES-------SGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEV 73

                            90       100       110
                    ....*....|....*....|....*....|..
gi 1958671442  1008 DVFQVVKSLRKARPGMVGSFEQYQFLYDIMAS 1039
Cdd:smart00012   74 DIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 830-1039 8.93e-27

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: 109.00  E-value: 8.93e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  830 YINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVML--TELMSGDQEVcaqYWGEGKQTYG--DMEVMLKD 905
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdNQGLAEDEFV---YWPSREESMNceAFTVTLIS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  906 TNK-----SSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEpkDLVTLIQNIKQklpksgsEGMKyhKHASILVH 980
Cdd:cd17670     78 KDRlclsnEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPIS--STFELINVIKE-------EALT--RDGPTIVH 146

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958671442  981 CRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIMAS 1039
Cdd:cd17670    147 DEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAMLS 205
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 830-1041 9.98e-27

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: 109.26  E-value: 9.98e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  830 YINASFV-MSYWKPEMM---IAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGE--GKQTYGDMEVML 903
Cdd:cd14601      2 YINANYInMEIPSSSIInryIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEpsGSSSYGGFQVTC 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  904 KDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKlpksgsegmKYHKHASILVHCRD 983
Cdd:cd14601     82 HSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNK---------RAGKDEPVVVHCSA 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958671442  984 GSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIMASIY 1041
Cdd:cd14601    153 GIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVY 210
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 520-724 1.75e-26

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: 108.18  E-value: 1.75e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  520 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTrcEEGNRNKCAEYWPcmEEGTRTFRDVVVTINDH 599
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLN--EMDAAQLCMQYWP--EKTSCCYGPIQVEFVSA 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  600 KRCPDYIIQKLSIAHKKEKATG-REVTHIQFTSWPDH-GVPEDPHLLLKLRRRVNAFSNFF---SGPIVVHCSAGVGRTG 674
Cdd:cd14634     77 DIDEDIISRIFRICNMARPQDGyRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQYdgrEGRTVVHCLNGGGRSG 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958671442  675 TYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 724
Cdd:cd14634    157 TFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 830-1037 3.65e-25

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: 105.06  E-value: 3.65e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  830 YINASFVM-----SYWKpemMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWG-----EGKQTYGDM 899
Cdd:cd14598      1 YINASHIKvtvggKEWD---YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgsrHNTVTYGRF 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  900 EVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSEGMKYHKHASILV 979
Cdd:cd14598     78 KITTRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTIDPKSPNPPVLV 157

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958671442  980 HCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIM 1037
Cdd:cd14598    158 HCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVL 215
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 520-724 1.93e-23

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: 99.38  E-value: 1.93e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  520 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRnkCAEYWPcmEEGTRTFRDVVVTINDH 599
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQL--CPQYWP--ENGVHRHGPIQVEFVSA 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  600 KRCPDYIIQKLSIAHKKEKATG-REVTHIQFTSWPDH-GVPEDPHLLLKLRRRVNAFSNFF---SGPIVVHCSAGVGRTG 674
Cdd:cd14635     77 DLEEDIISRIFRIYNAARPQDGyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYnggEGRTVVHCLNGGGRSG 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958671442  675 TYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 724
Cdd:cd14635    157 TFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
772-1040 2.06e-23

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 101.71  E-value: 2.06e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  772 TQHIGNQEeNKKKNRSSNVVPYDFNRVplkhelemskeseaesdessdedsdsEETSKYINASFVMSYwKPEMMIAAQGP 851
Cdd:COG5599     34 PQYLQNIN-GSPLNRFRDIQPYKETAL--------------------------RANLGYLNANYIQVI-GNHRYIATQYP 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  852 LKETIGDFWQMIFQRKVKVIVMLT--ELMSGDQEVCAQYWGEgKQTYGDMEVMLKDTNK---SSAYILRAFEL-RHSKRK 925
Cdd:COG5599     86 LEEQLEDFFQMLFDNNTPVLVVLAsdDEISKPKVKMPVYFRQ-DGEYGKYEVSSELTESiqlRDGIEARTYVLtIKGTGQ 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  926 EPRTVYQYQCTTWK-GEELPAEP-KDLVTLIqnIKQKLPKSGSEGmkyhkhaSILVHCRDGSQQTGLFCALFNLLES--A 1001
Cdd:COG5599    165 KKIEIPVLHVKNWPdHGAISAEAlKNLADLI--DKKEKIKDPDKL-------LPVVHCRAGVGRTGTLIACLALSKSinA 235

