ID ARI1A_HUMAN Reviewed; 2285 AA. AC O14497; D3DPL1; Q53FK9; Q5T0W1; Q5T0W2; Q5T0W3; Q8NFD6; Q96T89; Q9BY33; AC Q9HBJ5; Q9UPZ1; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 30-AUG-2005, sequence version 3. DT 27-MAR-2024, entry version 223. DE RecName: Full=AT-rich interactive domain-containing protein 1A; DE Short=ARID domain-containing protein 1A; DE AltName: Full=B120; DE AltName: Full=BRG1-associated factor 250; DE Short=BAF250; DE AltName: Full=BRG1-associated factor 250a; DE Short=BAF250A; DE AltName: Full=Osa homolog 1; DE Short=hOSA1; DE AltName: Full=SWI-like protein; DE AltName: Full=SWI/SNF complex protein p270; DE AltName: Full=SWI/SNF-related, matrix-associated, actin-dependent regulator of chromatin subfamily F member 1; DE AltName: Full=hELD; GN Name=ARID1A; Synonyms=BAF250, BAF250A, C1orf4, OSA1, SMARCF1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, TISSUE RP SPECIFICITY, AND IDENTIFICATION IN THE BAF COMPLEX. RX PubMed=11073988; DOI=10.1128/mcb.20.23.8879-8888.2000; RA Nie Z., Xue Y., Yang D., Zhou S., Deroo B.J., Archer T.K., Wang W.; RT "A specificity and targeting subunit of a human SWI/SNF family-related RT chromatin-remodeling complex."; RL Mol. Cell. Biol. 20:8879-8888(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 287-2285 (ISOFORM 1), TISSUE SPECIFICITY, RP INTERACTION WITH SMARCA2 AND SMARCA4, AND IDENTIFICATION IN A SWI/SNF RP COMPLEX WITH ARID1B. RX PubMed=12200431; DOI=10.1074/jbc.m205961200; RA Inoue H., Furukawa T., Giannakopoulos S., Zhou S., King D.S., Tanese N.; RT "Largest subunits of the human SWI/SNF chromatin-remodeling complex promote RT transcriptional activation by steroid hormone receptors."; RL J. Biol. Chem. 277:41674-41685(2002). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 347-2285 (ISOFORM 1), IDENTIFICATION BY MASS RP SPECTROMETRY, AND IDENTIFICATION IN THE BAF COMPLEX. RC TISSUE=Brain; RX PubMed=11734557; DOI=10.1074/jbc.m108702200; RA Kato H., Tjernberg A., Zhang W., Krutchinsky A.N., An W., Takeuchi T., RA Ohtsuki Y., Sugano S., de Bruijn D.R., Chait B.T., Roeder R.G.; RT "SYT associates with human SNF/SWI complexes and the C-terminal region of RT its fusion partner SSX1 targets histones."; RL J. Biol. Chem. 277:5498-5505(2002). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 358-2285 (ISOFORM 1), AND MUTAGENESIS OF RP TRP-1073 AND TYR-1096. RX PubMed=10757798; DOI=10.1128/mcb.20.9.3137-3146.2000; RA Dallas P.B., Pacchione S., Wilsker D., Bowrin V., Kobayashi R., Moran E.; RT "The human SWI-SNF complex protein p270 is an ARID family member with non- RT sequence-specific DNA binding activity."; RL Mol. Cell. Biol. 20:3137-3146(2000). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-1585 (ISOFORM 3). RX PubMed=9434167; DOI=10.1016/s0378-1119(97)00525-8; RA Takeuchi T., Chen B.-K., Qiu Y., Sonobe H., Ohtsuki Y.; RT "Molecular cloning and expression of a novel human cDNA containing CAG RT repeats."; RL Gene 204:71-77(1997). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 380-1515. RA Takeuchi T., Misaki A.; RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 384-2285 (ISOFORM 2), ALTERNATIVE SPLICING RP (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=11318604; DOI=10.1006/geno.2001.6477; RA Kozmik Z., Machon O., Kralova J., Kreslova J., Paces J., Vlcek C.; RT "Characterization of mammalian orthologues of the Drosophila osa gene: cDNA RT cloning, expression, chromosomal localization, and direct physical RT interaction with Brahma chromatin-remodeling complex."; RL Genomics 73:140-148(2001). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1104-2285 (ISOFORM 1). RC TISSUE=Gastric mucosa; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [11] RP IDENTIFICATION IN SWI/SNF COMPLEXES. RX PubMed=8804307; DOI=10.1101/gad.10.17.2117; RA Wang W., Xue Y., Zhou S., Kuo A., Cairns B.R., Crabtree G.R.; RT "Diversity and specialization of mammalian SWI/SNF complexes."; RL Genes Dev. 10:2117-2130(1996). RN [12] RP IDENTIFICATION IN A SWI/SNF COMPLEX. RX PubMed=11780067; DOI=10.1038/414924a; RA Lemon B., Inouye C., King D.S., Tjian R.; RT "Selectivity of chromatin-remodelling cofactors for ligand-activated RT transcription."; RL Nature 414:924-928(2001). RN [13] RP IDENTIFICATION IN A SWI/SNF-LIKE COMPLEX WITH ARID1A. RX PubMed=11988099; DOI=10.1042/bj3640255; RA Hurlstone A.F., Olave I.A., Barker N., van Noort M., Clevers H.; RT "Cloning and characterization of hELD/OSA1, a novel BRG1 interacting RT protein."; RL Biochem. J. 364:255-264(2002). