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Conserved domains on  [gi|261862269|ref|NP_001159862|]
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protein tyrosine phosphatase type IVA 3 isoform 2 [Mus musculus]

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 ...
 1-139 7.99e-92

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 cd18535:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 154  Bit Score: 263.04  E-value: 7.99e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269   1 MVRHLQVSEALAGNLQDLKKYGATTVVRVCEVTYDKTPLEKDGITVVDWPFDDGAPPPGKVVEDWLSLLKAKFYNDPGSC 80
Cdd:cd18535   16 LITHNPTNATLSTFIEDLKKYGATTVVRVCEVTYDKTPLEKDGITVVDWPFDDGAPPPGKVVEDWLSLLKTKFCEDPGCC 95

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 261862269  81 VAVHCVAGLGRAPVLVALALIESGMKYEDAIQFIRQKRRGAINSKQLTYLEKYRPKQRL 139
Cdd:cd18535   96 VAVHCVAGLGRAPVLVALALIESGMKYEDAIQFIRQKRRGAINSKQLTYLEKYRPKQRL 154
 
Name Accession Description Interval E-value
PTP-IVa3 cd18535
protein tyrosine phosphatase type IVA 3; Protein tyrosine phosphatase type IVA 3 (PTP-IVa3), ...
 1-139 7.99e-92

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: 263.04  E-value: 7.99e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269   1 MVRHLQVSEALAGNLQDLKKYGATTVVRVCEVTYDKTPLEKDGITVVDWPFDDGAPPPGKVVEDWLSLLKAKFYNDPGSC 80
Cdd:cd18535   16 LITHNPTNATLSTFIEDLKKYGATTVVRVCEVTYDKTPLEKDGITVVDWPFDDGAPPPGKVVEDWLSLLKTKFCEDPGCC 95

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 261862269  81 VAVHCVAGLGRAPVLVALALIESGMKYEDAIQFIRQKRRGAINSKQLTYLEKYRPKQRL 139
Cdd:cd18535   96 VAVHCVAGLGRAPVLVALALIESGMKYEDAIQFIRQKRRGAINSKQLTYLEKYRPKQRL 154
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 18-154 4.49e-64

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 193.32  E-value: 4.49e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269  18 LKKYGATTVVRVCEVTYDKTPLEKDGITVVDWPFDDGAPPPGKVVEDWLSLLKAKF--YNDPGSCVAVHCVAGLGRAPVL 95
Cdd:PTZ00242  36 LQRYNVTHLVRVCGPTYDAELLEKNGIEVHDWPFDDGAPPPKAVIDNWLRLLDQEFakQSTPPETIAVHCVAGLGRAPIL 115

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269  96 VALALIESG-MKYEDAIQFIRQKRRGAINSKQLTYLEKYRPKQRLRFkdphthktrCCVM 154
Cdd:PTZ00242 116 VALALVEYGgMEPLDAVGFVREKRKGAINQTQLQFLKKYKPRKKAAG---------CTIM 166
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
16-134 1.10e-18

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 76.93  E-value: 1.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269  16 QDLKKYGATTVVRVC-EVTYDKTPLEKDGITVVDWPFDDGAPPPgkvVEDWLSLLK-AKFYNDPGSCVAVHCVAGLGRAP 93
Cdd:COG2453   19 ADLKREGIDAVVSLTeEEELLLGLLEEAGLEYLHLPIPDFGAPD---DEQLQEAVDfIDEALREGKKVLVHCRGGIGRTG 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 261862269  94 VLVALALIESGMKYEDAIQFIRQKRRGAINSK-QLTYLEKYR 134
Cdd:COG2453   96 TVAAAYLVLLGLSAEEALARVRAARPGAVETPaQRAFLERFA 137
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
48-126 3.56e-12

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 58.91  E-value: 3.56e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269    48 DWPfDDGAPPPGKVVEDWLSLLKAKFY-NDPGSCVAVHCVAGLGRAPVLVALALIESGMKYE-------DAIQFIRQKRR 119
Cdd:smart00404   9 GWP-DHGVPESPDSILELLRAVKKNLNqSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEagevdifDTVKELRSQRP 87


                   ....*..
gi 261862269   120 GAINSKQ 126
Cdd:smart00404  88 GMVQTEE 94
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
14-130 5.50e-08

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 49.93  E-value: 5.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269   14 NLQDLKKYGATTVVRVCEVTYDKTPLEKdgiTV-----VDWPfDDGAPppgkvvEDWLSLLKA-----KFYNDPGSC-VA 82
Cdd:pfam00102 104 TLKKEKEDEKDYTVRTLEVSNGGSEETR---TVkhfhyTGWP-DHGVP------ESPNSLLDLlrkvrKSSLDGRSGpIV 173

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 261862269   83 VHCVAGLGRAPVLVALALIESGMKYE------DAIQFIRQKRRGAINSK-QLTYL 130
Cdd:pfam00102 174 VHCSAGIGRTGTFIAIDIALQQLEAEgevdifQIVKELRSQRPGMVQTLeQYIFL 228
 
Name Accession Description Interval E-value
PTP-IVa3 cd18535
protein tyrosine phosphatase type IVA 3; Protein tyrosine phosphatase type IVA 3 (PTP-IVa3), ...
 1-139 7.99e-92

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: 263.04  E-value: 7.99e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269   1 MVRHLQVSEALAGNLQDLKKYGATTVVRVCEVTYDKTPLEKDGITVVDWPFDDGAPPPGKVVEDWLSLLKAKFYNDPGSC 80
Cdd:cd18535   16 LITHNPTNATLSTFIEDLKKYGATTVVRVCEVTYDKTPLEKDGITVVDWPFDDGAPPPGKVVEDWLSLLKTKFCEDPGCC 95

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 261862269  81 VAVHCVAGLGRAPVLVALALIESGMKYEDAIQFIRQKRRGAINSKQLTYLEKYRPKQRL 139
Cdd:cd18535   96 VAVHCVAGLGRAPVLVALALIESGMKYEDAIQFIRQKRRGAINSKQLTYLEKYRPKQRL 154
PTP-IVa cd14500
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...
 15-139 1.63e-86

