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Conserved domains on  [gi|1869284269|ref|NP_001372191|]
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protein tyrosine phosphatase type IVA 1 isoform 1 [Homo sapiens]

Protein Classification

PTP-IVa1 domain-containing protein( domain architecture ID 13035233)

PTP-IVa1 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP-IVa1 cd18537
protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), ...
 1-167 2.27e-128

protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), also known as protein-tyrosine phosphatase of regenerating liver 1 (PRL-1), stimulates progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. It may play a role in the development and maintenance of differentiating epithelial tissues. PRL-1 promotes cell growth and migration by activating both the ERK1/2 and RhoA pathways. It is a member of the PTP-IVa/PRL family of small, prenylated phosphatases that are the most oncogenic of all PTPs. PRLs associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation.


:

Pssm-ID: 350513 [Multi-domain]  Cd Length: 167  Bit Score: 356.69  E-value: 2.27e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269   1 MARMNRPAPVEVTYKNMRFLITHNPTNATLNKFIEELKKYGVTTIVRVCEATYDTTLVEKEGIHVLDWPFDDGAPPSNQI 80
Cdd:cd18537     1 MARMNRPAPVEITYKNMRFLITHNPTNATLNKFIEELKKYGVTTVVRVCEATYDTTLVEKEGIQVLDWPFDDGAPPSNQI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  81 VDDWLSLVKIKFREEPGCCIAVHCVAGLGRAPVLVALALIEGGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRF 160
Cdd:cd18537    81 VDDWLNLLKVKFREEPGCCIAVHCVAGLGRAPVLVALALIECGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRF 160


                  ....*..
gi 1869284269 161 KDSNGHR 167
Cdd:cd18537   161 KDSNGHR 167
 
Name Accession Description Interval E-value
PTP-IVa1 cd18537
protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), ...
 1-167 2.27e-128

protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), also known as protein-tyrosine phosphatase of regenerating liver 1 (PRL-1), stimulates progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. It may play a role in the development and maintenance of differentiating epithelial tissues. PRL-1 promotes cell growth and migration by activating both the ERK1/2 and RhoA pathways. It is a member of the PTP-IVa/PRL family of small, prenylated phosphatases that are the most oncogenic of all PTPs. PRLs associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation.


Pssm-ID: 350513 [Multi-domain]  Cd Length: 167  Bit Score: 356.69  E-value: 2.27e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269   1 MARMNRPAPVEVTYKNMRFLITHNPTNATLNKFIEELKKYGVTTIVRVCEATYDTTLVEKEGIHVLDWPFDDGAPPSNQI 80
Cdd:cd18537     1 MARMNRPAPVEITYKNMRFLITHNPTNATLNKFIEELKKYGVTTVVRVCEATYDTTLVEKEGIQVLDWPFDDGAPPSNQI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  81 VDDWLSLVKIKFREEPGCCIAVHCVAGLGRAPVLVALALIEGGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRF 160
Cdd:cd18537    81 VDDWLNLLKVKFREEPGCCIAVHCVAGLGRAPVLVALALIECGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRF 160


                  ....*..
gi 1869284269 161 KDSNGHR 167
Cdd:cd18537   161 KDSNGHR 167
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 11-160 1.36e-71

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 213.35  E-value: 1.36e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  11 EVTYKNMRFLITHNPTNATLNKFIEELKKYGVTTIVRVCEATYDTTLVEKEGIHVLDWPFDDGAPPSNQIVDDWLSLVKI 90
Cdd:PTZ00242   10 QIEYVLFKFLILDAPSPSNLPLYIKELQRYNVTHLVRVCGPTYDAELLEKNGIEVHDWPFDDGAPPPKAVIDNWLRLLDQ 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1869284269  91 KFREE--PGCCIAVHCVAGLGRAPVLVALALIE-GGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRF 160
Cdd:PTZ00242   90 EFAKQstPPETIAVHCVAGLGRAPILVALALVEyGGMEPLDAVGFVREKRKGAINQTQLQFLKKYKPRKKAAG 162
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
35-156 2.88e-20

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 81.56  E-value: 2.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  35 EELKKYGVTTIVRVC-EATYDTTLVEKEGIHVLDWPFDDGAPPSnqiVDDWLSLVK-IKFREEPGCCIAVHCVAGLGRAP 112
Cdd:COG2453    19 ADLKREGIDAVVSLTeEEELLLGLLEEAGLEYLHLPIPDFGAPD---DEQLQEAVDfIDEALREGKKVLVHCRGGIGRTG 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1869284269 113 VLVALALIEGGMKYEDAVQFIRQKRRGAFNSK-QLLYLEKYRPKM 156
Cdd:COG2453    96 TVAAAYLVLLGLSAEEALARVRAARPGAVETPaQRAFLERFAKRL 140
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 64-149 4.44e-11

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: 56.60  E-value: 4.44e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269   64 HVLDWPfDDGAPPSNQIVDDWLSLVKIKFREEPGCC-IAVHCVAGLGRAPVLVALALIEGGMKYE-------DAVQFIRQ 135
Cdd:smart00012   6 HYTGWP-DHGVPESPDSILELLRAVKKNLNQSESSGpVVVHCSAGVGRTGTFVAIDILLQQLEAEagevdifDTVKELRS 84

                           90
                   ....*....|....*
gi 1869284269  136 KRRGAFNSK-QLLYL 149
Cdd:smart00012  85 QRPGMVQTEeQYLFL 99
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
29-149 8.86e-08

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 49.93  E-value: 8.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  29 TLNKFIEELKKYgVTTIVRVCEATYDTTLVEKEgIHVLDWPfDDGAPPSNQIVDDWLSLVKiKFREEPGCC-IAVHCVAG 107
Cdd:pfam00102 104 TLKKEKEDEKDY-TVRTLEVSNGGSEETRTVKH-FHYTGWP-DHGVPESPNSLLDLLRKVR-KSSLDGRSGpIVVHCSAG 179

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1869284269 108 LGRAPVLVALALIEGGMKYE------DAVQFIRQKRRGAFNSK-QLLYL 149
Cdd:pfam00102 180 IGRTGTFIAIDIALQQLEAEgevdifQIVKELRSQRPGMVQTLeQYIFL 228
 
Name Accession Description Interval E-value
PTP-IVa1 cd18537
protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), ...
 1-167 2.27e-128

protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), also known as protein-tyrosine phosphatase of regenerating liver 1 (PRL-1), stimulates progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. It may play a role in the development and maintenance of differentiating epithelial tissues. PRL-1 promotes cell growth and migration by activating both the ERK1/2 and RhoA pathways. It is a member of the PTP-IVa/PRL family of small, prenylated phosphatases that are the most oncogenic of all PTPs. PRLs associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation.