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-696; SER-698 AND SER-702, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-772, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-286; SER-301; SER-696; RP SER-698; SER-764; SER-772 AND SER-1944, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [19] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; THR-286; SER-363; RP SER-604; SER-696; SER-698; SER-702; SER-772 AND SER-1184, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [21] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1612 AND LYS-1905, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-772, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [23] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363; SER-696; SER-702 AND RP SER-1604, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [25] RP INVOLVEMENT IN CSS2. RX PubMed=22426308; DOI=10.1038/ng.2219; RA Tsurusaki Y., Okamoto N., Ohashi H., Kosho T., Imai Y., Hibi-Ko Y., RA Kaname T., Naritomi K., Kawame H., Wakui K., Fukushima Y., Homma T., RA Kato M., Hiraki Y., Yamagata T., Yano S., Mizuno S., Sakazume S., Ishii T., RA Nagai T., Shiina M., Ogata K., Ohta T., Niikawa N., Miyatake S., Okada I., RA Mizuguchi T., Doi H., Saitsu H., Miyake N., Matsumoto N.; RT "Mutations affecting components of the SWI/SNF complex cause Coffin-Siris RT syndrome."; RL Nat. Genet. 44:376-378(2012). RN [26] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-233; SER-363; RP SER-382; SER-604; SER-696; SER-698; SER-702; SER-764; SER-772; SER-1184; RP SER-1235; SER-1604; SER-1751; SER-1754; THR-1888; SER-1929 AND SER-1944, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [28] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363; SER-696 AND SER-1751, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [29] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-429 AND ARG-1276, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [30] RP REVIEW ON SWI/SNF CHROMATIN REMODELING COMPLEXES. RX PubMed=12672490; DOI=10.1016/s0959-437x(03)00022-4; RA Martens J.A., Winston F.; RT "Recent advances in understanding chromatin remodeling by SWI/SNF RT complexes."; RL Curr. Opin. Genet. Dev. 13:136-142(2003). RN [31] RP IDENTIFICATION IN A SWI/SNF-LIKE EBAFA COMPLEX, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=12665591; DOI=10.1128/mcb.23.8.2942-2952.2003; RA Nie Z., Yan Z., Chen E.H., Sechi S., Ling C., Zhou S., Xue Y., Yang D., RA Murray D., Kanakubo E., Cleary M.L., Wang W.; RT "Novel SWI/SNF chromatin-remodeling complexes contain a mixed-lineage RT leukemia chromosomal translocation partner."; RL Mol. Cell. Biol. 23:2942-2952(2003). RN [32] RP IDENTIFICATION IN SWI/SNF COMPLEXES, AND INTERACTION WITH SMARCA2; SMARCA4 RP AND SMARCC1. RX PubMed=15170388; DOI=10.1042/bj20040524; RA Wang X., Nagl N.G., Wilsker D., Van Scoy M., Pacchione S., Yaciuk P., RA Dallas P.B., Moran E.; RT "Two related ARID family proteins are alternative subunits of human SWI/SNF RT complexes."; RL Biochem. J. 383:319-325(2004). RN [33] RP IDENTIFICATION IN THE BAF COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=18765789; DOI=10.1101/gad.471408; RA Lange M., Kaynak B., Forster U.B., Toenjes M., Fischer J.J., Grimm C., RA Schlesinger J., Just S., Dunkel I., Krueger T., Mebus S., Lehrach H., RA Lurz R., Gobom J., Rottbauer W., Abdelilah-Seyfried S., Sperling S.; RT "Regulation of muscle development by DPF3, a novel histone acetylation and RT methylation reader of the BAF chromatin remodeling complex."; RL Genes Dev. 22:2370-2384(2008). RN [34] RP REVIEW ON SWI/SNF CHROMATIN REMODELING COMPLEXES. RX PubMed=22952240; DOI=10.1074/jbc.r111.309302; RA Euskirchen G., Auerbach R.K., Snyder M.; RT "SWI/SNF chromatin-remodeling factors: multiscale analyses and diverse RT functions."; RL J. Biol. Chem. 287:30897-30905(2012). RN [35] RP REVIEW ON SWI/SNF CHROMATIN REMODELING COMPLEXES. RX PubMed=26601204; DOI=10.1126/sciadv.1500447; RA Kadoch C., Crabtree G.R.; RT "Mammalian SWI/SNF chromatin remodeling complexes and cancer: Mechanistic RT insights gained from human genomics."; RL Sci. Adv. 1:E1500447-E1500447(2015). RN [36] RP SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, AND MUTAGENESIS OF RP 1370-LYS-ARG-1371; ARG-1383 AND 1656-ARG--ARG-1658. RX PubMed=26614907; DOI=10.1016/j.bbrc.2015.11.080; RA Bateman N.W., Shoji Y., Conrads K.A., Stroop K.D., Hamilton C.A., RA Darcy K.M., Maxwell G.L., Risinger J.I., Conrads T.P.; RT "Identification and functional characterization of a novel bipartite RT nuclear localization sequence in ARID1A."; RL Biochem. Biophys. Res. Commun. 