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Conserved domains on  [gi|399220337|ref|NP_001257765|]
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dual specificity protein phosphatase 14 [Rattus norvegicus]

Protein Classification

dual specificity protein phosphatase family protein( domain architecture ID 12998596)

dual specificity protein phosphatase family protein such as dual specificity phosphatases, which dephosphorylate phosphotyrosine, phosphoserine, and phosphothreonine residues, as well as tyrosine-specific protein phosphatases

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DUSP14 cd14572
dual specificity protein phosphatase 14; dual specificity protein phosphatase 14 (DUSP14), ...
20-169 1.53e-108

dual specificity protein phosphatase 14; dual specificity protein phosphatase 14 (DUSP14), also called mitogen-activated protein kinase (MAPK) phosphatase 6 (MKP-6) or MKP-1-like protein tyrosine phosphatase (MKP-L), 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. DUSP14 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. DUSP14 dephosphorylates JNK, ERK, and p38 in vitro. It also 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.


:

Pssm-ID: 350420 [Multi-domain]  Cd Length: 150  Bit Score: 307.18  E-value: 1.53e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  20 SEGDIGGIAQITSSLFLGRASVASNRHLLQARGITCVVNATIEIPNFNWPQFEYVKVPLADIPHAPIRLYFDTVADKIHS 99
Cdd:cd14572    1 SEGDLGGIAQITPSLYLSRGNVASNRHLLLSRGITCIVNATIEIPNFNWPQFEYVKVPLADMPHAPISLYFDSVADKIHS 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337 100 VSKKHGATLVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDYESQLFGKS 169
Cdd:cd14572   81 VGRKHGATLVHCAAGVSRSATLCIAYLMKYHRVSLLEAYNWVKARRPVIRPNVGFWRQLIDYERKLFGKS 150
 
Name Accession Description Interval E-value
DUSP14 cd14572
dual specificity protein phosphatase 14; dual specificity protein phosphatase 14 (DUSP14), ...
20-169 1.53e-108

dual specificity protein phosphatase 14; dual specificity protein phosphatase 14 (DUSP14), also called mitogen-activated protein kinase (MAPK) phosphatase 6 (MKP-6) or MKP-1-like protein tyrosine phosphatase (MKP-L), 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. DUSP14 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. DUSP14 dephosphorylates JNK, ERK, and p38 in vitro. It also 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.


Pssm-ID: 350420 [Multi-domain]  Cd Length: 150  Bit Score: 307.18  E-value: 1.53e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  20 SEGDIGGIAQITSSLFLGRASVASNRHLLQARGITCVVNATIEIPNFNWPQFEYVKVPLADIPHAPIRLYFDTVADKIHS 99
Cdd:cd14572    1 SEGDLGGIAQITPSLYLSRGNVASNRHLLLSRGITCIVNATIEIPNFNWPQFEYVKVPLADMPHAPISLYFDSVADKIHS 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337 100 VSKKHGATLVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDYESQLFGKS 169
Cdd:cd14572   81 VGRKHGATLVHCAAGVSRSATLCIAYLMKYHRVSLLEAYNWVKARRPVIRPNVGFWRQLIDYERKLFGKS 150
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
29-162 1.24e-47

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 152.44  E-value: 1.24e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337    29 QITSSLFLGRASVASNRHLLQARGITCVVNATIEIPNFNWPQFEYVKVPLADIPHAPIRLYFDTVADKIHSVSKKHGATL 108
Cdd:smart00195   3 EILPHLYLGSYSDALNLALLKKLGITHVINVTNEVPNYNGSDFTYLGVPIDDNTETKISPYFPEAVEFIEDAESKGGKVL 82
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 399220337   109 VHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDYE 162
Cdd:smart00195  83 VHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRPIISPNFGFLRQLIEYE 136
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
34-162 3.30e-43

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: 140.86  E-value: 3.30e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337   34 LFLGRASVASNRhLLQARGITCVVNATIEIPNFNwPQFEYVKVPLADIPHAPIRLYFDTVADKIHSVSKKHGATLVHCAA 113
Cdd:pfam00782   1 LYLGSKPTASDA-FLSKLGITAVINVTREVDLYN-SGILYLRIPVEDNHETNISKYLEEAVEFIDDARQKGGKVLVHCQA 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 399220337  114 GVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDYE 162
Cdd:pfam00782  79 GISRSATLIIAYLMKTRNLSLNEAYSFVKERRPGISPNFGFKRQLLEYE 127
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
30-165 7.11e-19

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 78.86  E-value: 7.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  30 ITSSLFLGRASvASNRHLLQARGITCVVNATIEIPNFNWPQ----FEYVKVPLADIpHAPIRLYFDTVADKIHSVSKKHG 105
Cdd:COG2453    4 IPGLLAGGPLP-GGGEADLKREGIDAVVSLTEEEELLLGLLeeagLEYLHLPIPDF-GAPDDEQLQEAVDFIDEALREGK 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337 106 ATLVHCAAGVSRSATLCIAYLMKfHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDYESQL 165
Cdd:COG2453   82 KVLVHCRGGIGRTGTVAAAYLVL-LGLSAEEALARVRAARPGAVETPAQRAFLERFAKRL 140
PRK12361 PRK12361
hypothetical protein; Provisional
27-158 2.14e-09

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 56.17  E-value: 2.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  27 IAQITSSLFLGRASVASNRHLLQARGITCVVNATIEIPNFNWP----QFEYVKVPLADipH-APIRLYFDTVADKIHSVS 101
Cdd:PRK12361  95 IQKIDENLYLGCRLFPADLEKLKSNKITAILDVTAEFDGLDWSlteeDIDYLNIPILD--HsVPTLAQLNQAINWIHRQV 172
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 399220337 102 KKHGATLVHCAAGVSRSATLCIAYLM-KFHNLCLLEAYNWVKARRPVIRPNLgfwRQL 158
Cdd:PRK12361 173 RANKSVVVHCALGRGRSVLVLAAYLLcKDPDLTVEEVLQQIKQIRKTARLNK---RQL 227
 
Name Accession Description Interval E-value
DUSP14 cd14572
dual specificity protein phosphatase 14; dual specificity protein phosphatase 14 (DUSP14), ...
20-169 1.53e-108

dual specificity protein phosphatase 14; dual specificity protein phosphatase 14 (DUSP14), also called mitogen-activated protein kinase (MAPK) phosphatase 6 (MKP-6) or MKP-1-like protein tyrosine phosphatase (MKP-L), 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. DUSP14 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. DUSP14 dephosphorylates JNK, ERK, and p38 in vitro. It also 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.


Pssm-ID: 350420 [Multi-domain]  Cd Length: 150  Bit Score: 307.18  E-value: 1.53e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  20 SEGDIGGIAQITSSLFLGRASVASNRHLLQARGITCVVNATIEIPNFNWPQFEYVKVPLADIPHAPIRLYFDTVADKIHS 99
Cdd:cd14572    1 SEGDLGGIAQITPSLYLSRGNVASNRHLLLSRGITCIVNATIEIPNFNWPQFEYVKVPLADMPHAPISLYFDSVADKIHS 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337 100 VSKKHGATLVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDYESQLFGKS 169
Cdd:cd14572   81 VGRKHGATLVHCAAGVSRSATLCIAYLMKYHRVSLLEAYNWVKARRPVIRPNVGFWRQLIDYERKLFGKS 150
DUSP18_21 cd14573
dual specificity protein phosphatases 18 and 21; This subfamily contains dual specificity ...
26-183 1.06e-76

dual specificity protein phosphatases 18 and 21; This subfamily contains dual specificity protein phosphatase 18 (DUSP18), dual specificity protein phosphatase 21 (DUSP21), 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. DUSP18, also called low molecular weight dual specificity phosphatase 20 (LMW-DSP20), is a catalytically active phosphatase with a preference for phosphotyrosine over phosphoserine/threonine oligopeptides in vitro. In vivo, it has been shown to interact and dephosphorylate SAPK/JNK, and may play a role in regulating the SAPK/JNK pathway. DUSP21 is also called low molecular weight dual specificity phosphatase 21 (LMW-DSP21). Its gene has been identified as a potential therapeutic target in human hepatocellular carcinoma. DUSP18 and DUSP21 target to opposing sides of the mitochondrial inner membrane.


