DUSP7
Dual specificity protein phosphatase 7
Also known as: DUS7_HUMAN, MKP-X, PYST2
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q16829
- Gene
- DUSP7
- Ensembl
- ENSG00000164086
- Chromosome
- 3
- Canonical length
- 419 aa
- Protein class
- Enzymes, Predicted intracellular proteins
OverviewNCBI Gene
Dual-specificity phosphatases (DUSPs) constitute a large heterogeneous subgroup of the type I cysteine-based protein-tyrosine phosphatase superfamily. DUSPs are characterized by their ability to dephosphorylate both tyrosine and serine/threonine residues. DUSP7 belongs to a class of DUSPs, designated MKPs, that dephosphorylate MAPK (mitogen-activated protein kinase) proteins ERK (see MIM 601795), JNK (see MIM 601158), and p38 (see MIM 600289) with specificity distinct from that of individual MKP proteins. MKPs contain a highly conserved C-terminal catalytic domain and an N-terminal Cdc25 (see MIM 116947)-like (CH2) domain. MAPK activation cascades mediate various physiologic processes, including cellular proliferation, apoptosis, differentiation, and stress responses (summary by Patterson et al., 2009 [PubMed 19228121]).[supplied by OMIM, Dec 2009]
Canonical amino-acid sequenceUniProt
419 residues, UniProt reviewed canonical sequence.
>Q16829|DUSP7
1 MKNQLRGPPA RAHMSTSGAA AAGGTRAGSE PGAGSGSGAG TGAGAATGAG AMPCKSAEWL
61 QEELEARGGA SLLLLDCRPH ELFESSHIET AINLAIPGLM LRRLRKGNLP IRSIIPNHAD
121 KERFATRCKA ATVLLYDEAT AEWQPEPGAP ASVLGLLLQK LRDDGCQAYY LQGGFNKFQT
181 EYSEHCETNV DSSSSPSSSP PTSVLGLGGL RISSDCSDGE SDRELPSSAT ESDGSPVPSS
241 QPAFPVQILP YLYLGCAKDS TNLDVLGKYG IKYILNVTPN LPNAFEHGGE FTYKQIPISD
301 HWSQNLSQFF PEAISFIDEA RSKKCGVLVH CLAGISRSVT VTVAYLMQKM NLSLNDAYDF
361 VKRKKSNISP NFNFMGQLLD FERTLGLSSP CDNHASSEQL YFSTPTNHNL FPLNTLESTLocalizationUniProt · AlphaFold · HPA
Whether an antibody against DUSP7 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)
- 0.41
- Highest tissue expression
- 63 nTPM
Expression across tissuesHPA
Tissue
- skin: 63 nTPM
- esophagus: 62 nTPM
- vagina: 44 nTPM
- cervix: 32 nTPM
- blood vessel: 30 nTPM
- spleen: 25 nTPM
Single-cell type
- basal keratinocytes: 98 nCPM
- suprabasal keratinocytes: 97 nCPM
- alveolar cells type 1: 85 nCPM
- ocular epithelial cells: 85 nCPM
- esophageal suprabasal cells: 80 nCPM
- esophageal basal cells: 58 nCPM
Immune cell
- intermediate monocyte: 10 nTPM
- non-classical monocyte: 10 nTPM
- MAIT T-cell: 7.2 nTPM
- plasmacytoid DC: 7.1 nTPM
- memory CD4 T-cell: 6.3 nTPM
- gdT-cell: 5.3 nTPM
Brain region
- white matter: 72 nTPM
- cerebral cortex: 56 nTPM
- basal ganglia: 51 nTPM
- midbrain: 50 nTPM
- thalamus: 49 nTPM
- medulla oblongata: 47 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)
- 0.5
- gnomAD pLI
- 0.69
- gnomAD missense Z
- 2.57
- DepMap mean gene effect
- 0.01
- DepMap dependency class
- none
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
- ERK1 and ERK2 cascade
- MAPK cascade
- negative regulation of ERK1 and ERK2 cascade
- negative regulation of MAP kinase activity
- peptidyl-tyrosine dephosphorylation
- signal transduction
Molecular functions
- MAP kinase tyrosine phosphatase activity
- MAP kinase tyrosine/serine/threonine phosphatase activity
- protein serine/threonine phosphatase activity
- protein tyrosine phosphatase activity
- protein tyrosine/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
- 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 DUSP7 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 DUSP7 as an antibody target. Whether an autoantibody or antibody against DUSP7 could matter depends on whether native DUSP7 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
DUSP7 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 DUSP7 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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