469:114-119(2016). RN [37] RP STRUCTURE BY NMR OF 1000-1159. RX PubMed=14722072; DOI=10.1074/jbc.m312115200; RA Kim S., Zhang Z., Upchurch S., Isern N., Chen Y.; RT "Structure and DNA-binding sites of the SWI1 AT-rich interaction domain RT (ARID) suggest determinants for sequence-specific DNA recognition."; RL J. Biol. Chem. 279:16670-16676(2004). RN [38] RP VARIANTS LYS-1020 AND PRO-2089. RX PubMed=21248752; DOI=10.1038/nature09639; RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H., RA Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J., RA Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M., RA Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L., RA Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J., RA Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A., RA Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K., RA Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.; RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene RT PBRM1 in renal carcinoma."; RL Nature 469:539-542(2011). RN [39] RP VARIANTS TRP-1658; PHE-1907 AND ARG-2087. RX PubMed=22009941; DOI=10.1002/humu.21633; RA Jones S., Li M., Parsons D.W., Zhang X., Wesseling J., Kristel P., RA Schmidt M.K., Markowitz S., Yan H., Bigner D., Hruban R.H., Eshleman J.R., RA Iacobuzio-Donahue C.A., Goggins M., Maitra A., Malek S.N., Powell S., RA Vogelstein B., Kinzler K.W., Velculescu V.E., Papadopoulos N.; RT "Somatic mutations in the chromatin remodeling gene ARID1A occur in several RT tumor types."; RL Hum. Mutat. 33:100-103(2012). RN [40] RP VARIANT SER-120. RX PubMed=23906836; DOI=10.1093/hmg/ddt366; RA Wieczorek D., Boegershausen N., Beleggia F., Steiner-Haldenstaett S., RA Pohl E., Li Y., Milz E., Martin M., Thiele H., Altmueller J., Alanay Y., RA Kayserili H., Klein-Hitpass L., Boehringer S., Wollstein A., Albrecht B., RA Boduroglu K., Caliebe A., Chrzanowska K., Cogulu O., Cristofoli F., RA Czeschik J.C., Devriendt K., Dotti M.T., Elcioglu N., Gener B., RA Goecke T.O., Krajewska-Walasek M., Guillen-Navarro E., Hayek J., Houge G., RA Kilic E., Simsek-Kiper P.O., Lopez-Gonzalez V., Kuechler A., Lyonnet S., RA Mari F., Marozza A., Mathieu Dramard M., Mikat B., Morin G., RA Morice-Picard F., Ozkinay F., Rauch A., Renieri A., Tinschert S., RA Utine G.E., Vilain C., Vivarelli R., Zweier C., Nuernberg P., Rahmann S., RA Vermeesch J., Luedecke H.J., Zeschnigk M., Wollnik B.; RT "A comprehensive molecular study on Coffin-Siris and Nicolaides-Baraitser RT syndromes identifies a broad molecular and clinical spectrum converging on RT altered chromatin remodeling."; RL Hum. Mol. Genet. 22:5121-5135(2013). CC -!- FUNCTION: Involved in transcriptional activation and repression of CC select genes by chromatin remodeling (alteration of DNA-nucleosome CC topology). Component of SWI/SNF chromatin remodeling complexes that CC carry out key enzymatic activities, changing chromatin structure by CC altering DNA-histone contacts within a nucleosome in an ATP-dependent CC manner. Binds DNA non-specifically. Belongs to the neural progenitors- CC specific chromatin remodeling complex (npBAF complex) and the neuron- CC specific chromatin remodeling complex (nBAF complex). During neural CC development a switch from a stem/progenitor to a postmitotic chromatin CC remodeling mechanism occurs as neurons exit the cell cycle and become CC committed to their adult state. The transition from proliferating CC neural stem/progenitor cells to postmitotic neurons requires a switch CC in subunit composition of the npBAF and nBAF complexes. As neural CC progenitors exit mitosis and differentiate into neurons, npBAF CC complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged CC for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C CC subunits in neuron-specific complexes (nBAF). The npBAF complex is CC essential for the self-renewal/proliferative capacity of the CC multipotent neural stem cells. The nBAF complex along with CREST plays CC a role regulating the activity of genes essential for dendrite growth CC (By similarity). {ECO:0000250|UniProtKB:A2BH40, CC ECO:0000303|PubMed:12672490, ECO:0000303|PubMed:22952240, CC ECO:0000303|PubMed:26601204}. CC -!- SUBUNIT: Component of SWI/SNF chromatin remodeling complexes, in some CC of which it can be mutually exclusive with ARID1B/BAF250B. The CC canonical complex contains a catalytic subunit (either CC SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B) and at least SMARCE1, CC ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and SMARCB1/SNF5/BAF47. CC Other subunits specific to each of the complexes may also be present CC permitting several possible combinations developmentally and tissue CC specific (PubMed:22952240, PubMed:26601204, PubMed:12200431, CC PubMed:8804307, PubMed:11780067, PubMed:11988099, PubMed:15170388). CC Component of the BAF (SWI/SNF-A) complex, which includes at least actin CC (ACTB), ARID1A/BAF250A, ARID1B/BAF250B, SMARCA2/BRM, CC SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, CC SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more CC SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C (PubMed:12200431, CC PubMed:11734557, PubMed:18765789). In muscle cells, the BAF complex CC also contains DPF3. Component of neural progenitors-specific chromatin CC remodeling