Pssm-ID: 350421 [Multi-domain]  Cd Length: 158  Bit Score: 226.98  E-value: 1.06e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  26 GIAQITSSLFLGRASVASNRHLLQARGITCVVNATIEIPNFNWPQFEYVKVPLADIPHAPIRLYFDTVADKIHSVSKKHG 105
Cdd:cd14573    1 RLSRITESLYLSNGVAANNRTLLAANRITCVINVSLEVANGLPPGIEYLHVPVADSPDTRLRDYFDPIADKIHTVEARGG 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 399220337 106 ATLVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDYESQLFGKSSVKMVQTPYGIIPD 183
Cdd:cd14573   81 RTLLHCVAGVSRSATLCLAYLMKYHAMSLLDAHTWVKSCRPIIRPNNGFWEQLIHYEFELFGKNTVHMITSPVGMIPD 158
DUSP14-like cd14514
dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is ...
27-160 8.99e-76

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: 223.58  E-value: 8.99e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  27 IAQITSSLFLGRASVASNRHLLQaRGITCVVNATIEIPNFNWPQFEYVKVPLADIPHAPIRLYFDTVADKIHSVSKKHGA 106
Cdd:cd14514    1 ISQITPHLFLSGASAATPPLLLS-RGITCIINATTELPDPSYPGIEYLRVPVEDSPHADLSPHFDEVADKIHQVKRRGGR 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 399220337 107 TLVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLID 160
Cdd:cd14514   80 TLVHCVAGVSRSATLCLAYLMKYEGMTLREAYKHVKAARPIIRPNVGFWRQLIE 133
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
27-160 7.74e-54

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: 168.11  E-value: 7.74e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  27 IAQITSSLFLGRASVASNRHLLQARGITCVVNATIEIPNFNWPQ-FEYVKVPLADIPHAPIRLYFDTVADKIHSVSKKHG 105
Cdd:cd14498    1 PSEILPGLYLGSLDAAQDKELLKKLGITHILNVAGEPPPNKFPDgIKYLRIPIEDSPDEDILSHFEEAIEFIEEALKKGG 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 399220337 106 ATLVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLID 160
Cdd:cd14498   81 KVLVHCQAGVSRSATIVIAYLMKKYGWSLEEALELVKSRRPIISPNPGFLKQLKE 135
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
29-162 1.24e-47

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 152.44  E-value: 1.24e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337    29 QITSSLFLGRASVASNRHLLQARGITCVVNATIEIPNFNWPQFEYVKVPLADIPHAPIRLYFDTVADKIHSVSKKHGATL 108
Cdd:smart00195   3 EILPHLYLGSYSDALNLALLKKLGITHVINVTNEVPNYNGSDFTYLGVPIDDNTETKISPYFPEAVEFIEDAESKGGKVL 82
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 399220337   109 VHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDYE 162
Cdd:smart00195  83 VHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRPIISPNFGFLRQLIEYE 136
DSP_MKP_classI cd14565
dual specificity phosphatase domain of class I mitogen-activated protein kinase phosphatase; ...
28-164 3.48e-45

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: 146.38  E-value: 3.48e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  28 AQITSSLFLGRASVASNRHLLQARGITCVVNATIEIPNFNWPQFEYVKVPLADIPHAPIRLYFDTVADKIHSVSKKHGAT 107
Cdd:cd14565    2 VEILPFLYLGSAYHASRREVLKALGITAVLNVSRNCPNHFEDHFQYKSIPVEDSHNADISSWFEEAIGFIDKVKASGGRV 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 399220337 108 LVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDYESQ 164
Cdd:cd14565   82 LVHCQAGISRSATICLAYLMTTRRVRLNEAFDYVKQRRSVISPNFNFMGQLLQYESQ 138
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
34-162 3.30e-43

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: 140.86  E-value: 3.30e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337   34 LFLGRASVASNRhLLQARGITCVVNATIEIPNFNwPQFEYVKVPLADIPHAPIRLYFDTVADKIHSVSKKHGATLVHCAA 113
Cdd:pfam00782   1 LYLGSKPTASDA-FLSKLGITAVINVTREVDLYN-SGILYLRIPVEDNHETNISKYLEEAVEFIDDARQKGGKVLVHCQA 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 399220337  114 GVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDYE 162
Cdd:pfam00782  79 GISRSATLIIAYLMKTRNLSLNEAYSFVKERRPGISPNFGFKRQLLEYE 127
DUSP28 cd14574
dual specificity protein phosphatase 28; Dual specificity protein phosphatase 28 (DUSP28), ...
27-165 5.55e-41

dual specificity protein phosphatase 28; Dual specificity protein phosphatase 28 (DUSP28), also called VHP, functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It is an atypical DUSP that 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 has been implicated in hepatocellular carcinoma progression and in migratory activity and drug resistance of pancreatic cancer cells. DUSP28 has an exceptionally low phosphatase activity due to the presence of bulky residues in the active site pocket resulting in low accessibility.


Pssm-ID: 350422 [Multi-domain]  Cd Length: 140  Bit Score: 135.67  E-value: 5.55e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  27 IAQITSSLFLGRASVASNRHLLQARGITCVVNATIEIPNFNWPQFEYVKVPLADIPHAPIRLYFDTVADKIHSVSKKHGA 106
Cdd:cd14574    1 LCRVTDSLFISNARAACNEELLAREGVTLCVNVSRQQPFPRAPRVSTLRVPVFDDPAEDLYRHFEQCADAIEAAVRRGGK 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 399220337 107 TLVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDYESQL 165
Cdd:cd14574   81 CLVYCKNGRSRSAAVCIAYLMKHRGLSLQDAFQVVKAARPVAEPNPGFWSQLQRYEEEL 139
DUSP3-like cd14515
dual specificity protein phosphatases 3, 13, 26, 27, and similar domains; This family is ...
29-165 6.37e-39

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: 130.41  E-value: 6.37e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  29 QITSSLFLGRASVASNRHLLQARGITCVVNA---TIEIPNFNWPQF------EYVKVPLADIPHAPIRLYFDTVADKIHS 99
Cdd:cd14515    3 EVWPGIYIGDESTAKNKAKLKKLGITHVLNAaegKKNGEVNTNAKFykgsgiIYLGIPASDLPTFDISQYFDEAADFIDK 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 399220337 100 -VSKKHGATLVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPvIRPNLGFWRQLIDYESQL 165
Cdd:cd14515   83 aLSDPGGKVLVHCVEGVSRSATLVLAYLMIYQNMTLEEAIRTVRKKRE-IRPNRGFLQQLCELNDKL 148
DSP_MKP cd14512
dual specificity phosphatase domain of mitogen-activated protein kinase phosphatase; ...
29-161 4.83e-38

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: 127.99  E-value: 4.83e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  29 QITSSLFLGRASVASNRHLLQARGITCVVNATIEIPNFNW-PQFEYVKVPLADIPHAPIRLYFDTVADKIHSVSKKHGAT 107
Cdd:cd14512    3 RILPNLYLGSQRDSLNLELMQQLGIGYVLNVSNTCPNPDFiGLFHYKRIPVNDSFCQNISPWFDEAIEFIEEAKASNGGV 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 399220337 108 LVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDY 161
Cdd:cd14512   83 LVHCLAGISRSATIAIAYLMKRMRMSLDEAYDFVKEKRPTISPNFNFMGQLLDF 136
DSP_DUSP2 cd14641
dual specificity phosphatase domain of dual specificity protein phosphatase 2; Dual ...
25-166 9.82e-38

dual specificity phosphatase domain of dual specificity protein phosphatase 2; Dual specificity protein phosphatase 2 (DUSP2), also called dual specificity protein phosphatase PAC-1, functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other mitogen-activated protein kinase (MAPK) phosphatases (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 I subfamily and is a mitogen- and stress-inducible nuclear MKP. DUSP2 can preferentially dephosphorylate ERK1/2 and p38, but not JNK in vitro. It is predominantly expressed in hematopoietic tissues with high T-cell content, such as thymus, spleen, lymph nodes, peripheral blood and other organs such as the brain and liver. It has a critical and positive role in inflammatory responses. DUSP2 mRNA and protein are significantly reduced in most solid cancers including breast, colon, lung, ovary, kidney and prostate, and the suppression of DUSP2 is associated with tumorigenesis and malignancy. DUSP2 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: 350489 [Multi-domain]  Cd Length: 144  Bit Score: 127.67  E-value: 9.82e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  25 GGIAQITSSLFLGRASVASNRHLLQARGITCVVNATIEIPNFNWPQFEYVKVPLADIPHAPIRLYFDTVADKIHSVSKKH 104
Cdd:cd14641    2 GGPVEILPFLFLGSAHHSSRRETLESLGITAVLNVSSSCPNYFEGQFQYKSIPVEDSHMADISAWFQEAIDFIDSVKNSG 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 399220337 105 GATLVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDYESQLF 166
Cdd:cd14641   82 GRVLVHCQAGISRSATICLAYLIQSQRVRLDEAFDFVKQRRGVISPNFSFMGQLLQFETQVL 143
DSP_MKP_classIII cd14568
dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; ...
27-165 1.02e-35