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: 249.83  E-value: 1.63e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269  15 LQDLKKYGATTVVRVCEVTYDKTPLEKDGITVVDWPFDDGAPPPGKVVEDWLSLLKAKFYND--PGSCVAVHCVAGLGRA 92
Cdd:cd14500   30 IKELKKYNVTDLVRVCEPTYDKEPLEKAGIKVHDWPFDDGSPPPDDVVDDWLDLLKTRFKEEgkPGACIAVHCVAGLGRA 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 261862269  93 PVLVALALIESGMKYEDAIQFIRQKRRGAINSKQLTYLEKYRPKQRL 139
Cdd:cd14500  110 PVLVAIALIELGMKPEDAVEFIRKKRRGAINSKQLQFLEKYKPKKKL 156
PTP-IVa1 cd18537
protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), ...
 1-148 1.52e-77

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: 227.65  E-value: 1.52e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269   1 MVRHLQVSEALAGNLQDLKKYGATTVVRVCEVTYDKTPLEKDGITVVDWPFDDGAPPPGKVVEDWLSLLKAKFYNDPGSC 80
Cdd:cd18537   20 LITHNPTNATLNKFIEELKKYGVTTVVRVCEATYDTTLVEKEGIQVLDWPFDDGAPPSNQIVDDWLNLLKVKFREEPGCC 99

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261862269  81 VAVHCVAGLGRAPVLVALALIESGMKYEDAIQFIRQKRRGAINSKQLTYLEKYRPKQRLRFKDPHTHK 148
Cdd:cd18537  100 IAVHCVAGLGRAPVLVALALIECGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRFKDSNGHR 167
PTP-IVa2 cd18536
protein tyrosine phosphatase type IVA 2; Protein tyrosine phosphatase type IVA 2 (PTP-IVa2), ...
 1-139 2.43e-76

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: 224.11  E-value: 2.43e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269   1 MVRHLQVSEALAGNLQDLKKYGATTVVRVCEVTYDKTPLEKDGITVVDWPFDDGAPPPGKVVEDWLSLLKAKFYNDPGSC 80
Cdd:cd18536   17 LITHNPTNATLNKFTEELKKYGVTTLVRVCDATYDKAPVEKEGIQVLDWPFDDGAPPPNQIVDDWLNLLKTKFREEPGCC 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 261862269  81 VAVHCVAGLGRAPVLVALALIESGMKYEDAIQFIRQKRRGAINSKQLTYLEKYRPKQRL 139
Cdd:cd18536   97 VAVHCVAGLGRAPVLVALALIECGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRL 155
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 18-154 4.49e-64

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 193.32  E-value: 4.49e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269  18 LKKYGATTVVRVCEVTYDKTPLEKDGITVVDWPFDDGAPPPGKVVEDWLSLLKAKF--YNDPGSCVAVHCVAGLGRAPVL 95
Cdd:PTZ00242  36 LQRYNVTHLVRVCGPTYDAELLEKNGIEVHDWPFDDGAPPPKAVIDNWLRLLDQEFakQSTPPETIAVHCVAGLGRAPIL 115

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269  96 VALALIESG-MKYEDAIQFIRQKRRGAINSKQLTYLEKYRPKQRLRFkdphthktrCCVM 154
Cdd:PTZ00242 116 VALALVEYGgMEPLDAVGFVREKRKGAINQTQLQFLKKYKPRKKAAG---------CTIM 166
PTZ00393 PTZ00393
protein tyrosine phosphatase; Provisional
 9-138 7.75e-39

protein tyrosine phosphatase; Provisional


Pssm-ID: 240399  Cd Length: 241  Bit Score: 131.59  E-value: 7.75e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269   9 EALAGNLQDLKKYGATTVVRVCEVTYDKTPLEKDGITVVDWPFDDGAPPPGKVVEDWLSLLKAKFYNDpgSCVAVHCVAG 88
Cdd:PTZ00393 103 DLLPLYIKEMKNYNVTDLVRTCERTYNDGEITSAGINVHELIFPDGDAPTVDIVSNWLTIVNNVIKNN--RAVAVHCVAG 180

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 261862269  89 LGRAPVLVALALIESGMKYEDAIQFIRQKRRGAINSKQLTYLEKYRPKQR 138
Cdd:PTZ00393 181 LGRAPVLASIVLIEFGMDPIDAIVFIRDRRKGAINKRQLQFLKAYKKKKK 230
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 19-136 2.68e-20

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: 81.73  E-value: 2.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269  19 KKYGATTVVRVCEVTYDKTPLEKDGITVVDWPFDDGAPPPGKVVEDWLSLLKakfyNDPGScVAVHCVAGLGRAPVLVAL 98
Cdd:cd14499   55 KKLGVTTVVRLNKKLYDAKRFTDAGIRHYDLYFPDGSTPSDDIVKKFLDICE----NEKGA-IAVHCKAGLGRTGTLIAC 129

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 261862269  99 ALI-ESGMKYEDAIQFIRQKRRGAINSKQLTYLEKYRPK 136
Cdd:cd14499  130 YLMkHYGFTAREAIAWLRICRPGSVIGPQQQFLEEKEAR 168
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
16-134 1.10e-18

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 76.93  E-value: 1.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269  16 QDLKKYGATTVVRVC-EVTYDKTPLEKDGITVVDWPFDDGAPPPgkvVEDWLSLLK-AKFYNDPGSCVAVHCVAGLGRAP 93
Cdd:COG2453   19 ADLKREGIDAVVSLTeEEELLLGLLEEAGLEYLHLPIPDFGAPD---DEQLQEAVDfIDEALREGKKVLVHCRGGIGRTG 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 261862269  94 VLVALALIESGMKYEDAIQFIRQKRRGAINSK-QLTYLEKYR 134
Cdd:COG2453   96 TVAAAYLVLLGLSAEEALARVRAARPGAVETPaQRAFLERFA 137
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 11-130 3.28e-15

