O95147 · DUS14_HUMAN
- ProteinDual specificity protein phosphatase 14
- GeneDUSP14
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids198 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the inactivation of MAP kinases. Dephosphorylates ERK, JNK and p38 MAP-kinases. Plays a negative role in TCR signaling by dephosphorylating MAP3K7 adapter TAB1 leading to its inactivation (PubMed:24403530).
Catalytic activity
- H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 111 | Phosphocysteine intermediate | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | MAP kinase tyrosine/serine/threonine phosphatase activity | |
Molecular Function | myosin phosphatase activity | |
Molecular Function | protein tyrosine phosphatase activity | |
Molecular Function | RNA binding |
Keywords
- Molecular function
Enzyme and pathway databases
Limits apoptotic and necroptotic cell death in keratinocytes. Promotes dephosphorylation of the deubiquitinase OTULIN.
Names & Taxonomy
Protein names
- Recommended nameDual specificity protein phosphatase 14
- EC number
- Alternative names
Gene names
- Community suggested namesDUSP14; Mkp6.
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO95147
Proteomes
Organism-specific databases
Disease & Variants
Variants
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The viewer provides 308 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000094822 | 1-198 | Dual specificity protein phosphatase 14 | |||
Sequence: MSSRGHSTLPRTLMAPRMISEGDIGGIAQITSSLFLGRGSVASNRHLLQARGITCIVNATIEIPNFNWPQFEYVKVPLADMPHAPIGLYFDTVADKIHSVSRKHGATLVHCAAGVSRSATLCIAYLMKFHNVCLLEAYNWVKARRPVIRPNVGFWRQLIDYERQLFGKSTVKMVQTPYGIVPDVYEKESRHLMPYWGI |
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with CD28.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O95147 | CBY2 Q8NA61 | 3 | EBI-3922653, EBI-741724 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 26-167 | Tyrosine-protein phosphatase | ||||
Sequence: GIAQITSSLFLGRGSVASNRHLLQARGITCIVNATIEIPNFNWPQFEYVKVPLADMPHAPIGLYFDTVADKIHSVSRKHGATLVHCAAGVSRSATLCIAYLMKFHNVCLLEAYNWVKARRPVIRPNVGFWRQLIDYERQLFG |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length198
- Mass (Da)22,255
- Last updated1999-05-01 v1
- Checksum6AAFAE1B3A24F9AA
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF038844 EMBL· GenBank· DDBJ | AAD02105.1 EMBL· GenBank· DDBJ | mRNA | ||
AF120032 EMBL· GenBank· DDBJ | AAF28861.1 EMBL· GenBank· DDBJ | mRNA | ||
BC000370 EMBL· GenBank· DDBJ | AAH00370.1 EMBL· GenBank· DDBJ | mRNA | ||
BC001894 EMBL· GenBank· DDBJ | AAH01894.1 EMBL· GenBank· DDBJ | mRNA | ||
BC004448 EMBL· GenBank· DDBJ | AAH04448.1 EMBL· GenBank· DDBJ | mRNA |