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Conserved domains on  [gi|1869284259|ref|NP_001372197|]
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protein tyrosine phosphatase type IVA 1 isoform 5 [Homo sapiens]

Protein Classification

protein-tyrosine phosphatase family protein( domain architecture ID 1000023)

cys-based protein-tyrosine phosphatase (PTP) family protein may be a PTP or a dual-specificity phosphatase (DUSP or DSP), and may catalyze the dephosphorylation of target phosphoproteins at tyrosine or tyrosine and serine/threonine residues, respectively

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1-154 7.37e-112

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


The actual alignment was detected with superfamily member cd18537:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 167  Bit Score: 314.70  E-value: 7.37e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284259   1 MARMNRPAPVEVTYKNMRFLITHNPTNATLNKFIEELKKYGVTTIVRVCEATYDTTLVEKEGIHVL-------------I 67
Cdd:cd18537     1 MARMNRPAPVEITYKNMRFLITHNPTNATLNKFIEELKKYGVTTVVRVCEATYDTTLVEKEGIQVLdwpfddgappsnqI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284259  68 VDDWLSLVKIKFREEPGCCIAVHCVAGLGRAPVLVALALIEGGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRF 147
Cdd:cd18537    81 VDDWLNLLKVKFREEPGCCIAVHCVAGLGRAPVLVALALIECGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRF 160


                  ....*..
gi 1869284259 148 KDSNGHR 154
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), ...
 1-154 7.37e-112

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: 314.70  E-value: 7.37e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284259   1 MARMNRPAPVEVTYKNMRFLITHNPTNATLNKFIEELKKYGVTTIVRVCEATYDTTLVEKEGIHVL-------------I 67
Cdd:cd18537     1 MARMNRPAPVEITYKNMRFLITHNPTNATLNKFIEELKKYGVTTVVRVCEATYDTTLVEKEGIQVLdwpfddgappsnqI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284259  68 VDDWLSLVKIKFREEPGCCIAVHCVAGLGRAPVLVALALIEGGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRF 147
Cdd:cd18537    81 VDDWLNLLKVKFREEPGCCIAVHCVAGLGRAPVLVALALIECGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRF 160


                  ....*..
gi 1869284259 148 KDSNGHR 154
Cdd:cd18537   161 KDSNGHR 167
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 11-147 1.33e-57

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 177.14  E-value: 1.33e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284259  11 EVTYKNMRFLITHNPTNATLNKFIEELKKYGVTTIVRVCEATYDTTLVEKEGIHV-------------LIVDDWLSLVKI 77
Cdd:PTZ00242   10 QIEYVLFKFLILDAPSPSNLPLYIKELQRYNVTHLVRVCGPTYDAELLEKNGIEVhdwpfddgapppkAVIDNWLRLLDQ 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1869284259  78 KFREE--PGCCIAVHCVAGLGRAPVLVALALIE-GGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRF 147
Cdd:PTZ00242   90 EFAKQstPPETIAVHCVAGLGRAPILVALALVEyGGMEPLDAVGFVREKRKGAINQTQLQFLKKYKPRKKAAG 162
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
35-143 2.92e-16

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 70.77  E-value: 2.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284259  35 EELKKYGVTTIVRVC-EATYDTTLVEKEGI---HVLIVD-------DWLSLVK-IKFREEPGCCIAVHCVAGLGRAPVLV 102
Cdd:COG2453    19 ADLKREGIDAVVSLTeEEELLLGLLEEAGLeylHLPIPDfgapddeQLQEAVDfIDEALREGKKVLVHCRGGIGRTGTVA 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1869284259 103 ALALIEGGMKYEDAVQFIRQKRRGAFNSK-QLLYLEKYRPKM 143
Cdd:COG2453    99 AAYLVLLGLSAEEALARVRAARPGAVETPaQRAFLERFAKRL 140
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
35-124 2.08e-07

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 47.28  E-value: 2.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284259   35 EELKKYGVTTIVRVCEATYDTTLVEKEGIHVLIVDDWLSLV---------KIKFREEPGCCIAVHCVAGLGRAPVLVALA 105
Cdd:smart00195  20 ALLKKLGITHVINVTNEVPNYNGSDFTYLGVPIDDNTETKIspyfpeaveFIEDAESKGGKVLVHCQAGVSRSATLIIAY 99

