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Conserved domains on  [gi|469608396|ref|NP_001013146|]
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dual specificity protein phosphatase 18 [Rattus norvegicus]

Protein Classification

dual specificity protein phosphatase family protein( domain architecture ID 12998597)

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
DUSP18_21 cd14573
dual specificity protein phosphatases 18 and 21; This subfamily contains dual specificity ...
 19-176 1.92e-105

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: 299.78  E-value: 1.92e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  19 GLSQITKSLFISNGAAANDKLLLSSNQITTVINVSVEVANTFYEDIQYVQVPVVDAPIARLSDFFDPIADHIHSVEMKQG 98
Cdd:cd14573    1 RLSRITESLYLSNGVAANNRTLLAANRITCVINVSLEVANGLPPGIEYLHVPVADSPDTRLRDYFDPIADKIHTVEARGG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 469608396  99 RTLLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYEFQLFGKNTMQMVNSPMGLIPD 176
Cdd:cd14573   81 RTLLHCVAGVSRSATLCLAYLMKYHAMSLLDAHTWVKSCRPIIRPNNGFWEQLIHYEFELFGKNTVHMITSPVGMIPD 158
 
Name Accession Description Interval E-value
DUSP18_21 cd14573
dual specificity protein phosphatases 18 and 21; This subfamily contains dual specificity ...
 19-176 1.92e-105

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: 299.78  E-value: 1.92e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  19 GLSQITKSLFISNGAAANDKLLLSSNQITTVINVSVEVANTFYEDIQYVQVPVVDAPIARLSDFFDPIADHIHSVEMKQG 98
Cdd:cd14573    1 RLSRITESLYLSNGVAANNRTLLAANRITCVINVSLEVANGLPPGIEYLHVPVADSPDTRLRDYFDPIADKIHTVEARGG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 469608396  99 RTLLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYEFQLFGKNTMQMVNSPMGLIPD 176
Cdd:cd14573   81 RTLLHCVAGVSRSATLCLAYLMKYHAMSLLDAHTWVKSCRPIIRPNNGFWEQLIHYEFELFGKNTVHMITSPVGMIPD 158
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
21-157 2.43e-44

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 144.35  E-value: 2.43e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396    21 SQITKSLFISNGAAANDKLLLSSNQITTVINVSVEVANTFYEDIQYVQVPVVDAPIARLSDFFDPIADHIHSVEMKQGRT 100
Cdd:smart00195   2 SEILPHLYLGSYSDALNLALLKKLGITHVINVTNEVPNYNGSDFTYLGVPIDDNTETKISPYFPEAVEFIEDAESKGGKV 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 469608396   101 LLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYEFQ 157
Cdd:smart00195  82 LVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRPIISPNFGFLRQLIEYERK 138
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 38-155 4.12e-38

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: 128.15  E-value: 4.12e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396   38 KLLLSSNQITTVINVSVEVaNTFYEDIQYVQVPVVDAPIARLSDFFDPIADHIHSVEMKQGRTLLHCAAGVSRSAALCLA 117
Cdd:pfam00782  11 DAFLSKLGITAVINVTREV-DLYNSGILYLRIPVEDNHETNISKYLEEAVEFIDDARQKGGKVLVHCQAGISRSATLIIA 89

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 469608396  118 YLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYE 155
Cdd:pfam00782  90 YLMKTRNLSLNEAYSFVKERRPGISPNFGFKRQLLEYE 127
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
41-155 9.02e-17

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 73.47  E-value: 9.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  41 LSSNQITTVINVSV--EVANTFYED--IQYVQVPVVDAPIARLSDFfDPIADHIHSVEMKQGRTLLHCAAGVSRSAALCL 116
Cdd:COG2453   21 LKREGIDAVVSLTEeeELLLGLLEEagLEYLHLPIPDFGAPDDEQL-QEAVDFIDEALREGKKVLVHCRGGIGRTGTVAA 99

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 469608396 117 AYLMkYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYE 155
Cdd:COG2453  100 AYLV-LLGLSAEEALARVRAARPGAVETPAQRAFLERFA 137
PRK12361 PRK12361
hypothetical protein; Provisional
 15-145 2.33e-06

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 47.31  E-value: 2.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  15 PSISglsQITKSLFISNGAAANDKLLLSSNQITTVINVSVEVA----NTFYEDIQYVQVPVVDAPIARLSDFFDPIAdHI 90
Cdd:PRK12361  93 PAIQ---KIDENLYLGCRLFPADLEKLKSNKITAILDVTAEFDgldwSLTEEDIDYLNIPILDHSVPTLAQLNQAIN-WI 168

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 469608396  91 HSvEMKQGRT-LLHCAAGVSRSAALCLAYLM-KYHAMSLLDAHAWTKSRRPIIRPNS 145
Cdd:PRK12361 169 HR-QVRANKSvVVHCALGRGRSVLVLAAYLLcKDPDLTVEEVLQQIKQIRKTARLNK 224
 
Name Accession Description Interval E-value
DUSP18_21 cd14573
dual specificity protein phosphatases 18 and 21; This subfamily contains dual specificity ...
 19-176 1.92e-105

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: 299.78  E-value: 1.92e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  19 GLSQITKSLFISNGAAANDKLLLSSNQITTVINVSVEVANTFYEDIQYVQVPVVDAPIARLSDFFDPIADHIHSVEMKQG 98
Cdd:cd14573    1 RLSRITESLYLSNGVAANNRTLLAANRITCVINVSLEVANGLPPGIEYLHVPVADSPDTRLRDYFDPIADKIHTVEARGG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 469608396  99 RTLLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYEFQLFGKNTMQMVNSPMGLIPD 176
Cdd:cd14573   81 RTLLHCVAGVSRSATLCLAYLMKYHAMSLLDAHTWVKSCRPIIRPNNGFWEQLIHYEFELFGKNTVHMITSPVGMIPD 158
DUSP14-like cd14514
dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is ...
 20-153 5.12e-73

