Biology:ARID4A

Short description: Protein-coding gene in humans

Generic protein structure example

AT rich interactive domain 4A (RBP1-like), also known as ARID4A, is a protein which in humans is encoded by the ARID4A gene.

Function

The protein encoded by this gene is a ubiquitously expressed nuclear protein. It binds directly, with several other proteins, to retinoblastoma protein (pRB) which regulates cell proliferation. pRB represses transcription by recruiting the encoded protein. This protein, in turn, serves as a bridging molecule to recruit HDACs and, in addition, provides a second HDAC-independent repression function. The encoded protein possesses transcriptional repression activity. Multiple alternatively spliced transcripts have been observed for this gene, although not all transcript variants have been fully described.

Interactions

ARID4A has been shown to interact with Retinoblastoma protein.

Further reading

• "Cloning of cDNAs for cellular proteins that bind to the retinoblastoma gene product". Nature 352 (6332): 251–4. Jul 1991. doi:10.1038/352251a0. PMID 1857421. Bibcode: 1991Natur.352..251D. 
• "Characterization of the retinoblastoma binding proteins RBP1 and RBP2". Oncogene 8 (11): 3149–56. Nov 1993. PMID 8414517. 
• "Alternative splicing of the RBP1 gene clusters in an internal exon that encodes potential phosphorylation sites". Oncogene 8 (4): 949–57. Apr 1993. PMID 8455946. 
• "A novel human WD protein, h-beta TrCp, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif". Molecular Cell 1 (4): 565–74. Mar 1998. doi:10.1016/S1097-2765(00)80056-8. PMID 9660940. 
• "RBP1 induces growth arrest by repression of E2F-dependent transcription". Oncogene 18 (12): 2091–100. Mar 1999. doi:10.1038/sj.onc.1202520. PMID 10321733. 
• "Recognition of an epitope of a breast cancer antigen by human antibody". Breast Cancer Research and Treatment 53 (3): 279–90. Feb 1999. doi:10.1023/A:1006115922401. PMID 10369074. 
• "RBP1 recruits both histone deacetylase-dependent and -independent repression activities to retinoblastoma family proteins". Molecular and Cellular Biology 19 (10): 6632–41. Oct 1999. doi:10.1128/mcb.19.10.6632. PMID 10490602. 
• "RBP1 recruits the mSIN3-histone deacetylase complex to the pocket of retinoblastoma tumor suppressor family proteins found in limited discrete regions of the nucleus at growth arrest". Molecular and Cellular Biology 21 (8): 2918–32. Apr 2001. doi:10.1128/MCB.21.8.2918-2932.2001. PMID 11283269. 
• "Identification and characterization of three new components of the mSin3A corepressor complex". Molecular and Cellular Biology 23 (10): 3456–67. May 2003. doi:10.1128/MCB.23.10.3456-3467.2003. PMID 12724404. 
• "Breast cancer metastasis suppressor 1 (BRMS1) forms complexes with retinoblastoma-binding protein 1 (RBP1) and the mSin3 histone deacetylase complex and represses transcription". The Journal of Biological Chemistry 279 (2): 1562–9. Jan 2004. doi:10.1074/jbc.M307969200. PMID 14581478. 
• "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America 101 (33): 12130–5. Aug 2004. doi:10.1073/pnas.0404720101. PMID 15302935. Bibcode: 2004PNAS..10112130B. 
• "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Research 16 (1): 55–65. Jan 2006. doi:10.1101/gr.4039406. PMID 16344560. 
• "Estrogen receptor isoform-specific regulation of the retinoblastoma-binding protein 1 (RBBP1) gene: roles of AF1 and enhancer elements". The Journal of Biological Chemistry 281 (39): 28596–604. Sep 2006. doi:10.1074/jbc.M605226200. PMID 16873370. 

External links

• ARID4A+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
• Human ARID4A genome location and ARID4A gene details page in the UCSC Genome Browser.
• Human RBP1 genome location and RBP1 gene details page in the UCSC Genome Browser.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.