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: 68.44  E-value: 3.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269  11 LAGNLQDLKKYGATTVVRVCE--------VTYDKTPLEKDGITVVDWPFDDGAPPP-----GKVVEDWLSLLKAkfyndp 77
Cdd:cd14505   32 LQADLEELKDQGVDDVVTLCTdgeleelgVPDLLEQYQQAGITWHHLPIPDGGVPSdiaqwQELLEELLSALEN------ 105

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 261862269  78 GSCVAVHCVAGLGRAPVLVALALIESG--MKYEDAIQFIRQKRRGAI-NSKQLTYL 130
Cdd:cd14505  106 GKKVLIHCKGGLGRTGLIAACLLLELGdtLDPEQAIAAVRALRPGAIqTPKQENFL 161
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 62-132 1.93e-13

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: 62.75  E-value: 1.93e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 261862269  62 VEDWLSLLKAKfyNDPGSCVAVHCVAGLGRAPVLVALALIE-SGMKYEDAIQFIRQKRRGAI--NSKQLTYLEK 132
Cdd:cd14494   42 VDRFLEVLDQA--EKPGEPVLVHCKAGVGRTGTLVACYLVLlGGMSAEEAVRIVRLIRPGGIpqTIEQLDFLIK 113
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 33-125 2.15e-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: 61.98  E-value: 2.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269  33 TYDKTPLEKDGITVVDWPFDD-GAPPPGKVvedwLSLLK-AKFYNDPGSCVAVHCVAGLGRAPVLVALALI-ESGMKYED 109
Cdd:cd14506   66 SYLPEAFMRAGIYFYNFGWKDyGVPSLTTI----LDIVKvMAFALQEGGKVAVHCHAGLGRTGVLIACYLVyALRMSADQ 141

                         90
                 ....*....|....*.
gi 261862269 110 AIQFIRQKRRGAINSK 125
Cdd:cd14506  142 AIRLVRSKRPNSIQTR 157
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
48-126 3.56e-12

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 58.91  E-value: 3.56e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269    48 DWPfDDGAPPPGKVVEDWLSLLKAKFY-NDPGSCVAVHCVAGLGRAPVLVALALIESGMKYE-------DAIQFIRQKRR 119
Cdd:smart00404   9 GWP-DHGVPESPDSILELLRAVKKNLNqSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEagevdifDTVKELRSQRP 87


                   ....*..
gi 261862269   120 GAINSKQ 126
Cdd:smart00404  88 GMVQTEE 94
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 48-126 3.56e-12

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: 58.91  E-value: 3.56e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269    48 DWPfDDGAPPPGKVVEDWLSLLKAKFY-NDPGSCVAVHCVAGLGRAPVLVALALIESGMKYE-------DAIQFIRQKRR 119
Cdd:smart00012   9 GWP-DHGVPESPDSILELLRAVKKNLNqSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEagevdifDTVKELRSQRP 87


                   ....*..
gi 261862269   120 GAINSKQ 126
Cdd:smart00012  88 GMVQTEE 94
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 14-133 1.69e-11

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: 58.06  E-value: 1.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269  14 NLQDLKKYGATTVVRVCEVTYDKTPLEKDGITVVDWPFDDGAPPPGKVVEDWLSLL-KAKFYNDPgscVAVHCVAGLGRA 92
Cdd:cd14504   20 HYAYLNENGIRHVVTLTEEPPPEHSDTCPGLRYHHIPIEDYTPPTLEQIDEFLDIVeEANAKNEA---VLVHCLAGKGRT 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 261862269  93 PVLVALALIESG-MKYEDAIQFIRQKRRGAI-NSKQLTYLEKY 133
Cdd:cd14504   97 GTMLACYLVKTGkISAVDAINEIRRIRPGSIeTSEQEKFVIQF 139
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 8-127 5.26e-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: 54.09  E-value: 5.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269   8 SEALAGNLQDLKKYGATTVVRVCEVTYDktPLEKDGITVVDWPFDDgapppgKVVEDWLSLLK--AKFYND---PGSCVA 82
Cdd:cd14498   12 SLDAAQDKELLKKLGITHILNVAGEPPP--NKFPDGIKYLRIPIED------SPDEDILSHFEeaIEFIEEalkKGGKVL 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 261862269  83 VHCVAGLGRAPVLVALALIES-GMKYEDAIQFIRQKRRGA-INS---KQL 127
Cdd:cd14498   84 VHCQAGVSRSATIVIAYLMKKyGWSLEEALELVKSRRPIIsPNPgflKQL 133
DUSP3-like cd14515
dual specificity protein phosphatases 3, 13, 26, 27, and similar domains; This family is ...
 9-132 6.73e-10

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: 54.14  E-value: 6.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269   9 EALAGNLQDLKKYGATTVV------RVCEVT-----YDKTPLEKDGITVVDWPFDDGAP---PPGKVVEDWLSllkakfy 74
Cdd:cd14515   13 ESTAKNKAKLKKLGITHVLnaaegkKNGEVNtnakfYKGSGIIYLGIPASDLPTFDISQyfdEAADFIDKALS------- 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261862269  75 nDPGSCVAVHCVAGLGRAPVLV-ALALIESGMKYEDAIQFIRQKRRGAINS---KQLTYLEK 132
Cdd:cd14515   86 -DPGGKVLVHCVEGVSRSATLVlAYLMIYQNMTLEEAIRTVRKKREIRPNRgflQQLCELND 146
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
14-130 5.50e-08

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 49.93  E-value: 5.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269   14 NLQDLKKYGATTVVRVCEVTYDKTPLEKdgiTV-----VDWPfDDGAPppgkvvEDWLSLLKA-----KFYNDPGSC-VA 82
Cdd:pfam00102 104 TLKKEKEDEKDYTVRTLEVSNGGSEETR---TVkhfhyTGWP-DHGVP------ESPNSLLDLlrkvrKSSLDGRSGpIV 173