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: 217.04  E-value: 5.12e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  20 LSQITKSLFISNGAAANDKLLLSSNqITTVINVSVEVANTFYEDIQYVQVPVVDAPIARLSDFFDPIADHIHSVEMKQGR 99
Cdd:cd14514    1 ISQITPHLFLSGASAATPPLLLSRG-ITCIINATTELPDPSYPGIEYLRVPVEDSPHADLSPHFDEVADKIHQVKRRGGR 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 469608396 100 TLLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIH 153
Cdd:cd14514   80 TLVHCVAGVSRSATLCLAYLMKYEGMTLREAYKHVKAARPIIRPNVGFWRQLIE 133
DUSP14 cd14572
dual specificity protein phosphatase 14; dual specificity protein phosphatase 14 (DUSP14), ...
 16-162 1.27e-67

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: 203.95  E-value: 1.27e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  16 SISGLSQITKSLFISNGAAANDKLLLSSNQITTVINVSVEVANTFYEDIQYVQVPVVDAPIARLSDFFDPIADHIHSVEM 95
Cdd:cd14572    4 DLGGIAQITPSLYLSRGNVASNRHLLLSRGITCIVNATIEIPNFNWPQFEYVKVPLADMPHAPISLYFDSVADKIHSVGR 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 469608396  96 KQGRTLLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYEFQLFGKN 162
Cdd:cd14572   84 KHGATLVHCAAGVSRSATLCIAYLMKYHRVSLLEAYNWVKARRPVIRPNVGFWRQLIDYERKLFGKS 150
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 21-152 3.94e-50

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: 158.86  E-value: 3.94e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  21 SQITKSLFISNGAAANDKLLLSSNQITTVINVSVEVANTFYED-IQYVQVPVVDAPIARLSDFFDPIADHIHSVEMKQGR 99
Cdd:cd14498    2 SEILPGLYLGSLDAAQDKELLKKLGITHILNVAGEPPPNKFPDgIKYLRIPIEDSPDEDILSHFEEAIEFIEEALKKGGK 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 469608396 100 TLLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLI 152
Cdd:cd14498   82 VLVHCQAGVSRSATIVIAYLMKKYGWSLEEALELVKSRRPIISPNPGFLKQLK 134
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
21-157 2.43e-44

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 144.35  E-value: 2.43e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396    21 SQITKSLFISNGAAANDKLLLSSNQITTVINVSVEVANTFYEDIQYVQVPVVDAPIARLSDFFDPIADHIHSVEMKQGRT 100
Cdd:smart00195   2 SEILPHLYLGSYSDALNLALLKKLGITHVINVTNEVPNYNGSDFTYLGVPIDDNTETKISPYFPEAVEFIEDAESKGGKV 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 469608396   101 LLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYEFQ 157
Cdd:smart00195  82 LVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRPIISPNFGFLRQLIEYERK 138
DUSP28 cd14574
dual specificity protein phosphatase 28; Dual specificity protein phosphatase 28 (DUSP28), ...
 20-158 1.37e-39

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: 132.21  E-value: 1.37e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  20 LSQITKSLFISNGAAANDKLLLSSNQITTVINVSVEVANTFYEDIQYVQVPVVDAPIARLSDFFDPIADHIHSVEMKQGR 99
Cdd:cd14574    1 LCRVTDSLFISNARAACNEELLAREGVTLCVNVSRQQPFPRAPRVSTLRVPVFDDPAEDLYRHFEQCADAIEAAVRRGGK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 469608396 100 TLLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYEFQL 158
Cdd:cd14574   81 CLVYCKNGRSRSAAVCIAYLMKHRGLSLQDAFQVVKAARPVAEPNPGFWSQLQRYEEEL 139
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 38-155 4.12e-38

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: 128.15  E-value: 4.12e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396   38 KLLLSSNQITTVINVSVEVaNTFYEDIQYVQVPVVDAPIARLSDFFDPIADHIHSVEMKQGRTLLHCAAGVSRSAALCLA 117
Cdd:pfam00782  11 DAFLSKLGITAVINVTREV-DLYNSGILYLRIPVEDNHETNISKYLEEAVEFIDDARQKGGKVLVHCQAGISRSATLIIA 89

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 469608396  118 YLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYE 155
Cdd:pfam00782  90 YLMKTRNLSLNEAYSFVKERRPGISPNFGFKRQLLEYE 127
DSP_MKP_classI cd14565
dual specificity phosphatase domain of class I mitogen-activated protein kinase phosphatase; ...
 22-157 1.49e-35

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: 121.73  E-value: 1.49e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  22 QITKSLFISNGAAANDKLLLSSNQITTVINVSVEVANTFYEDIQYVQVPVVDAPIARLSDFFDPIADHIHSVEMKQGRTL 101
Cdd:cd14565    3 EILPFLYLGSAYHASRREVLKALGITAVLNVSRNCPNHFEDHFQYKSIPVEDSHNADISSWFEEAIGFIDKVKASGGRVL 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 469608396 102 LHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYEFQ 157
Cdd:cd14565   83 VHCQAGISRSATICLAYLMTTRRVRLNEAFDYVKQRRSVISPNFNFMGQLLQYESQ 138
DUSP3-like cd14515
dual specificity protein phosphatases 3, 13, 26, 27, and similar domains; This family is ...
 21-158 1.69e-34

