InnateDB: Systems Biology of the Innate Immune Response

Homo sapiens Protein: DUSP8

Summary

InnateDB Protein

IDBP-19374.6

Last Modified

2014-10-13 [Report errors or provide feedback]

Gene Symbol

DUSP8

Protein Name

dual specificity phosphatase 8

Synonyms

C11orf81; HB5; HVH-5; HVH8;

Species

Homo sapiens

Ensembl Protein

ENSP00000329539

InnateDB Gene

IDBG-19372 (DUSP8)

Protein Structure

UniProt Annotation

Function

This protein shows both activity toward tyrosine-protein phosphate as well as with serine/threonine-protein phosphate. {ECO:0000250}.

Subcellular Localization

Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.

Disease Associations

Tissue Specificity

Abundant in brain, heart and skeletal muscle. {ECO:0000269PubMed:7561881}.

Comments

Interactions

Number of Interactions

This gene and/or its encoded proteins are associated with 5 experimentally validated interaction(s) in this database.

Experimentally validated
Total	5 [view]
Protein-Protein	5 [view]
Protein-DNA	0
Protein-RNA	0
DNA-DNA	0
RNA-RNA	0
DNA-RNA	0

Gene Ontology

Molecular Function

Accession	GO Term
GO:0004725	protein tyrosine phosphatase activity
GO:0008138	protein tyrosine/serine/threonine phosphatase activity
GO:0016791	phosphatase activity
GO:0017017	MAP kinase tyrosine/serine/threonine phosphatase activity

Biological Process

GO:0000188	inactivation of MAPK activity
GO:0006470	protein dephosphorylation
GO:0016311	dephosphorylation
GO:0035335	peptidyl-tyrosine dephosphorylation

Cellular Component

GO:0005634	nucleus
GO:0005737	cytoplasm

Protein Structure and Domains

PDB ID

InterPro

IPR000340 Dual specificity phosphatase, catalytic domain
IPR000387 Protein-tyrosine/Dual specificity phosphatase
IPR001763 Rhodanese-like domain
IPR008343 Mitogen-activated protein (MAP) kinase phosphatase
IPR020422 Dual specificity phosphatase, subgroup, catalytic domain
IPR029021 Protein-tyrosine phosphatase-like

PFAM

PF00782
PF00581

PRINTS

PR01764

PIRSF

PIRSF000939

SMART

SM00450
SM00195

TIGRFAMs

Post-translational Modifications

Modification

Cross-References