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AT-rich interactive domain-containing protein 1A (ARID domain-containing protein 1A) (B120) (BRG1-associated factor 250) (BAF250) (BRG1-associated factor 250a) (BAF250A) (Osa homolog 1) (hOSA1) (SWI-like protein) (SWI/SNF complex protein p270) (SWI/SNF-related, matrix-associated, actin-dependent regulator of chromatin subfamily F member 1) (hELD)

 ARI1A_HUMAN             Reviewed;        2285 AA.
O14497; D3DPL1; Q53FK9; Q5T0W1; Q5T0W2; Q5T0W3; Q8NFD6; Q96T89;
Q9BY33; Q9HBJ5; Q9UPZ1;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
30-AUG-2005, sequence version 3.
22-NOV-2017, entry version 182.
RecName: Full=AT-rich interactive domain-containing protein 1A;
Short=ARID domain-containing protein 1A;
AltName: Full=B120;
AltName: Full=BRG1-associated factor 250;
Short=BAF250;
AltName: Full=BRG1-associated factor 250a;
Short=BAF250A;
AltName: Full=Osa homolog 1;
Short=hOSA1;
AltName: Full=SWI-like protein;
AltName: Full=SWI/SNF complex protein p270;
AltName: Full=SWI/SNF-related, matrix-associated, actin-dependent regulator of chromatin subfamily F member 1;
AltName: Full=hELD;
Name=ARID1A; Synonyms=BAF250, BAF250A, C1orf4, OSA1, SMARCF1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE,
TISSUE SPECIFICITY, AND IDENTIFICATION IN THE BAF COMPLEX.
PubMed=11073988; DOI=10.1128/MCB.20.23.8879-8888.2000;
Nie Z., Xue Y., Yang D., Zhou S., Deroo B.J., Archer T.K., Wang W.;
"A specificity and targeting subunit of a human SWI/SNF family-related
chromatin-remodeling complex.";
Mol. Cell. Biol. 20:8879-8888(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 287-2285 (ISOFORM 1), TISSUE
SPECIFICITY, INTERACTION WITH SMARCA2 AND SMARCA4, AND IDENTIFICATION
IN A SWI/SNF COMPLEX WITH ARID1B.
PubMed=12200431; DOI=10.1074/jbc.M205961200;
Inoue H., Furukawa T., Giannakopoulos S., Zhou S., King D.S.,
Tanese N.;
"Largest subunits of the human SWI/SNF chromatin-remodeling complex
promote transcriptional activation by steroid hormone receptors.";
J. Biol. Chem. 277:41674-41685(2002).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 347-2285 (ISOFORM 1), IDENTIFICATION BY
MASS SPECTROMETRY, AND IDENTIFICATION IN THE BAF COMPLEX.
TISSUE=Brain;
PubMed=11734557; DOI=10.1074/jbc.M108702200;
Kato H., Tjernberg A., Zhang W., Krutchinsky A.N., An W., Takeuchi T.,
Ohtsuki Y., Sugano S., de Bruijn D.R., Chait B.T., Roeder R.G.;
"SYT associates with human SNF/SWI complexes and the C-terminal region
of its fusion partner SSX1 targets histones.";
J. Biol. Chem. 277:5498-5505(2002).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 358-2285 (ISOFORM 1), AND MUTAGENESIS OF
TRP-1073 AND TYR-1096.
PubMed=10757798; DOI=10.1128/MCB.20.9.3137-3146.2000;
Dallas P.B., Pacchione S., Wilsker D., Bowrin V., Kobayashi R.,
Moran E.;
"The human SWI-SNF complex protein p270 is an ARID family member with
non-sequence-specific DNA binding activity.";
Mol. Cell. Biol. 20:3137-3146(2000).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-1585 (ISOFORM 3).
PubMed=9434167; DOI=10.1016/S0378-1119(97)00525-8;
Takeuchi T., Chen B.-K., Qiu Y., Sonobe H., Ohtsuki Y.;
"Molecular cloning and expression of a novel human cDNA containing CAG
repeats.";
Gene 204:71-77(1997).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 380-1515.