                           90       100
                   ....*....|....*....|
gi 1869284259  106 LIE-GGMKYEDAVQFIRQKR 124
Cdd:smart00195 100 LMKtRNMSLNDAYDFVKDRR 119
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 37-124 4.26e-06

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: 43.79  E-value: 4.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284259  37 LKKYGVTTIVRvCEATYDTTLVEKEGIHVLIVDD-------WLSLVK--IKFREEPGCCIAVHCVAGLGRAPVLVALALI 107
Cdd:pfam00782  14 LSKLGITAVIN-VTREVDLYNSGILYLRIPVEDNhetniskYLEEAVefIDDARQKGGKVLVHCQAGISRSATLIIAYLM 92

                          90
                  ....*....|....*...
gi 1869284259 108 E-GGMKYEDAVQFIRQKR 124
Cdd:pfam00782  93 KtRNLSLNEAYSFVKERR 110
 
Name Accession Description Interval E-value
PTP-IVa1 cd18537
protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), ...
 1-154 7.37e-112

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: 314.70  E-value: 7.37e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284259   1 MARMNRPAPVEVTYKNMRFLITHNPTNATLNKFIEELKKYGVTTIVRVCEATYDTTLVEKEGIHVL-------------I 67
Cdd:cd18537     1 MARMNRPAPVEITYKNMRFLITHNPTNATLNKFIEELKKYGVTTVVRVCEATYDTTLVEKEGIQVLdwpfddgappsnqI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284259  68 VDDWLSLVKIKFREEPGCCIAVHCVAGLGRAPVLVALALIEGGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRF 147
Cdd:cd18537    81 VDDWLNLLKVKFREEPGCCIAVHCVAGLGRAPVLVALALIECGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRF 160


                  ....*..
gi 1869284259 148 KDSNGHR 154
Cdd:cd18537   161 KDSNGHR 167
PTP-IVa2 cd18536
protein tyrosine phosphatase type IVA 2; Protein tyrosine phosphatase type IVA 2 (PTP-IVa2), ...
 4-145 6.04e-97

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: 276.50  E-value: 6.04e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284259   4 MNRPAPVEVTYKNMRFLITHNPTNATLNKFIEELKKYGVTTIVRVCEATYDTTLVEKEGIHVL-------------IVDD 70
Cdd:cd18536     1 MNRPAPVEISYENMRFLITHNPTNATLNKFTEELKKYGVTTLVRVCDATYDKAPVEKEGIQVLdwpfddgapppnqIVDD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1869284259  71 WLSLVKIKFREEPGCCIAVHCVAGLGRAPVLVALALIEGGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRL 145
Cdd:cd18536    81 WLNLLKTKFREEPGCCVAVHCVAGLGRAPVLVALALIECGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRL 155
PTP-IVa cd14500
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...
 5-145 5.08e-93

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: 266.39  E-value: 5.08e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284259   5 NRPAPVEVTYKNMRFLITHNPTNATLNKFIEELKKYGVTTIVRVCEATYDTTLVEKEGIHVL-------------IVDDW 71
Cdd:cd14500     1 LRPAPTLIEYKGMRFLITDAPTDSNLPLYIKELKKYNVTDLVRVCEPTYDKEPLEKAGIKVHdwpfddgspppddVVDDW 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1869284259  72 LSLVKIKFREE--PGCCIAVHCVAGLGRAPVLVALALIEGGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRL 145
Cdd:cd14500    81 LDLLKTRFKEEgkPGACIAVHCVAGLGRAPVLVAIALIELGMKPEDAVEFIRKKRRGAINSKQLQFLEKYKPKKKL 156
PTP-IVa3 cd18535
protein tyrosine phosphatase type IVA 3; Protein tyrosine phosphatase type IVA 3 (PTP-IVa3), ...
 5-145 2.86e-89

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: 256.88  E-value: 2.86e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284259   5 NRPAPVEVTYKNMRFLITHNPTNATLNKFIEELKKYGVTTIVRVCEATYDTTLVEKEGIHVL-------------IVDDW 71
Cdd:cd18535     1 NRPAPVEVCYKNMRFLITHNPTNATLSTFIEDLKKYGATTVVRVCEVTYDKTPLEKDGITVVdwpfddgapppgkVVEDW 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1869284259  72 LSLVKIKFREEPGCCIAVHCVAGLGRAPVLVALALIEGGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRL 145
Cdd:cd18535    81 LSLLKTKFCEDPGCCVAVHCVAGLGRAPVLVALALIESGMKYEDAIQFIRQKRRGAINSKQLTYLEKYRPKQRL 154
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 11-147 1.33e-57