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1958671442 1002 ETEDVVDVFQVVKSLRKAR-PGMVGSFEQYQFLYDIMASI 1040
Cdd:COG5599    236 LVQITLSVEEIVIDMRTSRnGGMVQTSEQLDVLVKLAEQQ 275
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 520-723 1.96e-22

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: 96.60  E-value: 1.96e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  520 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAeYWPCMEE--GTRTFRdVVVTIN 597
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEpiNCETFK-VTLIAE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  598 DHKrC----PDYIIQKLsIAHKKEKATGREVTHIQFTSWPDhgvPEDP-HLLLKLRRRVNAFSNFFSGPIVVHCSAGVGR 672
Cdd:cd17669     79 EHK-ClsneEKLIIQDF-ILEATQDDYVLEVRHFQCPKWPN---PDSPiSKTFELISIIKEEAANRDGPMIVHDEHGGVT 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958671442  673 TGTYIGIDAMLESLEAEGKVDVYGYV--VNLRRQRcLMVQVEaQYILIHQALV 723
Cdd:cd17669    154 AGTFCALTTLMHQLEKENSVDVYQVAkmINLMRPG-VFTDIE-QYQFLYKAIL 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 520-723 2.71e-21

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: 93.20  E-value: 2.71e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  520 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRcEEGNRNKCAEYWPCMEEGTRTFRDVVVTINDH 599
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD-NQGLAEDEFVYWPSREESMNCEAFTVTLISKD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  600 KRC---PDYIIQKLSIAHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNffSGPIVVHCSAGVGRTGTY 676
Cdd:cd17670     80 RLClsnEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTR--DGPTIVHDEFGAVSAGTL 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958671442  677 IGIDAMLESLEAEGKVDVY--GYVVNLRRQRcLMVQVEaQYILIHQALV 723
Cdd:cd17670    158 CALTTLSQQLENENAVDVYqvAKMINLMRPG-VFTDIE-QYQFLYKAML 204
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 520-724 2.17e-20

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


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 90.47  E-value: 2.17e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  520 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGnrNKCAEYWPcmEEGTRTFRDVVVTINDH 599
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLA--QGCPQYWP--EEGMLRYGPIQVECMSC 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  600 KRCPDYIIQKLSIAHKKEKATGR-EVTHIQFTSWPDH-GVPEDPHLLLKLRRRVNAFS---NFFSGPIVVHCSAGVGRTG 674
Cdd:cd14636     77 SMDCDVISRIFRICNLTRPQEGYlMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQeecDEGEGRTIIHCLNGGGRSG 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958671442  675 TYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 724
Cdd:cd14636    157 MFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
PHA02738 PHA02738
hypothetical protein; Provisional
 757-1037 1.07e-19

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 91.52  E-value: 1.07e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  757 LEAEYQRLPSYRSWRTqhIGNQEENKKKNRSSNVVPYDFNRVPLKHElemskeseaesdessdedsdsEETSKYINASFV 836
Cdd:PHA02738    27 ITREHQKVISEKVDGT--FNAEKKNRKLNRYLDAVCFDHSRVILPAE---------------------RNRGDYINANYV 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  837 MSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGEGKQT---YGDMEVMLKDTNKSSAYI 913
Cdd:PHA02738    84 DGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGsirFGKFKITTTQVETHPHYV 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  914 LRAFELRHSKrKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSEGMKY-HKHAS---ILVHCRDGSQQTG 989
Cdd:PHA02738   164 KSTLLLTDGT-SATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCQKELAQESLQIgHNRLQpppIVVHCNAGLGRTP 242