Takeuchi T., Misaki A.;
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 384-2285 (ISOFORM 2), ALTERNATIVE
SPLICING (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=11318604; DOI=10.1006/geno.2001.6477;
Kozmik Z., Machon O., Kralova J., Kreslova J., Paces J., Vlcek C.;
"Characterization of mammalian orthologues of the Drosophila osa gene:
cDNA cloning, expression, chromosomal localization, and direct
physical interaction with Brahma chromatin-remodeling complex.";
Genomics 73:140-148(2001).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1104-2285 (ISOFORM 1).
TISSUE=Gastric mucosa;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[11]
IDENTIFICATION IN SWI/SNF COMPLEXES.
PubMed=8804307; DOI=10.1101/gad.10.17.2117;
Wang W., Xue Y., Zhou S., Kuo A., Cairns B.R., Crabtree G.R.;
"Diversity and specialization of mammalian SWI/SNF complexes.";
Genes Dev. 10:2117-2130(1996).
[12]
IDENTIFICATION IN A SWI/SNF COMPLEX.
PubMed=11780067; DOI=10.1038/414924a;
Lemon B., Inouye C., King D.S., Tjian R.;
"Selectivity of chromatin-remodelling cofactors for ligand-activated
transcription.";
Nature 414:924-928(2001).
[13]
IDENTIFICATION IN A SWI/SNF-LIKE COMPLEX WITH ARID1A.
PubMed=11988099;
Hurlstone A.F., Olave I.A., Barker N., van Noort M., Clevers H.;
"Cloning and characterization of hELD/OSA1, a novel BRG1 interacting
protein.";
Biochem. J. 364:255-264(2002).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-696; SER-698 AND
SER-702, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-772, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-286; SER-301; SER-696;
SER-698; SER-764; SER-772 AND SER-1944, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; THR-286; SER-363;
SER-604; SER-696; SER-698; SER-702; SER-772 AND SER-1184, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1612 AND LYS-1905, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-772, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363; SER-696; SER-702
AND SER-1604, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[25]
INVOLVEMENT IN CSS2.
PubMed=22426308; DOI=10.1038/ng.2219;
Tsurusaki Y., Okamoto N., Ohashi H., Kosho T., Imai Y., Hibi-Ko Y.,
Kaname T., Naritomi K., Kawame H., Wakui K., Fukushima Y., Homma T.,
Kato M., Hiraki Y., Yamagata T., Yano S., Mizuno S., Sakazume S.,
Ishii T., Nagai T., Shiina M., Ogata K., Ohta T., Niikawa N.,
Miyatake S., Okada I., Mizuguchi T., Doi H., Saitsu H., Miyake N.,
Matsumoto N.;
"Mutations affecting components of the SWI/SNF complex cause Coffin-
Siris syndrome.";
Nat. Genet. 44:376-378(2012).
[26]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-233; SER-363;
SER-382; SER-604; SER-696; SER-698; SER-702; SER-764; SER-772;
SER-1184; SER-1235; SER-1604; SER-1751; SER-1754; THR-1888; SER-1929
AND SER-1944, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363; SER-696 AND
SER-1751, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[29]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-429 AND ARG-1276, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[30]
REVIEW ON SWI/SNF CHROMATIN REMODELING COMPLEXES.
PubMed=12672490; DOI=10.1016/S0959-437X(03)00022-4;
Martens J.A., Winston F.;
"Recent advances in understanding chromatin remodeling by SWI/SNF
complexes.";
Curr. Opin. Genet. Dev. 13:136-142(2003).
[31]
IDENTIFICATION IN A SWI/SNF-LIKE EBAFA COMPLEX, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=12665591; DOI=10.1128/MCB.23.8.2942-2952.2003;
Nie Z., Yan Z., Chen E.H., Sechi S., Ling C., Zhou S., Xue Y.,
Yang D., Murray D., Kanakubo E., Cleary M.L., Wang W.;
"Novel SWI/SNF chromatin-remodeling complexes contain a mixed-lineage
leukemia chromosomal translocation partner.";
Mol. Cell. Biol. 23:2942-2952(2003).
[32]
IDENTIFICATION IN SWI/SNF COMPLEXES, AND INTERACTION WITH SMARCA2;
SMARCA4 AND SMARCC1.