Pssm-ID: 350513 [Multi-domain]  Cd Length: 167  Bit Score: 356.69  E-value: 2.27e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269   1 MARMNRPAPVEVTYKNMRFLITHNPTNATLNKFIEELKKYGVTTIVRVCEATYDTTLVEKEGIHVLDWPFDDGAPPSNQI 80
Cdd:cd18537     1 MARMNRPAPVEITYKNMRFLITHNPTNATLNKFIEELKKYGVTTVVRVCEATYDTTLVEKEGIQVLDWPFDDGAPPSNQI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  81 VDDWLSLVKIKFREEPGCCIAVHCVAGLGRAPVLVALALIEGGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRF 160
Cdd:cd18537    81 VDDWLNLLKVKFREEPGCCIAVHCVAGLGRAPVLVALALIECGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRF 160


                  ....*..
gi 1869284269 161 KDSNGHR 167
Cdd:cd18537   161 KDSNGHR 167
PTP-IVa2 cd18536
protein tyrosine phosphatase type IVA 2; Protein tyrosine phosphatase type IVA 2 (PTP-IVa2), ...
 4-158 2.87e-112

protein tyrosine phosphatase type IVA 2; Protein tyrosine phosphatase type IVA 2 (PTP-IVa2), also known as protein-tyrosine phosphatase of regenerating liver 2 (PRL-2), stimulates progression from G1 into S phase during mitosis and promotes tumors. It regulates tumor cell migration and invasion through an ERK-dependent signaling pathway. Its overexpression correlates with breast tumor formation and progression. PRL-2 is a member of the PTP-IVa/PRL family of small, prenylated phosphatases that are the most oncogenic of all PTPs. PRLs associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation.


Pssm-ID: 350512 [Multi-domain]  Cd Length: 155  Bit Score: 315.79  E-value: 2.87e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269   4 MNRPAPVEVTYKNMRFLITHNPTNATLNKFIEELKKYGVTTIVRVCEATYDTTLVEKEGIHVLDWPFDDGAPPSNQIVDD 83
Cdd:cd18536     1 MNRPAPVEISYENMRFLITHNPTNATLNKFTEELKKYGVTTLVRVCDATYDKAPVEKEGIQVLDWPFDDGAPPPNQIVDD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1869284269  84 WLSLVKIKFREEPGCCIAVHCVAGLGRAPVLVALALIEGGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRL 158
Cdd:cd18536    81 WLNLLKTKFREEPGCCVAVHCVAGLGRAPVLVALALIECGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRL 155
PTP-IVa cd14500
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...
 5-158 4.57e-108

protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), also known as protein-tyrosine phosphatases of regenerating liver (PRLs) constitute a family of small, prenylated phosphatases that are the most oncogenic of all PTPs. They stimulate progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. They associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation. Vertebrates contain three members: PRL-1, PRL-2, and PRL-3.


Pssm-ID: 350350 [Multi-domain]  Cd Length: 156  Bit Score: 304.91  E-value: 4.57e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269   5 NRPAPVEVTYKNMRFLITHNPTNATLNKFIEELKKYGVTTIVRVCEATYDTTLVEKEGIHVLDWPFDDGAPPSNQIVDDW 84
Cdd:cd14500     1 LRPAPTLIEYKGMRFLITDAPTDSNLPLYIKELKKYNVTDLVRVCEPTYDKEPLEKAGIKVHDWPFDDGSPPPDDVVDDW 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1869284269  85 LSLVKIKFREE--PGCCIAVHCVAGLGRAPVLVALALIEGGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRL 158
Cdd:cd14500    81 LDLLKTRFKEEgkPGACIAVHCVAGLGRAPVLVAIALIELGMKPEDAVEFIRKKRRGAINSKQLQFLEKYKPKKKL 156
PTP-IVa3 cd18535
protein tyrosine phosphatase type IVA 3; Protein tyrosine phosphatase type IVA 3 (PTP-IVa3), ...
 5-158 3.28e-103

protein tyrosine phosphatase type IVA 3; Protein tyrosine phosphatase type IVA 3 (PTP-IVa3), also known as protein-tyrosine phosphatase of regenerating liver 3 (PRL-3), stimulates progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. It exerts its oncogenic functions through activation of PI3K/Akt, which is a key regulator of the rapamycin-sensitive mTOR complex 1. PRL-3 is a member of the PTP-IVa/PRL family of small, prenylated phosphatases that are the most oncogenic of all PTPs. PRLs associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation.


Pssm-ID: 350511 [Multi-domain]  Cd Length: 154  Bit Score: 292.70  E-value: 3.28e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269   5 NRPAPVEVTYKNMRFLITHNPTNATLNKFIEELKKYGVTTIVRVCEATYDTTLVEKEGIHVLDWPFDDGAPPSNQIVDDW 84
Cdd:cd18535     1 NRPAPVEVCYKNMRFLITHNPTNATLSTFIEDLKKYGATTVVRVCEVTYDKTPLEKDGITVVDWPFDDGAPPPGKVVEDW 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1869284269  85 LSLVKIKFREEPGCCIAVHCVAGLGRAPVLVALALIEGGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRL 158
Cdd:cd18535    81 LSLLKTKFCEDPGCCVAVHCVAGLGRAPVLVALALIESGMKYEDAIQFIRQKRRGAINSKQLTYLEKYRPKQRL 154
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 11-160 1.36e-71