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1958671442  990 LFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIM 1037
Cdd:PHA02738   243 CYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
CD45 pfam12567
Leukocyte receptor CD45; This family of proteins is found in eukaryotes. Proteins in this ...
 47-103 1.20e-19

Leukocyte receptor CD45; This family of proteins is found in eukaryotes. Proteins in this family are typically between 77 and 1130 amino acids in length. The family is found in association with pfam00041. CD45 plays a critical role in T-cell receptor (TCR)-mediated signaling. CD45 interacts with SKAP55 which is a transcriptional activator of IL-2.


Pssm-ID: 432641  Cd Length: 59  Bit Score: 83.57  E-value: 1.20e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958671442   47 VRYIYDDSSKNFNANLEGDKKPKCEYTDCEK-ELKNLPECSQKNVTLSNGSCT-PDKII 103
Cdd:pfam12567    1 VEYTYNSENKSFTAKLNVNDNVECENNDCENnELHNLQECEQINVSISHNSCTsPNKIL 59
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 484-725 1.14e-17

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 85.02  E-value: 1.14e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  484 DARKSQNQNKNRYVD-ILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIV 562
Cdd:PHA02740    41 EANKACAQAENKAKDeNLALHITRLLHRRIKLFNDEKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIV 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  563 MVTRCEEgnRNKCAEYWPCMEEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKAtgREVTHIQFTSWPDHGVPEDPH 642
Cdd:PHA02740   121 LISRHAD--KKCFNQFWSLKEGCVITSDKFQIETLEIIIKPHFNLTLLSLTDKFGQA--QKISHFQYTAWPADGFSHDPD 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  643 -----------LLLKLRRRvNAFSNFfsGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQV 711
Cdd:PHA02740   197 afidffcniddLCADLEKH-KADGKI--APIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNC 273

                          250
                   ....*....|....
gi 1958671442  712 EAQYILIHQALVEY 725
Cdd:PHA02740   274 LDDYVFCYHLIAAY 287
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 520-724 3.63e-16

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: 78.41  E-value: 3.63e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  520 YINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRN-KCAEYWPcmEEGTRTFRDVVVTIND 598
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWP--EPGLQQYGPMEVEFVS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  599 HKRCPDYIIQKLSIAHKKEKATGR-EVTHIQFTSW-PDHGVPEDPHLLLKLRRRVNAF-SNFFSGPIVVHCSAGVGRTGT 675
Cdd:cd14637     79 GSADEDIVTRLFRVQNITRLQEGHlMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWqRESGEGRTVVHCLNGGGRSGT 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958671442  676 YIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVE 724
Cdd:cd14637    159 YCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 521-715 4.01e-13

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: 70.12  E-value: 4.01e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  521 INASYIDgFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWpcmeegTRTFRDVVVTINDHK 600
Cdd:cd14559     18 LNANRVQ-IGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYF------RQSGTYGSVTVKSKK 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  601 RCPDYIIQKLSIAHKKEKATGREVTH----IQFTSWPDHGvPEDPHLLLKLRRRVN----------------AFSNFFSG 660
Cdd:cd14559     91 TGKDELVDGLKADMYNLKITDGNKTItipvVHVTNWPDHT-AISSEGLKELADLVNksaeekrnfykskgssAINDKNKL 169

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958671442  661 PIVVHCSAGVGRTGTYIGIDAMLESleaEGKVDVYGYVVNLRRQRC-LMVQVEAQY 715
Cdd:cd14559    170 LPVIHCRAGVGRTGQLAAAMELNKS---PNNLSVEDIVSDMRTSRNgKMVQKDEQL 222
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 829-1038 3.79e-10