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 261862269   83 VHCVAGLGRAPVLVALALIESGMKYE------DAIQFIRQKRRGAINSK-QLTYL 130
Cdd:pfam00102 174 VHCSAGIGRTGTFIAIDIALQQLEAEgevdifQIVKELRSQRPGMVQTLeQYIFL 228
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 78-134 1.15e-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: 48.03  E-value: 1.15e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269  78 GSCVAVHCVAGLGRAPVLVALALIES-GMKYEDAIQFIRQKRRGAI--NSKQLTYLEKYR 134
Cdd:cd14524   89 GKSVYVHCKAGRGRSATIVACYLIQHkGWSPEEAQEFLRSKRPHILlrLSQREVLEEFYR 148
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 46-138 2.55e-07

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: 47.20  E-value: 2.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269  46 VVDWPFDDGAPPPGKV-------VEDWLSLlkakfynDPGSCVAVHCVAGLGRAPVLVALALIESGM--KYEDAIQFIRQ 116
Cdd:cd14509   62 VAEYPFDDHNPPPLELikpfcedVDEWLKE-------DEKNVAAVHCKAGKGRTGVMICCYLLYLGKfpSAKEALDFYGA 134

                         90       100
                 ....*....|....*....|..
gi 261862269 117 KRrgAINSKQLTYlekyrPKQR 138
Cdd:cd14509  135 KR--TKNKKGVTI-----PSQR 149
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 49-130 2.73e-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: 47.67  E-value: 2.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269  49 WPfDDGAPPPGKVVEDWLSLLKAKFYNDPGSCVaVHCVAGLGRAPVLVAL-ALIESgMKYE------DAIQFIRQKRRGA 121
Cdd:cd00047  112 WP-DHGVPSSPEDLLALVRRVRKEARKPNGPIV-VHCSAGVGRTGTFIAIdILLER-LEAEgevdvfEIVKALRKQRPGM 188

                         90
                 ....*....|
gi 261862269 122 I-NSKQLTYL 130
Cdd:cd00047  189 VqTLEQYEFI 198
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 81-123 1.90e-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: 44.56  E-value: 1.90e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 261862269   81 VAVHCVAGLGRAPVLVALALIES-GMKYEDAIQFIRQkRRGAIN 123
Cdd:pfam00782  72 VLVHCQAGISRSATLIIAYLMKTrNLSLNEAYSFVKE-RRPGIS 114
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
25-130 2.09e-06

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 45.73  E-value: 2.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269    25 TVVRVCEVTYDKTPLEKDgITVV---DWPfDDGAPPPGKVVedwLSLLKA--KFYNDPGSCVAVHCVAGLGRAPVLVALA 99
Cdd:smart00194 141 YTIRTLEVTNTGCSETRT-VTHYhytNWP-DHGVPESPESI---LDLIRAvrKSQSTSTGPIVVHCSAGVGRTGTFIAID 215

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 261862269   100 LIESGMKYE------DAIQFIRQKRRGAINSK-QLTYL 130
Cdd:smart00194 216 ILLQQLEAGkevdifEIVKELRSQRPGMVQTEeQYIFL 253
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
1-123 2.30e-06

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 44.58  E-value: 2.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269     1 MVRHLQV-SEALAGNLQDLKKYGATTVVRVCEVtydKTPLEKDGITVVDWPFDDGappPGKVVEDWLSLLKaKFYND--- 76
Cdd:smart00195   4 ILPHLYLgSYSDALNLALLKKLGITHVINVTNE---VPNYNGSDFTYLGVPIDDN---TETKISPYFPEAV-EFIEDaes 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 261862269    77 PGSCVAVHCVAGLGRAPVLVALALIES-GMKYEDAIQFIRQkRRGAIN 123
Cdd:smart00195  77 KGGKVLVHCQAGVSRSATLIIAYLMKTrNMSLNDAYDFVKD-RRPIIS 123
DSP_STYX cd14522
dual specificity phosphatase-like domain of serine/threonine/tyrosine-interacting protein; ...
 76-135 2.84e-06

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: 44.24  E-value: 2.84e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 261862269  76 DPGSCVAVHCVAGLGRAPVLVALALIES-GMKYEDAIQFIrQKRRGAINSKQ--LTYLEKYRP 135
Cdd:cd14522   87 QTGGKVLVHGNAGISRSAALVIAYIMETyGLSYRDAFAYV-QQRRFCINPNEgfVHQLKEYEA 148
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 30-131 2.89e-06

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: 44.49  E-value: 2.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269  30 CEVTYDktPLEKDGITVVDWPFDDGAPPP-------GKVVEDWLSLlkakfynDPGSCVAVHCVAGLGRAPVLVALALIE 102
Cdd:cd14497   49 SEEEYD--DDSKFEGRVLHYGFPDHHPPPlgllleiVDDIDSWLSE-------DPNNVAVVHCKAGKGRTGTVICAYLLY 119

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 261862269 103 SGM--KYEDAIQFIRQKRRGA------INSkQLTYLE 131
Cdd:cd14497  120 YGQysTADEALEYFAKKRFKEglpgvtIPS-QLRYLQ 155
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 48-134 7.59e-06

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: 44.34  E-value: 7.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269  48 DWPfDDGAPPPGKVVEDWLSLL---KAKFYNDpgSCVAVHCVAGLGRAPVLVALALIESGMKYE---DAIQFIRQKR--R 119
Cdd:cd14628  190 DWP-EQGVPKSGEGFIDFIGQVhktKEQFGQD--GPISVHCSAGVGRTGVFITLSIVLERMRYEgvvDIFQTVKMLRtqR 266

                         90
                 ....*....|....*
gi 261862269 120 GAINSKQLTYLEKYR 134
Cdd:cd14628  267 PAMVQTEDQYQFCYR 281
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 49-125 7.89e-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: 43.90  E-value: 7.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269  49 WPfDDGAPPPGKVVEDWLSLLKaKFYND-PgscVAVHCVAGLGRAPVL----VALALIESGMKYE--DAIQFIRQKRRGA 121
Cdd:cd14538  115 WP-DHGTPQSADPLLRFIRYMR-RIHNSgP---IVVHCSAGIGRTGVLitidVALGLIERDLPFDiqDIVKDLREQRQGM 189