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 177.14  E-value: 1.33e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284259  11 EVTYKNMRFLITHNPTNATLNKFIEELKKYGVTTIVRVCEATYDTTLVEKEGIHV-------------LIVDDWLSLVKI 77
Cdd:PTZ00242   10 QIEYVLFKFLILDAPSPSNLPLYIKELQRYNVTHLVRVCGPTYDAELLEKNGIEVhdwpfddgapppkAVIDNWLRLLDQ 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1869284259  78 KFREE--PGCCIAVHCVAGLGRAPVLVALALIE-GGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRF 147
Cdd:PTZ00242   90 EFAKQstPPETIAVHCVAGLGRAPILVALALVEyGGMEPLDAVGFVREKRKGAINQTQLQFLKKYKPRKKAAG 162
PTZ00393 PTZ00393
protein tyrosine phosphatase; Provisional
 4-142 6.80e-39

protein tyrosine phosphatase; Provisional


Pssm-ID: 240399  Cd Length: 241  Bit Score: 131.98  E-value: 6.80e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284259   4 MNRPAPVEvtYKNMRFLITHNPTNATLNKFIEELKKYGVTTIVRVCEATYDTTLVEKEGIHVL-------------IVDD 70
Cdd:PTZ00393   81 LNHPTKIE--HGKIKILILDAPTNDLLPLYIKEMKNYNVTDLVRTCERTYNDGEITSAGINVHelifpdgdaptvdIVSN 158

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1869284259  71 WLSLVK--IKFReepgCCIAVHCVAGLGRAPVLVALALIEGGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPK 142
Cdd:PTZ00393  159 WLTIVNnvIKNN----RAVAVHCVAGLGRAPVLASIVLIEFGMDPIDAIVFIRDRRKGAINKRQLQFLKAYKKK 228
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 17-138 2.82e-22

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: 85.48  E-value: 2.82e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284259  17 MRFLITHNPTNaTLNKFIEELKKYGVTTIVRVCEAtydttlvekegihvlIVDDWLSLVKIKfrEEPGCCIAVHCVAGLG 96
Cdd:cd14494     7 LRLIAGALPLS-PLEADSRFLKQLGVTTIVDLTLA---------------MVDRFLEVLDQA--EKPGEPVLVHCKAGVG 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1869284259  97 RAPVLVALALIE-GGMKYEDAVQFIRQKRRG--AFNSKQLLYLEK 138
Cdd:cd14494    69 RTGTLVACYLVLlGGMSAEEAVRIVRLIRPGgiPQTIEQLDFLIK 113
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
35-143 2.92e-16

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 70.77  E-value: 2.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284259  35 EELKKYGVTTIVRVC-EATYDTTLVEKEGI---HVLIVD-------DWLSLVK-IKFREEPGCCIAVHCVAGLGRAPVLV 102
Cdd:COG2453    19 ADLKREGIDAVVSLTeEEELLLGLLEEAGLeylHLPIPDfgapddeQLQEAVDfIDEALREGKKVLVHCRGGIGRTGTVA 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1869284259 103 ALALIEGGMKYEDAVQFIRQKRRGAFNSK-QLLYLEKYRPKM 143
Cdd:COG2453    99 AAYLVLLGLSAEEALARVRAARPGAVETPaQRAFLERFAKRL 140
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 22-144 8.20e-13

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: 62.47  E-value: 8.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284259  22 THNPtnatlNKFIEELKKYGVTTIVRVCEATYDTTLVEKEGIHVL-------------IVDDWLSLVkikfrEEPGCCIA 88
Cdd:cd14499    44 THTP-----EDYIPYFKKLGVTTVVRLNKKLYDAKRFTDAGIRHYdlyfpdgstpsddIVKKFLDIC-----ENEKGAIA 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1869284259  89 VHCVAGLGRAPVLVALALI-EGGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMR 144
Cdd:cd14499   114 VHCKAGLGRTGTLIACYLMkHYGFTAREAIAWLRICRPGSVIGPQQQFLEEKEARLW 170
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 34-124 1.95e-10

