ARI1B_HUMAN
ID ARI1B_HUMAN Reviewed; 2319 AA.
AC Q8NFD5; Q5JRD1; Q5VYC4; Q8IZY8; Q8TEV0; Q8TF02; Q99491; Q9ULI5;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 3.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=AT-rich interactive domain-containing protein 1B {ECO:0000305};
DE Short=ARID domain-containing protein 1B;
DE AltName: Full=BRG1-associated factor 250b;
DE Short=BAF250B;
DE AltName: Full=BRG1-binding protein hELD/OSA1;
DE AltName: Full=Osa homolog 2;
DE Short=hOsa2;
DE AltName: Full=p250R;
GN Name=ARID1B {ECO:0000312|HGNC:HGNC:18040};
GN Synonyms=BAF250B, DAN15, KIAA1235, OSA2;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-597 (ISOFORM 5).
RX PubMed=9804814; DOI=10.1074/jbc.273.46.30466;
RA Mangel L., Ternes T., Schmitz B., Doerfler W.;
RT "New 5'-(CGG)-3' repeats in the human genome.";
RL J. Biol. Chem. 273:30466-30471(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 92-281.
RX PubMed=8896557; DOI=10.1038/ng1196-285;
RA Imbert G., Saudou F., Yvert G., Devys D., Trottier Y., Garnier J.-M.,
RA Weber C., Mandel J.-L., Cancel G., Abbas N., Duerr A., Didierjean O.,
RA Stevanin G., Agid Y., Brice A.;
RT "Cloning of the gene for spinocerebellar ataxia 2 reveals a locus with high
RT sensitivity to expanded CAG/glutamine repeats.";
RL Nat. Genet. 14:285-291(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 155-2319 (ISOFORM 5), TISSUE SPECIFICITY,
RP INTERACTION WITH SMARCA2 AND SMARCA4, AND IDENTIFICATION IN A SWI/SNF-LIKE
RP COMPLEX WITH ARID1A.
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 353-2319 (ISOFORM 5), TISSUE SPECIFICITY,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN A SWI/SNF-LIKE
RP EBAFB COMPLEX.
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 574-2319 (ISOFORM 2), SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, INTERACTION WITH SMARCA4, IDENTIFICATION IN A COMPLEX
RP WITH SMARCA4 AND SMARCD1, AND IDENTIFICATION IN A SWI/SNF-LIKE COMPLEX WITH
RP 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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 788-2319 (ISOFORM 5), AND IDENTIFICATION IN
RP SWI/SNF COMPLEXES.
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 888-2319 (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-599; SER-1638 AND SER-1642,
RP AND IDENTIFICATION BY MASS 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM 1), CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [11]
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1860, AND IDENTIFICATION BY MASS
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1638 AND SER-1642, AND
RP IDENTIFICATION BY 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1638 AND SER-1798, AND
RP 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 [15]
RP INVOLVEMENT IN CSS1, AND VARIANTS ALA-94 INS; 128-ALA--ALA-130 DEL;
RP HIS-165; SER-329; 401-GLY-GLY-402 DEL; GLY-402 DEL; 410-GLY-GLY-411 DEL;
RP 416-GLY--GLY-420 DEL; VAL-446; ALA-479; VAL-512; PRO-533 INS; ASN-580;
RP THR-614; GLU-959; LEU-1063; ILE-1175; PRO-1332; GLU-1354; ARG-1386;
RP ASN-1404; SER-1494; LYS-1549; HIS-1589; MET-1656; SER-1742; GLU-1816 DEL;
RP ARG-1856; ASN-1934; ARG-1981; ARG-2037 AND ARG-2246.
RX PubMed=22405089; DOI=10.1016/j.ajhg.2012.02.007;
RA Hoyer J., Ekici A.B., Endele S., Popp B., Zweier C., Wiesener A.,
RA Wohlleber E., Dufke A., Rossier E., Petsch C., Zweier M., Gohring I.,
RA Zink A.M., Rappold G., Schrock E., Wieczorek D., Riess O., Engels H.,
RA Rauch A., Reis A.;
RT "Haploinsufficiency of ARID1B, a member of the SWI/SNF-a chromatin-
RT remodeling complex, is a frequent cause of intellectual disability.";
RL Am. J. Hum. Genet. 90:565-572(2012).