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: 119.62  E-value: 1.69e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  21 SQITKSLFISNGAAANDKLLLSSNQITTVINVS-----VEVANT--FYED--IQYVQVPVVDAPIARLSDFFDPIADHIH 91
Cdd:cd14515    2 DEVWPGIYIGDESTAKNKAKLKKLGITHVLNAAegkknGEVNTNakFYKGsgIIYLGIPASDLPTFDISQYFDEAADFID 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 469608396  92 S-VEMKQGRTLLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPiIRPNSGFWEQLIHYEFQL 158
Cdd:cd14515   82 KaLSDPGGKVLVHCVEGVSRSATLVLAYLMIYQNMTLEEAIRTVRKKRE-IRPNRGFLQQLCELNDKL 148
DSP_DUSP19 cd14523
dual specificity phosphatase domain of dual specificity protein phosphatase 19; Dual ...
 20-155 1.30e-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: 1.30e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  20 LSQITKSLFISNGAAANDKLLLSSNQITTVINVSVEVANTFYEDIQYVQVPVVDAPIARLSDFFDPIADHIHSVEMKQGR 99
Cdd:cd14523    2 VGVIKPWLLLSSQDVAHDLETLKKHKVTHILNVAYGVENAFPDDFTYKTISILDLPETDITSYFPECFEFIDEAKSQDGV 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 469608396 100 TLLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYE 155
Cdd:cd14523   82 VLVHCNAGVSRSASIVIGYLMATENLSFEDAFSLVKNARPSIRPNPGFMEQLKEYQ 137
DSP_MKP_classIII cd14568
dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; ...
 20-155 1.86e-32

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: 114.05  E-value: 1.86e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  20 LSQITKSLFISNGAAANDKLLLSSNQITTVINVSVEVAN-TFYEDIQYVQVPVVDAPIARLSDFFDPIADHIHSVEMKQG 98
Cdd:cd14568    1 PTRILPHLYLGSQRDVLDKDLMQRNGISYVLNVSNTCPKpDFIPDSHFLRIPVNDSYCEKLLPWLDKAVEFIEKARASNK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 469608396  99 RTLLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYE 155
Cdd:cd14568   81 RVLVHCLAGISRSATIAIAYIMKHMRMSLDDAYRFVKEKRPTISPNFNFLGQLLEFE 137
DSP_DUSP2 cd14641
dual specificity phosphatase domain of dual specificity protein phosphatase 2; Dual ...
 19-159 2.16e-30

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: 108.80  E-value: 2.16e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  19 GLSQITKSLFISNGAAANDKLLLSSNQITTVINVSVEVANTFYEDIQYVQVPVVDAPIARLSDFFDPIADHIHSVEMKQG 98
Cdd:cd14641    3 GPVEILPFLFLGSAHHSSRRETLESLGITAVLNVSSSCPNYFEGQFQYKSIPVEDSHMADISAWFQEAIDFIDSVKNSGG 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 469608396  99 RTLLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYEFQLF 159
Cdd:cd14641   83 RVLVHCQAGISRSATICLAYLIQSQRVRLDEAFDFVKQRRGVISPNFSFMGQLLQFETQVL 143
DSP_MKP cd14512
dual specificity phosphatase domain of mitogen-activated protein kinase phosphatase; ...
 20-154 2.44e-29

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: 106.03  E-value: 2.44e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  20 LSQITKSLFISNGAAANDKLLLSSNQITTVINVSVEVANTFYE-DIQYVQVPVVDAPIARLSDFFDPIADHIHSVEMKQG 98
Cdd:cd14512    1 PTRILPNLYLGSQRDSLNLELMQQLGIGYVLNVSNTCPNPDFIgLFHYKRIPVNDSFCQNISPWFDEAIEFIEEAKASNG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 469608396  99 RTLLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHY 154
Cdd:cd14512   81 GVLVHCLAGISRSATIAIAYLMKRMRMSLDEAYDFVKEKRPTISPNFNFMGQLLDF 136
DSP_DUSP22_15 cd14519
dual specificity phosphatase domain of dual specificity protein phosphatase 22, 15, and ...
 20-155 3.33e-29

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: 105.52  E-value: 3.33e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  20 LSQITKSLFISNGAAANDKLLLSSNQITTVINVSvEVANTFYEDIQYVQVPVVDAPIARLSDFFDPIADHIHSVEMKQGR 99
Cdd:cd14519    1 MNKILPGLYVGNFRDAKDAEQLRENGITHILSIH-DSARPLLEDIKYLCIPAADTPEQNISQHFRECINFIHEARLNGGN 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 469608396 100 TLLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYE 155
Cdd:cd14519   80 VLVHCLAGVSRSVTIVAAYLMTVTDLGWRDALKAVRAARPCANPNFGFQRQLQEFE 135
DSP_MKP_classII cd14566
dual specificity phosphatase domain of class II mitogen-activated protein kinase phosphatase; ...
 22-154 1.09e-28

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: 104.32  E-value: 1.09e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  22 QITKSLFISNGAAANDKLLLSSNQITTVINVSVEVANTFYED--IQYVQVPVVDAPIARLSDFFdPIADH-IHSVEMKQG 98
Cdd:cd14566    3 EILPFLYLGNAKDSANIDLLKKYNIKYILNVTPNLPNTFEEDggFKYLQIPIDDHWSQNLSAFF-PEAISfIDEARSKKC 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 469608396  99 RTLLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHY 154
Cdd:cd14566   82 GVLVHCLAGISRSVTVTVAYLMQKLHLSLNDAYDFVKKRKSNISPNFNFMGQLLDF 137
DSP_slingshot cd14513
dual specificity phosphatase domain of slingshot family phosphatases; The slingshot (SSH) ...
 21-155 1.78e-28

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: 103.63  E-value: 1.78e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  21 SQITKSLFISNGAAANDKLLLSSNQITTVINVSVEVANTFYEDIQYVQVPVVDAPIARLSDFFDPIADHIHSVEMKQGRT 100
Cdd:cd14513    2 SKIFDHLYLGSEWNASNLEELQNNGVKYILNVTREIDNFFPGRFTYHNIRVWDEESTNLLPYWNETYRFIKEARRKGSKV 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 469608396 101 LLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYE 155
Cdd:cd14513   82 LVHCKMGVSRSASTVIAYAMKEYGWSLEQALEHVKERRSCIKPNPGFLRQLITYE 136
DSP_DUSP4 cd14640
dual specificity phosphatase domain of dual specificity protein phosphatase 4; Dual ...
 22-159 2.95e-28

