DUSP10
Dual specificity protein phosphatase 10
Also known as: DUS10_HUMAN, MKP-5, MKP5
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q9Y6W6
- Gene
- DUSP10
- Ensembl
- ENSG00000143507
- Chromosome
- 1
- Canonical length
- 482 aa
- Protein class
- Enzymes, Predicted intracellular proteins
- Subcellular location
- Nucleoplasm,Cytosol
OverviewNCBI Gene
Dual specificity protein phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members of the MAP kinase superfamily, which is associated with cellular proliferation and differentiation. Different members of this family of dual specificity phosphatases show distinct substrate specificities for MAP kinases, different tissue distribution and subcellular localization, and different modes of expression induction by extracellular stimuli. This gene product binds to and inactivates p38 and SAPK/JNK. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Apr 2014]
Canonical amino-acid sequenceUniProt
482 residues, UniProt reviewed canonical sequence.
>Q9Y6W6|DUSP10
1 MPPSPLDDRV VVALSRPVRP QDLNLCLDSS YLGSANPGSN SHPPVIATTV VSLKAANLTY
61 MPSSSGSARS LNCGCSSASC CTVATYDKDN QAQTQAIAAG TTTTAIGTST TCPANQMVNN
121 NENTGSLSPS SGVGSPVSGT PKQLASIKII YPNDLAKKMT KCSKSHLPSQ GPVIIDCRPF
181 MEYNKSHIQG AVHINCADKI SRRRLQQGKI TVLDLISCRE GKDSFKRIFS KEIIVYDENT
241 NEPSRVMPSQ PLHIVLESLK REGKEPLVLK GGLSSFKQNH ENLCDNSLQL QECREVGGGA
301 SAASSLLPQP IPTTPDIENA ELTPILPFLF LGNEQDAQDL DTMQRLNIGY VINVTTHLPL
361 YHYEKGLFNY KRLPATDSNK QNLRQYFEEA FEFIEEAHQC GKGLLIHCQA GVSRSATIVI
421 AYLMKHTRMT MTDAYKFVKG KRPIISPNLN FMGQLLEFEE DLNNGVTPRI LTPKLMGVET
481 VVLocalizationUniProt · AlphaFold · HPA
Whether an antibody against DUSP10 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Intracellular
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.4
- Highest tissue expression
- 31 nTPM
Expression across tissuesHPA
Tissue
- liver: 31 nTPM
- bone marrow: 24 nTPM
- skeletal muscle: 22 nTPM
- pancreas: 16 nTPM
- retina: 14 nTPM
- lymph node: 8.5 nTPM
Single-cell type
- mast cells: 211 nCPM
- salivary ionocytes: 171 nCPM
- endometrial glandular cells: 126 nCPM
- ocular epithelial cells: 118 nCPM
- innate lymphoid cells: 112 nCPM
- endometrial ciliated cells: 107 nCPM
Immune cell
- NK-cell: 20 nTPM
- T-reg: 17 nTPM
- basophil: 8.3 nTPM
- myeloid DC: 7 nTPM
- classical monocyte: 5.5 nTPM
- gdT-cell: 4.6 nTPM
Brain region
- white matter: 29 nTPM
- thalamus: 22 nTPM
- cerebellum: 18 nTPM
- basal ganglia: 17 nTPM
- medulla oblongata: 17 nTPM
- cerebral cortex: 16 nTPM
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 0.43
- gnomAD pLI
- 0.83
- gnomAD missense Z
- 1.19
- DepMap mean gene effect
- 0.03
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 6% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- dephosphorylation
- negative regulation of cell migration
- negative regulation of epithelial cell migration
- negative regulation of epithelial cell proliferation
- negative regulation of ERK1 and ERK2 cascade
- negative regulation of JNK cascade
- negative regulation of oligodendrocyte differentiation
- negative regulation of p38MAPK cascade
- negative regulation of respiratory burst involved in inflammatory response
- negative regulation of stress-activated MAPK cascade
- oligodendrocyte differentiation
- positive regulation of regulatory T cell differentiation
- regulation of adaptive immune response
- regulation of brown fat cell differentiation
- response to lipopolysaccharide
- signal transduction
- stress-activated MAPK cascade
- negative regulation of epithelium regeneration
Molecular functions
- JUN kinase binding
- MAP kinase phosphatase activity
- MAP kinase tyrosine phosphatase activity
- MAP kinase tyrosine/serine/threonine phosphatase activity
- mitogen-activated protein kinase p38 binding
- phosphatase activity
- protein serine/threonine phosphatase activity
- protein tyrosine/threonine phosphatase activity
Cellular components
Protein domainsUniProt · Pfam · InterPro
- Dual specificity phosphatase, catalytic domain
- Tyrosine-specific protein phosphatases domain
- Rhodanese-like domain
- Mitogen-activated protein (MAP) kinase phosphatase
- Protein-tyrosine phosphatase, active site
- Dual specificity protein phosphatase domain
- Protein-tyrosine phosphatase-like
- Rhodanese-like domain superfamily
- Rhodanese-like domain
- Dual specificity phosphatase, catalytic domain
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of DUSP10 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads DUSP10 as an antibody target. Whether an autoantibody or antibody against DUSP10 could matter depends on whether native DUSP10 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
DUSP10 is annotated as predominantly intracellular. Intracellular proteins are common autoantibody markers, becoming visible to the immune system after cell injury or altered processing, but are usually markers of disease rather than direct drivers.
Annotation status
The present source text does not explicitly label DUSP10 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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