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: 122.14  E-value: 1.02e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  27 IAQITSSLFLGRASVASNRHLLQARGITCVVNATIEIPNFNW-PQFEYVKVPLADIPHAPIRLYFDTVADKIHSVSKKHG 105
Cdd:cd14568    1 PTRILPHLYLGSQRDVLDKDLMQRNGISYVLNVSNTCPKPDFiPDSHFLRIPVNDSYCEKLLPWLDKAVEFIEKARASNK 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337 106 ATLVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDYESQL 165
Cdd:cd14568   81 RVLVHCLAGISRSATIAIAYIMKHMRMSLDDAYRFVKEKRPTISPNFNFLGQLLEFEKKL 140
DSP_slingshot cd14513
dual specificity phosphatase domain of slingshot family phosphatases; The slingshot (SSH) ...
29-165 2.32e-35

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: 121.35  E-value: 2.32e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  29 QITSSLFLGRASVASNRHLLQARGITCVVNATIEIPNFNWPQFEYVKVPLADIPHAPIRLYFDTVADKIHSVSKKHGATL 108
Cdd:cd14513    3 KIFDHLYLGSEWNASNLEELQNNGVKYILNVTREIDNFFPGRFTYHNIRVWDEESTNLLPYWNETYRFIKEARRKGSKVL 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 399220337 109 VHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDYESQL 165
Cdd:cd14513   83 VHCKMGVSRSASTVIAYAMKEYGWSLEQALEHVKERRSCIKPNPGFLRQLITYEGML 139
DSP_DUSP10 cd14567
dual specificity phosphatase domain of dual specificity protein phosphatase 10; Dual ...
27-165 2.92e-33

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: 116.39  E-value: 2.92e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  27 IAQITSSLFLGRASVASNRHLLQARGITCVVNATIEIPNFNW--PQFEYVKVPLADIPHAPIRLYFDTVADKIHSVSKKH 104
Cdd:cd14567    1 LTPILPFLYLGNERDAQDIDTLQRLNIGYVLNVTTHLPLYHEgkGGFRYKRLPATDSNKQNLRQYFEEAFEFIEEAHQSG 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 399220337 105 GATLVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDYESQL 165
Cdd:cd14567   81 KGVLVHCQAGVSRSATIVIAYLMKHTRMTMTDAYKFVKNKRPIISPNLNFMGQLLEFEEDL 141
DSP_MKP_classII cd14566
dual specificity phosphatase domain of class II mitogen-activated protein kinase phosphatase; ...
28-161 8.00e-33

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: 114.72  E-value: 8.00e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  28 AQITSSLFLGRASVASNRHLLQARGITCVVNATIEIPN--FNWPQFEYVKVPLADIPHAPIRLYFDTVADKIHSVSKKHG 105
Cdd:cd14566    2 VEILPFLYLGNAKDSANIDLLKKYNIKYILNVTPNLPNtfEEDGGFKYLQIPIDDHWSQNLSAFFPEAISFIDEARSKKC 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 399220337 106 ATLVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDY 161
Cdd:cd14566   82 GVLVHCLAGISRSVTVTVAYLMQKLHLSLNDAYDFVKKRKSNISPNFNFMGQLLDF 137
DSP_DUSP19 cd14523
dual specificity phosphatase domain of dual specificity protein phosphatase 19; Dual ...
27-162 1.01e-32

dual specificity phosphatase domain of dual specificity protein phosphatase 19; Dual specificity protein phosphatase 19 (DUSP19), also called low molecular weight dual specificity phosphatase 3 (LMW-DSP3) or stress-activated protein kinase (SAPK) pathway-regulating phosphatase 1 (SKRP1), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It 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. DUSP19 interacts with the MAPK kinase MKK7, a JNK activator, and inactivates the JNK MAPK pathway.


Pssm-ID: 350373 [Multi-domain]  Cd Length: 137  Bit Score: 114.37  E-value: 1.01e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  27 IAQITSSLFLGRASVASNRHLLQARGITCVVNATIEIPNFNWPQFEYVKVPLADIPHAPIRLYFDTVADKIHSVSKKHGA 106
Cdd:cd14523    2 VGVIKPWLLLSSQDVAHDLETLKKHKVTHILNVAYGVENAFPDDFTYKTISILDLPETDITSYFPECFEFIDEAKSQDGV 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 399220337 107 TLVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDYE 162
Cdd:cd14523   82 VLVHCNAGVSRSASIVIGYLMATENLSFEDAFSLVKNARPSIRPNPGFMEQLKEYQ 137
DSP_DUSP4 cd14640
dual specificity phosphatase domain of dual specificity protein phosphatase 4; Dual ...
29-166 1.95e-32

dual specificity phosphatase domain of dual specificity protein phosphatase 4; Dual specificity protein phosphatase 4 (DUSP4), also called mitogen-activated protein kinase (MAPK) phosphatase 2 (MKP-2), 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 I subfamily and is a mitogen- and stress-inducible nuclear MKP. DUSP4 regulates either ERK or c-JUN N-terminal kinase (JNK), depending on the cell type. It dephosphorylates nuclear JNK and induces apoptosis in diffuse large B cell lymphoma (DLBCL) cells. It acts as a negative regulator of macrophage M1 activation and inhibits inflammation during macrophage-adipocyte interaction. It has been linked to different aspects of cancer: it may have a role in the development of ovarian cancers, oesophagogastric rib metastasis, and pancreatic tumours; it may also be a candidate tumor suppressor gene, with its deletion implicated in breast cancer, prostate cancer, and gliomas. DUSP4/MKP-2 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: 350488 [Multi-domain]  Cd Length: 141  Bit Score: 113.98  E-value: 1.95e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  29 QITSSLFLGRASVASNRHLLQARGITCVVNATIEIPNFNWPQFEYVKVPLADIPHAPIRLYFDTVADKIHSVSKKHGATL 108
Cdd:cd14640    3 EILPFLYLGSAYHAARRDMLDALGITALLNVSSDCPNHFEGHYQYKCIPVEDNHKADISSWFMEAIEYIDSVKDCNGRVL 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 399220337 109 VHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDYESQLF 166
Cdd:cd14640   83 VHCQAGISRSATICLAYLMMKKRVRLEEAFEFVKQRRSIISPNFSFMGQLLQFESQVL 140
DSP_DUSP1 cd14638
dual specificity phosphatase domain of dual specificity protein phosphatase 1; Dual ...
29-177 1.15e-31

dual specificity phosphatase domain of dual specificity protein phosphatase 1; Dual specificity protein phosphatase 1 (DUSP1), also called mitogen-activated protein kinase (MAPK) phosphatase 1 (MKP-1), 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 I subfamily and is a mitogen- and stress-inducible nuclear MKP. Human MKP-1 dephosphorylates MAPK1/ERK2, regulating its activity during the meiotic cell cycle. Although initially MKP-1 was considered to be ERK-specific, it has been shown that MKP-1 also dephosphorylates both JNK and p38 MAPKs. DUSP1/MKP-1 is involved in various functions, including proliferation, differentiation, and apoptosis in normal cells. It is a central regulator of a variety of functions in the immune, metabolic, cardiovascular, and nervous systems. It 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: 350486 [Multi-domain]  Cd Length: 151  Bit Score: 112.08  E-value: 1.15e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  29 QITSSLFLGRASVASNRHLLQARGITCVVNATIEIPNFNWPQFEYVKVPLADIPHAPIRLYFDTVADKIHSVSKKHGATL 108
Cdd:cd14638    3 EILPFLYLGSAYHASRKDMLDTLGITALINVSANCPNHFEGHYQYKSIPVEDNHKADISSWFNEAIDFIDSVKNAGGRVF 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 399220337 109 VHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDYESQLFGKSSVKMVQTP 177
Cdd:cd14638   83 VHCQAGISRSATICLAYLMRTNRVKLDEAFEFVKQRRSIISPNFSFMGQLLQFESQVLAPSCSAEAGSP 151
DSP_DUSP5 cd14639
dual specificity phosphatase domain of dual specificity protein phosphatase 5; Dual ...
29-164 2.32e-28

dual specificity phosphatase domain of dual specificity protein phosphatase 5; Dual specificity protein phosphatase 5 (DUSP5) functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other mitogen-activated protein kinase (MAPK) phosphatases (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 I subfamily and is a mitogen- and stress-inducible nuclear MKP. DUSP5 preferentially dephosphorylates extracellular signal-regulated kinase (ERK), and is involved in ERK signaling and ERK-dependent inflammatory gene expression in adipocytes. It also plays a role in regulating pressure-dependent myogenic cerebral arterial constriction, which is crucial for the maintenance of constant cerebral blood flow to the brain. DUSP5 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: 350487 [Multi-domain]  Cd Length: 138  Bit Score: 103.46  E-value: 2.32e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  29 QITSSLFLGRASVASNRHLLQARGITCVVNATIEIPNFNWPQFEYVKVPLADIPHAPIRLYFDTVADKIHSVSKKHGATL 108
Cdd:cd14639    3 EILPFLYLGSAYHASKCEFLANLHITALLNVSRRSSEACKGQYHYKWIPVEDSHTADISSHFQEAIDFIDCVRRAGGKVL 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 399220337 109 VHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDYESQ 164
Cdd:cd14639   83 VHCEAGISRSPTICMAYLMKTKRFRLEEAFDYIKQRRSLISPNFGFMGQLLQYESE 138
DUSP13A cd14580
dual specificity protein phosphatase 13 isoform A; Dual specificity protein phosphatase 13 ...
34-165 2.62e-28