complex (npBAF complex) composed of at least, ARID1A/BAF250A CC or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, CC SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, CC SMARCC2/BAF170, PHF10/BAF45A, ACTL6A/BAF53A and actin. Component of CC neuron-specific chromatin remodeling complex (nBAF complex) composed of CC at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, CC SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, CC SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, CC DPF1/BAF45B, DPF3/BAF45C, ACTL6B/BAF53B and actin (By similarity). CC Component of a SWI/SNF-like EBAFa complex, at least composed of CC SMARCA4/BRG1/BAF190A, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A, SMARCE1/BAF57, CC SMARCD1/BAF60A, SMARCC1/BAF155, SMARCC2/BAF170, BAF250A and MLLT1/ENL CC (PubMed:12665591). Interacts through its C-terminus with CC SMARCA2/BRM/BAF190B and SMARCA4/BRG1/BAF190A (PubMed:12200431, CC PubMed:15170388). Interacts with SMARCC1/BAF155 (PubMed:15170388). CC Interacts with FOS, FOSB isoform 1 and 2, FOSL1 and FOSL2 (By CC similarity). {ECO:0000250|UniProtKB:A2BH40, CC ECO:0000269|PubMed:11734557, ECO:0000269|PubMed:11780067, CC ECO:0000269|PubMed:11988099, ECO:0000269|PubMed:12200431, CC ECO:0000269|PubMed:12665591, ECO:0000269|PubMed:15170388, CC ECO:0000269|PubMed:18765789, ECO:0000269|PubMed:8804307, CC ECO:0000303|PubMed:12672490, ECO:0000303|PubMed:22952240, CC ECO:0000303|PubMed:26601204}. CC -!- INTERACTION: CC O14497; P50553: ASCL1; NbExp=2; IntAct=EBI-637887, EBI-957042; CC O14497; Q14526: HIC1; NbExp=2; IntAct=EBI-637887, EBI-2507362; CC O14497; P51531: SMARCA2; NbExp=5; IntAct=EBI-637887, EBI-679562; CC O14497; P51532: SMARCA4; NbExp=26; IntAct=EBI-637887, EBI-302489; CC O14497; Q92925: SMARCD2; NbExp=4; IntAct=EBI-637887, EBI-358441; CC O14497-1; P11388: TOP2A; NbExp=2; IntAct=EBI-15956509, EBI-539628; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355, CC ECO:0000269|PubMed:11318604, ECO:0000269|PubMed:26614907}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=O14497-1; Sequence=Displayed; CC Name=2; CC IsoId=O14497-2; Sequence=VSP_015225; CC Name=3; CC IsoId=O14497-3; Sequence=VSP_037157; CC -!- TISSUE SPECIFICITY: Highly expressed in spleen, thymus, prostate, CC testis, ovary, small intestine, colon, and PBL, and at a much lower CC level in heart, brain, placenta, lung, liver, skeletal muscle, kidney, CC and pancreas. {ECO:0000269|PubMed:11073988, CC ECO:0000269|PubMed:11318604, ECO:0000269|PubMed:12200431}. CC -!- DISEASE: Coffin-Siris syndrome 2 (CSS2) [MIM:614607]: A form of Coffin- CC Siris syndrome, a congenital multiple malformation syndrome with broad CC phenotypic and genetic variability. Cardinal features are intellectual CC disability, coarse facial features, hypertrichosis, and hypoplastic or CC absent fifth digit nails or phalanges. Additional features include CC malformations of the cardiac, gastrointestinal, genitourinary, and/or CC central nervous systems. Sucking/feeding difficulties, poor growth, CC ophthalmologic abnormalities, hearing impairment, and spinal anomalies CC are common findings. Both autosomal dominant and autosomal recessive CC inheritance patterns have been reported. {ECO:0000269|PubMed:22426308}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- SEQUENCE CAUTION: CC Sequence=AAF75765.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAG33967.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAA23269.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAA83073.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=BAA83073.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF231056; AAG33967.1; ALT_FRAME; mRNA. DR EMBL; AL512408; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL034380; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471059; EAX07795.1; -; Genomic_DNA. DR EMBL; CH471059; EAX07796.1; -; Genomic_DNA. DR EMBL; AF521670; AAN03446.1; -; mRNA. DR EMBL; AF219114; AAG17549.2; -; mRNA. DR EMBL; AF265208; AAF75765.1; ALT_FRAME; mRNA. DR EMBL; AB001895; BAA23269.1; ALT_FRAME; mRNA. DR EMBL; AB024075; BAA83073.1; ALT_SEQ; Genomic_DNA. DR EMBL; AF268913; AAK54505.1; -; mRNA. DR EMBL; AK223275; BAD96995.1; -; mRNA. DR CCDS; CCDS285.1; -. [O14497-1] DR CCDS; CCDS44091.1; -. [O14497-2] DR PIR; T00022; T00022. DR RefSeq; NP_006006.3; NM_006015.4. [O14497-1] DR RefSeq; NP_624361.1; NM_139135.2. [O14497-2] DR PDB; 1RYU; NMR; -; A=1000-1119. DR PDB; 6LTH; EM; 3.00 A; L=1-2285. DR PDB; 6LTJ; EM; 3.70 A; L=991-2285. DR PDBsum; 1RYU; -. DR PDBsum; 6LTH; -. DR PDBsum; 6LTJ; -. DR AlphaFoldDB; O14497; -. DR BMRB; O14497; -. DR EMDB; EMD-0974; -. DR SMR; O14497; -. DR BioGRID; 113894; 240. DR ComplexPortal; CPX-1164; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant. DR ComplexPortal; CPX-1194; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant. DR