DUSP8
Dual specificity protein phosphatase 8
Also known as: C11orf81, DUS8_HUMAN, FLJ42958, HB5, HVH-5
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q13202
- Gene
- DUSP8
- Ensembl
- ENSG00000184545
- Chromosome
- 11
- Canonical length
- 625 aa
- Protein class
- Enzymes, Predicted intracellular proteins
- Subcellular location
- Cytosol
OverviewNCBI Gene
The protein encoded by this gene is a member of the dual specificity protein phosphatase subfamily. These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members of the mitogen-activated protein (MAP) kinase superfamily (MAPK/ERK, SAPK/JNK, p38), which is associated with cellular proliferation and differentiation. Different members of the family of dual specificity phosphatases show distinct substrate specificities for various MAP kinases, different tissue distribution and subcellular localization, and different modes of inducibility of their expression by extracellular stimuli. This gene product inactivates SAPK/JNK and p38, is expressed predominantly in the adult brain, heart, and skeletal muscle, is localized in the cytoplasm, and is induced by nerve growth factor and insulin. An intronless pseudogene for DUSP8 is present on chromosome 10q11.2. [provided by RefSeq, Jul 2008]
Canonical amino-acid sequenceUniProt
625 residues, UniProt reviewed canonical sequence.
>Q13202|DUSP8
1 MAGDRLPRKV MDAKKLASLL RGGPGGPLVI DSRSFVEYNS WHVLSSVNIC CSKLVKRRLQ
61 QGKVTIAELI QPAARSQVEA TEPQDVVVYD QSTRDASVLA ADSFLSILLS KLDGCFDSVA
121 ILTGGFATFS SCFPGLCEGK PAALLPMSLS QPCLPVPSVG LTRILPHLYL GSQKDVLNKD
181 LMTQNGISYV LNASNSCPKP DFICESRFMR VPINDNYCEK LLPWLDKSIE FIDKAKLSSC
241 QVIVHCLAGI SRSATIAIAY IMKTMGMSSD DAYRFVKDRR PSISPNFNFL GQLLEYERSL
301 KLLAALQGDP GTPSGTPEPP PSPAAGAPLP RLPPPTSESA ATGNAAAREG GLSAGGEPPA
361 PPTPPATSAL QQGLRGLHLS SDRLQDTNRL KRSFSLDIKS AYAPSRRPDG PGPPDPGEAP
421 KLCKLDSPSG AALGLSSPSP DSPDAAPEAR PRPRRRPRPP AGSPARSPAH SLGLNFGDAA
481 RQTPRHGLSA LSAPGLPGPG QPAGPGAWAP PLDSPGTPSP DGPWCFSPEG AQGAGGVLFA
541 PFGRAGAPGP GGGSDLRRRE AARAEPRDAR TGWPEEPAPE TQFKRRSCQM EFEEGMVEGR
601 ARGEELAALG KQASFSGSVE VIEVSLocalizationUniProt · AlphaFold · HPA
Whether an antibody against DUSP8 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)
- 0.52
- Highest tissue expression
- 44 nTPM
Expression across tissuesHPA
Tissue
- cerebellum: 44 nTPM
- cerebral cortex: 43 nTPM
- hippocampal formation: 42 nTPM
- amygdala: 39 nTPM
- basal ganglia: 38 nTPM
- pituitary gland: 25 nTPM
Single-cell type
- brain inhibitory neurons: 24 nCPM
- brain excitatory neurons: 22 nCPM
- other brain neurons: 20 nCPM
- oligodendrocytes: 9.2 nCPM
- oligodendrocyte progenitor cells: 8.4 nCPM
- podocytes: 8 nCPM
Immune cell
- basophil: 0 nTPM
- classical monocyte: 0 nTPM
- eosinophil: 0 nTPM
- gdT-cell: 0 nTPM
- intermediate monocyte: 0 nTPM
- MAIT T-cell: 0 nTPM
Brain region
- cerebral cortex: 30 nTPM
- hippocampal formation: 23 nTPM
- amygdala: 20 nTPM
- basal ganglia: 19 nTPM
- white matter: 17 nTPM
- medulla oblongata: 13 nTPM
DiseaseUniProt · ClinVar · IEDB · PubMed
Four sources answering four different questions about DUSP8.
Disease | ImmuneIEDB
Conditions an epitope on DUSP8 was assayed in.
- narcolepsy B cell
- multiple sclerosis B cell
- peripheral nervous system disease B cell
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)
- 0.5
- gnomAD pLI
- 0.7
- gnomAD missense Z
- 2.33
- DepMap mean gene effect
- -0.1
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
Molecular functions
- MAP kinase tyrosine phosphatase activity
- MAP kinase tyrosine/serine/threonine phosphatase activity
- 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
- Dual specificity protein phosphatase 8, dual specificity phosphatase domain
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of DUSP8 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 DUSP8 as an antibody target. Whether an autoantibody or antibody against DUSP8 could matter depends on whether native DUSP8 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
DUSP8 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 DUSP8 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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