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: 103.30  E-value: 2.62e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  34 LFLGRASVASNRHLLQARGITCVVNATIEI------PNFNWPQFEYVKVPLADIPHAPIRLYFDTVADKIHSVSKKHGA- 106
Cdd:cd14580    8 LFLGDLATAHNRFGLWKLGITHVLNAAHGKlfcqggDDFYGTSVDYYGVPANDLPDFDISPYFYSAAEFIHRALNTPGAk 87
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 399220337 107 TLVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRpVIRPNLGFWRQLIDYESQL 165
Cdd:cd14580   88 VLVHCAVGVSRSATLVLAYLMIYHQLSLVQAIKTVKERR-WIFPNRGFLKQLRKLDQQL 145
DSP_fungal_YVH1 cd14518
dual specificity phosphatase domain of fungal YVH1-like dual specificity protein phosphatase; ...
30-168 8.71e-28

dual specificity phosphatase domain of fungal YVH1-like dual specificity protein phosphatase; This family is composed of Saccharomyces cerevisiae dual specificity protein phosphatase Yvh1 and similar fungal proteins. Yvh1 could function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It regulates cell growth, sporulation, and glycogen accumulation. It plays an important role in ribosome assembly. Yvh1 associates transiently with late pre-60S particles and is required for the release of the nucleolar/nuclear pre-60S factor Mrt4, which is necessary to construct a translation-competent 60S subunit and mature ribosome stalk. Yvh1 contains an N-terminal catalytic dual specificity phosphatase domain and a C-terminal tail.


Pssm-ID: 350368 [Multi-domain]  Cd Length: 153  Bit Score: 102.40  E-value: 8.71e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  30 ITSSLFLGrASVASNRH-LLQARGITCVVNA-TIEIPNFNWPQFEYVKVPLADIPHAPIRLYFDTVADKIHS-------- 99
Cdd:cd14518    4 ILGGLYLG-GIEPLNRNrLLKAENITHILSViPGDVPEEYFKGYEHKQIEIDDVEDENILQHFPETNRFIDSalfgngkd 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 399220337 100 ---VSKKHGATLVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLidyesQLFGK 168
Cdd:cd14518   83 edeEKKHGGAVLVHCAMGKSRSVTVVIAYLMYKYNLSVSQALHAVRRKRPIAEPNDGFMEQL-----ELYHE 149
DSP_slingshot_1 cd14570
dual specificity phosphatase domain of slingshot homolog 1; Dual specificity protein ...
30-165 2.05e-27

dual specificity phosphatase domain of slingshot homolog 1; Dual specificity protein phosphatase slingshot homolog 1 (SSH1), also called SSH-like protein 1, is part of the slingshot (SSH) family, whose members specifically dephosphorylate and reactivate Ser-3-phosphorylated cofilin (P-cofilin), an actin-binding protein that plays an essential role in actin filament dynamics. SSH1 links NOD1 signaling to actin remodeling, facilitating the changes that leads to NF-kappaB activation and innate immune responses. There are at least two human SSH1 isoforms reported: hSSH-1L (long) and hSSH-1S (short). As SSH family phosphatases, they 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. They also contain C-terminal tails, differing in the lengths of the tail.


Pssm-ID: 350418 [Multi-domain]  Cd Length: 144  Bit Score: 100.92  E-value: 2.05e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  30 ITSSLFLGRASVASNRHLLQARGITCVVNATIEIPNFNWPQFEYVKVPLADIPHAPIRLYFDTVADKIHSVSKKHGATLV 109
Cdd:cd14570    7 IFDHLYLGSEWNASNLEELQGSGVGYILNVTREIDNFFPGLFAYHNIRVYDEETTDLLAHWNDAYHFINKAKKNHSKCLV 86
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 399220337 110 HCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDYESQL 165
Cdd:cd14570   87 HCKMGVSRSASTVIAYAMKEFGWSLEKAYNFVKQKRSITRPNAGFMRQLLEYEGIL 142
DSP_DUSP22_15 cd14519
dual specificity phosphatase domain of dual specificity protein phosphatase 22, 15, and ...
29-162 2.31e-27

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: 100.52  E-value: 2.31e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  29 QITSSLFLGRASVASNRHLLQARGITCVVnATIEIPNFNWPQFEYVKVPLADIPHAPIRLYFDTVADKIHSVSKKHGATL 108
Cdd:cd14519    3 KILPGLYVGNFRDAKDAEQLRENGITHIL-SIHDSARPLLEDIKYLCIPAADTPEQNISQHFRECINFIHEARLNGGNVL 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 399220337 109 VHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDYE 162
Cdd:cd14519   82 VHCLAGVSRSVTIVAAYLMTVTDLGWRDALKAVRAARPCANPNFGFQRQLQEFE 135
DSP_DUSP16 cd14646
dual specificity phosphatase domain of dual specificity protein phosphatase 16; Dual ...
26-165 2.64e-27

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: 100.87  E-value: 2.64e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  26 GIAQITSSLFLGRASVASNRHLLQARGITCVVNATIEIPNFNW-PQFEYVKVPLADIPHAPIRLYFDTVADKIHSVSKKH 104
Cdd:cd14646    2 GPTRILPHLYLGCQRDVLNKELMQQNGIGYVLNASNTCPKPDFiPESHFLRVPVNDSFCEKILPWLDKSVDFIEKAKASN 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 399220337 105 GATLVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDYESQL 165
Cdd:cd14646   82 GRVLVHCLAGISRSATIAIAYIMKRMDMSLDEAYRFVKEKRPTISPNFNFLGQLLDFEKKI 142
DUSP26 cd14578
dual specificity protein phosphatase 26; Dual specificity protein phosphatase 26 (DUSP26), ...
29-165 5.00e-26

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: 97.60  E-value: 5.00e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  29 QITSSLFLGRASVASNRHLLQARGITCVVNATI-----EIPNFNWPQFEYVKVPLADIPHAPIRLYFDTVADKIH-SVSK 102
Cdd:cd14578    3 EVWPGLYLGDQDIAANRRELRRLGITHILNASHskwrgGAEYYEGLNIRYLGIEAHDSPAFDMSIHFYPAADFIHrALSQ 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 399220337 103 KHGATLVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIrPNLGFWRQLIDYESQL 165
Cdd:cd14578   83 PGGKILVHCAVGVSRSATLVLAYLMIHHHMTLVEAIKTVKDHRGII-PNRGFLRQLLALDRRL 144
DSP_DUSP7 cd14643
dual specificity phosphatase domain of dual specificity protein phosphatase 7; Dual ...
29-165 1.57e-25

dual specificity phosphatase domain of dual specificity protein phosphatase 7; Dual specificity protein phosphatase 7 (DUSP7), also called mitogen-activated protein kinase (MAPK) phosphatase X (MKP-X) or dual specificity protein phosphatase PYST2, 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 II subfamily and is an ERK-selective cytoplasmic MKP. DUSP7 has been shown as an essential regulator of multiple steps in oocyte meiosis. Due to alternative promoter usage, the PYST2 gene gives rise to two isoforms, PYST2-S and PYST2-L. PYST2-L is over-expressed in leukocytes derived from AML and ALL patients as well as in some solid tumors and lymphoblastoid cell lines; it plays a role in cell-crowding. It 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: 350491 [Multi-domain]  Cd Length: 149  Bit Score: 96.24  E-value: 1.57e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  29 QITSSLFLGRASVASNRHLLQARGITCVVNATIEIPNF--NWPQFEYVKVPLADIPHAPIRLYFDTVADKIHSVSKKHGA 106
Cdd:cd14643    8 QILPYLYLGCAKDSTNLDVLGKYGIKYILNVTPNLPNMfeHDGEFKYKQIPISDHWSQNLSQFFPEAISFIDEARSKKCG 87
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 399220337 107 TLVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDYESQL 165
Cdd:cd14643   88 ILVHCLAGISRSVTVTVAYLMQKLNLSLNDAYDFVKRKKSNISPNFNFMGQLLDFERTL 146
DSP_slingshot_2 cd14569
dual specificity phosphatase domain of slingshot homolog 2; Dual specificity protein ...
29-167 2.04e-25

dual specificity phosphatase domain of slingshot homolog 2; Dual specificity protein phosphatase slingshot homolog 2 (SSH2), also called SSH-like protein 2, is part of the slingshot (SSH) family, whose members specifically dephosphorylate and reactivate Ser-3-phosphorylated cofilin (P-cofilin), an actin-binding protein that plays an essential role in actin filament dynamics. SSH2 has been identified as a target of protein kinase D1 that regulates cofilin phosphorylation and remodeling of the actin cytoskeleton during neutrophil chemotaxis. There are at least two human SSH2 isoforms reported: hSSH-2L (long) and hSSH-2. As SSH family phosphatases, they 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, hSSH-2L contains a long C-terminal tail while hSSH-2 does not.