ComplexPortal; CPX-1195; Embryonic stem cell-specific SWI/SNF ATP-dependent chromatin remodeling complex. DR ComplexPortal; CPX-1201; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant. DR ComplexPortal; CPX-1202; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant. DR ComplexPortal; CPX-1203; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant. DR ComplexPortal; CPX-1204; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant. DR ComplexPortal; CPX-1207; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant. DR ComplexPortal; CPX-1209; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant. DR ComplexPortal; CPX-1212; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant. DR ComplexPortal; CPX-1216; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant. DR ComplexPortal; CPX-1219; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant. DR ComplexPortal; CPX-1222; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant. DR ComplexPortal; CPX-1225; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant. DR ComplexPortal; CPX-1226; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant. DR CORUM; O14497; -. DR DIP; DIP-33016N; -. DR IntAct; O14497; 89. DR MINT; O14497; -. DR STRING; 9606.ENSP00000320485; -. DR GlyCosmos; O14497; 19 sites, 2 glycans. DR GlyGen; O14497; 23 sites, 2 O-linked glycans (23 sites). DR iPTMnet; O14497; -. DR MetOSite; O14497; -. DR PhosphoSitePlus; O14497; -. DR SwissPalm; O14497; -. DR BioMuta; ARID1A; -. DR EPD; O14497; -. DR jPOST; O14497; -. DR MassIVE; O14497; -. DR MaxQB; O14497; -. DR PaxDb; 9606-ENSP00000320485; -. DR PeptideAtlas; O14497; -. DR ProteomicsDB; 48041; -. [O14497-1] DR ProteomicsDB; 48042; -. [O14497-2] DR ProteomicsDB; 48043; -. [O14497-3] DR Pumba; O14497; -. DR Antibodypedia; 1691; 271 antibodies from 34 providers. DR DNASU; 8289; -. DR Ensembl; ENST00000324856.13; ENSP00000320485.7; ENSG00000117713.21. [O14497-1] DR Ensembl; ENST00000374152.7; ENSP00000363267.2; ENSG00000117713.21. [O14497-3] DR Ensembl; ENST00000457599.6; ENSP00000387636.2; ENSG00000117713.21. [O14497-2] DR GeneID; 8289; -. DR KEGG; hsa:8289; -. DR MANE-Select; ENST00000324856.13; ENSP00000320485.7; NM_006015.6; NP_006006.3. DR UCSC; uc001bmu.2; human. [O14497-1] DR AGR; HGNC:11110; -. DR CTD; 8289; -. DR DisGeNET; 8289; -. DR GeneCards; ARID1A; -. DR GeneReviews; ARID1A; -. DR HGNC; HGNC:11110; ARID1A. DR HPA; ENSG00000117713; Low tissue specificity. DR MalaCards; ARID1A; -. DR MIM; 603024; gene. DR MIM; 614607; phenotype. DR neXtProt; NX_O14497; -. DR OpenTargets; ENSG00000117713; -. DR Orphanet; 1465; Coffin-Siris syndrome. DR PharmGKB; PA35960; -. DR VEuPathDB; HostDB:ENSG00000117713; -. DR eggNOG; KOG2510; Eukaryota. DR GeneTree; ENSGT00940000155194; -. DR HOGENOM; CLU_000974_1_1_1; -. DR InParanoid; O14497; -. DR OMA; CRPIDMD; -. DR OrthoDB; 5477968at2759; -. DR PhylomeDB; O14497; -. DR TreeFam; TF320364; -. DR PathwayCommons; O14497; -. DR Reactome; R-HSA-3214858; RMTs methylate histone arginines. DR Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known. DR SignaLink; O14497; -. DR SIGNOR; O14497; -. DR BioGRID-ORCS; 8289; 177 hits in 1228 CRISPR screens. DR ChiTaRS; ARID1A; human. DR EvolutionaryTrace; O14497; -. DR GeneWiki; ARID1A; -. DR GenomeRNAi; 8289; -. DR Pharos; O14497; Tbio. DR PRO; PR:O14497; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; O14497; Protein. DR Bgee; ENSG00000117713; Expressed in bone marrow cell and 207 other cell types or tissues. DR ExpressionAtlas; O14497; baseline and differential. DR GO; GO:0140092; C:bBAF complex; NAS:ComplexPortal. DR GO; GO:0035060; C:brahma complex; NAS:ComplexPortal. DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL. DR GO; GO:0071565; C:nBAF complex; ISS:UniProtKB. DR GO; GO:0071564; C:npBAF complex; ISS:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; TAS:UniProtKB. DR GO; GO:0016514; C:SWI/SNF complex; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; IDA:MGI. DR GO; GO:0016922; F:nuclear receptor binding; IPI:BHF-UCL. DR GO; GO:0003713; F:transcription coactivator activity; NAS:BHF-UCL. DR GO; GO:0030521; P:androgen receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0006338; P:chromatin remodeling; IDA:BHF-UCL. DR GO; GO:0042921; P:glucocorticoid receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW. DR GO; GO:0006337; P:nucleosome disassembly; IDA:BHF-UCL. DR GO; GO:0045597; P:positive regulation of cell differentiation; NAS:ComplexPortal. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:2000781; P:positive regulation of double-strand break repair; NAS:ComplexPortal. DR GO; GO:0045663; P:positive regulation of myoblast differentiation; NAS:ComplexPortal. DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; NAS:ComplexPortal. DR GO; GO:0045582; P:positive regulation of T cell differentiation; NAS:ComplexPortal. DR GO; GO:0070316; P:regulation of G0 to G1 transition; NAS:ComplexPortal. DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; NAS:ComplexPortal. DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; NAS:ComplexPortal. DR GO; GO:2000819; P:regulation of nucleotide-excision repair; NAS:ComplexPortal. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; TAS:UniProtKB. DR CDD; cd16876; ARID_ARID1A; 1. DR Gene3D; 1.10.150.60; ARID DNA-binding domain; 1. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1. DR InterPro; IPR030094; ARID1A_ARID_BRIGHT_DNA-bd. DR InterPro; IPR001606; ARID_dom. DR InterPro; IPR036431; ARID_dom_sf. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR021906; BAF250/Osa. DR InterPro; IPR033388; BAF250_C. DR PANTHER; PTHR12656:SF12; AT-RICH INTERACTIVE DOMAIN-CONTAINING PROTEIN 1A; 1. DR PANTHER; PTHR12656; BRG-1 ASSOCIATED FACTOR 250 BAF250; 1. DR Pfam; PF01388; ARID; 1. DR Pfam; PF12031; BAF250_C; 1. DR SMART; SM01014; ARID; 1. DR SMART; SM00501; BRIGHT; 1. DR SUPFAM; SSF46774; ARID-like; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR PROSITE; PS51011; ARID; 1. DR Genevisible; O14497; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Chromatin regulator; KW Direct protein sequencing; DNA-binding; Intellectual disability; KW Methylation; Neurogenesis; Nucleus; Phosphoprotein; Reference proteome; KW Transcription; Transcription regulation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22814378" FT CHAIN 2..2285 FT /note="AT-rich interactive domain-containing protein 1A" FT /id="PRO_0000200575" FT DOMAIN 1017..1108 FT /note="ARID" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355" FT REGION 1..820 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 978..1005 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1113..1483 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1539..1603 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1747..1774 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1859..1907 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 295..299 FT /note="LXXLL" FT MOTIF 1368..1387 FT /note="Nuclear localization signal" FT /evidence="ECO:0000269|PubMed:26614907" FT MOTIF 1709..1713 FT /note="LXXLL" FT MOTIF 1967..1971 FT /note="LXXLL" FT MOTIF 2085..2089 FT /note="LXXLL" FT COMPBIAS 202..218 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 251..270 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 285..307 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 370..386 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 396..411 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 418..481 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 492..518 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 533..641 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 657..685 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 701..716 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 728..799 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1127..1157 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1173..1223 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1301..1372 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1392..1437 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1467..1481 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1553..1576 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1760..1774 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22814378" FT MOD_RES 58 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 79 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 233 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 286 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332" FT MOD_RES 301 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 363 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 382 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 429 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 604 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 696 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 698 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 702 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 730 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:A2BH40" FT MOD_RES 764 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 772 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 1184 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1235 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1276 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 1604 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1612 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 1751 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 1754 