                 ....
gi 261862269 122 INSK 125
Cdd:cd14538  190 IQTK 193
DSP_laforin-like cd14526
dual specificity phosphatase domain of laforin and similar domains; This family is composed of ...
 12-118 9.65e-06

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: 42.95  E-value: 9.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269  12 AGNLQDLKKYGATTVVRV---CEVTYDKTPLE-------KDGITVVDWPFDDGAP-------PpgKVVEDWLSLLKAkfy 74
Cdd:cd14526   19 PEDVDRLKKEGVTAVLNLqtdSDMEYWGVDIDsirkackESGIRYVRLPIRDFDTedlrqklP--QAVALLYRLLKN--- 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 261862269  75 ndpGSCVAVHCVAGLGRAP--VLVALALIeSGMKYEDAIQFIRQKR 118
Cdd:cd14526   94 ---GGTVYVHCTAGLGRAPatVIAYLYWV-LGYSLDEAYYLLTSKR 135
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 48-125 1.98e-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: 43.18  E-value: 1.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269  48 DWPfDDGAPPPGKVVEDWLSLL---KAKFYNDpgSCVAVHCVAGLGRAPVLVALALIESGMKYE------DAIQFIRQKR 118
Cdd:cd14627  191 DWP-EQGVPKSGEGFIDFIGQVhktKEQFGQD--GPISVHCSAGVGRTGVFITLSIVLERMRYEgvvdifQTVKMLRTQR 267


                 ....*..
gi 261862269 119 RGAINSK 125
Cdd:cd14627  268 PAMVQTE 274
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 48-134 3.01e-05

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: 42.41  E-value: 3.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269  48 DWPfDDGAPPPGKVVEDWLSLL---KAKFYNDpgSCVAVHCVAGLGRAPVLVALALIESGMKYE---DAIQFIRQKR--R 119
Cdd:cd14629  191 DWP-EQGVPKTGEGFIDFIGQVhktKEQFGQD--GPITVHCSAGVGRTGVFITLSIVLERMRYEgvvDMFQTVKTLRtqR 267

                         90
                 ....*....|....*
gi 261862269 120 GAINSKQLTYLEKYR 134
Cdd:cd14629  268 PAMVQTEDQYQLCYR 282
PRK12361 PRK12361
hypothetical protein; Provisional
 11-144 6.58e-05

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 41.53  E-value: 6.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269  11 LAGNLQDLKKYGATTVVRVC------EVTYDKTPLEKDGITVvdwpFDDGAPPPGKVVE--DWLSLLKAKfyndpGSCVA 82
Cdd:PRK12361 109 FPADLEKLKSNKITAILDVTaefdglDWSLTEEDIDYLNIPI----LDHSVPTLAQLNQaiNWIHRQVRA-----NKSVV 179

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261862269  83 VHCVAGLGRApVLVALALIESGMK---YEDAIQFIRQKRRGA-INSKQLTYLEKYRPKQRLRFKDP 144
Cdd:PRK12361 180 VHCALGRGRS-VLVLAAYLLCKDPdltVEEVLQQIKQIRKTArLNKRQLRALEKMLEQGKLNIHKR 244
DUPD1 cd14575
dual specificity phosphatase and pro isomerase domain containing 1; Dual specificity ...
 75-138 6.97e-05

dual specificity phosphatase and pro isomerase domain containing 1; Dual specificity phosphatase and pro isomerase domain containing 1 (DUPD1) was initially named as such because computational prediction appeared to encode a protein of 446 amino acids in length that included two catalytic domains: a proline isomerase and a dual specificity phosphatase (DUSP). However, it was subsequently shown that the true open reading frame only encompassed the DUSP domain and the gene product was therefore renamed DUSP27. This is distinct from inactive DUSP27. DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). DUPD1/DUSP27 has been shown to have catalytic activity with preference for phosphotyrosine over phosphothreonine and phosphoserine residues. It associates with the short form of the prolactin (PRL) receptor and plays a role in PRL-mediated MAPK inhibition in ovarian cells.


Pssm-ID: 350423 [Multi-domain]  Cd Length: 160  Bit Score: 40.58  E-value: 6.97e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269  75 NDPGSCVAVHCVAGLGRAPVLV-ALALIESGMKYEDAIQFIRQKR-----RGAInsKQLTYLEKYRPKQR 138
Cdd:cd14575   93 SDPHNKLLVHCVMGRSRSATLVlAYLMIYKNMTVVDAIEQVAQRRcilpnRGFL--KQLRELDIQLAEER 160
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 18-138 7.54e-05

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: 40.44  E-value: 7.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269  18 LKKYGATTVV---RVCEVTYDKTPLEK-DGITVVDWPFDDGAPPPgkvvEDWLSLLKAKFYNDPGSCVAVHCVAGLGRAP 93
Cdd:cd14529   29 LKKLGIKTVIdlrGADERAASEEAAAKiDGVKYVNLPLSATRPTE----SDVQSFLLIMDLKLAPGPVLIHCKHGKDRTG 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 261862269  94 VLVALALIESGMKYEDAI-QFIRQKRRGAINSKQLTYLEKYRPKQR 138
Cdd:cd14529  105 LVSALYRIVYGGSKEEANeDYRLSNRHLEGLRSGIALDSKGGVKGR 150
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 47-134 1.02e-04

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: 40.97  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269  47 VDWPfDDGAPPPGKVVEDWLSLL---KAKFYND-PgscVAVHCVAGLGRAPVLVALALIESGMKYEDA------IQFIRQ 116
Cdd:cd14554  143 TDWP-EQGVPKSGEGFIDFIGQVhktKEQFGQEgP---ITVHCSAGVGRTGVFITLSIVLERMRYEGVvdvfqtVKLLRT 218