Pssm-ID: 350417 [Multi-domain]  Cd Length: 144  Bit Score: 95.86  E-value: 2.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  29 QITSSLFLGRASVASNRHLLQARGITCVVNATIEIPNFNWPQFEYVKVPLADIPHAPIRLYFDTVAdKIHSVSKKHGAT- 107
Cdd:cd14569    6 QIFEHVFLGSEWNASNLEDLQNRGVRYILNVTREIDNFFPGLFEYHNIRVYDEEATDLLAYWNDTY-KFISKAKKHGSKc 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337 108 LVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDYESQLFG 167
Cdd:cd14569   85 LVHCKMGVSRSASTVIAYAMKEYGWNLDRAYDYVKERRTVTKPNPSFMRQLEEYQGILLA 144
DSP_STYX cd14522
dual specificity phosphatase-like domain of serine/threonine/tyrosine-interacting protein; ...
29-162 7.11e-25

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: 94.71  E-value: 7.11e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  29 QITSSLFLGRASVASNRHL--LQARGITCVV--NATIEI----PNFnwPQ-FEYVKVPLADIPHAPIRLYFDTVADKIHS 99
Cdd:cd14522    7 EILPGLYLGPYSAAMKSKLevLLKHGITHIVcvRQNIEAnfikPNF--PDhFRYLVLDVADNPTENIIRHFPTVKEFIDD 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 399220337 100 VSKKHGATLVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDYE 162
Cdd:cd14522   85 CLQTGGKVLVHGNAGISRSAALVIAYIMETYGLSYRDAFAYVQQRRFCINPNEGFVHQLKEYE 147
DSP_DUSP9 cd14644
dual specificity phosphatase domain of dual specificity protein phosphatase 9; Dual ...
29-165 1.07e-24

dual specificity phosphatase domain of dual specificity protein phosphatase 9; Dual specificity protein phosphatase 9 (DUSP9), also called mitogen-activated protein kinase (MAPK) phosphatase 4 (MKP-4), 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 II subfamily and is an ERK-selective cytoplasmic MKP. DUSP9 is a mediator of bone morphogenetic protein (BMP) signaling to control the appropriate ERK activity critical for the determination of embryonic stem cell fate. Down-regulation of DUSP9 expression has been linked to severe pre-eclamptic placenta as well as cancers such as hepatocellular carcinoma. DUSP9 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: 350492 [Multi-domain]  Cd Length: 145  Bit Score: 93.91  E-value: 1.07e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  29 QITSSLFLGRASVASNRHLLQARGITCVVNATIEIPNF--NWPQFEYVKVPLADIPHAPIRLYFDTVADKIHSVSKKHGA 106
Cdd:cd14644    5 QILPNLYLGSARDSANLETLAKLGIRYILNVTPNLPNFfeKNGDFHYKQIPISDHWSQNLSQFFPEAIEFIDEALSQNCG 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 399220337 107 TLVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDYESQL 165
Cdd:cd14644   85 VLVHCLAGISRSVTVTVAYLMQKLNLSLNDAYDLVKRKKSNISPNFNFMGQLLDFEKSL 143
DSP_DUSP12 cd14520
dual specificity phosphatase domain of dual specificity protein phosphatase 12 and similar ...
29-166 1.27e-24

dual specificity phosphatase domain of dual specificity protein phosphatase 12 and similar proteins; Dual specificity protein phosphatase 12 (DUSP12), also called YVH1, 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. DUSP12 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 targets p38 MAPK to regulate macrophage response to bacterial infection. It also ameliorates cardiac hypertrophy in response to pressure overload through c-Jun N-terminal kinase (JNK) inhibition. DUSP12 has been identified as a modulator of cell cycle progression, a function independent of phosphatase activity and mediated by its C-terminal zinc-binding domain.


Pssm-ID: 350370 [Multi-domain]  Cd Length: 144  Bit Score: 93.85  E-value: 1.27e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  29 QITSSLFLGRASVASNRHLLQARGITCVVNATIEIPNFNWP--QFEYVKVPLADIPHAPIRLYFDTVADKIhSVSKKHGA 106
Cdd:cd14520    3 LVRPGLYIGNADDAADYLSLREAGITHVLTVDSEEPIDAPPvgKLVRKFVPALDEESTDLLSRLDECLDFI-DEGRAEGA 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337 107 TLVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDYESQLF 166
Cdd:cd14520   82 VLVHCHAGVSRSAAVVTAYLMKTEQLSFEEALASLRECKPDVKPNDGFLKQLKLYEAMGC 141
DSP_slingshot_3 cd14571
dual specificity phosphatase domain of slingshot homolog 3; Dual specificity protein ...
28-165 2.02e-23

dual specificity phosphatase domain of slingshot homolog 3; Dual specificity protein phosphatase slingshot homolog 3 (SSH3), also called SSH-like protein 3, is part of the slingshot (SSH) family, whose members specifically dephosphorylate and reactivate Ser-3-phosphorylated cofilin (P-cofilin), an actin-binding protein that plays an essential role in actin filament dynamics. The Xenopus homolog (xSSH) is involved in the gastrulation movement. Mouse SSH3 dephosphorylates actin-depolymerizing factor (ADF) and cofilin but is dispensable for development. There are at least two human SSH3 isoforms reported: hSSH-3L (long) and hSSH-3. As SSH family phosphatases, they 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, hSSH-3L contains a C-terminal tail while hSSH-3 does not.


Pssm-ID: 350419 [Multi-domain]  Cd Length: 144  Bit Score: 90.69  E-value: 2.02e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  28 AQITSSLFLGRASVASNRHLLQARGITCVVNATIEIPNFNWPQFEYVKVPLADIPHAPIRLYFDTVADKIHSVSKKHGAT 107
Cdd:cd14571    5 SRIFPYLYLGSEWNAANLEELQRNRVSHILNVTREIDNFFPERFTYMNIRVYDEEATQLLPHWKETHRFIEAARAQGTRV 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 399220337 108 LVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDYESQL 165
Cdd:cd14571   85 LVHCKMGVSRSASTVIAYAMKQYGWTLEQALRHVRERRPIVQPNPGFLRQLQTYQGIL 142
DSP_DUSP6 cd14642
dual specificity phosphatase domain of dual specificity protein phosphatase 6; Dual ...
29-165 1.35e-22

dual specificity phosphatase domain of dual specificity protein phosphatase 6; Dual specificity protein phosphatase 6 (DUSP6), also called mitogen-activated protein kinase (MAPK) phosphatase 3 (MKP-3) or dual specificity protein phosphatase PYST1, 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 II subfamily and is an ERK-selective cytoplasmic MKP. DUSP6/MKP-3 plays an important role in obesity-related hyperglycemia by promoting hepatic glucose output. MKP-3 deficiency attenuates body weight gain induced by a high-fat diet, protects mice from developing obesity-related hepatosteatosis, and reduces adiposity, possibly by repressing adipocyte differentiation. It also contributes to p53-controlled cellular senescence. It 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: 350490 [Multi-domain]  Cd Length: 143  Bit Score: 88.59  E-value: 1.35e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  29 QITSSLFLGRASVASNRHLLQARGITCVVNATIEIPNF--NWPQFEYVKVPLADIPHAPIRLYFDTVADKIHSVSKKHGA 106
Cdd:cd14642    5 EILPYLYLGCAKDSTNLDVLEEFGIKYILNVTPNLPNLfeNAGEFKYKQIPISDHWSQNLSQFFPEAISFIDEARGKNCG 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 399220337 107 TLVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDYESQL 165
Cdd:cd14642   85 VLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFERTL 143
DSP_DUSP8 cd14645
dual specificity phosphatase domain of dual specificity protein phosphatase 8; Dual ...
26-165 2.24e-22

