ARI1A_HUMAN
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 03-AUG-2022, entry version 214.
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; Q14526: HIC1; NbExp=2; IntAct=EBI-637887, EBI-2507362;
CC O14497; P51531: SMARCA2; NbExp=3; IntAct=EBI-637887, EBI-679562;
CC O14497; P51532: SMARCA4; NbExp=23; IntAct=EBI-637887, EBI-302489;
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 ---------------------------------------------------------------------------
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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 SMR; O14497; -.
DR BioGRID; 113894; 161.
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; 81.
DR MINT; O14497; -.
DR STRING; 9606.ENSP00000320485; -.
DR GlyGen; O14497; 19 sites, 2 O-linked glycans (19 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; O14497; -.
DR PeptideAtlas; O14497; -.
DR PRIDE; O14497; -.
DR ProteomicsDB; 48041; -. [O14497-1]
DR ProteomicsDB; 48042; -. [O14497-2]
DR ProteomicsDB; 48043; -. [O14497-3]
DR Antibodypedia; 1691; 238 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 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; 256110at2759; -.
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; 166 hits in 1128 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 205 other tissues.
DR ExpressionAtlas; O14497; baseline and differential.
DR Genevisible; O14497; HS.
DR GO; GO:0140092; C:bBAF complex; IC:ComplexPortal.
DR GO; GO:0035060; C:brahma complex; IC: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:0045815; P:epigenetic maintenance of chromatin in transcription-competent conformation; TAS:UniProtKB.
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; IC:ComplexPortal.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IC:ComplexPortal.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0045582; P:positive regulation of T cell differentiation; IC:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0070316; P:regulation of G0 to G1 transition; IC:ComplexPortal.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IC:ComplexPortal.
DR GO; GO:2000819; P:regulation of nucleotide-excision repair; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.150.60; -; 1.
DR Gene3D; 1.25.10.10; -; 1.
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 InterPro; IPR030094; BAF250a.
DR PANTHER; PTHR12656; PTHR12656; 1.
DR PANTHER; PTHR12656:SF12; PTHR12656:SF12; 1.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF12031; BAF250_C; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SUPFAM; SSF46774; SSF46774; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51011; ARID; 1.
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