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 213.35  E-value: 1.36e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  11 EVTYKNMRFLITHNPTNATLNKFIEELKKYGVTTIVRVCEATYDTTLVEKEGIHVLDWPFDDGAPPSNQIVDDWLSLVKI 90
Cdd:PTZ00242   10 QIEYVLFKFLILDAPSPSNLPLYIKELQRYNVTHLVRVCGPTYDAELLEKNGIEVHDWPFDDGAPPPKAVIDNWLRLLDQ 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1869284269  91 KFREE--PGCCIAVHCVAGLGRAPVLVALALIE-GGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRF 160
Cdd:PTZ00242   90 EFAKQstPPETIAVHCVAGLGRAPILVALALVEyGGMEPLDAVGFVREKRKGAINQTQLQFLKKYKPRKKAAG 162
PTZ00393 PTZ00393
protein tyrosine phosphatase; Provisional
 4-155 3.51e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 240399  Cd Length: 241  Bit Score: 148.54  E-value: 3.51e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269   4 MNRPAPVEvtYKNMRFLITHNPTNATLNKFIEELKKYGVTTIVRVCEATYDTTLVEKEGIHVLDWPFDDGAPPSNQIVDD 83
Cdd:PTZ00393   81 LNHPTKIE--HGKIKILILDAPTNDLLPLYIKEMKNYNVTDLVRTCERTYNDGEITSAGINVHELIFPDGDAPTVDIVSN 158

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1869284269  84 WLSLVK--IKFReepgCCIAVHCVAGLGRAPVLVALALIEGGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPK 155
Cdd:PTZ00393  159 WLTIVNnvIKNN----RAVAVHCVAGLGRAPVLASIVLIEFGMDPIDAIVFIRDRRKGAINKRQLQFLKAYKKK 228
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 22-157 2.34e-22

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: 87.89  E-value: 2.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  22 THNPtnatlNKFIEELKKYGVTTIVRVCEATYDTTLVEKEGIHVLDWPFDDGAPPSNQIVDDWLSLVkikfrEEPGCCIA 101
Cdd:cd14499    44 THTP-----EDYIPYFKKLGVTTVVRLNKKLYDAKRFTDAGIRHYDLYFPDGSTPSDDIVKKFLDIC-----ENEKGAIA 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1869284269 102 VHCVAGLGRAPVLVALALI-EGGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMR 157
Cdd:cd14499   114 VHCKAGLGRTGTLIACYLMkHYGFTAREAIAWLRICRPGSVIGPQQQFLEEKEARLW 170
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 17-151 4.50e-21

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: 82.78  E-value: 4.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  17 MRFLITHNPTNaTLNKFIEELKKYGVTTIVRVCEAtydttlvekegihvldwpfddgappsnqIVDDWLSLVKIKfrEEP 96
Cdd:cd14494     7 LRLIAGALPLS-PLEADSRFLKQLGVTTIVDLTLA----------------------------MVDRFLEVLDQA--EKP 55

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1869284269  97 GCCIAVHCVAGLGRAPVLVALALIE-GGMKYEDAVQFIRQKRRG--AFNSKQLLYLEK 151
Cdd:cd14494    56 GEPVLVHCKAGVGRTGTLVACYLVLlGGMSAEEAVRIVRLIRPGgiPQTIEQLDFLIK 113
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
35-156 2.88e-20

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 81.56  E-value: 2.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  35 EELKKYGVTTIVRVC-EATYDTTLVEKEGIHVLDWPFDDGAPPSnqiVDDWLSLVK-IKFREEPGCCIAVHCVAGLGRAP 112
Cdd:COG2453    19 ADLKREGIDAVVSLTeEEELLLGLLEEAGLEYLHLPIPDFGAPD---DEQLQEAVDfIDEALREGKKVLVHCRGGIGRTG 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1869284269 113 VLVALALIEGGMKYEDAVQFIRQKRRGAFNSK-QLLYLEKYRPKM 156
Cdd:COG2453    96 TVAAAYLVLLGLSAEEALARVRAARPGAVETPaQRAFLERFAKRL 140
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 34-149 5.77e-14

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: 65.75  E-value: 5.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  34 IEELKKYGVTTIVRVCE----ATYDT----TLVEKEGIHVLDWPFDDGAPPSNqiVDDWLSLVK-IKFREEPGCCIAVHC 104
Cdd:cd14505    36 LEELKDQGVDDVVTLCTdgelEELGVpdllEQYQQAGITWHHLPIPDGGVPSD--IAQWQELLEeLLSALENGKKVLIHC 113

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1869284269 105 VAGLGRAPVLVA--LALIEGGMKYEDAVQFIRQKRRGAF-NSKQLLYL 149
Cdd:cd14505   114 KGGLGRTGLIAAclLLELGDTLDPEQAIAAVRALRPGAIqTPKQENFL 161
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 25-150 2.31e-12

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: 62.37  E-value: 2.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  25 PTNATLNKF--IEELKKYGVTTIVRVCEA----------------TYDTTLVEKEGIHVLDWPFDD-GAPPSNQIVDdwl 85
Cdd:cd14506    21 PSTELIDKYgiIEQFKEKGIKTVINLQEPgehascgpglepesgfSYLPEAFMRAGIYFYNFGWKDyGVPSLTTILD--- 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1869284269  86 sLVKI-KFREEPGCCIAVHCVAGLGRAPVLVALALIEG-GMKYEDAVQFIRQKRRGAFNSK-QLLYLE 150
Cdd:cd14506    98 -IVKVmAFALQEGGKVAVHCHAGLGRTGVLIACYLVYAlRMSADQAIRLVRSKRPNSIQTRgQVLCVR 164
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 34-137 2.40e-11

dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in typical and atypical dual-specificity phosphatases (DUSPs), which function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). Typical DUSPs, also called mitogen-activated protein kinase (MAPK) phosphatases (MKPs), deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain. Atypical DUSPs contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. Also included in this family are dual specificity phosphatase-like domains of catalytically inactive members such as serine/threonine/tyrosine-interacting protein (STYX) and serine/threonine/tyrosine interacting like 1 (STYXL1), as well as active phosphatases with substrates that are not phosphoproteins such as PTP localized to the mitochondrion 1 (PTPMT1), which is a lipid phosphatase, and laforin, which is a glycogen phosphatase.