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1888 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1905 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 1929 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1944 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..383 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:9434167" FT /id="VSP_037157" FT VAR_SEQ 1367..1583 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11318604" FT /id="VSP_015225" FT VARIANT 120 FT /note="P -> S (in dbSNP:rs571264557)" FT /evidence="ECO:0000269|PubMed:23906836" FT /id="VAR_076938" FT VARIANT 1020 FT /note="R -> K (found in a clear cell renal carcinoma; FT somatic mutation)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064695" FT VARIANT 1658 FT /note="R -> W (found in a gastric cancer sample; somatic FT mutation; dbSNP:rs1442666063)" FT /evidence="ECO:0000269|PubMed:22009941" FT /id="VAR_068021" FT VARIANT 1907 FT /note="I -> F (found in a breast cancer sample; somatic FT mutation; dbSNP:rs139230162)" FT /evidence="ECO:0000269|PubMed:22009941" FT /id="VAR_068022" FT VARIANT 2087 FT /note="G -> R (found in a breast cancer sample; somatic FT mutation; dbSNP:rs1553153748)" FT /evidence="ECO:0000269|PubMed:22009941" FT /id="VAR_068023" FT VARIANT 2089 FT /note="L -> P (found in a clear cell renal carcinoma case; FT somatic mutation)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064696" FT MUTAGEN 1073 FT /note="W->A: Partial loss of DNA-binding activity. Complete FT loss of activity; when associated with A-1096." FT /evidence="ECO:0000269|PubMed:10757798" FT MUTAGEN 1096 FT /note="Y->A: Partial loss of DNA-binding activity. Complete FT loss of activity; when associated with A-1073." FT /evidence="ECO:0000269|PubMed:10757798" FT MUTAGEN 1370..1371 FT /note="KR->TT: Displays nucleocytoplasmic localization and FT increased stability; when associated with T-1383." FT /evidence="ECO:0000269|PubMed:26614907" FT MUTAGEN 1383 FT /note="R->T: Displays nucleocytoplasmic localization and FT increased stability; when associated with 1370-T-T-1371." FT /evidence="ECO:0000269|PubMed:26614907" FT MUTAGEN 1656..1658 FT /note="RRR->TTT: No effect on subcellular localization." FT /evidence="ECO:0000269|PubMed:26614907" FT CONFLICT 410 FT /note="G -> D (in Ref. 1; AAG33967, 7; BAA23269 and 8; FT BAA83073)" FT /evidence="ECO:0000305" FT CONFLICT 434 FT /note="M -> V (in Ref. 1; AAG33967, 7; BAA23269 and 8; FT BAA83073)" FT /evidence="ECO:0000305" FT CONFLICT 636 FT /note="P -> T (in Ref. 9; AAK54505)" FT /evidence="ECO:0000305" FT CONFLICT 732 FT /note="Q -> S (in Ref. 1; AAG33967, 5; AAG17549 and 7; FT BAA23269)" FT /evidence="ECO:0000305" FT CONFLICT 750 FT /note="R -> RG (in Ref. 8; BAA83073)" FT /evidence="ECO:0000305" FT CONFLICT 757 FT /note="P -> S (in Ref. 1; AAG33967, 5; AAG17549 and 7; FT BAA23269)" FT /evidence="ECO:0000305" FT CONFLICT 776 FT /note="P -> L (in Ref. 1; AAG33967, 5; AAG17549 and 7; FT BAA23269)" FT /evidence="ECO:0000305" FT CONFLICT 858 FT /note="M -> V (in Ref. 9; AAK54505)" FT /evidence="ECO:0000305" FT CONFLICT 871 FT /note="N -> T (in Ref. 7; BAA23269)" FT /evidence="ECO:0000305" FT CONFLICT 875 FT /note="M -> I (in Ref. 9; AAK54505)" FT /evidence="ECO:0000305" FT CONFLICT 1017 FT /note="E -> G (in Ref. 1; AAG33967, 5; AAG17549 and 7; FT BAA23269)" FT /evidence="ECO:0000305" FT CONFLICT 1180 FT /note="Missing (in Ref. 10; BAD96995)" FT /evidence="ECO:0000305" FT CONFLICT 1307 FT /note="P -> S (in Ref. 1; AAG33967, 5; AAG17549 and 7; FT BAA23269)" FT /evidence="ECO:0000305" FT CONFLICT 1389 FT /note="Y -> F (in Ref. 5; AAG17549)" FT /evidence="ECO:0000305" FT CONFLICT 1399 FT /note="Q -> L (in Ref. 1; AAG33967 and 7; BAA23269)" FT /evidence="ECO:0000305" FT CONFLICT 1416 FT /note="Q -> P (in Ref. 1; AAG33967 and 7; BAA23269)" FT /evidence="ECO:0000305" FT CONFLICT 1532 FT /note="M -> V (in Ref. 1; AAG33967)" FT /evidence="ECO:0000305" FT CONFLICT 1638 FT /note="D -> A (in Ref. 9; AAK54505)" FT /evidence="ECO:0000305" FT CONFLICT 1789 FT /note="A -> T (in Ref. 10; BAD96995)" FT /evidence="ECO:0000305" FT CONFLICT 1839 FT /note="S -> R (in Ref. 9; AAK54505)" FT /evidence="ECO:0000305" FT CONFLICT 2131 FT /note="N -> D (in Ref. 9; AAK54505)" FT /evidence="ECO:0000305" FT CONFLICT 2143 FT /note="R -> H (in Ref. 9; AAK54505)" FT /evidence="ECO:0000305" FT CONFLICT 2159 FT /note="K -> E (in Ref. 9; AAK54505)" FT /evidence="ECO:0000305" FT CONFLICT 2182 FT /note="A -> T (in Ref. 10; BAD96995)" FT /evidence="ECO:0000305" FT HELIX 1010..1012 FT /evidence="ECO:0007829|PDB:1RYU" FT STRAND 1014..1016 FT /evidence="ECO:0007829|PDB:1RYU" FT HELIX 1018..1033 FT /evidence="ECO:0007829|PDB:1RYU" FT STRAND 1045..1048 FT /evidence="ECO:0007829|PDB:1RYU" FT HELIX 1051..1061 FT /evidence="ECO:0007829|PDB:1RYU" FT