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 62.29  E-value: 3.79e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  829 KYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELmsGDQEVCAQYWGEGKQ---TYGDMEVMLKD 905
Cdd:PHA02740    77 KVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRH--ADKKCFNQFWSLKEGcviTSDKFQIETLE 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  906 TNKSSAYILRAFELRHSKRKEpRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQ---KLPKSGSEGmkyhKHASILVHCR 982
Cdd:PHA02740   155 IIIKPHFNLTLLSLTDKFGQA-QKISHFQYTAWPADGFSHDPDAFIDFFCNIDDlcaDLEKHKADG----KIAPIIIDCI 229

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958671442  983 DGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIMA 1038
Cdd:PHA02740   230 DGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIA 285
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 210-275 5.54e-09

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 54.42  E-value: 5.54e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958671442  210 HVQCKNSTNSTTLVSWAEPA---SKHHGYILCYKKTPSE---KCENLANDVNSFEVKNLRPYTEYTVSLFAY 275
Cdd:cd00063      6 NLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGdwkEVEVTPGSETSYTLTGLKPGTEYEFRVRAV 77
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 298-378 5.07e-08

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 51.73  E-value: 5.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  298 PGKVNGMKTSRASDNSINVTCNSPYEINGPEARYILEVKSGGS----LVKTFNQSTCKFVVDNLYYSTDYEFLVYFYNGE 373
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSgdwkEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80


                   ....*
gi 1958671442  374 YLGDP 378
Cdd:cd00063     81 GESPP 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 209-275 2.49e-07

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 49.54  E-value: 2.49e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958671442   209 PHVQCKNSTNSTTLVSWAEPASKHH-GYILCYK-----KTPSEKCENLANDVNSFEVKNLRPYTEYTVSLFAY 275
Cdd:smart00060    5 SNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRveyreEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77
fn3 pfam00041
Fibronectin type III domain;
211-275 5.01e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 48.57  E-value: 5.01e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958671442  211 VQCKNSTNSTTLVSWAEPASKH---HGYILCYKKTPSEKCE---NLANDVNSFEVKNLRPYTEYTVSLFAY 275
Cdd:pfam00041    6 LTVTDVTSTSLTVSWTPPPDGNgpiTGYEVEYRPKNSGEPWneiTVPGTTTSVTLTGLKPGTEYEVRVQAV 76
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
632-720 1.21e-05

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 46.12  E-value: 1.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  632 WPDHGVPEDPHL---LLKLRRRVNAfsnffSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEgkvDVYGYVvnlRRQRCLM 708
Cdd:COG2453     55 IPDFGAPDDEQLqeaVDFIDEALRE-----GKKVLVHCRGGIGRTGTVAAAYLVLLGLSAE---EALARV---RAARPGA 123

                           90
                   ....*....|..
gi 1958671442  709 VQVEAQYILIHQ 720
Cdd:COG2453    124 VETPAQRAFLER 135
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 977-1035 4.26e-05

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 44.95  E-value: 4.26e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958671442  977 ILVHCRDGSQQTGLFCALFnLLEsaeTEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYD 1035
Cdd:cd14505    109 VLIHCKGGLGRTGLIAACL-LLE---LGDTLDPEQAIAAVRALRPGAIQTPKQENFLHQ 163
Wzy_O6_O28 NF033860
oligosaccharide repeat unit polymerase; Members of this family are oligosaccharide repeat unit ...
 365-424 3.50e-04

oligosaccharide repeat unit polymerase; Members of this family are oligosaccharide repeat unit polymerases in a subfamily that includes the Wzy proteins for polymerization of the O-antigens O6, O28, O39, O59, and several others.