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: 88.14  E-value: 2.24e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  26 GIAQITSSLFLGRASVASNRHLLQARGITCVVNATIEIPNfnwPQF----EYVKVPLADIPHAPIRLYFDTVADKIHSVS 101
Cdd:cd14645   11 GPTRILPHLYLGSQKDVLNKDLMAQNGITYVLNASNSCPK---PDFicesHFMRIPVNDNYCEKLLPWLDKSIEFIDKAK 87
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 399220337 102 KKHGATLVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDYESQL 165
Cdd:cd14645   88 VSNCRVIVHCLAGISRSATIAIAYIMKTMGLSSDDAYRFVKDRRPSISPNFNFLGQLLEYEKSL 151
DUSP13B cd14577
dual specificity protein phosphatase 13 isoform B; Dual specificity protein phosphatase 13 ...
25-158 3.05e-22

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: 88.32  E-value: 3.05e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  25 GGIAQITSSLFLGRASVASNRHLLQARGITCVVNATIEIPNFNW-PQF------EYVKVPLADIPHAPIRLYFDTVADKI 97
Cdd:cd14577   16 GHVNEVWPNLYLGDAYAARDKSVLIQLGITHIVNAASGKFHVNTgPKFyrdmniDYYGVEADDNPFFDLSVYFYPVARFI 95
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 399220337  98 HS-VSKKHGATLVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPvIRPNLGFWRQL 158
Cdd:cd14577   96 RAaLSSPNGRVLVHCAMGISRSATLVLAFLMICEDLTLVDAIQTVRAHRD-ICPNSGFLRQL 156
DUSP3 cd14579
dual specificity protein phosphatase 3; Dual specificity protein phosphatase 3 (DUSP3), also ...
29-165 3.28e-22

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: 88.28  E-value: 3.28e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  29 QITSSLFLGRASVASNRHLLQARGITCVVNATIEIP----NFNwPQF------EYVKVPLADIPHAPIRLYFDTVADKIH 98
Cdd:cd14579   23 EVYPRIYVGNASVAQNIMRLQRLGITHVLNAAEGKSfmhvNTN-AEFyedtgiTYHGIKANDTQHFNLSAYFEEAADFID 101
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 399220337  99 -SVSKKHGATLVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPvIRPNLGFWRQLIDYESQL 165
Cdd:cd14579  102 kALAQKNGRVLVHCREGYSRSPTLVIAYLMLRQKMDVKSALSTVRQKRE-IGPNDGFLKQLCQLNDKL 168
DSP_fungal_SDP1-like cd14521
dual specificity phosphatase domain of fungal dual specificity protein phosphatase SDP1, MSG5, ...
69-165 1.76e-21

dual specificity phosphatase domain of fungal dual specificity protein phosphatase SDP1, MSG5, and similar proteins; This family is composed of fungal dual specificity protein phosphatases (DUSPs) including Saccharomyces cerevisiae SDP1 and MSG5, and Schizosaccharomyces pombe Pmp1. 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. SDP1 is oxidative stress-induced and dephosphorylates MAPK substrates such as SLT2. MSG5 dephosphorylates the Fus3 and Slt2 MAPKs operating in the mating and cell wall integrity (CWI) pathways, respectively. Pmp1 is responsible for dephosphorylating the CWI MAPK Pmk1. These phosphatases bind to their target MAPKs through a conserved IYT motif located outside of the dual specificity phosphatase domain.


Pssm-ID: 350371 [Multi-domain]  Cd Length: 155  Bit Score: 85.84  E-value: 1.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  69 PQFEYVKVPlaDIPHAPIRLYFDTVADKIHSVSKKHGATLVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVI 148
Cdd:cd14521   61 KNPEYIHVP--WDHNSQIQKDLPKLTSIIEDATQSGKKVLIHCQCGVSRSASLIIAYIMKKLGLSLNDAYDLLKSRSPWI 138
                         90
                 ....*....|....*..
gi 399220337 149 RPNLGFWRQLIDYESQL 165
Cdd:cd14521  139 GPNMSLIFQLMEFEKVL 155
DSP_DUSP15 cd14582
dual specificity phosphatase domain of dual specificity protein phosphatase 15; Dual ...
26-158 3.84e-21

dual specificity phosphatase domain of dual specificity protein phosphatase 15; Dual specificity protein phosphatase 15 (DUSP15), also called Vaccinia virus VH1-related dual-specific protein phosphatase Y (VHY) or VH1-related member Y, functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). DUSP15 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 highly expressed in the testis and is located in the plasma membrane in a myristoylation-dependent manner. It may be involved in the regulation of meiotic signal transduction in testis cells. It is also expressed in the brain and has been identified as a regulator of oligodendrocyte differentiation. DUSP15 contains an N-terminal catalytic dual specificity phosphatase domain and a short C-terminal tail.


Pssm-ID: 350430 [Multi-domain]  Cd Length: 146  Bit Score: 85.00  E-value: 3.84e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  26 GIAQITSSLFLGRASVASNRHLLQARGITCVVNATiEIPNFNWPQFEYVKVPLADIPHAPIRLYFDTVADKIHSVSKKHG 105
Cdd:cd14582    4 GMTKVLPGLYLGNFIDAKDLEQLSRNKITHIISIH-ESPQPLLQDITYLRIPLPDTPEAPIKKHFKECISFIHQCRLNGG 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 399220337 106 ATLVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQL 158
Cdd:cd14582   83 NCLVHCLAGISRSTTIVVAYVMAVTELSWQEVLEAIRAVRPIANPNPGFKQQL 135
DSP_fungal_PPS1 cd14516
dual specificity phosphatase domain of fungal dual specificity protein phosphatase PPS1-like; ...
34-162 4.73e-21

dual specificity phosphatase domain of fungal dual specificity protein phosphatase PPS1-like; This subfamily contains fungal proteins with similarity to dual specificity protein phosphatase PPS1 from Saccharomyces cerevisiae, which has a role in the DNA synthesis phase of the cell cycle. As a dual specificity protein phosphatase, PPS1 functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It contains a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350366 [Multi-domain]  Cd Length: 177  Bit Score: 85.40  E-value: 4.73e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  34 LFLGRASVASNRHLLQARGITCVV--------------------------NATIEIPNFNWPQFEYVKVPLADIPHA--- 84
Cdd:cd14516   14 LYLGSLNHASNATLLESLGITHIVsvgespswfsnlkikyifdfslqdlsNLDSNSEGSLWAAEYKGLISVLYIHNLkdd 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  85 ---PIRLYFDTVADKIHSVSKKHGATLVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARR--PVIRPNLGFWRQLI 159
Cdd:cd14516   94 gidSLLPQLTDALDFIQKARLLGGKTLVHCRVGVSRSATVVIAEVMKHLRMSLVDAYLFVRVRRlnIIIQPNLRFFYELF 173

                 ...
gi 399220337 160 DYE 162
Cdd:cd14516  174 KWE 176
DSP_STYXL1 cd14517
dual specificity phosphatase-like domain of serine/threonine/tyrosine interacting like 1; ...
34-169 5.00e-21

dual specificity phosphatase-like domain of serine/threonine/tyrosine interacting like 1; Serine/threonine/tyrosine interacting like 1 (STYXL1), also known as DUSP24 and MK-STYX, is a catalytically inactive phosphatase with homology to the mitogen-activated protein kinase (MAPK) phosphatases (MKPs). STYXL1 plays a role in regulating pathways by competing with active phosphatases for binding to MAPKs. Similar to MKPs, STYXL1 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, however its C-terminal dual specificity phosphatase-like domain is a pseudophosphatase missing the catalytic cysteine.


Pssm-ID: 350367 [Multi-domain]  Cd Length: 155  Bit Score: 84.64  E-value: 5.00e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  34 LFLGRASVASNRHLLQARGITCVVNATIEIPNFNWPQF-EYVKVPLADIPHAPIRLYFDTVADKIHSVSKKHGATLVHCA 112
Cdd:cd14517   19 LYMGNYKQACDKKIQKDLKIKAHINVSMDADELFKSGNdQVLHIPVEDSVEADLLSFFERACSFIDKHKNNGSRVLVFST 98
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 399220337 113 AGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDYESQLFGKS 169
Cdd:cd14517   99 LGISRSVAVAIAYLMYHYKWSLKDAWKYLLKCKNNMRPNRGFVKQLSEWEEKLLGTT 155
DUSP22 cd14581
dual specificity protein phosphatase 22; Dual specificity protein phosphatase 22 (DUSP22), ...
26-162 1.19e-20

dual specificity protein phosphatase 22; Dual specificity protein phosphatase 22 (DUSP22), also called JNK-stimulatory phosphatase-1 (JSP-1), low molecular weight dual specificity phosphatase 2 (LMW-DSP2), mitogen-activated protein kinase phosphatase x (MKP-x) or VHR-related MKPx (VHX), 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. DUSP22 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. DUSP22 negatively regulates the estrogen receptor-alpha-mediated signaling pathway and the IL6-leukemia inhibitory factor (LIF)-STAT3-mediated signaling pathway. It also regulates cell death by acting as a scaffold protein for the ASK1-MKK7-JNK signal transduction pathway independently of its phosphatase activity.