Pssm-ID: 350348 [Multi-domain]  Cd Length: 135  Bit Score: 57.94  E-value: 2.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  34 IEELKKYGVTTIVRVCEATYDTTlvEKEGIHVLDWPFDDGapPSNQIVDDWLSLVK-IKFREEPGCCIAVHCVAGLGRAP 112
Cdd:cd14498    19 KELLKKLGITHILNVAGEPPPNK--FPDGIKYLRIPIEDS--PDEDILSHFEEAIEfIEEALKKGGKVLVHCQAGVSRSA 94

                          90       100
                  ....*....|....*....|....*.
gi 1869284269 113 VLVALALI-EGGMKYEDAVQFIRQKR 137
Cdd:cd14498    95 TIVIAYLMkKYGWSLEEALELVKSRR 120
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 64-149 4.44e-11

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: 56.60  E-value: 4.44e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269   64 HVLDWPfDDGAPPSNQIVDDWLSLVKIKFREEPGCC-IAVHCVAGLGRAPVLVALALIEGGMKYE-------DAVQFIRQ 135
Cdd:smart00012   6 HYTGWP-DHGVPESPDSILELLRAVKKNLNQSESSGpVVVHCSAGVGRTGTFVAIDILLQQLEAEagevdifDTVKELRS 84

                           90
                   ....*....|....*
gi 1869284269  136 KRRGAFNSK-QLLYL 149
Cdd:smart00012  85 QRPGMVQTEeQYLFL 99
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
64-149 4.44e-11

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 56.60  E-value: 4.44e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269   64 HVLDWPfDDGAPPSNQIVDDWLSLVKIKFREEPGCC-IAVHCVAGLGRAPVLVALALIEGGMKYE-------DAVQFIRQ 135
Cdd:smart00404   6 HYTGWP-DHGVPESPDSILELLRAVKKNLNQSESSGpVVVHCSAGVGRTGTFVAIDILLQQLEAEagevdifDTVKELRS 84

                           90
                   ....*....|....*
gi 1869284269  136 KRRGAFNSK-QLLYL 149
Cdd:smart00404  85 QRPGMVQTEeQYLFL 99
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 34-139 4.10e-10

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: 54.98  E-value: 4.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  34 IEELKKYGVTTIVRVCEATYDTTLVEKEGIHVLDWPFDDGAPPSNQIVDDWLSLV-KIKFREEPgccIAVHCVAGLGRAP 112
Cdd:cd14504    21 YAYLNENGIRHVVTLTEEPPPEHSDTCPGLRYHHIPIEDYTPPTLEQIDEFLDIVeEANAKNEA---VLVHCLAGKGRTG 97

                          90       100
                  ....*....|....*....|....*...
gi 1869284269 113 VLVALALI-EGGMKYEDAVQFIRQKRRG 139
Cdd:cd14504    98 TMLACYLVkTGKISAVDAINEIRRIRPG 125
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
29-149 8.86e-08

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 49.93  E-value: 8.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  29 TLNKFIEELKKYgVTTIVRVCEATYDTTLVEKEgIHVLDWPfDDGAPPSNQIVDDWLSLVKiKFREEPGCC-IAVHCVAG 107
Cdd:pfam00102 104 TLKKEKEDEKDY-TVRTLEVSNGGSEETRTVKH-FHYTGWP-DHGVPESPNSLLDLLRKVR-KSSLDGRSGpIVVHCSAG 179

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1869284269 108 LGRAPVLVALALIEGGMKYE------DAVQFIRQKRRGAFNSK-QLLYL 149
Cdd:pfam00102 180 IGRTGTFIAIDIALQQLEAEgevdifQIVKELRSQRPGMVQTLeQYIFL 228
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 35-157 3.19e-07

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


Pssm-ID: 350378 [Multi-domain]  Cd Length: 158  Bit Score: 47.37  E-value: 3.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  35 EELKKYGVTTIV----RVCEATYDTTLVEKEGIHVLDWPFDDGAPPSNQiVDDWLSLVKIKFREEPgccIAVHCVAGLGR 110
Cdd:cd14529    27 ALLKKLGIKTVIdlrgADERAASEEAAAKIDGVKYVNLPLSATRPTESD-VQSFLLIMDLKLAPGP---VLIHCKHGKDR 102

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1869284269 111 APVLVALALIE-GGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMR 157
Cdd:cd14529   103 TGLVSALYRIVyGGSKEEANEDYRLSNRHLEGLRSGIALDSKGGVKGR 150
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 63-149 3.70e-07

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: 48.05  E-value: 3.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  63 IHVLDWPfDDGAPPSNQIVDDWLSLVKiKFREEPGCCIAVHCVAGLGRAPVLVALALIEGGMKYE------DAVQFIRQK 136
Cdd:cd00047   107 LHYTGWP-DHGVPSSPEDLLALVRRVR-KEARKPNGPIVVHCSAGVGRTGTFIAIDILLERLEAEgevdvfEIVKALRKQ 184

                          90
                  ....*....|....
gi 1869284269 137 RRGAF-NSKQLLYL 149
Cdd:cd00047   185 RPGMVqTLEQYEFI 198
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 64-156 3.99e-07

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: 48.29  E-value: 3.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  64 HVLDWPfDDGAPPSNQIVDDWLSLVKiKFREEPGCC--IAVHCVAGLGRAPVLVALALIEGGMKYEDAVQFirqkrrgaF 141
Cdd:cd14554   141 QFTDWP-EQGVPKSGEGFIDFIGQVH-KTKEQFGQEgpITVHCSAGVGRTGVFITLSIVLERMRYEGVVDV--------F 210

                          90
                  ....*....|....*
gi 1869284269 142 NSKQLLYLEkyRPKM 156
Cdd:cd14554   211 QTVKLLRTQ--RPAM 223
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
35-137 5.79e-07

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 46.51  E-value: 5.79e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269   35 EELKKYGVTTIVRVCEATYDTTLVEKEGIHVldwPFDDGapPSNQIVDDWLSLVK-IKFREEPGCCIAVHCVAGLGRAPV 113
Cdd:smart00195  20 ALLKKLGITHVINVTNEVPNYNGSDFTYLGV---PIDDN--TETKISPYFPEAVEfIEDAESKGGKVLVHCQAGVSRSAT 94

                           90       100
                   ....*....|....*....|....*
gi 1869284269  114 LVALALIE-GGMKYEDAVQFIRQKR 137
Cdd:smart00195  95 LIIAYLMKtRNMSLNDAYDFVKDRR 119
DUSP3-like cd14515
dual specificity protein phosphatases 3, 13, 26, 27, and similar domains; This family is ...
 30-151 7.61e-07

dual specificity protein phosphatases 3, 13, 26, 27, and similar domains; This family is composed of dual specificity protein phosphatase 3 (DUSP3, also known as VHR), 13B (DUSP13B, also known as TMDP), 26 (DUSP26, also known as MPK8), 13A (DUSP13A, also known as MDSP), dual specificity phosphatase and pro isomerase domain containing 1 (DUPD1), and inactive DUSP27. In general, DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). Members of this family are atypical DUSPs; they contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. Inactive DUSP27 contains a dual specificity phosphatase-like domain with the active site cysteine substituted to serine.