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: 103.19  E-value: 2.95e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  22 QITKSLFISNGAAANDKLLLSSNQITTVINVSVEVANTFYEDIQYVQVPVVDAPIARLSDFFDPIADHIHSVEMKQGRTL 101
Cdd:cd14640    3 EILPFLYLGSAYHAARRDMLDALGITALLNVSSDCPNHFEGHYQYKCIPVEDNHKADISSWFMEAIEYIDSVKDCNGRVL 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 469608396 102 LHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYEFQLF 159
Cdd:cd14640   83 VHCQAGISRSATICLAYLMMKKRVRLEEAFEFVKQRRSIISPNFSFMGQLLQFESQVL 140
DSP_DUSP1 cd14638
dual specificity phosphatase domain of dual specificity protein phosphatase 1; Dual ...
 22-170 5.42e-28

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: 102.84  E-value: 5.42e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  22 QITKSLFISNGAAANDKLLLSSNQITTVINVSVEVANTFYEDIQYVQVPVVDAPIARLSDFFDPIADHIHSVEMKQGRTL 101
Cdd:cd14638    3 EILPFLYLGSAYHASRKDMLDTLGITALINVSANCPNHFEGHYQYKSIPVEDNHKADISSWFNEAIDFIDSVKNAGGRVF 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 469608396 102 LHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYEFQLFGKNTMQMVNSP 170
Cdd:cd14638   83 VHCQAGISRSATICLAYLMRTNRVKLDEAFEFVKQRRSIISPNFSFMGQLLQFESQVLAPSCSAEAGSP 151
DUSP13B cd14577
dual specificity protein phosphatase 13 isoform B; Dual specificity protein phosphatase 13 ...
 14-158 8.75e-27

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: 100.26  E-value: 8.75e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  14 QPSISGLSQITKSLFISNGAAANDKLLLSSNQITTVINVS-----VEVANTFYED--IQYVQVPVVDAPIARLSDFFDPI 86
Cdd:cd14577   12 RAPTGHVNEVWPNLYLGDAYAARDKSVLIQLGITHIVNAAsgkfhVNTGPKFYRDmnIDYYGVEADDNPFFDLSVYFYPV 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 469608396  87 ADHIHS-VEMKQGRTLLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIrPNSGFWEQLIHYEFQL 158
Cdd:cd14577   92 ARFIRAaLSSPNGRVLVHCAMGISRSATLVLAFLMICEDLTLVDAIQTVRAHRDIC-PNSGFLRQLRELDNRL 163
DSP_DUSP5 cd14639
dual specificity phosphatase domain of dual specificity protein phosphatase 5; Dual ...
 22-155 1.50e-26

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: 98.83  E-value: 1.50e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  22 QITKSLFISNGAAANDKLLLSSNQITTVINVSVEVANTFYEDIQYVQVPVVDAPIARLSDFFDPIADHIHSVEMKQGRTL 101
Cdd:cd14639    3 EILPFLYLGSAYHASKCEFLANLHITALLNVSRRSSEACKGQYHYKWIPVEDSHTADISSHFQEAIDFIDCVRRAGGKVL 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 469608396 102 LHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYE 155
Cdd:cd14639   83 VHCEAGISRSPTICMAYLMKTKRFRLEEAFDYIKQRRSLISPNFGFMGQLLQYE 136
DSP_DUSP10 cd14567
dual specificity phosphatase domain of dual specificity protein phosphatase 10; Dual ...
 20-155 3.28e-25

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: 95.59  E-value: 3.28e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  20 LSQITKSLFISNGAAANDKLLLSSNQITTVINVSVEVANTFYED--IQYVQVPVVDAPIARLSDFFDPIADHIHSVEMKQ 97
Cdd:cd14567    1 LTPILPFLYLGNERDAQDIDTLQRLNIGYVLNVTTHLPLYHEGKggFRYKRLPATDSNKQNLRQYFEEAFEFIEEAHQSG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 469608396  98 GRTLLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYE 155
Cdd:cd14567   81 KGVLVHCQAGVSRSATIVIAYLMKHTRMTMTDAYKFVKNKRPIISPNLNFMGQLLEFE 138
DUSP13A cd14580
dual specificity protein phosphatase 13 isoform A; Dual specificity protein phosphatase 13 ...
 27-158 5.51e-25

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: 94.82  E-value: 5.51e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  27 LFISNGAAANDKLLLSSNQITTVINVS-----VEVANTFY-EDIQYVQVPVVDAPIARLSDFFDPIADHIH-SVEMKQGR 99
Cdd:cd14580    8 LFLGDLATAHNRFGLWKLGITHVLNAAhgklfCQGGDDFYgTSVDYYGVPANDLPDFDISPYFYSAAEFIHrALNTPGAK 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 469608396 100 TLLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIrPNSGFWEQLIHYEFQL 158
Cdd:cd14580   88 VLVHCAVGVSRSATLVLAYLMIYHQLSLVQAIKTVKERRWIF-PNRGFLKQLRKLDQQL 145
DUPD1 cd14575
dual specificity phosphatase and pro isomerase domain containing 1; Dual specificity ...
 13-158 1.45e-24