                         90
                 ....*....|....*...
gi 261862269 117 KRRGAINSKQlTYLEKYR 134
Cdd:cd14554  219 QRPAMVQTED-QYQFCYR 235
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 49-126 1.56e-04

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: 40.12  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269  49 WPfDDGAPPPGKVVEDWLSLLKAKFYNDPgscVAVHCVAGLGRAPVL----VALALIESGMKYE--DAIQFIRQKRRGAI 122
Cdd:cd14596  114 WP-DHGTPQSSDQLVKFICYMRKVHNTGP---IVVHCSAGIGRAGVLicvdVLLSLIEKDLSFNikDIVREMRQQRYGMI 189


                 ....
gi 261862269 123 NSKQ 126
Cdd:cd14596  190 QTKD 193
DUSP13B cd14577
dual specificity protein phosphatase 13 isoform B; Dual specificity protein phosphatase 13 ...
 75-132 1.71e-04

dual specificity protein phosphatase 13 isoform B; Dual specificity protein phosphatase 13 isoform B (DUSP13B), also called testis- and skeletal-muscle-specific DSP (TMDP) or dual specificity phosphatase SKRP4, 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. DUSP13B 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. DUSP13B inactivates MAPK activation in the order of selectivity, JNK = p38 > ERK in cells. It may play a role in protection from external stress during spermatogenesis.


Pssm-ID: 350425 [Multi-domain]  Cd Length: 163  Bit Score: 39.78  E-value: 1.71e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261862269  75 NDPGSCVAVHCVAGLGRAPVLV-ALALIESGMKYEDAIQFIRQKRRGAINS---KQLTYLEK 132
Cdd:cd14577  100 SSPNGRVLVHCAMGISRSATLVlAFLMICEDLTLVDAIQTVRAHRDICPNSgflRQLRELDN 161
DSP_MKP_classIII cd14568
dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; ...
 78-118 1.78e-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: 39.32  E-value: 1.78e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 261862269  78 GSCVAVHCVAGLGRAPVL-VALALIESGMKYEDAIQFIRQKR 118
Cdd:cd14568   79 NKRVLVHCLAGISRSATIaIAYIMKHMRMSLDDAYRFVKEKR 120
PTP_tensin-3 cd14561
protein tyrosine phosphatase-like domain of tensin-3; Tensin-3 (TNS3) is also called ...
 9-97 3.49e-04

protein tyrosine phosphatase-like domain of tensin-3; Tensin-3 (TNS3) is also called tensin-like SH2 domain-containing protein 1 (TENS1) or tumor endothelial marker (TEM6). It is part of the tensin family of intracellular proteins (tensin-1, -2, -3 and -4), which act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. Tensin-3 contributes to cell migration, anchorage-independent growth, tumorigenesis, and metastasis of cancer cells. It cooperates with Dock5, an exchange factor for the small GTPase Rac, for osteoclast activity to ensure the correct organization of podosomes. Tensin-3 contains an N-terminal region with a protein tyrosine phosphatase (PTP)-like domain followed by a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains.


Pssm-ID: 350409 [Multi-domain]  Cd Length: 159  Bit Score: 38.77  E-value: 3.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269   9 EALAGNLQDL-----KKYGAT-TVVRVCEVTYDKTPLEKDgITVVDWPfDDGAPPPGKV------VEDWLSllkakfyND 76
Cdd:cd14561   21 ETYLHNLQDVtrmlkSKHGDNyLVLNLSEKRYELTKLNPK-IMDVGWP-DLHAPPLDKMctickaMESWLN-------SD 91

                         90       100
                 ....*....|....*....|.
gi 261862269  77 PGSCVAVHCVAGLGRAPVLVA 97
Cdd:cd14561   92 PLHVVVIHCRGGKGRIGVVIS 112
DSP_slingshot cd14513
dual specificity phosphatase domain of slingshot family phosphatases; The slingshot (SSH) ...
 8-133 4.01e-04

dual specificity phosphatase domain of slingshot family phosphatases; The slingshot (SSH) family of dual specificity protein phosphatases is composed of Drosophila slingshot phosphatase and its vertebrate homologs: SSH1, SSH2 and SSH3. Its members specifically dephosphorylate and reactivate Ser-3-phosphorylated cofilin (P-cofilin), an actin-binding protein that plays an essential role in actin filament dynamics. In Drosophila, loss of ssh gene function causes prominent elevation in the levels of P-cofilin and filamentous actin and disorganized epidermal cell morphogenesis, including bifurcation phenotypes of bristles and wing hairs. SSH family phosphatases contain an N-terminal, SSH family-specific non-catalytic (SSH-N) domain, followed by a short domain with similarity to the C-terminal domain of the chromatin-associated protein DEK, and a dual specificity phosphatase catalytic domain. In addition, many members contain a C-terminal tail. The SSH-N domain plays critical roles in P-cofilin recognition, F-actin-mediated activation, and subcellular localization of SSHs.


Pssm-ID: 350363 [Multi-domain]  Cd Length: 139  Bit Score: 38.14  E-value: 4.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269   8 SEALAGNLQDLKKYGATTVVRV-CEV--------TYDKtplekdgITVVD------WPFDDgapppgkvvEDWLSLLKAK 72
Cdd:cd14513   12 SEWNASNLEELQNNGVKYILNVtREIdnffpgrfTYHN-------IRVWDeestnlLPYWN---------ETYRFIKEAR 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 261862269  73 fynDPGSCVAVHCVAGLGR-APVLVALALIESGMKYEDAIQFIrQKRRGAINSKQ--LTYLEKY 133
Cdd:cd14513   76 ---RKGSKVLVHCKMGVSRsASTVIAYAMKEYGWSLEQALEHV-KERRSCIKPNPgfLRQLITY 135
DSP_MKP_classI cd14565
dual specificity phosphatase domain of class I mitogen-activated protein kinase phosphatase; ...
 8-118 4.48e-04

