nuclear receptor-interacting factor 3; centromere protein R; CENP-R; beta-3-endonexin; integrin beta-3-binding protein (ITGB3BP, CENPR, NRIF3)

Function: 1) transcription coregulator 2) both coactivator & corepressor functions 3) coactivation of nuclear receptors for retinoid X receptor & thyroid hormone receptor (isoform 1 only) 4) coactivator for estrogen receptor alpha 5) transcriptional corepressor via interaction with NFKB1 6) induces apoptosis in breast cancer cells via caspase-2 7) inhibitor of cyclin A-associated kinase (putative) 8) component of the CENPA-CAD complex 9) homodimer, mediated by the coiled coil domain 10) isoform 3, but not other isoforms, interacts with the cytoplasmic tail of integrin ITGB3 (relevance is uncertain, since isoform 3 is mainly nuclear) 11) interacts with CCNA2 & MTA1 Structure: - the DD1 domain (also called repD1 domain) mediates the corepressor function & is essential in the triggering of apoptosis - contains one Leu-Xaa-Xaa-Leu-Leu (LXXLL) motif, a motif known to be important for the association with nuclear receptors (but not essential) - contains one Leu-Xaa-Xaa-Ile-Leu (LXXIL) motif, essential for the association with nuclear receptors Compartment: - isoform 1 & 2 are nuclear - isoform 3 is predominantly nuclear - isoform 4 is cytoplasmic Alternative splicing: named isoforms=5 Expression: - widely expressed, spleen, thymus, prostate, ovary, small intestine, white blood cells, testis, colon - isoform 4 is expressed in platelets, lymphocytes, granulocytes - expression is induced by estrogen

General

transcriptional adaptor protein; transcriptional coactivator transcriptional silencer (transcriptional repressor)

Properties

SIZE: entity length = 177 aa MW = 20 kD COMPARTMENT: cytoplasm cell nucleus MOTIF: LXXLL {9-13} Ser phosphorylation site {S17} DD1 {20-50} MOTIF: Ser phosphorylation site {S28} nuclear translocation signal {63-66} coiled coil {83-113} LXXIL {172-176}

Database Correlations

OMIM 605494 UniProt Q13352 Pfam PF06729 Entrez Gene 23421 Kegg hsa:23421

References

UniProt :accession Q13352