Pssm-ID: 350429 [Multi-domain]  Cd Length: 149  Bit Score: 83.69  E-value: 1.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  26 GIAQITSSLFLGRASVASNRHLLQARGITCVVNatieIPNFNWPQFE---YVKVPLADIPHAPIRLYFDTVADKIHSVSK 102
Cdd:cd14581    3 GMNKVLPGLYLGNFKDARDREQLSKNNITHILS----VHDSARPMLEgmtYLCIPAADSPSQNLTQHFKESIKFIHECRL 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337 103 KHGATLVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDYE 162
Cdd:cd14581   79 RGEGCLVHCLAGVSRSVTLVVAYIMTVTDFGWEDALSAVKAARSCANPNMGFQRQLQEFE 138
DUPD1 cd14575
dual specificity phosphatase and pro isomerase domain containing 1; Dual specificity ...
29-165 5.16e-20

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: 82.18  E-value: 5.16e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  29 QITSSLFLGRASVASNRHLLQARGITCVVNATIEIPNFNWP-------QFEYVKVPLADIPHAPIRLYFDTVADKIH-SV 100
Cdd:cd14575   13 EVWPGLYIGDEKTALDRYSLQKLGITHILNAAHGKWNVDTGaeyykdmTIHYYGVEADDLPTFNLSQFFYSAAEFIHqAL 92
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 399220337 101 SKKHGATLVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRpVIRPNLGFWRQLIDYESQL 165
Cdd:cd14575   93 SDPHNKLLVHCVMGRSRSATLVLAYLMIYKNMTVVDAIEQVAQRR-CILPNRGFLKQLRELDIQL 156
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
30-165 7.11e-19

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 78.86  E-value: 7.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  30 ITSSLFLGRASvASNRHLLQARGITCVVNATIEIPNFNWPQ----FEYVKVPLADIpHAPIRLYFDTVADKIHSVSKKHG 105
Cdd:COG2453    4 IPGLLAGGPLP-GGGEADLKREGIDAVVSLTEEEELLLGLLeeagLEYLHLPIPDF-GAPDDEQLQEAVDFIDEALREGK 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337 106 ATLVHCAAGVSRSATLCIAYLMKfHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDYESQL 165
Cdd:COG2453   82 KVLVHCRGGIGRTGTVAAAYLVL-LGLSAEEALARVRAARPGAVETPAQRAFLERFAKRL 140
DSP_plant_IBR5-like cd18534
dual specificity phosphatase domain of plant IBR5-like protein phosphatases; This subfamily is ...
30-161 1.51e-18

dual specificity phosphatase domain of plant IBR5-like protein phosphatases; This subfamily is composed of Arabidopsis thaliana INDOLE-3-BUTYRIC ACID (IBA) RESPONSE 5 (IBR5) and similar plant proteins. IBR5 protein is also called SKP1-interacting partner 33. The IBR5 gene encodes a dual-specificity phosphatase (DUSP) which acts as a positive regulator of plant responses to auxin and abscisic acid. DUSPs 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. IBR5 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. It has been shown to target MPK12, which is a negative regulator of auxin signaling.


Pssm-ID: 350510 [Multi-domain]  Cd Length: 130  Bit Score: 77.57  E-value: 1.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  30 ITSSLFLGRASVASNRHLLQARGITCVVNATIEIPNFNWPQFEYVKVPLADIPHapirlyFDTVADKIHSVSKKHGATLV 109
Cdd:cd18534    5 LPGFLYLGSYDNASRAELLKAQGITRILNTVPDCQNLYKNSFTYHVLSEEKTVP------FAEAVDFIEQCRKDKARVLV 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 399220337 110 HCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDY 161
Cdd:cd18534   79 HCMSGQSRSPAVVIAYLMKHKGWRLAESYQWVKERRPSINLSPAVAKQLQEF 130
DSP_iDUSP27 cd14576
dual specificity phosphatase-like domain of inactive dual specificity protein phosphatase 27; ...
21-165 1.84e-18

dual specificity phosphatase-like domain of inactive dual specificity protein phosphatase 27; Inactive dual specificity protein phosphatase 27 (DUSP27) may play a role in myofiber maturation. It is a pseudophosphatase containing a substitution of the active site cysteine into a serine. It is a large protein of more than 1000 amino acids in length with an N-terminal dual specificity phosphatase-like domain.


Pssm-ID: 350424  Cd Length: 159  Bit Score: 78.37  E-value: 1.84e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  21 EGDIGGIAQITSSLFLGRASVASNRHLLQARGITCVVNATIEIPNFNWPQF------EYVKVPLADIPHAPIRLYFDTVA 94
Cdd:cd14576    5 EAPRNAVDEVWPNVFIAEKSVAVNKGRLKRLGITHVLNAAHGTGVYTGPEFysgmniQYMGIEVDDFPDVDISKHFRKGA 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 399220337  95 DKIHSVSKKH-GATLVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPvIRPNLGFWRQLIDYESQL 165
Cdd:cd14576   85 EFLDEALLTYrGKVLVSSEMGISRSAVLVAAYLMIFHNMTIMEALMTLRKKRA-IYPNEGFLKQLRELNEKL 155
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
29-161 1.40e-16

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: 73.06  E-value: 1.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  29 QITSSLFLGRASVAS-NRHLLQARGITCVVNAT--IEIPNFNWPQFEYVK-------VPLADIPHAPIRLYFDTVADKIH 98
Cdd:cd14524    4 RIDDTVILGALPFRSmTVALVAKENVRGVITMNeeYETRFFCNSKEEWKAlgveqlrLPTVDFTGVPSLEDLEKGVDFIL 83
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 399220337  99 SVSKKHGATLVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPVIRPNLGFWRQLIDY 161
Cdd:cd14524   84 KHREKGKSVYVHCKAGRGRSATIVACYLIQHKGWSPEEAQEFLRSKRPHILLRLSQREVLEEF 146
DSP_bac cd14527
unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily ...
27-151 1.08e-14

unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily is composed of uncharacterized bacterial and plant dual-specificity protein phosphatases. DUSPs function as a protein-serine/threonine phosphatases (EC 3.1.3.16) and a protein-tyrosine-phosphatases (EC 3.1.3.48).


Pssm-ID: 350376 [Multi-domain]  Cd Length: 136  Bit Score: 67.69  E-value: 1.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  27 IAQITSSLFLGRASvaSNRHLlqARGITCVVNATIEIPnFNWPQFEYVKVPLAD-IPHAPIRLyfDTVADKIHSVSKKHG 105
Cdd:cd14527    5 YDEVLPGLYLGRWP--SADEL--PPGVPAVLDLTAELP-RPRKRQAYRCVPLLDlVAPTPEQL--ERAVAWIEELRAQGG 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 399220337 106 ATLVHCAAGVSRSATLCIAYLMKF-HNLCLLEAYNWVKARRPVIRPN 151
Cdd:cd14527   78 PVLVHCALGYGRSATVVAAWLLAYgRAKSVAEAEALIRAARPQVVLN 124
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
48-160 1.93e-10

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: 55.82  E-value: 1.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  48 LQARGITCVVNATIEipnfnwpqfeyvkvpladiphapirlYFDTVADKIHSVSKKHGATLVHCAAGVSRSATLCIAYLM 127
Cdd:cd14494   26 LKQLGVTTIVDLTLA--------------------------MVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLV 79
                         90       100       110
                 ....*....|....*....|....*....|....
gi 399220337 128 KFHNLCLLEAYNWVKARRPV-IRPNLGFWRQLID 160
Cdd:cd14494   80 LLGGMSAEEAVRIVRLIRPGgIPQTIEQLDFLIK 113
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
37-146 4.28e-10

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


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 55.36  E-value: 4.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  37 GRASVASNRHL--LQARGITCVVNATIEIPNFNWpqFEYVKVPLADIP----HAPIRLYFDTVADKIHSVSKKHGATLVH 110
Cdd:cd14504   11 GMAFPRLPEHYayLNENGIRHVVTLTEEPPPEHS--DTCPGLRYHHIPiedyTPPTLEQIDEFLDIVEEANAKNEAVLVH 88
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 399220337 111 CAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRP 146
Cdd:cd14504   89 CLAGKGRTGTMLACYLVKTGKISAVDAINEIRRIRP 124
PRK12361 PRK12361
hypothetical protein; Provisional
27-158 2.14e-09