dual specificity phosphatase domain of class I 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 I MKPs consist of DUSP1/MKP-1, DUSP2 (PAC1), DUSP4/MKP-2 and DUSP5. They are all mitogen- and stress-inducible nuclear 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: 350413 [Multi-domain]  Cd Length: 138  Bit Score: 38.14  E-value: 4.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269   8 SEALAGNLQDLKKYGATTVVRVC---------EVTYDKTPLEKDGITVVDWPFDDGApppgkvveDWLSLLKAKfyndpG 78
Cdd:cd14565   12 SAYHASRREVLKALGITAVLNVSrncpnhfedHFQYKSIPVEDSHNADISSWFEEAI--------GFIDKVKAS-----G 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 261862269  79 SCVAVHCVAGLGRAPVlVALA-LIES-GMKYEDAIQFIRQKR 118
Cdd:cd14565   79 GRVLVHCQAGISRSAT-ICLAyLMTTrRVRLNEAFDYVKQRR 119
DSP_DUSP11 cd17665
dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar ...
 57-118 1.13e-03

dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar proteins; dual specificity protein phosphatase 11 (DUSP11), also known as RNA/RNP complex-1-interacting phosphatase or phosphatase that interacts with RNA/RNP complex 1 (PIR1), has RNA 5'-triphosphatase and diphosphatase activity, but only poor protein-tyrosine phosphatase activity. It has activity for short RNAs but is less active toward mononucleotide triphosphates, suggesting that its primary function in vivo is to dephosphorylate RNA 5'-ends. It may play a role in nuclear mRNA metabolism. Also included in this subfamily is baculovirus RNA 5'-triphosphatase for Autographa californica nuclear polyhedrosis virus.


Pssm-ID: 350503  Cd Length: 169  Bit Score: 37.26  E-value: 1.13e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261862269  57 PPGKVVEDWLSLLKaKFYN---DPGSCVAVHCVAGLGRAPVLVALALIES-GMKYEDAIQFIRQKR 118
Cdd:cd17665   90 PDDKTIQSFKDAVK-DFLEknkDNDKLIGVHCTHGLNRTGYLICRYLIDVdGMSPDDAIEAFEQAR 154
DUSP13A cd14580
dual specificity protein phosphatase 13 isoform A; Dual specificity protein phosphatase 13 ...
 75-131 1.33e-03

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: 37.04  E-value: 1.33e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261862269  75 NDPGSCVAVHCVAGLGRAPVLV-ALALIESGMKYEDAIQFIRQKRRGAINS---KQLTYLE 131
Cdd:cd14580   82 NTPGAKVLVHCAVGVSRSATLVlAYLMIYHQLSLVQAIKTVKERRWIFPNRgflKQLRKLD 142
DSP_DUSP22_15 cd14519
dual specificity phosphatase domain of dual specificity protein phosphatase 22, 15, and ...
 78-118 1.47e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 22, 15, and similar proteins; Dual specificity protein phosphatase 22 (DUSP22, also known as VHX) and 15 (DUSP15, also known as VHY) function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). They 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. The both contain N-terminal myristoylation recognition sequences and myristoylation regulates their subcellular location. DUSP22 negatively regulates the estrogen receptor-alpha-mediated signaling pathway and the IL6-leukemia inhibitory factor (LIF)-STAT3-mediated signaling pathway. DUSP15 has been identified as a regulator of oligodendrocyte differentiation. DUSP22 is a single domain protein containing only the catalytic dual specificity phosphatase domain while DUSP15 contains a short C-terminal tail.


Pssm-ID: 350369 [Multi-domain]  Cd Length: 136  Bit Score: 36.57  E-value: 1.47e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 261862269  78 GSCVaVHCVAGLGRApVLVALALIES--GMKYEDAIQFIRQKR 118
Cdd:cd14519   78 GNVL-VHCLAGVSRS-VTIVAAYLMTvtDLGWRDALKAVRAAR 118
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 44-118 1.50e-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: 37.23  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269  44 ITVVDWPfDDGAPPPGKVVEDWLSLLKAKFYNDPGScVAVHCVAGLGRAPVLV----ALALIESGMKYE--DAIQFIRQK 117
Cdd:cd14601  111 IQYIAWP-DHGVPDDSSDFLDFVCLVRNKRAGKDEP-VVVHCSAGIGRTGVLItmetAMCLIECNQPVYplDIVRTMRDQ 188


                 .
gi 261862269 118 R 118
Cdd:cd14601  189 R 189
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 46-105 2.21e-03

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


Pssm-ID: 350360 [Multi-domain]  Cd Length: 177  Bit Score: 36.57  E-value: 2.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 261862269  46 VVDWPFDDGAPPP-------GKVVEDWLSllkakfyNDPGSCVAVHCVAGLGRAPVLVALALIESGM 105
Cdd:cd14510   76 VERVPIDDHNVPTldemlsfTAEVREWMA-------ADPKNVVAIHCKGGKGRTGTMVCAWLIYSGQ 135
DSP_DUSP16 cd14646
dual specificity phosphatase domain of dual specificity protein phosphatase 16; Dual ...
 70-118 2.25e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 16; Dual specificity protein phosphatase 16 (DUSP16), also called mitogen-activated protein kinase (MAPK) phosphatase 7 (MKP-7), 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. DUSP16/MKP-7 plays an essential role in perinatal survival and selectively controls the differentiation and cytokine production of myeloid cells. It is acetylated by Mycobacterium tuberculosis Eis protein, which leads to the inhibition of JNK-dependent autophagy, phagosome maturation, and ROS generation, and thus, initiating suppression of host immune responses. DUSP16/MKP-7 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: 350494 [Multi-domain]  Cd Length: 145  Bit Score: 36.16  E-value: 2.25e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 261862269  70 KAKFYNDpgsCVAVHCVAGLGR-APVLVALALIESGMKYEDAIQFIRQKR 118
Cdd:cd14646   76 KAKASNG---RVLVHCLAGISRsATIAIAYIMKRMDMSLDEAYRFVKEKR 122
DSP_MKP cd14512
dual specificity phosphatase domain of mitogen-activated protein kinase phosphatase; ...
 78-118 2.36e-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: 36.31  E-value: 2.36e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 261862269  78 GSCVAVHCVAGLGR-APVLVALALIESGMKYEDAIQFIRQKR 118
Cdd:cd14512   79 NGGVLVHCLAGISRsATIAIAYLMKRMRMSLDEAYDFVKEKR 120
DUSP26 cd14578
dual specificity protein phosphatase 26; Dual specificity protein phosphatase 26 (DUSP26), ...
 11-132 2.74e-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: 35.97  E-value: 2.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269  11 LAGNLQDLKKYGATTVVRVC-------EVTYDKTPLEKDGITVVDWPFDDGAP---PPGKVVEDWLSllkakfynDPGSC 80
Cdd:cd14578   15 IAANRRELRRLGITHILNAShskwrggAEYYEGLNIRYLGIEAHDSPAFDMSIhfyPAADFIHRALS--------QPGGK 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 261862269  81 VAVHCVAGLGRAPVLV-ALALIESGMKYEDAIQFIRQkRRGAINSK----QLTYLEK 132
Cdd:cd14578   87 ILVHCAVGVSRSATLVlAYLMIHHHMTLVEAIKTVKD-HRGIIPNRgflrQLLALDR 142
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 49-126 3.52e-03

