ARID1A is a member of the SWI/SNF family, whose members have helicase and ATPase activities and are thought to regulate transcription of certain genes by altering the chromatin structure around those genes. The encoded protein is part of the large ATP-dependent chromatin remodeling complex SNF/SWI, which is required for transcriptional activation of genes normally repressed by chromatin. It possesses at least two conserved domains that could be important for its function. First, it has an ARID domain, which is a DNA-binding domain that can specifically bind an AT-rich DNA sequence known to be recognized by a SNF/SWI complex at the beta-globin locus. Second, the C-terminus of the protein can stimulate glucocorticoid receptor-dependent transcriptional activation. It is thought that the protein encoded by this gene confers specificity to the SNF/SWI complex and may recruit the complex to its targets through either protein-DNA or protein-protein interactions. Two transcript variants encoding different isoforms have been found for this gene. This gene has been commonly found mutated in gastric cancers, ovarian clear cell carcinoma, and pancreatic cancer.
^Wang K, Kan J, Yuen ST, Shi ST, Chu KM, Law S, Chan TL, Kan Z, Chan AS, Tsui WY, Lee SP, Ho SL, Chan AK, Cheng GH, Roberts PC, Rejto PA, Gibson NW, Pocalyko DJ, Mao M, Xu J, Leung SY (December 2011). "Exome sequencing identifies frequent mutation of ARID1A in molecular subtypes of gastric cancer". Nat. Genet.43 (12): 1219–23. doi:10.1038/ng.982. PMID22037554.
^Wiegand KC, Shah SP, Al-Agha OM, Zhao Y, Tse K, Zeng T, Senz J, McConechy MK, Anglesio MS, Kalloger SE, Yang W, Heravi-Moussavi A, Giuliany R, Chow C, Fee J, Zayed A, Prentice L, Melnyk N, Turashvili G, Delaney AD, Madore J, Yip S, McPherson AW, Ha G, Bell L, Fereday S, Tam A, Galletta L, Tonin PN, Provencher D, Miller D, Jones SJ, Moore RA, Morin GB, Oloumi A, Boyd N, Aparicio SA, Shih IeM, Mes-Masson AM, Bowtell DD, Hirst M, Gilks B, Marra MA, Huntsman DG (October 2010). "ARID1A mutations in endometriosis-associated ovarian carcinomas". N. Engl. J. Med.363 (16): 1532–43. doi:10.1056/NEJMoa1008433. PMC2976679. PMID20942669.
^Kato H, Tjernberg A, Zhang W, Krutchinsky AN, An W, Takeuchi T, Ohtsuki Y, Sugano S, de Bruijn DR, Chait BT, Roeder RG (February 2002). "SYT associates with human SNF/SWI complexes and the C-terminal region of its fusion partner SSX1 targets histones". J. Biol. Chem.277 (7): 5498–505. doi:10.1074/jbc.M108702200. PMID11734557.
^Zhao K, Wang W, Rando OJ, Xue Y, Swiderek K, Kuo A, Crabtree GR (November 1998). "Rapid and phosphoinositol-dependent binding of the SWI/SNF-like BAF complex to chromatin after T lymphocyte receptor signaling". Cell95 (5): 625–36. doi:10.1016/S0092-8674(00)81633-5. PMID9845365.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K; et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID9373149.
Kozmik Z, Machon O, Králová J; et al. (2001). "Characterization of mammalian orthologues of the Drosophila osa gene: cDNA cloning, expression, chromosomal localization, and direct physical interaction with Brahma chromatin-remodeling complex". Genomics73 (2): 140–8. doi:10.1006/geno.2001.6477. PMID11318604.
Kato H, Tjernberg A, Zhang W; et al. (2002). "SYT associates with human SNF/SWI complexes and the C-terminal region of its fusion partner SSX1 targets histones". J. Biol. Chem.277 (7): 5498–505. doi:10.1074/jbc.M108702200. PMID11734557.
Lemon B, Inouye C, King DS, Tjian R (2002). "Selectivity of chromatin-remodelling cofactors for ligand-activated transcription". Nature414 (6866): 924–8. doi:10.1038/414924a. PMID11780067.
Kitagawa H, Fujiki R, Yoshimura K; et al. (2003). "The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome". Cell113 (7): 905–17. doi:10.1016/S0092-8674(03)00436-7. PMID12837248.