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 56.17  E-value: 2.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  27 IAQITSSLFLGRASVASNRHLLQARGITCVVNATIEIPNFNWP----QFEYVKVPLADipH-APIRLYFDTVADKIHSVS 101
Cdd:PRK12361  95 IQKIDENLYLGCRLFPADLEKLKSNKITAILDVTAEFDGLDWSlteeDIDYLNIPILD--HsVPTLAQLNQAINWIHRQV 172
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 399220337 102 KKHGATLVHCAAGVSRSATLCIAYLM-KFHNLCLLEAYNWVKARRPVIRPNLgfwRQL 158
Cdd:PRK12361 173 RANKSVVVHCALGRGRSVLVLAAYLLcKDPDLTVEEVLQQIKQIRKTARLNK---RQL 227
DSP_laforin-like cd14526
dual specificity phosphatase domain of laforin and similar domains; This family is composed of ...
29-157 2.27e-08

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: 51.04  E-value: 2.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  29 QITSSLFLGRA--SVASNRHLLQArGITCVVNATIEIPNFNWP-------------QFEYVKVPLADIPHAPIRLYFDTV 93
Cdd:cd14526    5 RILPNLIVGSCpqNPEDVDRLKKE-GVTAVLNLQTDSDMEYWGvdidsirkackesGIRYVRLPIRDFDTEDLRQKLPQA 83
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 399220337  94 ADKIHSVSKKHGATLVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRPViRPNLGFWRQ 157
Cdd:cd14526   84 VALLYRLLKNGGTVYVHCTAGLGRAPATVIAYLYWVLGYSLDEAYYLLTSKRPC-GPDEEAIRG 146
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
60-135 5.03e-05

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1), also called protein-tyrosine phosphatase 1B (PTP-1B), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1/PTP-1B is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It contains an N-terminal catalytic PTP domain, followed by two tandem proline-rich motifs that mediate interaction with SH3-domain-containing proteins, and a small hydrophobic stretch that localizes the enzyme to the endoplasmic reticulum (ER). It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor.


Pssm-ID: 350456 [Multi-domain]  Cd Length: 277  Bit Score: 42.71  E-value: 5.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  60 TIEIPNFN---WPQFeyvkvplaDIPHAPIR-LYFDTVADKIHSVSKKHGATLVHCAAGVSRSATLCIAylmkfhNLCLL 135
Cdd:cd14608  153 TREILHFHyttWPDF--------GVPESPASfLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLA------DTCLL 218
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
66-127 5.32e-05

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 40.81  E-value: 5.32e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 399220337    66 FNWPQFeyvKVPladIPHAPIRLYFDTVaDKIHSVSKKHGATLVHCAAGVSRSATLCIAYLM 127
Cdd:smart00404   8 TGWPDH---GVP---ESPDSILELLRAV-KKNLNQSESSGPVVVHCSAGVGRTGTFVAIDIL 62
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
66-127 5.32e-05

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: 40.81  E-value: 5.32e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 399220337    66 FNWPQFeyvKVPladIPHAPIRLYFDTVaDKIHSVSKKHGATLVHCAAGVSRSATLCIAYLM 127
Cdd:smart00012   8 TGWPDH---GVP---ESPDSILELLRAV-KKNLNQSESSGPVVVHCSAGVGRTGTFVAIDIL 62
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
67-127 1.50e-04

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 41.11  E-value: 1.50e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 399220337    67 NWPqfeYVKVPlaDIPHAPIRLyfdtVADKIHSVSKKHGATLVHCAAGVSRSATLC-IAYLM 127
Cdd:smart00194 166 NWP---DHGVP--ESPESILDL----IRAVRKSQSTSTGPIVVHCSAGVGRTGTFIaIDILL 218
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
70-124 2.12e-04

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1) type 2 (PTPN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases, (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1 (or PTP-1B) is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor. PTPN2 (or TCPTP), a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner.


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 40.84  E-value: 2.12e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 399220337  70 QFEYVKVPLADIPHAPIR-LYFDTVADKIHSVSKKHGATLVHCAAGVSRSATLCIA 124
Cdd:cd14545  133 HFHYTTWPDFGVPESPAAfLNFLQKVRESGSLSSDVGPPVVHCSAGIGRSGTFCLV 188
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
70-132 5.09e-04

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type tyrosine-protein phosphatase V (PTPRV or R-PTP-V), also known as embryonic stem cell protein-tyrosine phosphatase (ES cell phosphatase) or osteotesticular protein-tyrosine phosphatase (OST-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRV is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. In rodents, it may play a role in the maintenance of pluripotency and may function in signaling pathways during bone remodeling. It is the only PTP whose function has been lost between rodent and human. The human OST-PTP gene is a pseudogene.


Pssm-ID: 350466 [Multi-domain]  Cd Length: 230  Bit Score: 39.54  E-value: 5.09e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 399220337  70 QFEYVKVPLADIPHAPIRL--YFDTVADKIHSvSKKHGATLVHCAAGVSRSATLcIAYLMKFHNL 132
Cdd:cd14618  131 HLHYTAWPDHGIPESTSSLmaFRELVREHVQA-TKGKGPTLVHCSAGVGRSGTF-IALDRLLRQL 193
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
67-145 7.17e-04

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: 38.81  E-value: 7.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  67 NWPQFeyvKVPlaDIPHAPIRLyfdtVADKIHSVSKKHGATLVHCAAGVSRSATLCIAYLMkfhnLCLLEA------YNW 140
Cdd:cd00047  111 GWPDH---GVP--SSPEDLLAL----VRRVRKEARKPNGPIVVHCSAGVGRTGTFIAIDIL----LERLEAegevdvFEI 177

                 ....*
gi 399220337 141 VKARR 145
Cdd:cd00047  178 VKALR 182
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
105-166 7.48e-04

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: 38.59  E-value: 7.48e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 399220337 105 GATLVHCAAGVSRSATLCIAYLMKFHNLCLLEAYNWVKARRP--VIRPNLGFwrqLIDYESQLF 166
Cdd:cd14499  110 GAIAVHCKAGLGRTGTLIACYLMKHYGFTAREAIAWLRICRPgsVIGPQQQF---LEEKEARLW 170
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
95-128 1.59e-03

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


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 37.56  E-value: 1.59e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 399220337  95 DKIH---SVSKKHGAtLVHCAAGVSRSATLCIAYLMK 128
Cdd:cd14497   84 DDIDswlSEDPNNVA-VVHCKAGKGRTGTVICAYLLY 119
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
49-122 1.67e-03

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein phosphatase non-receptor type 12 (PTPN12), also called PTP-PEST or protein-tyrosine phosphatase G1 (PTPG1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling. It regulates various physiological processes, including cell migration, immune response, and neuronal activity, by dephosphorylating multiple substrates including HER2, FAK, PYK2, PSTPIP, WASP, p130Cas, paxillin, Shc, catenin, c-Abl, ArgBP2, p190RhoGAP, RhoGDI, cell adhesion kinase beta, and Rho GTPase.


Pssm-ID: 350452 [Multi-domain]  Cd Length: 297  Bit Score: 38.38  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  49 QARGITCVVNATIEIPN--FNWPQFEYVKVPLADIPHApirlyFDTVADKIhSVSKKHGA-----TLVHCAAGVSRSATL 121
Cdd:cd14604  167 QARTDYFIRTLLLEFQNetRRLYQFHYVNWPDHDVPSS-----FDSILDMI-SLMRKYQEhedvpICIHCSAGCGRTGAI 240

                 .
gi 399220337 122 C 122
Cdd:cd14604  241 C 241
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
46-123 3.86e-03

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


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 37.25  E-value: 3.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399220337  46 HLLQARGITcvVNATIEIPNFN---WPQFeyvkvplaDIPHAPIR-LYFDTVADKIHSVSKKHGATLVHCAAGVSRSATL 121
Cdd:cd14607  140 HLLQLENIN--SGETRTISHFHyttWPDF--------GVPESPASfLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTF 209

                 ..
gi 399220337 122 CI 123
Cdd:cd14607  210 SL 211
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
67-137 9.96e-03

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 35.68  E-value: 9.96e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 399220337   67 NWPQFeyvKVPlaDIPHAPIRLYFDTvadKIHSVSKKHGATLVHCAAGVSRSATLCIAYLMkfhnLCLLEA 137
Cdd:pfam00102 140 GWPDH---GVP--ESPNSLLDLLRKV---RKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIA----LQQLEA 198
 
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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