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: 94.51  E-value: 1.45e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  13 PQPSISGLSQITKSLFISNGAAANDKLLLSSNQITTVINV-----SVEVANTFYED--IQYVQVPVVDAPIARLSDFFDP 85
Cdd:cd14575    4 GGPKYTHVNEVWPGLYIGDEKTALDRYSLQKLGITHILNAahgkwNVDTGAEYYKDmtIHYYGVEADDLPTFNLSQFFYS 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 469608396  86 IADHIH-SVEMKQGRTLLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIrPNSGFWEQLIHYEFQL 158
Cdd:cd14575   84 AAEFIHqALSDPHNKLLVHCVMGRSRSATLVLAYLMIYKNMTVVDAIEQVAQRRCIL-PNRGFLKQLRELDIQL 156
DUSP26 cd14578
dual specificity protein phosphatase 26; Dual specificity protein phosphatase 26 (DUSP26), ...
 22-152 4.85e-24

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: 92.59  E-value: 4.85e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  22 QITKSLFISNGAAANDKLLLSSNQITTVINVSVEV---ANTFYED--IQYVQVPVVDAPIARLSDFFDPIADHIH-SVEM 95
Cdd:cd14578    3 EVWPGLYLGDQDIAANRRELRRLGITHILNASHSKwrgGAEYYEGlnIRYLGIEAHDSPAFDMSIHFYPAADFIHrALSQ 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 469608396  96 KQGRTLLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIrPNSGFWEQLI 152
Cdd:cd14578   83 PGGKILVHCAVGVSRSATLVLAYLMIHHHMTLVEAIKTVKDHRGII-PNRGFLRQLL 138
DSP_fungal_YVH1 cd14518
dual specificity phosphatase domain of fungal YVH1-like dual specificity protein phosphatase; ...
 20-155 3.50e-23

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: 90.46  E-value: 3.50e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  20 LSQITKSLFISNGAAANDKLLLSSNQITTVINV-SVEVANTFYEDIQYVQVPVVDAPIARLSDFFDPIADHIHS------ 92
Cdd:cd14518    1 LSRILGGLYLGGIEPLNRNRLLKAENITHILSViPGDVPEEYFKGYEHKQIEIDDVEDENILQHFPETNRFIDSalfgng 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 469608396  93 -----VEMKQGRTLLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYE 155
Cdd:cd14518   81 kdedeEKKHGGAVLVHCAMGKSRSVTVVIAYLMYKYNLSVSQALHAVRRKRPIAEPNDGFMEQLELYH 148
DSP_DUSP15 cd14582
dual specificity phosphatase domain of dual specificity protein phosphatase 15; Dual ...
 18-151 3.57e-23

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: 90.39  E-value: 3.57e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  18 SGLSQITKSLFISNGAAANDKLLLSSNQITTVINVSvEVANTFYEDIQYVQVPVVDAPIARLSDFFDPIADHIHSVEMKQ 97
Cdd:cd14582    3 NGMTKVLPGLYLGNFIDAKDLEQLSRNKITHIISIH-ESPQPLLQDITYLRIPLPDTPEAPIKKHFKECISFIHQCRLNG 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 469608396  98 GRTLLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQL 151
Cdd:cd14582   82 GNCLVHCLAGISRSTTIVVAYVMAVTELSWQEVLEAIRAVRPIANPNPGFKQQL 135
DSP_STYXL1 cd14517
dual specificity phosphatase-like domain of serine/threonine/tyrosine interacting like 1; ...
 27-162 1.01e-22

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: 89.26  E-value: 1.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  27 LFISNGAAANDKLLLSSNQITTVINVSVEVANTFYEDI-QYVQVPVVDAPIARLSDFFDPIADHIHSVEMKQGRTLLHCA 105
Cdd:cd14517   19 LYMGNYKQACDKKIQKDLKIKAHINVSMDADELFKSGNdQVLHIPVEDSVEADLLSFFERACSFIDKHKNNGSRVLVFST 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 469608396 106 AGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYEFQLFGKN 162
Cdd:cd14517   99 LGISRSVAVAIAYLMYHYKWSLKDAWKYLLKCKNNMRPNRGFVKQLSEWEEKLLGTT 155
DUSP3 cd14579
dual specificity protein phosphatase 3; Dual specificity protein phosphatase 3 (DUSP3), also ...
 22-158 1.09e-21

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: 87.13  E-value: 1.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  22 QITKSLFISNGAAANDKLLLSSNQITTVINVS-------VEVANTFYED--IQYVQVPVVDAPIARLSDFFDPIADHIH- 91
Cdd:cd14579   23 EVYPRIYVGNASVAQNIMRLQRLGITHVLNAAegksfmhVNTNAEFYEDtgITYHGIKANDTQHFNLSAYFEEAADFIDk 102

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 469608396  92 SVEMKQGRTLLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPiIRPNSGFWEQLIHYEFQL 158
Cdd:cd14579  103 ALAQKNGRVLVHCREGYSRSPTLVIAYLMLRQKMDVKSALSTVRQKRE-IGPNDGFLKQLCQLNDKL 168
DSP_DUSP8 cd14645
dual specificity phosphatase domain of dual specificity protein phosphatase 8; Dual ...
 12-158 1.95e-21

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: 85.83  E-value: 1.95e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  12 FPQPSIsGLSQITKSLFISNGAAANDKLLLSSNQITTVINVSVEVAN-TFYEDIQYVQVPVVDAPIARLSDFFDPIADHI 90
Cdd:cd14645    5 LPVANV-GPTRILPHLYLGSQKDVLNKDLMAQNGITYVLNASNSCPKpDFICESHFMRIPVNDNYCEKLLPWLDKSIEFI 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 469608396  91 HSVEMKQGRTLLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYEFQL 158
Cdd:cd14645   84 DKAKVSNCRVIVHCLAGISRSATIAIAYIMKTMGLSSDDAYRFVKDRRPSISPNFNFLGQLLEYEKSL 151
DUSP22 cd14581
dual specificity protein phosphatase 22; Dual specificity protein phosphatase 22 (DUSP22), ...
 18-155 2.90e-21