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: 55.24  E-value: 1.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284259  34 IEELKKYGVTTIVRVCEATYDTTLVEKEGIHVLIVDDwLSLVKIK--FRE---------EPGCCIAVHCVAGLGRAPVLV 102
Cdd:cd14498    19 KELLKKLGITHILNVAGEPPPNKFPDGIKYLRIPIED-SPDEDILshFEEaiefieealKKGGKVLVHCQAGVSRSATIV 97

                          90       100
                  ....*....|....*....|...
gi 1869284259 103 ALALI-EGGMKYEDAVQFIRQKR 124
Cdd:cd14498    98 IAYLMkKYGWSLEEALELVKSRR 120
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 34-136 1.52e-09

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: 53.42  E-value: 1.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284259  34 IEELKKYGVTTIVRVCE----ATYDT----TLVEKEGIHVL---IVDD--------WLSLVK-IKFREEPGCCIAVHCVA 93
Cdd:cd14505    36 LEELKDQGVDDVVTLCTdgelEELGVpdllEQYQQAGITWHhlpIPDGgvpsdiaqWQELLEeLLSALENGKKVLIHCKG 115

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1869284259  94 GLGRAPVLVA--LALIEGGMKYEDAVQFIRQKRRGAF-NSKQLLYL 136
Cdd:cd14505   116 GLGRTGLIAAclLLELGDTLDPEQAIAAVRALRPGAIqTPKQENFL 161
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 87-137 6.32e-09

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: 52.74  E-value: 6.32e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1869284259  87 IAVHCVAGLGRAPVLVALALIEG-GMKYEDAVQFIRQKRRGAFNSK-QLLYLE 137
Cdd:cd14506   112 VAVHCHAGLGRTGVLIACYLVYAlRMSADQAIRLVRSKRPNSIQTRgQVLCVR 164
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
35-124 2.08e-07

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 47.28  E-value: 2.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284259   35 EELKKYGVTTIVRVCEATYDTTLVEKEGIHVLIVDDWLSLV---------KIKFREEPGCCIAVHCVAGLGRAPVLVALA 105
Cdd:smart00195  20 ALLKKLGITHVINVTNEVPNYNGSDFTYLGVPIDDNTETKIspyfpeaveFIEDAESKGGKVLVHCQAGVSRSATLIIAY 99

                           90       100
                   ....*....|....*....|
gi 1869284259  106 LIE-GGMKYEDAVQFIRQKR 124
Cdd:smart00195 100 LMKtRNMSLNDAYDFVKDRR 119
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
87-136 6.27e-07

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 45.43  E-value: 6.27e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1869284259   87 IAVHCVAGLGRAPVLVALALIEGGMKYE-------DAVQFIRQKRRGAFNSK-QLLYL 136
Cdd:smart00404  42 VVVHCSAGVGRTGTFVAIDILLQQLEAEagevdifDTVKELRSQRPGMVQTEeQYLFL 99
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 87-136 6.27e-07

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: 45.43  E-value: 6.27e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1869284259   87 IAVHCVAGLGRAPVLVALALIEGGMKYE-------DAVQFIRQKRRGAFNSK-QLLYL 136
Cdd:smart00012  42 VVVHCSAGVGRTGTFVAIDILLQQLEAEagevdifDTVKELRSQRPGMVQTEeQYLFL 99
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 12-139 6.60e-07

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: 6.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284259  12 VTYKNMRFLITHN---PTNATLNKFiEELKKYGVTTIvRVceATYDTTLV-EKEGIH--VLIVDDWLSLvkikfreepGC 85
Cdd:cd14524    24 VAKENVRGVITMNeeyETRFFCNSK-EEWKALGVEQL-RL--PTVDFTGVpSLEDLEkgVDFILKHREK---------GK 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1869284259  86 CIAVHCVAGLGRAPVLVALALIE-GGMKYEDAVQFIRQKRRG-AFNSKQLLYLEKY 139
Cdd:cd14524    91 SVYVHCKAGRGRSATIVACYLIQhKGWSPEEAQEFLRSKRPHiLLRLSQREVLEEF 146
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 37-124 4.26e-06

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: 43.79  E-value: 4.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284259  37 LKKYGVTTIVRvCEATYDTTLVEKEGIHVLIVDD-------WLSLVK--IKFREEPGCCIAVHCVAGLGRAPVLVALALI 107
Cdd:pfam00782  14 LSKLGITAVIN-VTREVDLYNSGILYLRIPVEDNhetniskYLEEAVefIDDARQKGGKVLVHCQAGISRSATLIIAYLM 92