PubMed=15170388; DOI=10.1042/BJ20040524;
Wang X., Nagl N.G., Wilsker D., Van Scoy M., Pacchione S., Yaciuk P.,
Dallas P.B., Moran E.;
"Two related ARID family proteins are alternative subunits of human
SWI/SNF complexes.";
Biochem. J. 383:319-325(2004).
[33]
IDENTIFICATION IN THE BAF COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=18765789; DOI=10.1101/gad.471408;
Lange M., Kaynak B., Forster U.B., Toenjes M., Fischer J.J., Grimm C.,
Schlesinger J., Just S., Dunkel I., Krueger T., Mebus S., Lehrach H.,
Lurz R., Gobom J., Rottbauer W., Abdelilah-Seyfried S., Sperling S.;
"Regulation of muscle development by DPF3, a novel histone acetylation
and methylation reader of the BAF chromatin remodeling complex.";
Genes Dev. 22:2370-2384(2008).
[34]
REVIEW ON SWI/SNF CHROMATIN REMODELING COMPLEXES.
PubMed=22952240; DOI=10.1074/jbc.R111.309302;
Euskirchen G., Auerbach R.K., Snyder M.;
"SWI/SNF chromatin-remodeling factors: multiscale analyses and diverse
functions.";
J. Biol. Chem. 287:30897-30905(2012).
[35]
REVIEW ON SWI/SNF CHROMATIN REMODELING COMPLEXES.
PubMed=26601204; DOI=10.1126/sciadv.1500447;
Kadoch C., Crabtree G.R.;
"Mammalian SWI/SNF chromatin remodeling complexes and cancer:
Mechanistic insights gained from human genomics.";
Sci. Adv. 1:E1500447-E1500447(2015).
[36]
SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, AND MUTAGENESIS OF
1370-LYS-ARG-1371; ARG-1383 AND 1656-ARG--ARG-1658.
PubMed=26614907; DOI=10.1016/j.bbrc.2015.11.080;
Bateman N.W., Shoji Y., Conrads K.A., Stroop K.D., Hamilton C.A.,
Darcy K.M., Maxwell G.L., Risinger J.I., Conrads T.P.;
"Identification and functional characterization of a novel bipartite
nuclear localization sequence in ARID1A.";
Biochem. Biophys. Res. Commun. 469:114-119(2016).
[37]
STRUCTURE BY NMR OF 1000-1159.
PubMed=14722072; DOI=10.1074/jbc.M312115200;
Kim S., Zhang Z., Upchurch S., Isern N., Chen Y.;
"Structure and DNA-binding sites of the SWI1 AT-rich interaction
domain (ARID) suggest determinants for sequence-specific DNA
recognition.";
J. Biol. Chem. 279:16670-16676(2004).
[38]
VARIANTS LYS-1020 AND PRO-2089.
PubMed=21248752; DOI=10.1038/nature09639;
Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P.,
Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A.,
Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C.,
Jia M., Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A.,
Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S.,
Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A.,
Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C.,
Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R.,
Futreal P.A.;
"Exome sequencing identifies frequent mutation of the SWI/SNF complex
gene PBRM1 in renal carcinoma.";
Nature 469:539-542(2011).
[39]
VARIANTS TRP-1658; PHE-1907 AND ARG-2087.
PubMed=22009941; DOI=10.1002/humu.21633;
Jones S., Li M., Parsons D.W., Zhang X., Wesseling J., Kristel P.,
Schmidt M.K., Markowitz S., Yan H., Bigner D., Hruban R.H.,
Eshleman J.R., Iacobuzio-Donahue C.A., Goggins M., Maitra A.,
Malek S.N., Powell S., Vogelstein B., Kinzler K.W., Velculescu V.E.,
Papadopoulos N.;
"Somatic mutations in the chromatin remodeling gene ARID1A occur in
several tumor types.";
Hum. Mutat. 33:100-103(2012).
[40]
VARIANT SER-120.
