ARID1A

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ARID1A
Protein ARID1A PDB 1ryu.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases ARID1A, B120, BAF250, BAF250a, BM029, C1orf4, ELD, MRD14, OSA1, P270, SMARCF1, hELD, hOSA1, CSS2, AT-rich interaction domain 1A
External IDs MGI: 1935147 HomoloGene: 21216 GeneCards: ARID1A
RNA expression pattern
PBB GE ARID1A 210649 s at fs.png

PBB GE ARID1A 212152 x at fs.png

PBB GE ARID1A 218917 s at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez

8289

93760
Ensembl

ENSG00000117713

ENSMUSG00000007880
UniProt

O14497

A2BH40
RefSeq (mRNA)

NM_139135
NM_006015
NM_018450

NM_001080819
RefSeq (protein)

NP_006006
NP_624361

NP_001074288
Location (UCSC) Chr 1: 26.69 – 26.78 Mb Chr 4: 133.68 – 133.76 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

AT-rich interactive domain-containing protein 1A is a protein that in humans is encoded by the ARID1A gene.[3][4][5]

Function[edit]

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.[5]

Clinical significance[edit]

This gene has been commonly found mutated in gastric cancers,[6] ovarian clear cell carcinoma,[7] and pancreatic cancer.[8]

Research[edit]

Lack of this gene/protein seems to protect rats from some types of liver damage.[9]

Interactions[edit]

ARID1A has been shown to interact with SMARCB1[10][11] and SMARCA4.[11][12]

References[edit]

  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ Takeuchi T, Furihata M, Heng HH, Sonobe H, Ohtsuki Y (Aug 1998). "Chromosomal mapping and expression of the human B120 gene". Gene. 213 (1–2): 189–93. PMID 9630625. doi:10.1016/S0378-1119(98)00194-2. 
  4. ^ Takeuchi T, Chen BK, Qiu Y, Sonobe H, Ohtsuki Y (Feb 1998). "Molecular cloning and expression of a novel human cDNA containing CAG repeats". Gene. 204 (1–2): 71–7. PMID 9434167. doi:10.1016/S0378-1119(97)00525-8. 
  5. ^ a b "Entrez Gene: ARID1A AT rich interactive domain 1A (SWI-like)". 
  6. ^ 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. PMID 22037554. doi:10.1038/ng.982. 
  7. ^ 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 I-M, 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. PMC 2976679 Freely accessible. PMID 20942669. doi:10.1056/NEJMoa1008433. 
  8. ^ Shain AH, Giacomini CP, Matsukuma K, Karikari CA, Bashyam MD, Hidalgo M, Maitra A, Pollack JR (January 2012). "Convergent structural alterations define SWItch/Sucrose NonFermentable (SWI/SNF) chromatin remodeler as a central tumor suppressive complex in pancreatic cancer". Proc. Natl. Acad. Sci. U.S.A. 109 (5): E252–9. PMC 3277150 Freely accessible. PMID 22233809. doi:10.1073/pnas.1114817109. 
  9. ^ Tissue Regeneration Promoted through Gene Suppression. March 2016
  10. ^ 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. PMID 11734557. doi:10.1074/jbc.M108702200. 
  11. ^ a b Wang W, Côté J, Xue Y, Zhou S, Khavari PA, Biggar SR, Muchardt C, Kalpana GV, Goff SP, Yaniv M, Workman JL, Crabtree GR (October 1996). "Purification and biochemical heterogeneity of the mammalian SWI-SNF complex". EMBO J. 15 (19): 5370–82. PMC 452280 Freely accessible. PMID 8895581. 
  12. ^ 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". Cell. 95 (5): 625–36. PMID 9845365. doi:10.1016/S0092-8674(00)81633-5. 

Further reading[edit]

External links[edit]

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

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