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: 85.62  E-value: 2.90e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  18 SGLSQITKSLFISNGAAANDKLLLSSNQITTVINVSvEVANTFYEDIQYVQVPVVDAPIARLSDFFDPIADHIHSVEMKQ 97
Cdd:cd14581    2 NGMNKVLPGLYLGNFKDARDREQLSKNNITHILSVH-DSARPMLEGMTYLCIPAADSPSQNLTQHFKESIKFIHECRLRG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 469608396  98 GRTLLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYE 155
Cdd:cd14581   81 EGCLVHCLAGVSRSVTLVVAYIMTVTDFGWEDALSAVKAARSCANPNMGFQRQLQEFE 138
DSP_DUSP16 cd14646
dual specificity phosphatase domain of dual specificity protein phosphatase 16; Dual ...
 19-155 5.71e-21

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: 84.69  E-value: 5.71e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  19 GLSQITKSLFISNGAAANDKLLLSSNQITTVINVSVEVAN-TFYEDIQYVQVPVVDAPIARLSDFFDPIADHIHSVEMKQ 97
Cdd:cd14646    2 GPTRILPHLYLGCQRDVLNKELMQQNGIGYVLNASNTCPKpDFIPESHFLRVPVNDSFCEKILPWLDKSVDFIEKAKASN 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 469608396  98 GRTLLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYE 155
Cdd:cd14646   82 GRVLVHCLAGISRSATIAIAYIMKRMDMSLDEAYRFVKEKRPTISPNFNFLGQLLDFE 139
DSP_STYX cd14522
dual specificity phosphatase-like domain of serine/threonine/tyrosine-interacting protein; ...
 33-155 1.19e-20

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: 83.92  E-value: 1.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  33 AAANDKL-LLSSNQITTVINV-SVEVANT----FYEDIQYVQVPVVDAPIARLSDFFDPIADHIHSVEMKQGRTLLHCAA 106
Cdd:cd14522   19 AAMKSKLeVLLKHGITHIVCVrQNIEANFikpnFPDHFRYLVLDVADNPTENIIRHFPTVKEFIDDCLQTGGKVLVHGNA 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 469608396 107 GVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYE 155
Cdd:cd14522   99 GISRSAALVIAYIMETYGLSYRDAFAYVQQRRFCINPNEGFVHQLKEYE 147
DSP_DUSP12 cd14520
dual specificity phosphatase domain of dual specificity protein phosphatase 12 and similar ...
 27-155 1.37e-20

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: 83.45  E-value: 1.37e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  27 LFISNGAAANDKLLLSSNQITTVINVSVEVANTFYEDIQYVQ--VPVVDAPIARLSDFFDPIADHIhSVEMKQGRTLLHC 104
Cdd:cd14520    8 LYIGNADDAADYLSLREAGITHVLTVDSEEPIDAPPVGKLVRkfVPALDEESTDLLSRLDECLDFI-DEGRAEGAVLVHC 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 469608396 105 AAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYE 155
Cdd:cd14520   87 HAGVSRSAAVVTAYLMKTEQLSFEEALASLRECKPDVKPNDGFLKQLKLYE 137
DSP_slingshot_3 cd14571
dual specificity phosphatase domain of slingshot homolog 3; Dual specificity protein ...
 21-155 4.70e-20

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: 82.22  E-value: 4.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  21 SQITKSLFISNGAAANDKLLLSSNQITTVINVSVEVANTFYEDIQYVQVPVVDAPIARLSDFFDPIADHIHSVEMKQGRT 100
Cdd:cd14571    5 SRIFPYLYLGSEWNAANLEELQRNRVSHILNVTREIDNFFPERFTYMNIRVYDEEATQLLPHWKETHRFIEAARAQGTRV 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 469608396 101 LLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYE 155
Cdd:cd14571   85 LVHCKMGVSRSASTVIAYAMKQYGWTLEQALRHVRERRPIVQPNPGFLRQLQTYQ 139
DSP_slingshot_1 cd14570
dual specificity phosphatase domain of slingshot homolog 1; Dual specificity protein ...
 41-155 1.19e-17

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: 75.88  E-value: 1.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  41 LSSNQITTVINVSVEVANTFYEDIQYVQVPVVDAPIARLSDFFDPIADHIHSVEMKQGRTLLHCAAGVSRSAALCLAYLM 120
Cdd:cd14570   25 LQGSGVGYILNVTREIDNFFPGLFAYHNIRVYDEETTDLLAHWNDAYHFINKAKKNHSKCLVHCKMGVSRSASTVIAYAM 104

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 469608396 121 KYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYE 155
Cdd:cd14570  105 KEFGWSLEKAYNFVKQKRSITRPNAGFMRQLLEYE 139
DSP_fungal_SDP1-like cd14521
dual specificity phosphatase domain of fungal dual specificity protein phosphatase SDP1, MSG5, ...
 49-155 3.54e-17

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: 75.05  E-value: 3.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  49 VINVSVEVANTFYEDIQYVQVPVVDAPI----------------ARLSDFFDPIADHIHSVEMKQGRTLLHCAAGVSRSA 112
Cdd:cd14521   30 VINVAKEVKNPFLSDASLAEKEKTILPGqqvknpeyihvpwdhnSQIQKDLPKLTSIIEDATQSGKKVLIHCQCGVSRSA 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 469608396 113 ALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYE 155
Cdd:cd14521  110 SLIIAYIMKKLGLSLNDAYDLLKSRSPWIGPNMSLIFQLMEFE 152
DSP_DUSP7 cd14643
dual specificity phosphatase domain of dual specificity protein phosphatase 7; Dual ...
 22-158 5.19e-17

