InnateDB: Systems Biology of the Innate Immune Response

Homo sapiens Protein: TNFAIP1

Summary

InnateDB Protein

IDBP-36401.6

Last Modified

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

Gene Symbol

TNFAIP1

Protein Name

tumor necrosis factor, alpha-induced protein 1 (endothelial)

Synonyms

B12; B61; BTBD34; EDP1; hBACURD2;

Species

Homo sapiens

Ensembl Protein

ENSP00000226225

InnateDB Gene

IDBG-36399 (TNFAIP1)

Protein Structure

UniProt Annotation

Function

Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex involved in regulation of cytoskeleton structure. The BCR(BACURD2) E3 ubiquitin ligase complex mediates the ubiquitination of RHOA, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and cell migration. Its interaction with RHOB may regulate apoptosis. May enhance the PCNA-dependent DNA polymerase delta activity. {ECO:0000269PubMed:19637314, ECO:0000269PubMed:19782033}.

Subcellular Localization

Cytoplasm. Nucleus. Endosome. Note=Colocalizes with RHOB in endosomes.

Disease Associations

Tissue Specificity

Comments

Interactions

Number of Interactions

This gene and/or its encoded proteins are associated with 26 experimentally validated interaction(s) in this database.

Experimentally validated
Total	26 [view]
Protein-Protein	23 [view]
Protein-DNA	3 [view]
Protein-RNA	0
DNA-DNA	0
RNA-RNA	0
DNA-RNA	0

Gene Ontology

Molecular Function

Accession	GO Term
GO:0004842	ubiquitin-protein transferase activity
GO:0005515	protein binding
GO:0017049	GTP-Rho binding
GO:0019904	protein domain specific binding

Biological Process

GO:0006260	DNA replication
GO:0006915	apoptotic process
GO:0006955	immune response
GO:0009790	embryo development
GO:0016477	cell migration
GO:0016567	protein ubiquitination
GO:0035024	negative regulation of Rho protein signal transduction
GO:0043149	stress fiber assembly
GO:0043161	proteasome-mediated ubiquitin-dependent protein catabolic process
GO:0045740	positive regulation of DNA replication
GO:0051260	protein homooligomerization