DUSP2
Dual specificity protein phosphatase 2
Also known as: DUSP2_HUMAN, PAC-1
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q05923
- Gene
- DUSP2
- Ensembl
- ENSG00000158050
- Chromosome
- 2
- Canonical length
- 314 aa
- Protein class
- Enzymes, Predicted intracellular proteins
- Subcellular location
- Nucleoplasm,Nuclear membrane
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 are 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 ERK1 and ERK2, is predominantly expressed in hematopoietic tissues, and is localized in the nucleus. [provided by RefSeq, Jul 2008]
Canonical amino-acid sequenceUniProt
314 residues, UniProt reviewed canonical sequence.
>Q05923|DUSP2
1 MGLEAARELE CAALGTLLRD PREAERTLLL DCRPFLAFCR RHVRAARPVP WNALLRRRAR
61 GPPAAVLACL LPDRALRTRL VRGELARAVV LDEGSASVAE LRPDSPAHVL LAALLHETRA
121 GPTAVYFLRG GFDGFQGCCP DLCSEAPAPA LPPTGDKTSR SDSRAPVYDQ GGPVEILPYL
181 FLGSCSHSSD LQGLQACGIT AVLNVSASCP NHFEGLFRYK SIPVEDNQMV EISAWFQEAI
241 GFIDWVKNSG GRVLVHCQAG ISRSATICLA YLMQSRRVRL DEAFDFVKQR RGVISPNFSF
301 MGQLLQFETQ VLCHLocalizationUniProt · AlphaFold · HPA
Whether an antibody against DUSP2 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)
- 0.27
- Highest tissue expression
- 122 nTPM
Expression across tissuesHPA
Tissue
- bone marrow: 122 nTPM
- seminal vesicle: 58 nTPM
- urinary bladder: 46 nTPM
- lymph node: 44 nTPM
- thymus: 44 nTPM
- spleen: 41 nTPM
Single-cell type
- nk-cells: 663 nCPM
- t-cells: 613 nCPM
- cdc: 607 nCPM
- innate lymphoid cells: 538 nCPM
- epididymal principal cells: 497 nCPM
- endometrial glandular cells: 358 nCPM
Immune cell
- gdT-cell: 200 nTPM
- memory CD8 T-cell: 176 nTPM
- NK-cell: 148 nTPM
- naive CD8 T-cell: 100 nTPM
- MAIT T-cell: 96 nTPM
- memory CD4 T-cell: 47 nTPM
Brain region
- cerebral cortex: 93 nTPM
- hippocampal formation: 16 nTPM
- choroid plexus: 9.6 nTPM
- white matter: 8.5 nTPM
- basal ganglia: 7.3 nTPM
- medulla oblongata: 6.4 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)
- 1.61
- gnomAD pLI
- 0
- gnomAD missense Z
- 0.08
- DepMap mean gene effect
- 0.05
- 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/serine/threonine phosphatase activity
- mitogen-activated protein kinase binding
- phosphoprotein phosphatase activity
- protein serine/threonine phosphatase activity
- protein tyrosine 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
- Protein-tyrosine phosphatase, catalytic
- 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 DUSP2 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 DUSP2 as an antibody target. Whether an autoantibody or antibody against DUSP2 could matter depends on whether native DUSP2 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
DUSP2 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 DUSP2 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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