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: 74.29  E-value: 5.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  22 QITKSLFISNGAAANDKLLLSSNQITTVINVSVEVANTFYED--IQYVQVPVVDAPIARLSDFFDPIADHIHSVEMKQGR 99
Cdd:cd14643    8 QILPYLYLGCAKDSTNLDVLGKYGIKYILNVTPNLPNMFEHDgeFKYKQIPISDHWSQNLSQFFPEAISFIDEARSKKCG 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 469608396 100 TLLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYEFQL 158
Cdd:cd14643   88 ILVHCLAGISRSVTVTVAYLMQKLNLSLNDAYDFVKRKKSNISPNFNFMGQLLDFERTL 146
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
41-155 9.02e-17

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 73.47  E-value: 9.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  41 LSSNQITTVINVSV--EVANTFYED--IQYVQVPVVDAPIARLSDFfDPIADHIHSVEMKQGRTLLHCAAGVSRSAALCL 116
Cdd:COG2453   21 LKREGIDAVVSLTEeeELLLGLLEEagLEYLHLPIPDFGAPDDEQL-QEAVDFIDEALREGKKVLVHCRGGIGRTGTVAA 99

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 469608396 117 AYLMkYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYE 155
Cdd:COG2453  100 AYLV-LLGLSAEEALARVRAARPGAVETPAQRAFLERFA 137
DSP_fungal_PPS1 cd14516
dual specificity phosphatase domain of fungal dual specificity protein phosphatase PPS1-like; ...
 79-155 2.76e-16

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: 73.07  E-value: 2.76e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 469608396  79 LSDFFDPIADHIHSVEMKQGRTLLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRR--PIIRPNSGFWEQLIHYE 155
Cdd:cd14516   98 LLPQLTDALDFIQKARLLGGKTLVHCRVGVSRSATVVIAEVMKHLRMSLVDAYLFVRVRRlnIIIQPNLRFFYELFKWE 176
DSP_DUSP9 cd14644
dual specificity phosphatase domain of dual specificity protein phosphatase 9; Dual ...
 22-158 3.58e-16

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: 71.95  E-value: 3.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  22 QITKSLFISNGAAANDKLLLSSNQITTVINVSVEVANTFYE--DIQYVQVPVVDAPIARLSDFFDPIADHIHSVEMKQGR 99
Cdd:cd14644    5 QILPNLYLGSARDSANLETLAKLGIRYILNVTPNLPNFFEKngDFHYKQIPISDHWSQNLSQFFPEAIEFIDEALSQNCG 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 469608396 100 TLLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYEFQL 158
Cdd:cd14644   85 VLVHCLAGISRSVTVTVAYLMQKLNLSLNDAYDLVKRKKSNISPNFNFMGQLLDFEKSL 143
DSP_iDUSP27 cd14576
dual specificity phosphatase-like domain of inactive dual specificity protein phosphatase 27; ...
 18-151 8.07e-16

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: 71.44  E-value: 8.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  18 SGLSQITKSLFISNGAAANDKLLLSSNQITTVINVS----VEVANTFYE--DIQYVQVPVVDAPIARLSDFFDPIADHIH 91
Cdd:cd14576    9 NAVDEVWPNVFIAEKSVAVNKGRLKRLGITHVLNAAhgtgVYTGPEFYSgmNIQYMGIEVDDFPDVDISKHFRKGAEFLD 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 469608396  92 SVEMK-QGRTLLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPiIRPNSGFWEQL 151
Cdd:cd14576   89 EALLTyRGKVLVSSEMGISRSAVLVAAYLMIFHNMTIMEALMTLRKKRA-IYPNEGFLKQL 148
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 62-154 3.63e-15

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: 69.21  E-value: 3.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  62 EDIQYVQVPVVD----APIARLS---DFfdpiadhIHSVEMKQGRTLLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWT 134
Cdd:cd14524   54 LGVEQLRLPTVDftgvPSLEDLEkgvDF-------ILKHREKGKSVYVHCKAGRGRSATIVACYLIQHKGWSPEEAQEFL 126

                         90       100
                 ....*....|....*....|
gi 469608396 135 KSRRPIIRPNSGFWEQLIHY 154
Cdd:cd14524  127 RSKRPHILLRLSQREVLEEF 146
DSP_slingshot_2 cd14569
dual specificity phosphatase domain of slingshot homolog 2; Dual specificity protein ...
 21-155 4.49e-15

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: 69.28  E-value: 4.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  21 SQITKSLFISNGAAANDKLLLSSNQITTVINVSVEVANTFYEDIQYVQVPVVDAPIARLSDFFDPIADHIHSVEMKQGRT 100
Cdd:cd14569    5 TQIFEHVFLGSEWNASNLEDLQNRGVRYILNVTREIDNFFPGLFEYHNIRVYDEEATDLLAYWNDTYKFISKAKKHGSKC 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 469608396 101 LLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYE 155
Cdd:cd14569   85 LVHCKMGVSRSASTVIAYAMKEYGWNLDRAYDYVKERRTVTKPNPSFMRQLEEYQ 139
DSP_plant_IBR5-like cd18534
dual specificity phosphatase domain of plant IBR5-like protein phosphatases; This subfamily is ...
 83-154 1.84e-13

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: 64.48  E-value: 1.84e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 469608396  83 FDPIADHIHSVEMKQGRTLLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHY 154
Cdd:cd18534   59 FAEAVDFIEQCRKDKARVLVHCMSGQSRSPAVVIAYLMKHKGWRLAESYQWVKERRPSINLSPAVAKQLQEF 130
DSP_DUSP6 cd14642
dual specificity phosphatase domain of dual specificity protein phosphatase 6; Dual ...
 22-158 1.32e-12

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: 62.40  E-value: 1.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  22 QITKSLFISNGAAANDKLLLSSNQITTVINVSVEVANTFYE--DIQYVQVPVVDAPIARLSDFFDPIADHIHSVEMKQGR 99
Cdd:cd14642    5 EILPYLYLGCAKDSTNLDVLEEFGIKYILNVTPNLPNLFENagEFKYKQIPISDHWSQNLSQFFPEAISFIDEARGKNCG 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 469608396 100 TLLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYEFQL 158
Cdd:cd14642   85 VLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFERTL 143
DSP_laforin-like cd14526
dual specificity phosphatase domain of laforin and similar domains; This family is composed of ...
 21-139 3.93e-09

