ARID4A

AT rich interactive domain 4A (RBP1-like)
Identifiers
Symbols	ARID4A; RBBP-1; RBBP1; RBP-1; RBP1
External IDs	OMIM: 180201 MGI: 2444354 HomoloGene: 11303 GeneCards: ARID4A Gene
Gene Ontology Molecular function • DNA binding • sequence-specific DNA binding transcription factor activity Cellular component • intracellular • nucleus • transcriptional repressor complex Biological process • regulation of transcription, DNA-dependent • transcription from RNA polymerase II promoter • negative regulation of transcription, DNA-dependent Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	5926	238247
Ensembl	ENSG00000032219	ENSMUSG00000048118
UniProt	P29374	n/a
RefSeq (mRNA)	NM_002892.3	NM_001081195.1
RefSeq (protein)	NP_002883.3	NP_001074664.1
Location (UCSC)	Chr 14: 58.77 – 58.84 Mb	Chr 12: 72.12 – 72.2 Mb
PubMed search	[1]	[2]

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

• Defeo-Jones D, Huang PS, Jones RE, et al. (1991). "Cloning of cDNAs for cellular proteins that bind to the retinoblastoma gene product.". Nature 352 (6332): 251–4. doi:10.1038/352251a0. PMID 1857421. 
• Fattaey AR, Helin K, Dembski MS, et al. (1993). "Characterization of the retinoblastoma binding proteins RBP1 and RBP2.". Oncogene 8 (11): 3149–56. PMID 8414517. 
• Otterson GA, Kratzke RA, Lin AY, et al. (1993). "Alternative splicing of the RBP1 gene clusters in an internal exon that encodes potential phosphorylation sites.". Oncogene 8 (4): 949–57. PMID 8455946. 
• Margottin F, Bour SP, Durand H, et al. (1998). "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.". Mol. Cell 1 (4): 565–74. doi:10.1016/S1097-2765(00)80056-8. PMID 9660940. 
• Lai A, Marcellus RC, Corbeil HB, Branton PE (1999). "RBP1 induces growth arrest by repression of E2F-dependent transcription.". Oncogene 18 (12): 2091–100. doi:10.1038/sj.onc.1202520. PMID 10321733. 
• Cao J, Gao T, Giuliano AE, Irie RF (1999). "Recognition of an epitope of a breast cancer antigen by human antibody.". Breast Cancer Res. Treat. 53 (3): 279–90. doi:10.1023/A:1006115922401. PMID 10369074. 
• Lai A, Lee JM, Yang WM, et al. (2000). "RBP1 recruits both histone deacetylase-dependent and -independent repression activities to retinoblastoma family proteins.". Mol. Cell. Biol. 19 (10): 6632–41. PMC 84642. PMID 10490602. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=84642. 
• Lai A, Kennedy BK, Barbie DA, et al. (2001). "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.". Mol. Cell. Biol. 21 (8): 2918–32. doi:10.1128/MCB.21.8.2918-2932.2001. PMC 86920. PMID 11283269. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=86920. 
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Fleischer TC, Yun UJ, Ayer DE (2003). "Identification and characterization of three new components of the mSin3A corepressor complex.". Mol. Cell. Biol. 23 (10): 3456–67. doi:10.1128/MCB.23.10.3456-3467.2003. PMC 164750. PMID 12724404. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=164750. 
• Meehan WJ, Samant RS, Hopper JE, et al. (2004). "Breast cancer metastasis suppressor 1 (BRMS1) forms complexes with retinoblastoma-binding protein 1 (RBP1) and the mSin3 histone deacetylase complex and represses transcription.". J. Biol. Chem. 279 (2): 1562–9. doi:10.1074/jbc.M307969200. PMID 14581478. 
• Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins.". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=514446. 
• Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1356129. 
• Monroe DG, Secreto FJ, Hawse JR, et al. (2006). "Estrogen receptor isoform-specific regulation of the retinoblastoma-binding protein 1 (RBBP1) gene: roles of AF1 and enhancer elements.". J. Biol. Chem. 281 (39): 28596–604. doi:10.1074/jbc.M605226200. PMID 16873370. 

External links

• MeSH ARID4A+protein,+human

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