                          90
                  ....*....|....*...
gi 1869284259 108 E-GGMKYEDAVQFIRQKR 124
Cdd:pfam00782  93 KtRNLSLNEAYSFVKERR 110
DSP_MKP_classII cd14566
dual specificity phosphatase domain of class II mitogen-activated protein kinase phosphatase; ...
 9-125 4.64e-06

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: 43.85  E-value: 4.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284259   9 PVEVTykNMRFLithnpTNATLNKFIEELKKYGVTTIVRVceaTYD--TTLVEKEGIHVL---IVDDW---LSLV---KI 77
Cdd:cd14566     1 PVEIL--PFLYL-----GNAKDSANIDLLKKYNIKYILNV---TPNlpNTFEEDGGFKYLqipIDDHWsqnLSAFfpeAI 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1869284259  78 KFREEP---GCCIAVHCVAGLGRA-PVLVALALIEGGMKYEDAVQFIRQKRR 125
Cdd:cd14566    71 SFIDEArskKCGVLVHCLAGISRSvTVTVAYLMQKLHLSLNDAYDFVKKRKS 122
DUSP3-like cd14515
dual specificity protein phosphatases 3, 13, 26, 27, and similar domains; This family is ...
 89-138 6.27e-06

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: 43.35  E-value: 6.27e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1869284259  89 VHCVAGLGRAPVLV-ALALIEGGMKYEDAVQFIRQKRRGAFNS---KQLLYLEK 138
Cdd:cd14515    93 VHCVEGVSRSATLVlAYLMIYQNMTLEEAIRTVRKKREIRPNRgflQQLCELND 146
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 34-126 3.16e-05

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


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 41.49  E-value: 3.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284259  34 IEELKKYGVTTIVRVCEATYDTTLVEKEGI---HVLIVD-------DWLSLVKI-KFREEPGCCIAVHCVAGLGRAPVLV 102
Cdd:cd14504    21 YAYLNENGIRHVVTLTEEPPPEHSDTCPGLryhHIPIEDytpptleQIDEFLDIvEEANAKNEAVLVHCLAGKGRTGTML 100

                          90       100
                  ....*....|....*....|....*
gi 1869284259 103 ALALI-EGGMKYEDAVQFIRQKRRG 126
Cdd:cd14504   101 ACYLVkTGKISAVDAINEIRRIRPG 125
DSP_MKP_classIII cd14568
dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; ...
 84-124 1.27e-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: 1.27e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1869284259  84 GCCIAVHCVAGLGRAPVL-VALALIEGGMKYEDAVQFIRQKR 124
Cdd:cd14568    79 NKRVLVHCLAGISRSATIaIAYIMKHMRMSLDDAYRFVKEKR 120
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 87-131 1.29e-04

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: 40.44  E-value: 1.29e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1869284259  87 IAVHCVAGLGRAPVL----VALALIEGGMKYE--DAVQFIRQKRRGAFNSK 131
Cdd:cd14538   143 IVVHCSAGIGRTGVLitidVALGLIERDLPFDiqDIVKDLREQRQGMIQTK 193
DSP_laforin-like cd14526
dual specificity phosphatase domain of laforin and similar domains; This family is composed of ...
 84-124 1.87e-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: 39.49  E-value: 1.87e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1869284259  84 GCCIAVHCVAGLGRAP--VLVALALIEgGMKYEDAVQFIRQKR 124
Cdd:cd14526    94 GGTVYVHCTAGLGRAPatVIAYLYWVL-GYSLDEAYYLLTSKR 135
DUSP14-like cd14514
dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is ...
 35-124 1.08e-03

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: 37.15  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1869284259  35 EELKKYGVTTIVRVCEATYDTTLVEKEGIHVLIVD-------DWLSLV--KIKFREEPGCCIAVHCVAGLGRAPVLVALA 105
Cdd:cd14514    19 PLLLSRGITCIINATTELPDPSYPGIEYLRVPVEDsphadlsPHFDEVadKIHQVKRRGGRTLVHCVAGVSRSATLCLAY 98