PubMed=23906836; DOI=10.1093/hmg/ddt366;
Wieczorek D., Boegershausen N., Beleggia F., Steiner-Haldenstaett S.,
Pohl E., Li Y., Milz E., Martin M., Thiele H., Altmueller J.,
Alanay Y., Kayserili H., Klein-Hitpass L., Boehringer S.,
Wollstein A., Albrecht B., Boduroglu K., Caliebe A., Chrzanowska K.,
Cogulu O., Cristofoli F., Czeschik J.C., Devriendt K., Dotti M.T.,
Elcioglu N., Gener B., Goecke T.O., Krajewska-Walasek M.,
Guillen-Navarro E., Hayek J., Houge G., Kilic E., Simsek-Kiper P.O.,
Lopez-Gonzalez V., Kuechler A., Lyonnet S., Mari F., Marozza A.,
Mathieu Dramard M., Mikat B., Morin G., Morice-Picard F., Ozkinay F.,
Rauch A., Renieri A., Tinschert S., Utine G.E., Vilain C.,
Vivarelli R., Zweier C., Nuernberg P., Rahmann S., Vermeesch J.,
Luedecke H.J., Zeschnigk M., Wollnik B.;
"A comprehensive molecular study on Coffin-Siris and Nicolaides-
Baraitser syndromes identifies a broad molecular and clinical spectrum
converging on altered chromatin remodeling.";
Hum. Mol. Genet. 22:5121-5135(2013).
-!- FUNCTION: Involved in transcriptional activation and repression of
select genes by chromatin remodeling (alteration of DNA-nucleosome
topology). Component of SWI/SNF chromatin remodeling complexes
that carry out key enzymatic activities, changing chromatin
structure by altering DNA-histone contacts within a nucleosome in
an ATP-dependent manner. Binds DNA non-specifically. Belongs to
the neural progenitors-specific chromatin remodeling complex
(npBAF complex) and the neuron-specific chromatin remodeling
complex (nBAF complex). During neural development a switch from a
stem/progenitor to a postmitotic chromatin remodeling mechanism
occurs as neurons exit the cell cycle and become committed to
their adult state. The transition from proliferating neural
stem/progenitor cells to postmitotic neurons requires a switch in
subunit composition of the npBAF and nBAF complexes. As neural
progenitors exit mitosis and differentiate into neurons, npBAF
complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are
exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B
or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The
npBAF complex is essential for the self-renewal/proliferative
capacity of the multipotent neural stem cells. The nBAF complex
along with CREST plays a role regulating the activity of genes
essential for dendrite growth (By similarity).
{ECO:0000250|UniProtKB:A2BH40, ECO:0000303|PubMed:12672490,
ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}.
-!- SUBUNIT: Component of SWI/SNF chromatin remodeling complexes, in
some of which it can be mutually exclusive with ARID1B/BAF250B.
The canonical complex contains a catalytic subunit (either
SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B) and at least SMARCE1,
ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and
SMARCB1/SNF5/BAF47. Other subunits specific to each of the
complexes may also be present permitting several possible
combinations developmentally and tissue specific (PubMed:22952240,
PubMed:26601204, PubMed:12200431, PubMed:8804307, PubMed:11780067,
PubMed:11988099, PubMed:15170388). Component of the BAF (SWI/SNF-
A) complex, which includes at least actin (ACTB), ARID1A/BAF250A,
ARID1B/BAF250B, SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53,
ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170,
SMARCB1/SNF5/INI1, and one or more SMARCD1/BAF60A, SMARCD2/BAF60B,
or SMARCD3/BAF60C (PubMed:12200431, PubMed:11734557,
PubMed:18765789,). In muscle cells, the BAF complex also contains
DPF3. Component of neural progenitors-specific chromatin
remodeling complex (npBAF complex) composed of at least,
ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C,
SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47,
SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, PHF10/BAF45A,
ACTL6A/BAF53A and actin. Component of neuron-specific chromatin
remodeling complex (nBAF complex) composed of at least,
ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C,
SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47,
SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B,
DPF3/BAF45C, ACTL6B/BAF53B and actin (By similarity). Component of
a SWI/SNF-like EBAFa complex, at least composed of
SMARCA4/BRG1/BAF190A, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A,
SMARCE1/BAF57, SMARCD1/BAF60A, SMARCC1/BAF155, SMARCC2/BAF170,
BAF250A and MLLT1/ENL (PubMed:12665591). Interacts through its C-
terminus with SMARCA2/BRM/BAF190B and SMARCA4/BRG1/BAF190A
(PubMed:12200431, PubMed:15170388). Interacts with SMARCC1/BAF155
(PubMed:15170388). {ECO:0000250|UniProtKB:A2BH40,
ECO:0000269|PubMed:11734557, ECO:0000269|PubMed:11780067,
ECO:0000269|PubMed:11988099, ECO:0000269|PubMed:12200431,
ECO:0000269|PubMed:12665591, ECO:0000269|PubMed:15170388,
ECO:0000269|PubMed:18765789, ECO:0000269|PubMed:8804307,
ECO:0000303|PubMed:12672490, ECO:0000303|PubMed:22952240,
ECO:0000303|PubMed:26601204}.