Pssm-ID: 350365 [Multi-domain]  Cd Length: 148  Bit Score: 46.44  E-value: 7.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  30 LNKFieELKKYGVTTIVRVCEAT-----------YDTTLVEKEGIHVLDWPFDDGAP---PSNQIVDDWLSlvkikfreE 95
Cdd:cd14515    17 KNKA--KLKKLGITHVLNAAEGKkngevntnakfYKGSGIIYLGIPASDLPTFDISQyfdEAADFIDKALS--------D 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  96 PGCCIAVHCVAGLGRAPVLV-ALALIEGGMKYEDAVQFIRQKRRGAFNS---KQLLYLEK 151
Cdd:cd14515    87 PGGKVLVHCVEGVSRSATLVlAYLMIYQNMTLEEAIRTVRKKREIRPNRgflQQLCELND 146
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 95-152 1.07e-06

protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or PTP localized to the mitochondrion 1 (PTPMT1), also called phosphoinositide lipid phosphatase (PLIP), phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1, or PTEN-like phosphatase, is a lipid phosphatase or phosphatidylglycerophosphatase (EC 3.1.3.27) which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG). It is targeted to the mitochondrion by an N-terminal signal sequence and is found anchored to the matrix face of the inner membrane. It is essential for the biosynthesis of cardiolipin, a mitochondrial-specific phospholipid regulating the membrane integrity and activities of the organelle. PTPMT1 also plays a crucial role in hematopoietic stem cell (HSC) function, and has been shown to display activity toward phosphoprotein substrates.


Pssm-ID: 350374 [Multi-domain]  Cd Length: 149  Bit Score: 46.10  E-value: 1.07e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  95 EPGCCIAVHCVAGLGRAPVLVALALIE-GGMKYEDAVQFIRQKRRG-AFNSKQLLYLEKY 152
Cdd:cd14524    87 EKGKSVYVHCKAGRGRSATIVACYLIQhKGWSPEEAQEFLRSKRPHiLLRLSQREVLEEF 146
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 68-144 2.99e-06

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: 45.44  E-value: 2.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  68 WPfDDGAPPSNQIVDDWLSLVKIKFREEPgccIAVHCVAGLGRAPVL----VALALIEGGMKYE--DAVQFIRQKRRGAF 141
Cdd:cd14538   115 WP-DHGTPQSADPLLRFIRYMRRIHNSGP---IVVHCSAGIGRTGVLitidVALGLIERDLPFDiqDIVKDLREQRQGMI 190


                  ...
gi 1869284269 142 NSK 144
Cdd:cd14538   191 QTK 193
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
63-149 5.50e-06

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 44.96  E-value: 5.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269   63 IHVLDWPfDDGAPPSNQIVDDWLSLVKiKFREEPGCCIAVHCVAGLGRAPVLVALALIEGGMKYE------DAVQFIRQK 136
Cdd:smart00194 162 YHYTNWP-DHGVPESPESILDLIRAVR-KSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGkevdifEIVKELRSQ 239

                           90
                   ....*....|....
gi 1869284269  137 RRGAFNSK-QLLYL 149
Cdd:smart00194 240 RPGMVQTEeQYIFL 253
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 50-152 7.08e-06

protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; Phosphatase and tensin homolog (PTEN), also phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN or mutated in multiple advanced cancers 1 (MMAC1), is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It is a critical endogenous inhibitor of phosphoinositide signaling. It dephosphorylates phosphoinositide trisphosphate, and therefore, has the function of negatively regulating Akt. The PTEN/PI3K/AKT pathway regulates the signaling of multiple biological processes such as apoptosis, metabolism, cell proliferation, and cell growth. PTEN contains an N-terminal PIP-binding domain, a protein tyrosine phosphatase (PTP)-like catalytic domain, a regulatory C2 domain responsible for its cellular location, a C-tail containing phosphorylation sites, and a C-terminal PDZ domain.


Pssm-ID: 350359 [Multi-domain]  Cd Length: 158  Bit Score: 43.73  E-value: 7.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  50 EATYDTTLVEKEgihVLDWPFDDGAPPSNQI-------VDDWLSlvkikfrEEPGCCIAVHCVAGLGRAPVLVALALIEG 122
Cdd:cd14509    50 ERSYDPSKFNGR---VAEYPFDDHNPPPLELikpfcedVDEWLK-------EDEKNVAAVHCKAGKGRTGVMICCYLLYL 119

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1869284269 123 GM--KYEDAVQFIRQKRrgAFNSK------QLLYLEKY 152
Cdd:cd14509   120 GKfpSAKEALDFYGAKR--TKNKKgvtipsQRRYVYYY 155
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 63-137 7.36e-06

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: 44.55  E-value: 7.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  63 IHVLDWPfDDGAPPSNQIVDDWLSLVKIK--FREEPgccIAVHCVAGLGRAPVLV----ALALIEGGMKYE--DAVQFIR 134
Cdd:cd14601   111 IQYIAWP-DHGVPDDSSDFLDFVCLVRNKraGKDEP---VVVHCSAGIGRTGVLItmetAMCLIECNQPVYplDIVRTMR 186


                  ...
gi 1869284269 135 QKR 137
Cdd:cd14601   187 DQR 189
DUSP14-like cd14514
dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is ...
 35-137 1.07e-05

dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is composed of dual specificity protein phosphatase 14 (DUSP14, also known as MKP-6), 18 (DUSP18), 21 (DUSP21), 28 (DUSP28), and similar proteins. They function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48), and are atypical DUSPs. They contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. DUSP14 directly interacts and dephosphorylates TGF-beta-activated kinase 1 (TAK1)-binding protein 1 (TAB1) in T cells, and negatively regulates TCR signaling and immune responses. DUSP18 has been shown to interact and dephosphorylate SAPK/JNK, and may play a role in regulating the SAPK/JNK pathway. DUSP18 and DUSP21 target to opposing sides of the mitochondrial inner membrane. DUSP28 has been implicated in hepatocellular carcinoma progression and in migratory activity and drug resistance of pancreatic cancer cells.