                          90       100
                  ....*....|....*....|....
gi 1869284259 106 LieggMKYE-----DAVQFIRQKR 124
Cdd:cd14514    99 L----MKYEgmtlrEAYKHVKAAR 118
DSP_MKP cd14512
dual specificity phosphatase domain of mitogen-activated protein kinase phosphatase; ...
 77-124 1.16e-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: 1.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1869284259  77 IKFREEP---GCCIAVHCVAGLGR-APVLVALALIEGGMKYEDAVQFIRQKR 124
Cdd:cd14512    69 IEFIEEAkasNGGVLVHCLAGISRsATIAIAYLMKRMRMSLDEAYDFVKEKR 120
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 87-132 1.17e-03

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: 37.80  E-value: 1.17e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1869284259  87 IAVHCVAGLGRAPVL----VALALIEGGMKYE--DAVQFIRQKRRGAFNSKQ 132
Cdd:cd14596   142 IVVHCSAGIGRAGVLicvdVLLSLIEKDLSFNikDIVREMRQQRYGMIQTKD 193
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 78-143 1.31e-03

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: 37.89  E-value: 1.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1869284259  78 KFREEPGCC--IAVHCVAGLGRAPVLVALALIEGGMKYEDAVQFirqkrrgaFNSKQLLYLEkyRPKM 143
Cdd:cd14554   166 KTKEQFGQEgpITVHCSAGVGRTGVFITLSIVLERMRYEGVVDV--------FQTVKLLRTQ--RPAM 223
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
87-136 2.06e-03

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 37.22  E-value: 2.06e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1869284259  87 IAVHCVAGLGRAPVLVALALIEGGMKYE------DAVQFIRQKRRGAFNSK-QLLYL 136
Cdd:pfam00102 172 IVVHCSAGIGRTGTFIAIDIALQQLEAEgevdifQIVKELRSQRPGMVQTLeQYIFL 228
DSP_STYX cd14522
dual specificity phosphatase-like domain of serine/threonine/tyrosine-interacting protein; ...
 82-124 2.06e-03

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: 36.54  E-value: 2.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1869284259  82 EPGCCIAVHCVAGLGRAPVLVALALIEG-GMKYEDAVQFIRQKR 124
Cdd:cd14522    87 QTGGKVLVHGNAGISRSAALVIAYIMETyGLSYRDAFAYVQQRR 130
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 70-124 2.44e-03

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: 36.85  E-value: 2.44e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1869284259  70 DWLSLVKIK--FREEPgccIAVHCVAGLGRAPVLV----ALALIEGGMKYE--DAVQFIRQKR 124
Cdd:cd14601   130 DFVCLVRNKraGKDEP---VVVHCSAGIGRTGVLItmetAMCLIECNQPVYplDIVRTMRDQR 189
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
87-136 2.68e-03

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 36.87  E-value: 2.68e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1869284259   87 IAVHCVAGLGRAPVLVALALIEGGMKYE------DAVQFIRQKRRGAFNSK-QLLYL 136
Cdd:smart00194 197 IVVHCSAGVGRTGTFIAIDILLQQLEAGkevdifEIVKELRSQRPGMVQTEeQYIFL 253
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 87-136 3.47e-03

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: 36.49  E-value: 3.47e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1869284259  87 IAVHCVAGLGRAPVLVALALIEGGMKYE------DAVQFIRQKRRGAF-NSKQLLYL 136
Cdd:cd00047   142 IVVHCSAGVGRTGTFIAIDILLERLEAEgevdvfEIVKALRKQRPGMVqTLEQYEFI 198
DSP_DUSP8 cd14645
dual specificity phosphatase domain of dual specificity protein phosphatase 8; Dual ...
 85-124 9.51e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 8; Dual specificity protein phosphatase 8 (DUSP8), also called DUSP hVH-5 or M3/6, functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other MKPs, it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class III subfamily and is a JNK/p38-selective cytoplasmic MKP. DUSP8 controls basal and acute stress-induced ERK1/2 signaling in adult cardiac myocytes, which impacts contractility, ventricular remodeling, and disease susceptibility. It also plays a role in decreasing ureteric branching morphogenesis by inhibiting p38MAPK. DUSP8 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350493 [Multi-domain]  Cd Length: 151  Bit Score: 34.60  E-value: 9.51e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1869284259  85 CCIAVHCVAGLGR-APVLVALALIEGGMKYEDAVQFIRQKR 124
Cdd:cd14645    91 CRVIVHCLAGISRsATIAIAYIMKTMGLSSDDAYRFVKDRR 131
 
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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