-!- INTERACTION:
Q14526:HIC1; NbExp=2; IntAct=EBI-637887, EBI-2507362;
P51531:SMARCA2; NbExp=3; IntAct=EBI-637887, EBI-679562;
P51532:SMARCA4; NbExp=22; IntAct=EBI-637887, EBI-302489;
P11388:TOP2A; NbExp=2; IntAct=EBI-15956509, EBI-539628;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00355, ECO:0000269|PubMed:11318604,
ECO:0000269|PubMed:26614907}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O14497-1; Sequence=Displayed;
Name=2;
IsoId=O14497-2; Sequence=VSP_015225;
Name=3;
IsoId=O14497-3; Sequence=VSP_037157;
-!- TISSUE SPECIFICITY: Highly expressed in spleen, thymus, prostate,
testis, ovary, small intestine, colon, and PBL, and at a much
lower level in heart, brain, placenta, lung, liver, skeletal
muscle, kidney, and pancreas. {ECO:0000269|PubMed:11073988,
ECO:0000269|PubMed:11318604, ECO:0000269|PubMed:12200431}.
-!- DISEASE: Coffin-Siris syndrome 2 (CSS2) [MIM:614607]: A form of
Coffin-Siris syndrome, a congenital multiple malformation syndrome
with broad phenotypic and genetic variability. Cardinal features
are intellectual disability, coarse facial features,
hypertrichosis, and hypoplastic or absent fifth digit nails or
phalanges. Additional features include malformations of the
cardiac, gastrointestinal, genitourinary, and/or central nervous
systems. Sucking/feeding difficulties, poor growth, ophthalmologic
abnormalities, hearing impairment, and spinal anomalies are common
findings. Both autosomal dominant and autosomal recessive
inheritance patterns have been reported.
{ECO:0000269|PubMed:22426308}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=AAF75765.1; Type=Frameshift; Positions=374; Evidence={ECO:0000305};
Sequence=AAG33967.1; Type=Frameshift; Positions=872, 885; Evidence={ECO:0000305};
Sequence=BAA23269.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
Sequence=BAA83073.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=BAA83073.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF231056; AAG33967.1; ALT_FRAME; mRNA.
EMBL; AL512408; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL034380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471059; EAX07795.1; -; Genomic_DNA.
EMBL; CH471059; EAX07796.1; -; Genomic_DNA.
EMBL; AF521670; AAN03446.1; -; mRNA.
EMBL; AF219114; AAG17549.2; -; mRNA.
EMBL; AF265208; AAF75765.1; ALT_FRAME; mRNA.
EMBL; AB001895; BAA23269.1; ALT_FRAME; mRNA.
EMBL; AB024075; BAA83073.1; ALT_SEQ; Genomic_DNA.
EMBL; AF268913; AAK54505.1; -; mRNA.
EMBL; AK223275; BAD96995.1; -; mRNA.
CCDS; CCDS285.1; -. [O14497-1]
CCDS; CCDS44091.1; -. [O14497-2]
PIR; T00022; T00022.
RefSeq; NP_006006.3; NM_006015.4. [O14497-1]
RefSeq; NP_624361.1; NM_139135.2. [O14497-2]
UniGene; Hs.468972; -.
PDB; 1RYU; NMR; -; A=1000-1119.
PDBsum; 1RYU; -.