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) and type 6 (PTPN6) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 and PTPN6, are also called SH2 domain-containing tyrosine phosphatase 2 (SHP2) and 1 (SHP1), respectively. They contain two tandem SH2 domains: a catalytic PTP domain, and a C-terminal tail with regulatory properties. Although structurally similar, they have different localization and different roles in signal transduction. PTPN11/SHP2 is expressed ubiquitously and plays a positive role in cell signaling, leading to cell activation, while PTPN6/SHP1 expression is restricted mainly to hematopoietic and epithelial cells and functions as a negative regulator of signaling events.


Pssm-ID: 350392 [Multi-domain]  Cd Length: 251  Bit Score: 36.29  E-value: 3.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269  49 WPfDDGAPP-PGKVvedwLSLL-----KAKFYNDPGSCVaVHCVAGLGR-APVLVALALIE--------SGMKYEDAIQF 113
Cdd:cd14544  150 WP-DHGVPSdPGGV----LNFLedvnqRQESLPHAGPIV-VHCSAGIGRtGTFIVIDMLLDqikrkgldCDIDIQKTIQM 223

                         90
                 ....*....|...
gi 261862269 114 IRQKRRGAINSKQ 126
Cdd:cd14544  224 VRSQRSGMVQTEA 236
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 15-98 3.85e-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: 36.04  E-value: 3.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269  15 LQDLK--KYGATTVVRVCEVTydktplekdgitvvDWPfDDGAPPPGKVVEDWLSLLKAKFYNDpGSCVAVHCVAGLGRA 92
Cdd:cd14616  114 IRDLKieRHGDYMMVRQCNFT--------------SWP-EHGVPESSAPLIHFVKLVRASRAHD-NTPMIVHCSAGVGRT 177


                 ....*.
gi 261862269  93 PVLVAL 98
Cdd:cd14616  178 GVFIAL 183
DUSP3 cd14579
dual specificity protein phosphatase 3; Dual specificity protein phosphatase 3 (DUSP3), also ...
 81-130 5.20e-03

dual specificity protein phosphatase 3; Dual specificity protein phosphatase 3 (DUSP3), also called vaccinia H1-related phosphatase (VHR), 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. DUSP3 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 favors bisphosphorylated substrates over monophosphorylated ones, and prefers pTyr peptides over pSer/pThr peptides. Reported physiological substrates includes MAPKs ERK1/2, JNK, and p38, as well as STAT5, EGFR, and ErbB2. DUSP3 has been linked to breast and prostate cancer, and may also play a role in thrombosis.


Pssm-ID: 350427 [Multi-domain]  Cd Length: 168  Bit Score: 35.51  E-value: 5.20e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 261862269  81 VAVHCVAGLGRAPVLV-ALALIESGMKYEDAIQFIRQKRRGAINS---KQLTYL 130
Cdd:cd14579  111 VLVHCREGYSRSPTLViAYLMLRQKMDVKSALSTVRQKREIGPNDgflKQLCQL 164
DUSP14-like cd14514
dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is ...
 4-118 6.59e-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: 34.84  E-value: 6.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862269   4 HLQVSEALAGNLQDLKKYGATTVVrvcEVTYDKTPLEKDGITVVDWPFDDGappPGKVVEDWLSLLKAKFYN--DPGSCV 81
Cdd:cd14514    7 HLFLSGASAATPPLLLSRGITCII---NATTELPDPSYPGIEYLRVPVEDS---PHADLSPHFDEVADKIHQvkRRGGRT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 261862269  82 AVHCVAGLGRAPVLVALALiesgMKYE-----DAIQFIRQKR 118
Cdd:cd14514   81 LVHCVAGVSRSATLCLAYL----MKYEgmtlrEAYKHVKAAR 118
DSP_DUSP10 cd14567
dual specificity phosphatase domain of dual specificity protein phosphatase 10; Dual ...
 78-118 7.74e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 10; Dual specificity protein phosphatase 10 (DUSP10), also called mitogen-activated protein kinase (MAPK) phosphatase 5 (MKP-5), 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. DUSP10/MKP-5 coordinates skeletal muscle regeneration by negatively regulating mitochondria-mediated apoptosis. It is also an important regulator of intestinal epithelial barrier function and a suppressor of colon tumorigenesis. DUSP10/MKP-5 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: 350415 [Multi-domain]  Cd Length: 152  Bit Score: 34.73  E-value: 7.74e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 261862269  78 GSCVAVHCVAGLGRAP-VLVALALIESGMKYEDAIQFIRQKR 118
Cdd:cd14567   80 GKGVLVHCQAGVSRSAtIVIAYLMKHTRMTMTDAYKFVKNKR 121
 
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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