Pssm-ID: 350364 [Multi-domain]  Cd Length: 133  Bit Score: 42.93  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  35 EELKKYGVTTIVrvcEATYDTTLVEKEGIHVLDWPFDDGapPSNQIvDDWLSLV--KIKFREEPGCCIAVHCVAGLGRAP 112
Cdd:cd14514    19 PLLLSRGITCII---NATTELPDPSYPGIEYLRVPVEDS--PHADL-SPHFDEVadKIHQVKRRGGRTLVHCVAGVSRSA 92

                          90       100       110
                  ....*....|....*....|....*....|
gi 1869284269 113 VLVALALieggMKYE-----DAVQFIRQKR 137
Cdd:cd14514    93 TLCLAYL----MKYEgmtlrEAYKHVKAAR 118
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 37-137 1.48e-05

Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The enzyme's tertiary fold is highly similar to that of tyrosine-specific phosphatases, except for a "recognition" region.


Pssm-ID: 395632 [Multi-domain]  Cd Length: 127  Bit Score: 42.25  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  37 LKKYGVTTIVRVCEATY-DTTLVEKEGIHVLDWPFDDGAPPSNQIVDdwlslvKIKFREEPGCCIAVHCVAGLGRAPVLV 115
Cdd:pfam00782  14 LSKLGITAVINVTREVDlYNSGILYLRIPVEDNHETNISKYLEEAVE------FIDDARQKGGKVLVHCQAGISRSATLI 87

                          90       100
                  ....*....|....*....|...
gi 1869284269 116 ALALIE-GGMKYEDAVQFIRQKR 137
Cdd:pfam00782  88 IAYLMKtRNLSLNEAYSFVKERR 110
PRK12361 PRK12361
hypothetical protein; Provisional
 34-163 1.97e-05

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 43.84  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  34 IEELKKYGVTTIVRV-CE-ATYDTTLVEKEgIHVLDWP-FDDGAPPSNQIVD--DWL-SLVKIKFReepgccIAVHCVAG 107
Cdd:PRK12361  113 LEKLKSNKITAILDVtAEfDGLDWSLTEED-IDYLNIPiLDHSVPTLAQLNQaiNWIhRQVRANKS------VVVHCALG 185

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1869284269 108 LGRAPVLVALALI--EGGMKYEDAVQFIRQKRRGA-FNSKQLLYLEKYRPKMRLRFKDS 163
Cdd:PRK12361  186 RGRSVLVLAAYLLckDPDLTVEEVLQQIKQIRKTArLNKRQLRALEKMLEQGKLNIHKR 244
DSP_MKP_classII cd14566
dual specificity phosphatase domain of class II mitogen-activated protein kinase phosphatase; ...
 9-138 2.33e-05

dual specificity phosphatase domain of class II mitogen-activated protein kinase phosphatase; Mitogen-activated protein kinase (MAPK) phosphatases (MKPs) are eukaryotic dual-specificity phosphatases (DUSPs) that act on MAPKs and function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). They deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. Based on sequence homology, subcellular localization and substrate specificity, 10 MKPs can be subdivided into three subfamilies (class I-III). Class II MKPs consist of DUSP6/MKP-3, DUSP7/MKP-X and DUSP9/MKP-4, and are ERK-selective cytoplasmic MKPs. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350414 [Multi-domain]  Cd Length: 137  Bit Score: 41.92  E-value: 2.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269   9 PVEVTykNMRFLithnpTNATLNKFIEELKKYGVTTIVRVceaTYD--TTLVEKEGIHVLDWPfddgappsnqIVDDW-- 84
Cdd:cd14566     1 PVEIL--PFLYL-----GNAKDSANIDLLKKYNIKYILNV---TPNlpNTFEEDGGFKYLQIP----------IDDHWsq 60

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1869284269  85 -LSLV---KIKFREEP---GCCIAVHCVAGLGRA-PVLVALALIEGGMKYEDAVQFIRQKRR 138
Cdd:cd14566    61 nLSAFfpeAISFIDEArskKCGVLVHCLAGISRSvTVTVAYLMQKLHLSLNDAYDFVKKRKS 122
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 67-156 2.72e-05

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: 43.18  E-value: 2.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  67 DWPfDDGAPPSNQIVDDWLSLVKiKFREEPG--CCIAVHCVAGLGRAPVLVALALIEGGMKYE---DAVQFIRQKR--RG 139
Cdd:cd14628   190 DWP-EQGVPKSGEGFIDFIGQVH-KTKEQFGqdGPISVHCSAGVGRTGVFITLSIVLERMRYEgvvDIFQTVKMLRtqRP 267

                          90
                  ....*....|....*..
gi 1869284269 140 AFNSKQLLYLEKYRPKM 156
Cdd:cd14628   268 AMVQTEDQYQFCYRAAL 284
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 67-134 3.24e-05

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: 42.80  E-value: 3.24e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  67 DWPfDDGAPPSNQIVDDWLSLVKiKFREEPG--CCIAVHCVAGLGRAPVLVALALIEGGMKYEDAVQFIR 134
Cdd:cd14627   191 DWP-EQGVPKSGEGFIDFIGQVH-KTKEQFGqdGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQ 258
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 56-145 4.37e-05

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: 42.04  E-value: 4.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  56 TLVEKEG--------IHVLDWPfDDGAPPSNQIVDDWLSLVKIKFREEPgccIAVHCVAGLGRAPVL----VALALIEGG 123
Cdd:cd14596    94 KLVEKETgenrlikhLQFTTWP-DHGTPQSSDQLVKFICYMRKVHNTGP---IVVHCSAGIGRAGVLicvdVLLSLIEKD 169

