1YZ4,1WRM


Conserved Protein Domain Family
DSP_DUSP22_15

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cd14519: DSP_DUSP22_15 
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.
Statistics
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PSSM-Id: 350369
Aligned: 9 rows
Threshold Bit Score: 228.788
Created: 30-Sep-2010
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
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:1YZ4: Human DUSP15 binds a sulfate ion in the active site; contacts at 4A
  • Structure:1WRM: Human JSP-1 binds an MES molecule in the active site; contacts at 4A
  • Comment:also based on the structures of some DUSP family members with bound phosphorylated substrates (peptide and non-peptide)

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                   #                                           #                        
1YZ4_A         8 MTKVLPGLYLGNFIDAKDLDQLGRNkiTHIISIHespq---pllqDITYLRIPVADtpevpiKKHFKECINFIHCCRLng 84  human
1WRM_A         7 MNKILPGLYIGNFKDARDAEQLSKNkvTHILSVHdsar---pmleGVKYLCIPAADspsqnlTRHFKESIKFIHECRLrg 83  human
XP_002408685   5 MNKVLPGVFIGNFRDSKDPEQLRANniTHIISIHdtar---klheDKEYLCIQASDtpgqnlTQFFSQSNDFIHHARIeg 81  black-legged tick
XP_002116159   5 MCKILPGLYVGSYRDVHDNNQLKKNgiTHILAVHdnsr---plhdHMVYKCIECMDtpqqdiSQHFRECINFIHRSRInd 81  Trichoplax adha...
XP_001627020   5 MNKIIPGLYLGNIRDSKDAEQLQEHniTHILSIHdnan---plreDIMYKCIHAADspdqdlMPFFQECIEFIHSCRVke 81  starlet sea ane...
AAP06063       5 MSKIVPGLYVGGVASAQSKSQLDENgiTHVCSVLhynf----kcpSRKQIILRADDdskeniAKYFRDACFFIHEARVyn 80  Schistosoma jap...
NP_648654      5 MNKVLPGLYVGNYRDSKDHAQLERFkiSHIIAIHdspr---rllpDKHYLCVMASDtpdqnlSQYFSVCNDFIHAARLre 81  fruit fly
EFO18643      29 MTQILPYLYLGSICDANDVEQLREKqiDHVVSLHelsgrtgsilnELNILRIHMADmpeaniSEHFAETATFIHRARLlk 108 Loa loa
XP_019640309   5 MNKVLPGLYIGNFRDSKDREQLTTHgiTHILAIHdnak---klheDMNYLCIPASDsphqnlTQHFRKSIKFIHESRLgg 81  Belcher's lancelet
Feature 1              #######                                              
1YZ4_A        85 GNCLVHSFAGISRSTTIVTAYVMTVtglgwRDVLEAIKATRpiaNPNPGFRQQLEEFGW 143 human
1WRM_A        84 ESCLVHCLAGVSRSVTLVIAYIMTVtdfgwEDALHTVRAGRscaNPNVGFQRQLQEFEK 142 human
XP_002408685  82 GNVLIHCLAGVSRSVTIAVAYVMSVtslnwRESLKAVRGARsiaNPNFGFQKQLHEYEC 140 black-legged tick
XP_002116159  82 GSVLVHCLAGVSRSVTIVLAYLITVtdmkwEDALKAVRASRtqaNPNLGFRRQLQIYTE 140 Trichoplax adhaerens
XP_001627020  82 MNCLVHCIAGISRSTTICAAYIMTItelswRQTLQAIRANRsiaNPNYGFKRQLQDFYN 140 starlet sea anemone
AAP06063      81 GAVLVHCACGVSRSVTITLAYLMTVtnmplPKLVRAVVGARpcaCPNSGFLEQLIEFGK 139 Schistosoma japonicum
NP_648654     82 GNVLIHCLAGMSRSVTVAVAYIMTAthlnwKEALKVVRAGRavaNPNAGFQSQLQEFEQ 140 fruit fly
EFO18643     109 KSVLVHCIAGVSRSVCIVAAYLIAAcdmsyAASLAYIVSKRpcaNPNFGFRMQLAKYAG 167 Loa loa
XP_019640309  82 GACLIHCLAGVSRSVTVAAAYVMTVtnlgwRDTLKAIRQARavaNPNFGFQRQLQEFDA 140 Belcher's lancelet

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