Pssm-ID: 468211  Cd Length: 384  Bit Score: 44.14  E-value: 3.50e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  365 FLVYFYNGEYLGDpeikPQSTSYNSKALIIFLVFLIIVTSIALLVVLYKIYDLRKKRSSN 424
Cdd:NF033860    18 FIYFIITGELGGD----FSGVEINLSNILLLIILLLILLFFLFLYLLYKLFKKIKVKNKS 73
fn3 pfam00041
Fibronectin type III domain;
299-378 5.73e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 39.71  E-value: 5.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  299 GKVNGMKTSRASDNSINVTCNSPYEINGPEARYILEVKS--GGSLVKTFN--QSTCKFVVDNLYYSTDYEFLVYFYNGEY 374
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPknSGEPWNEITvpGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....
gi 1958671442  375 LGDP 378
Cdd:pfam00041   81 EGPP 84
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 660-686 6.90e-04

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: 40.41  E-value: 6.90e-04
                           10        20
                   ....*....|....*....|....*..
gi 1958671442  660 GPIVVHCSAGVGRTGTYIGIDAMLESL 686
Cdd:cd14494     57 EPVLVHCKAGVGRTGTLVACYLVLLGG 83
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 846-1033 8.27e-04

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: 42.39  E-value: 8.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  846 IAAQGPLKETIGDFWQMIFQRKVKVIVMLTelmSGDQEVCAQ---YWGEGKqTYGDMEVMLKDTNKSSA--------YIL 914
Cdd:cd14559     32 IACQYPKNEQLEDHLKMLADNRTPCLVVLA---SNKDIQRKGlppYFRQSG-TYGSVTVKSKKTGKDELvdglkadmYNL 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  915 RafeLRHSKRKEPRTVYQyqCTTWKG------EELpAEPKDLVTL-IQNIKQKLPKSGSEGMKYHKHASILVHCRDGSQQ 987
Cdd:cd14559    108 K---ITDGNKTITIPVVH--VTNWPDhtaissEGL-KELADLVNKsAEEKRNFYKSKGSSAINDKNKLLPVIHCRAGVGR 181

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1958671442  988 TGLFCALFNLLESaetEDVVDVFQVVKSLRKARPG-MVGSFEQYQFL 1033
Cdd:cd14559    182 TGQLAAAMELNKS---PNNLSVEDIVSDMRTSRNGkMVQKDEQLDTL 225
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 977-1035 9.78e-04

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: 40.03  E-value: 9.78e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958671442  977 ILVHCRDGSQQTGLFCALFNLLESAETedvvdVFQVVKSLRKARPGMVG-SFEQYQFLYD 1035
Cdd:cd14494     59 VLVHCKAGVGRTGTLVACYLVLLGGMS-----AEEAVRIVRLIRPGGIPqTIEQLDFLIK 113
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 660-682 1.04e-03

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


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 41.28  E-value: 1.04e-03
                           10        20
                   ....*....|....*....|...
gi 1958671442  660 GPIVVHCSAGVGRTGTYIGIDAM 682
Cdd:cd14499    110 GAIAVHCKAGLGRTGTLIACYLM 132
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 298-368 1.77e-03

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 38.36  E-value: 1.77e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958671442   298 PGKVNGMKTSRASDNSINVTCNSPYE--INGPEARYILEVKSGGSLVKTFN--QSTCKFVVDNLYYSTDYEFLVY 368
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDdgITGYIVGYRVEYREEGSEWKEVNvtPSSTSYTLTGLKPGTEYEFRVR 75
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
971-1036 4.50e-03

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 38.80  E-value: 4.50e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958671442  971 YHKHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVfqvvksLRKARPGMVGSFEQYQFLYDI 1036
Cdd:COG2453     77 LREGKKVLVHCRGGIGRTGTVAAAYLVLLGLSAEEALAR------VRAARPGAVETPAQRAFLERF 136
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 631-677 4.88e-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: 39.64  E-value: 4.88e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958671442  631 SWPDHGVPEdPHLLLKLRRrVNAFSNFFSGPIVVHCSAGVGRTGTYI 677
Cdd:cd14506     83 GWKDYGVPS-LTTILDIVK-VMAFALQEGGKVAVHCHAGLGRTGVLI 127
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 656-684 7.84e-03

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: 38.03  E-value: 7.84e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1958671442  656 NFFSGPIVVHCSAGVGRTGT----YI-------GIDAMLE 684
Cdd:cd14504     79 NAKNEAVLVHCLAGKGRTGTmlacYLvktgkisAVDAINE 118
 
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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