                          90       100
                  ....*....|....*....|....
gi 1869284269 124 MKYE--DAVQFIRQKRRGAFNSKQ 145
Cdd:cd14596   170 LSFNikDIVREMRQQRYGMIQTKD 193
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 67-134 1.10e-04

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: 41.25  E-value: 1.10e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  67 DWPfDDGAPPSNQIVDDWLSLVKiKFREEPG--CCIAVHCVAGLGRAPVLVALALIEGGMKYEDAVQFIR 134
Cdd:cd14629   191 DWP-EQGVPKTGEGFIDFIGQVH-KTKEQFGqdGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQ 258
DSP_MKP_classIII cd14568
dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; ...
 97-137 1.52e-04

dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; Mitogen-activated protein kinase (MAPK) phosphatases (MKPs) are eukaryotic dual-specificity phosphatases (DUSPs) that act on MAPKs and function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). They deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. Based on sequence homology, subcellular localization and substrate specificity, 10 MKPs can be subdivided into three subfamilies (class I-III). Class III MKPs consist of DUSP8, DUSP10/MKP-5 and DUSP16/MKP-7, and are JNK/p38-selective phosphatases, which are found in both the cell nucleus and cytoplasm. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350416 [Multi-domain]  Cd Length: 140  Bit Score: 39.71  E-value: 1.52e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1869284269  97 GCCIAVHCVAGLGRAPVL-VALALIEGGMKYEDAVQFIRQKR 137
Cdd:cd14568    79 NKRVLVHCLAGISRSATIaIAYIMKHMRMSLDDAYRFVKEKR 120
DSP_laforin-like cd14526
dual specificity phosphatase domain of laforin and similar domains; This family is composed of ...
 97-137 1.78e-04

dual specificity phosphatase domain of laforin and similar domains; This family is composed of glucan phosphatases including vertebrate dual specificity protein phosphatase laforin, also called lafora PTPase (LAFPTPase), and plant starch excess4 (SEX4). Laforin is a glycogen phosphatase; its gene is mutated in Lafora progressive myoclonus epilepsy or Lafora disease (LD), a fatal autosomal recessive neurodegenerative disorder characterized by the presence of progressive neurological deterioration, myoclonus, and epilepsy. One characteristic of LD is the accumulation of insoluble glucans. Laforin prevents LD by at least two mechanisms: by preventing hyperphosphorylation of glycogen by dephosphorylating it, allowing proper glycogen formation, and by promoting the ubiquitination of proteins involved in glycogen metabolism via its interaction with malin. Laforin contains an N-terminal CBM20 (carbohydrate-binding module, family 20) domain and a C-terminal catalytic dual specificity phosphatase (DSP) domain. Plant SEX4 regulate starch metabolism by selectively dephosphorylating glucose moieties within starch glucan chains. It contains an N-terminal catalytic DSP domain and a C-terminal Early (E) set domain.


Pssm-ID: 350375 [Multi-domain]  Cd Length: 146  Bit Score: 39.87  E-value: 1.78e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1869284269  97 GCCIAVHCVAGLGRAP--VLVALALIEgGMKYEDAVQFIRQKR 137
Cdd:cd14526    94 GGTVYVHCTAGLGRAPatVIAYLYWVL-GYSLDEAYYLLTSKR 135
DSP_STYX cd14522
dual specificity phosphatase-like domain of serine/threonine/tyrosine-interacting protein; ...
 75-137 2.53e-04

dual specificity phosphatase-like domain of serine/threonine/tyrosine-interacting protein; Serine/threonine/tyrosine-interacting protein (STYX), also called protein tyrosine phosphatase-like protein, is a catalytically inactive member of the protein tyrosine phosphatase family that plays an integral role in regulating pathways by competing with active phosphatases for binding to MAPKs. It acts as a nuclear anchor for MAPKs, affecting their nucleocytoplasmic shuttling.


Pssm-ID: 350372 [Multi-domain]  Cd Length: 151  Bit Score: 39.24  E-value: 2.53e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1869284269  75 PPSNQIVDDWLSlvkikfreePGCCIAVHCVAGLGRAPVLVALALIEG-GMKYEDAVQFIRQKR 137
Cdd:cd14522    76 PTVKEFIDDCLQ---------TGGKVLVHGNAGISRSAALVIAYIMETyGLSYRDAFAYVQQRR 130
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 31-117 2.66e-04

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: 40.04  E-value: 2.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  31 NKFIEELKKYGVTTIVRVCEATYDTTLVekegIH--VLDWPfDDGAPPSNQIVDDWLSLVKIKFR------------EEP 96
Cdd:cd14543   135 NLSVENKEHYKKTTLEIHNTETDESRQV----THfqFTSWP-DFGVPSSAAALLDFLGEVRQQQAlavkamgdrwkgHPP 209

                          90       100
                  ....*....|....*....|.
gi 1869284269  97 GCCIAVHCVAGLGRAPVLVAL 117
Cdd:cd14543   210 GPPIVVHCSAGIGRTGTFCTL 230
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 64-145 3.08e-04

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: 39.92  E-value: 3.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  64 HVLDWPfDDGAPPSNQIVDDWLSLVKiKFREEPGCCIAVHCVAGLGRAPVLVAL----ALIEGGMKYED-----AVQFIR 134
Cdd:cd14604   192 HYVNWP-DHDVPSSFDSILDMISLMR-KYQEHEDVPICIHCSAGCGRTGAICAIdytwNLLKAGKIPEEfnvfnLIQEMR 269

                          90
                  ....*....|.
gi 1869284269 135 QKRRGAFNSKQ 145
Cdd:cd14604   270 TQRHSAVQTKE 280
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 32-117 9.15e-04

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: 38.38  E-value: 9.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  32 KFIEELKKYGVTTIVRVCEATYDTTlVEKE--GIHVLDWPfDDGAPPSnqiVDDWLSLVKIK-------FREEPgccIAV 102
Cdd:cd18533    76 ELVSEEENDDGGFIVREFELSKEDG-KVKKvyHIQYKSWP-DFGVPDS---PEDLLTLIKLKrelndsaSLDPP---IIV 147

                          90
                  ....*....|....*
gi 1869284269 103 HCVAGLGRAPVLVAL 117
Cdd:cd18533   148 HCSAGVGRTGTFIAL 162
DUSP13A cd14580
dual specificity protein phosphatase 13 isoform A; Dual specificity protein phosphatase 13 ...
 31-150 9.62e-04

dual specificity protein phosphatase 13 isoform A; Dual specificity protein phosphatase 13 isoform A (DUSP13A), also called branching-enzyme interacting DSP or muscle-restricted DSP (MDSP), 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. DUSP13A 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. DUSP13A also functions as a regulator of apoptosis signal-regulating kinase 1 (ASK1), a MAPK kinase kinase, by interacting with its N-terminal domain and inducing ASK1-mediated apoptosis through the activation of caspase-3. This function is independent of phosphatase activity.