ProteinModelPortal; O14497; -.
SMR; O14497; -.
BioGrid; 113894; 68.
CORUM; O14497; -.
DIP; DIP-33016N; -.
IntAct; O14497; 17.
MINT; MINT-2795087; -.
STRING; 9606.ENSP00000320485; -.
iPTMnet; O14497; -.
PhosphoSitePlus; O14497; -.
BioMuta; ARID1A; -.
EPD; O14497; -.
MaxQB; O14497; -.
PaxDb; O14497; -.
PeptideAtlas; O14497; -.
PRIDE; O14497; -.
Ensembl; ENST00000324856; ENSP00000320485; ENSG00000117713. [O14497-1]
Ensembl; ENST00000374152; ENSP00000363267; ENSG00000117713. [O14497-3]
Ensembl; ENST00000457599; ENSP00000387636; ENSG00000117713. [O14497-2]
GeneID; 8289; -.
KEGG; hsa:8289; -.
UCSC; uc001bmu.2; human. [O14497-1]
CTD; 8289; -.
DisGeNET; 8289; -.
EuPathDB; HostDB:ENSG00000117713.17; -.
GeneCards; ARID1A; -.
GeneReviews; ARID1A; -.
HGNC; HGNC:11110; ARID1A.
HPA; CAB016334; -.
HPA; HPA005456; -.
MalaCards; ARID1A; -.
MIM; 603024; gene.
MIM; 614607; phenotype.
neXtProt; NX_O14497; -.
OpenTargets; ENSG00000117713; -.
Orphanet; 1465; Coffin-Siris syndrome.
PharmGKB; PA35960; -.
eggNOG; KOG2510; Eukaryota.
eggNOG; ENOG410Y034; LUCA.
GeneTree; ENSGT00550000074575; -.
HOVERGEN; HBG058196; -.
InParanoid; O14497; -.
KO; K11653; -.
OMA; YSTMVRF; -.
OrthoDB; EOG091G00GP; -.
PhylomeDB; O14497; -.
TreeFam; TF320364; -.
Reactome; R-HSA-3214858; RMTs methylate histone arginines.
Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
SIGNOR; O14497; -.
ChiTaRS; ARID1A; human.
EvolutionaryTrace; O14497; -.
GeneWiki; ARID1A; -.
GenomeRNAi; 8289; -.
PRO; PR:O14497; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000117713; -.
ExpressionAtlas; O14497; baseline and differential.
Genevisible; O14497; HS.
GO; GO:0071565; C:nBAF complex; ISS:UniProtKB.
GO; GO:0071564; C:npBAF complex; ISS:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; TAS:UniProtKB.
GO; GO:0016514; C:SWI/SNF complex; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0016922; F:ligand-dependent nuclear receptor binding; IPI:BHF-UCL.
GO; GO:0031491; F:nucleosome binding; IEA:Ensembl.
GO; GO:0003713; F:transcription coactivator activity; NAS:BHF-UCL.
GO; GO:0030521; P:androgen receptor signaling pathway; IDA:UniProtKB.
GO; GO:0043044; P:ATP-dependent chromatin remodeling; IEA:Ensembl.
GO; GO:0003205; P:cardiac chamber development; IEA:Ensembl.
GO; GO:0055007; P:cardiac muscle cell differentiation; IEA:Ensembl.
GO; GO:0006338; P:chromatin remodeling; IDA:BHF-UCL.
GO; GO:0048096; P:chromatin-mediated maintenance of transcription; TAS:UniProtKB.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
GO; GO:0030900; P:forebrain development; IEA:Ensembl.
GO; GO:0001704; P:formation of primary germ layer; IEA:Ensembl.
GO; GO:0042921; P:glucocorticoid receptor signaling pathway; IDA:UniProtKB.
GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IDA:UniProtKB.
GO; GO:0006344; P:maintenance of chromatin silencing; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
GO; GO:0006337; P:nucleosome disassembly; IDA:BHF-UCL.
GO; GO:0042766; P:nucleosome mobilization; TAS:UniProtKB.
GO; GO:0003408; P:optic cup formation involved in camera-type eye development; IEA:Ensembl.
