2OUD


Conserved Protein Domain Family
DSP_DUSP10
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cd14567: DSP_DUSP10 
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.
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Statistics
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PSSM-Id: 350415
Aligned: 8 rows
Threshold Bit Score: 261.608
Created: 30-Sep-2010
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
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active sitecatalytic site
Conserved site includes 9 residues -Click on image for an interactive view with Cn3D
Feature 1: active site [active site], 9 residue positions
Conserved feature residue pattern:x x C x x x x x RClick to see conserved feature residue pattern help
Evidence:
  • Structure:2OUD: Human MKP5 binds a chloride ion in the active site; contacts at 4A
  • Comment:mostly based on the structures of some DUSP family members with bound phosphorylated substrates (peptide and non-peptide)
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Sequence Alignment
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Format: Row Display: Color Bits: Type Selection: 
Feature 1                   #                                             #                      
2OUD_A         8 LTPILPFLFLGNEQDAQDLDTMQRLnIGYVINVTTHLPLYHYek--gLFNYKRLPATDSNkQNLRQYFEEAFEFIEE--- 82  human
XP_002604428 180 PSLVLPFMYLGNERDAADIRTLLRLnIGYILNVTSHIPLHHEgf--cGIKYKRLPATDSQhQNLLQYFEEAFEFIDE--- 254 Florida lancelet
XP_002411928 254 VTRVLPFLFLGNERDARDADLLDRLgVGYVLHVTTTPPPGLQarhgpGLRCKRLPASDSChQNLKQFFEEAFAFLDE--- 330 black-legged tick
CAX73575     368 ISRIFPFLYLGNEFDSQNEKILNKYsIDSILNVTVKTPFLDEs----RYQCCRLSATDSHsQDLRSYFTTAFQFIED--- 440 Schistosoma jap...
CAG09195     323 LTPILPFLYLGNEHDAQDISLLQRFhIGYILNVTTHLPLYHYds--gLFVYKRLPVTDSNkQNLRQYFEEAFEFIGMvli 400 spotted green p...
XP_789413    349 MTQILPHLYVGNEVDAANIDALRLHgISHVLNVTNSVPCFHEge--sAMRYMRIPVRDNGlINLRMHFQAALEFIEE--- 423 purple urchin
NP_001026215 318 LTPILPFLFLGNEHDAQDLEKMQRMnIGYVINVTTHLPLYHYek--gMFNYKRLPATDSNkQNLRQYFEEAFEFIEE--- 392 chicken
Q9Y6W6       322 LTPILPFLFLGNEQDAQDLDTMQRLnIGYVINVTTHLPLYHYek--gLFNYKRLPATDSNkQNLRQYFEEAFEFIEE--- 396 human

Feature 1                     #######                                                           
2OUD_A        83 --AHQCGKGLLIHCQAGVSRSATIVIAYLMKHTRMTMTDAYKFVKGKRPIISPNLNFMGQLLEFEEDLNNGVTPRILTP 159 human
XP_002604428 255 --ARSSGRNLLIHCQAGVSRSATIAIGYIMKHTRMTMMDAYKFVKNKRTVISPNLNFMGQLVEYETALNIGLTPRVLYP 331 Florida lancelet
XP_002411928 331 --AHANGSRVLVHCHAGISRSPTITVAYLMRHLRLPLVDAYRYLKAKRPIISPNLNFMGQLMELEQNLAQQPEQAPCAQ 407 black-legged tick
CAX73575     441 --ARCSGKTVLVHCQAGVSRSPALIIAYLMAYSSLSLLDAYQYVKLKRSVIAPNFAFMGQLYELESDLTSGRLLRQSDT 517 Schistosoma japo...
CAG09195     401 eeAHQAGIGLLIHCQAGVSRSATIVIAYLMKHTWMTMTDAYKFVKTRRPIISPNLNFMGQLLEFEEDLNNGITPRILTP 479 spotted green pu...
XP_789413    424 --ARRRNARVLVHCHAGISRSSTVVIAYVMKHMNQAMSQAYQFVKNKRPIIAPNLGFVGQLMEFEQILNKMNAPRSAGC 500 purple urchin
NP_001026215 393 --AHQCGKGLLIHCQAGVSRSATIVIAYLMKHTRMTMTDAYKFVKGKRPIISPNLNFMGQLLEFEEDLNNGVTPRILTP 469 chicken
Q9Y6W6       397 --AHQCGKGLLIHCQAGVSRSATIVIAYLMKHTRMTMTDAYKFVKGKRPIISPNLNFMGQLLEFEEDLNNGVTPRILTP 473 human

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