Pssm-ID: 350428 [Multi-domain]  Cd Length: 145  Bit Score: 37.81  E-value: 9.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  31 NKFieELKKYGVTTIV------RVCEATYD--TTLVEKEGIHVLDWPFDDGAP---PSNQIVDDWLSlvkikfreEPGCC 99
Cdd:cd14580    18 NRF--GLWKLGITHVLnaahgkLFCQGGDDfyGTSVDYYGVPANDLPDFDISPyfySAAEFIHRALN--------TPGAK 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1869284269 100 IAVHCVAGLGRAPVLV-ALALIEGGMKYEDAVQFIRQKRRGAFNS---KQLLYLE 150
Cdd:cd14580    88 VLVHCAVGVSRSATLVlAYLMIYHQLSLVQAIKTVKERRWIFPNRgflKQLRKLD 142
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 4-150 9.85e-04

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


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 37.94  E-value: 9.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269   4 MNRPA--PVEVTYKN-----MRFLITHNPtnatlnkfieelKKYgvtTIVRVCEATYDTTlvEKEGIHVLDWPFDDGAPP 76
Cdd:cd14497    12 MSFPAtgYPESLYRNsiddvANFLNTHHP------------DHY---MIFNLSEEEYDDD--SKFEGRVLHYGFPDHHPP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  77 S----NQIVDD---WLSlvkikfrEEPGCCIAVHCVAGLGRAPVLVALALIEGGM--KYEDAVQFIRQKR-----RGAFN 142
Cdd:cd14497    75 PlgllLEIVDDidsWLS-------EDPNNVAVVHCKAGKGRTGTVICAYLLYYGQysTADEALEYFAKKRfkeglPGVTI 147


                  ....*...
gi 1869284269 143 SKQLLYLE 150
Cdd:cd14497   148 PSQLRYLQ 155
DSP_MKP cd14512
dual specificity phosphatase domain of mitogen-activated protein kinase phosphatase; ...
 90-137 1.38e-03

dual specificity phosphatase domain of mitogen-activated protein kinase phosphatase; Mitogen-activated protein kinase (MAPK) phosphatases (MKPs) are eukaryotic dual-specificity phosphatases (DUSPs) that act on MAPKs, which are involved in gene regulation, cell proliferation, programmed cell death and stress responses, as an important feedback control mechanism that limits MAPK cascades. MKPs, also referred to as typical DUSPs, function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). They deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain. Based on sequence homology, subcellular localization and substrate specificity, 10 MKPs can be subdivided into three subfamilies (class I-III).


Pssm-ID: 350362 [Multi-domain]  Cd Length: 136  Bit Score: 37.08  E-value: 1.38e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1869284269  90 IKFREEP---GCCIAVHCVAGLGR-APVLVALALIEGGMKYEDAVQFIRQKR 137
Cdd:cd14512    69 IEFIEEAkasNGGVLVHCLAGISRsATIAIAYLMKRMRMSLDEAYDFVKEKR 120
DUSP26 cd14578
dual specificity protein phosphatase 26; Dual specificity protein phosphatase 26 (DUSP26), ...
 36-151 1.77e-03

dual specificity protein phosphatase 26; Dual specificity protein phosphatase 26 (DUSP26), also called mitogen-activated protein kinase (MAPK) phosphatase 8 (MKP-8) or low-molecular-mass dual-specificity phosphatase 4 (LDP-4), 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. DUSP26 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 a brain phosphatase highly overexpressed in neuroblastoma and has also been identified as a p53 phosphatase, dephosphorylating phospho-Ser20 and phospho-Ser37 in the p53 transactivation domain.


Pssm-ID: 350426 [Multi-domain]  Cd Length: 144  Bit Score: 36.74  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  36 ELKKYGVTTIVRVCEAT-------YDTTLVEKEGIHVLDWPFDDGAP---PSNQIVDDWLSlvkikfreEPGCCIAVHCV 105
Cdd:cd14578    21 ELRRLGITHILNASHSKwrggaeyYEGLNIRYLGIEAHDSPAFDMSIhfyPAADFIHRALS--------QPGGKILVHCA 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1869284269 106 AGLGRAPVLV-ALALIEGGMKYEDAVQFIRQKR-----RGAFnsKQLLYLEK 151
Cdd:cd14578    93 VGVSRSATLVlAYLMIHHHMTLVEAIKTVKDHRgiipnRGFL--RQLLALDR 142
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 64-130 2.12e-03

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: 37.49  E-value: 2.12e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1869284269  64 HVLDWPfDDGAPPSNQIVDDWLSLVKIKFREEP-GCCIAVHCVAGLGRAPVLVALALIEGGMKYEDAV 130
Cdd:cd14615   131 HFTSWP-DHGVPETTDLLINFRHLVREYMKQNPpNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVV 197
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 34-117 2.32e-03

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: 37.19  E-value: 2.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284269  34 IEELK--KYGVTTIVRVCEATydttlvekegihvlDWPfDDGAPPSNQIVDDWLSLVKIKfREEPGCCIAVHCVAGLGRA 111
Cdd:cd14616   114 IRDLKieRHGDYMMVRQCNFT--------------SWP-EHGVPESSAPLIHFVKLVRAS-RAHDNTPMIVHCSAGVGRT 177


                  ....*.
gi 1869284269 112 PVLVAL 117
Cdd:cd14616   178 GVFIAL 183
 
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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