HELIX 1066..1068 FT /evidence="ECO:0007829|PDB:1RYU" FT HELIX 1072..1079 FT /evidence="ECO:0007829|PDB:1RYU" FT HELIX 1087..1099 FT /evidence="ECO:0007829|PDB:1RYU" FT TURN 1100..1107 FT /evidence="ECO:0007829|PDB:1RYU" FT TURN 1109..1111 FT /evidence="ECO:0007829|PDB:1RYU" FT HELIX 1646..1648 FT /evidence="ECO:0007829|PDB:6LTH" FT TURN 1662..1664 FT /evidence="ECO:0007829|PDB:6LTH" FT HELIX 1669..1678 FT /evidence="ECO:0007829|PDB:6LTH" FT HELIX 1681..1696 FT /evidence="ECO:0007829|PDB:6LTH" FT HELIX 1698..1700 FT /evidence="ECO:0007829|PDB:6LTH" FT TURN 1701..1703 FT /evidence="ECO:0007829|PDB:6LTH" FT HELIX 1706..1708 FT /evidence="ECO:0007829|PDB:6LTH" FT HELIX 1712..1728 FT /evidence="ECO:0007829|PDB:6LTH" FT STRAND 1734..1738 FT /evidence="ECO:0007829|PDB:6LTH" FT HELIX 1741..1744 FT /evidence="ECO:0007829|PDB:6LTH" FT TURN 1803..1805 FT /evidence="ECO:0007829|PDB:6LTH" FT STRAND 1814..1816 FT /evidence="ECO:0007829|PDB:6LTH" FT STRAND 1822..1825 FT /evidence="ECO:0007829|PDB:6LTH" FT STRAND 1830..1833 FT /evidence="ECO:0007829|PDB:6LTH" FT HELIX 1841..1845 FT /evidence="ECO:0007829|PDB:6LTH" FT HELIX 1972..1991 FT /evidence="ECO:0007829|PDB:6LTH" FT HELIX 1997..2001 FT /evidence="ECO:0007829|PDB:6LTH" FT HELIX 2005..2015 FT /evidence="ECO:0007829|PDB:6LTH" FT HELIX 2050..2067 FT /evidence="ECO:0007829|PDB:6LTH" FT HELIX 2068..2070 FT /evidence="ECO:0007829|PDB:6LTH" FT STRAND 2074..2076 FT /evidence="ECO:0007829|PDB:6LTH" FT HELIX 2078..2093 FT /evidence="ECO:0007829|PDB:6LTH" FT STRAND 2096..2101 FT /evidence="ECO:0007829|PDB:6LTH" FT HELIX 2114..2126 FT /evidence="ECO:0007829|PDB:6LTH" FT HELIX 2129..2136 FT /evidence="ECO:0007829|PDB:6LTH" FT HELIX 2141..2157 FT /evidence="ECO:0007829|PDB:6LTH" FT HELIX 2161..2177 FT /evidence="ECO:0007829|PDB:6LTH" FT HELIX 2179..2186 FT /evidence="ECO:0007829|PDB:6LTH" FT HELIX 2191..2208 FT /evidence="ECO:0007829|PDB:6LTH" FT HELIX 2229..2242 FT /evidence="ECO:0007829|PDB:6LTH" FT STRAND 2245..2247 FT /evidence="ECO:0007829|PDB:6LTH" FT HELIX 2248..2251 FT /evidence="ECO:0007829|PDB:6LTH" FT TURN 2252..2254 FT /evidence="ECO:0007829|PDB:6LTH" FT HELIX 2255..2263 FT /evidence="ECO:0007829|PDB:6LTH" FT HELIX 2269..2283 FT /evidence="ECO:0007829|PDB:6LTH" SQ SEQUENCE 2285 AA; 242045 MW; 85BC5B6061625D8E CRC64; MAAQVAPAAA SSLGNPPPPP PSELKKAEQQ QREEAGGEAA AAAAAERGEM KAAAGQESEG PAVGPPQPLG KELQDGAESN GGGGGGGAGS GGGPGAEPDL KNSNGNAGPR PALNNNLTEP PGGGGGGSSD GVGAPPHSAA AALPPPAYGF GQPYGRSPSA VAAAAAAVFH QQHGGQQSPG LAALQSGGGG GLEPYAGPQQ NSHDHGFPNH QYNSYYPNRS AYPPPAPAYA LSSPRGGTPG SGAAAAAGSK PPPSSSASAS SSSSSFAQQR FGAMGGGGPS AAGGGTPQPT ATPTLNQLLT SPSSARGYQG YPGGDYSGGP QDGGAGKGPA DMASQCWGAA AAAAAAAAAS GGAQQRSHHA PMSPGSSGGG GQPLARTPQP SSPMDQMGKM RPQPYGGTNP YSQQQGPPSG PQQGHGYPGQ PYGSQTPQRY PMTMQGRAQS AMGGLSYTQQ IPPYGQQGPS GYGQQGQTPY YNQQSPHPQQ QQPPYSQQPP SQTPHAQPSY QQQPQSQPPQ LQSSQPPYSQ QPSQPPHQQS PAPYPSQQST TQQHPQSQPP YSQPQAQSPY QQQQPQQPAP STLSQQAAYP QPQSQQSQQT AYSQQRFPPP QELSQDSFGS QASSAPSMTS SKGGQEDMNL SLQSRPSSLP DLSGSIDDLP MGTEGALSPG VSTSGISSSQ GEQSNPAQSP FSPHTSPHLP GIRGPSPSPV GSPASVAQSR SGPLSPAAVP GNQMPPRPPS GQSDSIMHPS MNQSSIAQDR GYMQRNPQMP QYSSPQPGSA LSPRQPSGGQ IHTGMGSYQQ NSMGSYGPQG GQYGPQGGYP RQPNYNALPN ANYPSAGMAG GINPMGAGGQ MHGQPGIPPY GTLPPGRMSH ASMGNRPYGP NMANMPPQVG SGMCPPPGGM NRKTQETAVA MHVAANSIQN RPPGYPNMNQ GGMMGTGPPY GQGINSMAGM INPQGPPYSM GGTMANNSAG MAASPEMMGL GDVKLTPATK MNNKADGTPK TESKSKKSSS STTTNEKITK LYELGGEPER KMWVDRYLAF TEEKAMGMTN LPAVGRKPLD LYRLYVSVKE IGGLTQVNKN KKWRELATNL NVGTSSSAAS SLKKQYIQCL YAFECKIERG EDPPPDIFAA ADSKKSQPKI QPPSPAGSGS MQGPQTPQST SSSMAEGGDL KPPTPASTPH SQIPPLPGMS RSNSVGIQDA FNDGSDSTFQ KRNSMTPNPG YQPSMNTSDM MGRMSYEPNK DPYGSMRKAP GSDPFMSSGQ GPNGGMGDPY SRAAGPGLGN VAMGPRQHYP YGGPYDRVRT EPGIGPEGNM STGAPQPNLM PSNPDSGMYS PSRYPPQQQQ QQQQRHDSYG NQFSTQGTPS GSPFPSQQTT MYQQQQQNYK RPMDGTYGPP AKRHEGEMYS VPYSTGQGQP QQQQLPPAQP QPASQQQAAQ PSPQQDVYNQ YGNAYPATAT AATERRPAGG PQNQFPFQFG RDRVSAPPGT NAQQNMPPQM MGGPIQASAE VAQQGTMWQG RNDMTYNYAN RQSTGSAPQG PAYHGVNRTD EMLHTDQRAN HEGSWPSHGT RQPPYGPSAP VPPMTRPPPS NYQPPPSMQN HIPQVSSPAP LPRPMENRTS PSKSPFLHSG MKMQKAGPPV PASHIAPAPV QPPMIRRDIT FPPGSVEATQ PVLKQRRRLT MKDIGTPEAW RVMMSLKSGL LAESTWALDT INILLYDDNS IMTFNLSQLP GLLELLVEYF RRCLIEIFGI LKEYEVGDPG QRTLLDPGRF SKVSSPAPME GGEEEEELLG PKLEEEEEEE VVENDEEIAF SGKDKPASEN SEEKLISKFD KLPVKIVQKN DPFVVDCSDK LGRVQEFDSG LLHWRIGGGD TTEHIQTHFE SKTELLPSRP HAPCPPAPRK HVTTAEGTPG TTDQEGPPPD GPPEKRITAT MDDMLSTRSS TLTEDGAKSS EAIKESSKFP FGISPAQSHR NIKILEDEPH SKDETPLCTL LDWQDSLAKR CVCVSNTIRS LSFVPGNDFE MSKHPGLLLI LGKLILLHHK HPERKQAPLT YEKEEEQDQG VSCNKVEWWW DCLEMLRENT LVTLANISGQ LDLSPYPESI CLPVLDGLLH WAVCPSAEAQ DPFSTLGPNA VLSPQRLVLE TLSKLSIQDN NVDLILATPP FSRLEKLYST MVRFLSDRKN PVCREMAVVL LANLAQGDSL AARAIAVQKG SIGNLLGFLE DSLAATQFQQ SQASLLHMQN PPFEPTSVDM MRRAARALLA LAKVDENHSE FTLYESRLLD ISVSPLMNSL VSQVICDVLF LIGQS //