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: 52.97  E-value: 3.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  21 SQITKSL----FISNGAaanDKLLLSSNQITTVIN-----------VSVEVANTFYE--DIQYVQVPVVDApiarlsDFF 83
Cdd:cd14526    4 SRILPNLivgsCPQNPE---DVDRLKKEGVTAVLNlqtdsdmeywgVDIDSIRKACKesGIRYVRLPIRDF------DTE 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 469608396  84 D-----PIADHIHSVEMKQGRTL-LHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRP 139
Cdd:cd14526   75 DlrqklPQAVALLYRLLKNGGTVyVHCTAGLGRAPATVIAYLYWVLGYSLDEAYYLLTSKRP 136
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 81-153 4.00e-08

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: 49.66  E-value: 4.00e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 469608396  81 DFFDPIADHIHSVEMKQGRTLLHCAAGVSRSAALCLAYLMKYHAMSLLDAHAWTKSRRP-IIRPNSGFWEQLIH 153
Cdd:cd14494   40 AMVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGMSAEEAVRIVRLIRPgGIPQTIEQLDFLIK 113
DSP_bac cd14527
unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily ...
 66-144 3.45e-07

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: 47.65  E-value: 3.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  66 YVQVPVVD--AP----IARLSDFFDPIADhihsvemKQGRTLLHCAAGVSRSAALCLAYLMKY-HAMSLLDAHAWTKSRR 138
Cdd:cd14527   46 YRCVPLLDlvAPtpeqLERAVAWIEELRA-------QGGPVLVHCALGYGRSATVVAAWLLAYgRAKSVAEAEALIRAAR 118


                 ....*.
gi 469608396 139 PIIRPN 144
Cdd:cd14527  119 PQVVLN 124
PRK12361 PRK12361
hypothetical protein; Provisional
 15-145 2.33e-06

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 47.31  E-value: 2.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  15 PSISglsQITKSLFISNGAAANDKLLLSSNQITTVINVSVEVA----NTFYEDIQYVQVPVVDAPIARLSDFFDPIAdHI 90
Cdd:PRK12361  93 PAIQ---KIDENLYLGCRLFPADLEKLKSNKITAILDVTAEFDgldwSLTEEDIDYLNIPILDHSVPTLAQLNQAIN-WI 168

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 469608396  91 HSvEMKQGRT-LLHCAAGVSRSAALCLAYLM-KYHAMSLLDAHAWTKSRRPIIRPNS 145
Cdd:PRK12361 169 HR-QVRANKSvVVHCALGRGRSVLVLAAYLLcKDPDLTVEEVLQQIKQIRKTARLNK 224
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 41-139 8.91e-06

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: 43.81  E-value: 8.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  41 LSSNQITTVINVSVEVANT---FYEDIQYVQVPVVD--AP----IARLSDFfdpiadhIHSVEMKQGRTLLHCAAGVSRS 111
Cdd:cd14504   24 LNENGIRHVVTLTEEPPPEhsdTCPGLRYHHIPIEDytPPtleqIDEFLDI-------VEEANAKNEAVLVHCLAGKGRT 96

                         90       100
                 ....*....|....*....|....*...
gi 469608396 112 AALCLAYLMKYHAMSLLDAHAWTKSRRP 139
Cdd:cd14504   97 GTMLACYLVKTGKISAVDAINEIRRIRP 124
RNA_5'-triphosphatase cd14502
RNA 5'-triphosphatase domain; This family of RNA-specific cysteine phosphatases includes ...
 42-151 6.42e-04

RNA 5'-triphosphatase domain; This family of RNA-specific cysteine phosphatases includes baculovirus RNA 5'-triphosphatase, dual specificity protein phosphatase 11 (DUSP11), and the RNA triphosphatase domains of metazoan and plant mRNA capping enzymes. RNA/polynucleotide 5'-triphosphatase (EC 3.1.3.33) catalyzes the removal of the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end. mRNA capping enzyme is a bifunctional enzyme that catalyzes the first two steps of cap formation. DUSP11 has RNA 5'-triphosphatase and diphosphatase activity, but only poor protein-tyrosine phosphatase activity.


Pssm-ID: 350352 [Multi-domain]  Cd Length: 167  Bit Score: 38.79  E-value: 6.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469608396  42 SSNQITTVINVSVEvaNTFY-----EDIQYVQVPVV----DAPIARLSDFFDPIADHIHSVEMKQGRTLLHCAAGVSRSA 112
Cdd:cd14502   49 QDRKVGLVIDLTNT--DRYYdpndlDDDGYVYYKKVcvrkEPPDAEEVNKFIELVDKFLAEDNPDKLIAVHCTHGFNRTG 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 469608396 113 ALCLAYLMKYHAMSLLDA-HAWTKSRRPIIRpNSGFWEQL 151
Cdd:cd14502  127 FMIVSYLVERLGLTVEQAlEAFAQARPPGIY-KPHYIDEL 165
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
81-120 7.29e-04

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 37.72  E-value: 7.29e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 469608396    81 DFFDPIADHIHSVE------MKQGRTLLHCAAGVSRSAALCLAYLM 120
Cdd:smart00404  17 ESPDSILELLRAVKknlnqsESSGPVVVHCSAGVGRTGTFVAIDIL 62
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 81-120 7.29e-04

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: 37.72  E-value: 7.29e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 469608396    81 DFFDPIADHIHSVE------MKQGRTLLHCAAGVSRSAALCLAYLM 120
Cdd:smart00012  17 ESPDSILELLRAVKknlnqsESSGPVVVHCSAGVGRTGTFVAIDIL 62
 
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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