GO; GO:0060674; P:placenta blood vessel development; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; NAS:BHF-UCL.
GO; GO:0019827; P:stem cell population maintenance; IEA:Ensembl.
GO; GO:1901998; P:toxin transport; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.10.150.60; -; 1.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR001606; ARID_dom.
InterPro; IPR036431; ARID_dom_sf.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR021906; BAF250/Osa.
InterPro; IPR033388; BAF250_C.
InterPro; IPR030094; BAF250a.
PANTHER; PTHR12656; PTHR12656; 1.
PANTHER; PTHR12656:SF12; PTHR12656:SF12; 1.
Pfam; PF01388; ARID; 1.
Pfam; PF12031; BAF250_C; 1.
SMART; SM00501; BRIGHT; 1.
SUPFAM; SSF46774; SSF46774; 1.
SUPFAM; SSF48371; SSF48371; 1.
PROSITE; PS51011; ARID; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Chromatin regulator;
Complete proteome; Direct protein sequencing; DNA-binding;
Mental retardation; Methylation; Neurogenesis; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Transcription;
Transcription regulation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378}.
CHAIN 2 2285 AT-rich interactive domain-containing
protein 1A.
/FTId=PRO_0000200575.
DOMAIN 1017 1108 ARID. {ECO:0000255|PROSITE-
ProRule:PRU00355}.
MOTIF 295 299 LXXLL.
MOTIF 1368 1387 Nuclear localization signal.
{ECO:0000269|PubMed:26614907}.
MOTIF 1709 1713 LXXLL.
MOTIF 1967 1971 LXXLL.
MOTIF 2085 2089 LXXLL.
COMPBIAS 479 482 Poly-Gln.
COMPBIAS 561 567 Poly-Gln.
COMPBIAS 998 1001 Poly-Ser.
COMPBIAS 1327 1404 Gln-rich.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378}.
MOD_RES 58 58 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 79 79 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 233 233 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 286 286 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 301 301 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 363 363 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 382 382 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 429 429 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 604 604 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 696 696 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 698 698 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 702 702 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 730 730 Phosphoserine.
{ECO:0000250|UniProtKB:A2BH40}.
MOD_RES 764 764 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 772 772 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1184 1184 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 1235 1235 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1276 1276 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1604 1604 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1612 1612 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1751 1751 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1754 1754 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1888 1888 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1905 1905 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1929 1929 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1944 1944 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 383 Missing (in isoform 3).
{ECO:0000303|PubMed:9434167}.
/FTId=VSP_037157.
VAR_SEQ 1367 1583 Missing (in isoform 2).
{ECO:0000303|PubMed:11318604}.
/FTId=VSP_015225.
VARIANT 120 120 P -> S (in dbSNP:rs571264557).
{ECO:0000269|PubMed:23906836}.
/FTId=VAR_076938.
VARIANT 1020 1020 R -> K (found in a clear cell renal
carcinoma; somatic mutation).
{ECO:0000269|PubMed:21248752}.
/FTId=VAR_064695.
VARIANT 1658 1658 R -> W (found in a gastric cancer sample;
somatic mutation).
{ECO:0000269|PubMed:22009941}.
/FTId=VAR_068021.
VARIANT 1907 1907 I -> F (found in a breast cancer sample;
somatic mutation; dbSNP:rs139230162).
{ECO:0000269|PubMed:22009941}.
/FTId=VAR_068022.
VARIANT 2087 2087 G -> R (found in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:22009941}.
/FTId=VAR_068023.
VARIANT 2089 2089 L -> P (found in a clear cell renal
carcinoma case; somatic mutation).
{ECO:0000269|PubMed:21248752}.
/FTId=VAR_064696.
MUTAGEN 1073 1073 W->A: Partial loss of DNA-binding
activity. Complete loss of activity; when
associated with A-1096.
{ECO:0000269|PubMed:10757798}.
MUTAGEN 1096 1096 Y->A: Partial loss of DNA-binding
activity. Complete loss of activity; when
associated with A-1073.
{ECO:0000269|PubMed:10757798}.
MUTAGEN 1370 1371 KR->TT: Displays nucleocytoplasmic
localization and increased stability;
when associated with T-1383.
{ECO:0000269|PubMed:26614907}.
MUTAGEN 1383 1383 R->T: Displays nucleocytoplasmic
localization and increased stability;
when associated with 1370-T-T-1371.
{ECO:0000269|PubMed:26614907}.
MUTAGEN 1656 1658 RRR->TTT: No effect on subcellular
localization.
{ECO:0000269|PubMed:26614907}.
CONFLICT 410 410 G -> D (in Ref. 1; AAG33967, 7; BAA23269
and 8; BAA83073). {ECO:0000305}.
CONFLICT 434 434 M -> V (in Ref. 1; AAG33967, 7; BAA23269
and 8; BAA83073). {ECO:0000305}.
CONFLICT 636 636 P -> T (in Ref. 9; AAK54505).
{ECO:0000305}.
CONFLICT 732 732 Q -> S (in Ref. 1; AAG33967, 5; AAG17549
and 7; BAA23269). {ECO:0000305}.
CONFLICT 750 750 R -> RG (in Ref. 8; BAA83073).
{ECO:0000305}.
CONFLICT 757 757 P -> S (in Ref. 1; AAG33967, 5; AAG17549
and 7; BAA23269). {ECO:0000305}.
CONFLICT 776 776 P -> L (in Ref. 1; AAG33967, 5; AAG17549
and 7; BAA23269). {ECO:0000305}.
CONFLICT 858 858 M -> V (in Ref. 9; AAK54505).
{ECO:0000305}.
CONFLICT 871 871 N -> T (in Ref. 7; BAA23269).
{ECO:0000305}.
CONFLICT 875 875 M -> I (in Ref. 9; AAK54505).
{ECO:0000305}.
CONFLICT 1017 1017 E -> G (in Ref. 1; AAG33967, 5; AAG17549
and 7; BAA23269). {ECO:0000305}.
CONFLICT 1180 1180 Missing (in Ref. 10; BAD96995).
{ECO:0000305}.
CONFLICT 1307 1307 P -> S (in Ref. 1; AAG33967, 5; AAG17549
and 7; BAA23269). {ECO:0000305}.
CONFLICT 1389 1389 Y -> F (in Ref. 5; AAG17549).
{ECO:0000305}.
CONFLICT 1399 1399 Q -> L (in Ref. 1; AAG33967 and 7;
BAA23269). {ECO:0000305}.
CONFLICT 1416 1416 Q -> P (in Ref. 1; AAG33967 and 7;
BAA23269). {ECO:0000305}.
CONFLICT 1532 1532 M -> V (in Ref. 1; AAG33967).
{ECO:0000305}.
CONFLICT 1638 1638 D -> A (in Ref. 9; AAK54505).
{ECO:0000305}.
CONFLICT 1789 1789 A -> T (in Ref. 10; BAD96995).
{ECO:0000305}.
CONFLICT 1839 1839 S -> R (in Ref. 9; AAK54505).
{ECO:0000305}.
CONFLICT 2131 2131 N -> D (in Ref. 9; AAK54505).
{ECO:0000305}.
CONFLICT 2143 2143 R -> H (in Ref. 9; AAK54505).
{ECO:0000305}.
CONFLICT 2159 2159 K -> E (in Ref. 9; AAK54505).
{ECO:0000305}.
CONFLICT 2182 2182 A -> T (in Ref. 10; BAD96995).
{ECO:0000305}.
HELIX 1010 1012 {ECO:0000244|PDB:1RYU}.
STRAND 1014 1016 {ECO:0000244|PDB:1RYU}.
HELIX 1018 1033 {ECO:0000244|PDB:1RYU}.
STRAND 1045 1048 {ECO:0000244|PDB:1RYU}.
HELIX 1051 1061 {ECO:0000244|PDB:1RYU}.
HELIX 1066 1068 {ECO:0000244|PDB:1RYU}.
HELIX 1072 1079 {ECO:0000244|PDB:1RYU}.
HELIX 1087 1099 {ECO:0000244|PDB:1RYU}.
TURN 1100 1107 {ECO:0000244|PDB:1RYU}.
TURN 1109 1111 {ECO:0000244|PDB:1RYU}.
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


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