RN [16]
RP INVOLVEMENT IN CSS1.
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 [17]
RP INVOLVEMENT IN CSS1.
RX PubMed=22426309; DOI=10.1038/ng.2217;
RA Santen G.W., Aten E., Sun Y., Almomani R., Gilissen C., Nielsen M.,
RA Kant S.G., Snoeck I.N., Peeters E.A., Hilhorst-Hofstee Y., Wessels M.W.,
RA den Hollander N.S., Ruivenkamp C.A., van Ommen G.J., Breuning M.H.,
RA den Dunnen J.T., van Haeringen A., Kriek M.;
RT "Mutations in SWI/SNF chromatin remodeling complex gene ARID1B cause
RT Coffin-Siris syndrome.";
RL Nat. Genet. 44:379-380(2012).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-585; SER-599; SER-1625;
RP SER-1638 AND SER-1642, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [19]
RP 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 [20]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-640, AND IDENTIFICATION BY MASS
RP 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 [21]
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 [22]
RP DNA-BINDING, IDENTIFICATION IN SWI/SNF COMPLEXES, AND INTERACTION WITH
RP SMARCA2; SMARCA4 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 [23]
RP DNA-BINDING.
RX PubMed=14982958; DOI=10.1093/nar/gkh277;
RA Wilsker D., Patsialou A., Zumbrun S.D., Kim S., Chen Y., Dallas P.B.,
RA Moran E.;
RT "The DNA-binding properties of the ARID-containing subunits of yeast and
RT mammalian SWI/SNF complexes.";
RL Nucleic Acids Res. 32:1345-1353(2004).
RN [24]
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 [25]
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 [26]
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 [27]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1124-1242.
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of the HBAF250B AT-rich interaction domain (ARID).";
RL Submitted (OCT-2006) to the PDB data bank.
RN [28]
RP VARIANT [LARGE SCALE ANALYSIS] ALA-897.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [29]
RP VARIANTS LEU-854; ALA-1519; LEU-1646 AND TYR-2070.
RX PubMed=26376624; DOI=10.1186/s12864-015-1898-1;
RA Yu Y., Yao R., Wang L., Fan Y., Huang X., Hirschhorn J., Dauber A.,
RA Shen Y.;
RT "De novo mutations in ARID1B associated with both syndromic and non-
RT syndromic short stature.";
RL BMC Genomics 16:701-701(2015).
RN [30]
RP VARIANTS ARG-571 AND SER-1496.
RX PubMed=26637798; DOI=10.1016/j.neuron.2015.11.009;
RA D'Gama A.M., Pochareddy S., Li M., Jamuar S.S., Reiff R.E., Lam A.T.,
RA Sestan N., Walsh C.A.;
RT "Targeted DNA Sequencing from Autism Spectrum Disorder Brains Implicates
RT Multiple Genetic Mechanisms.";
RL Neuron 88:910-917(2015).
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. Belongs to the neural progenitors-specific chromatin remodeling
CC complex (npBAF complex) and the neuron-specific chromatin remodeling
CC complex (nBAF complex). During neural development a switch from a
CC stem/progenitor to a postmitotic chromatin remodeling mechanism occurs
CC as neurons exit the cell cycle and become committed to their adult
CC state. The transition from proliferating neural stem/progenitor cells
CC to postmitotic neurons requires a switch in subunit composition of the
CC npBAF and nBAF complexes. As neural progenitors exit mitosis and
CC differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A
CC and PHF10/BAF45A, are exchanged for homologous alternative
CC ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-
CC specific complexes (nBAF). The npBAF complex is essential for the self-
CC renewal/proliferative capacity of the multipotent neural stem cells.
CC The nBAF complex along with CREST plays a role regulating the activity
CC of genes essential for dendrite growth (By similarity). Binds DNA non-
CC specifically (PubMed:14982958, PubMed:15170388).
CC {ECO:0000250|UniProtKB:E9Q4N7, ECO:0000269|PubMed:14982958,
CC ECO:0000269|PubMed:15170388, ECO:0000303|PubMed:12672490,
CC ECO:0000303|PubMed:22952240, 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
CC (PubMed:12672490, PubMed:22952240, PubMed:26601204, PubMed:12200431,
CC PubMed:11988099, PubMed:15170388). The canonical complex contains a
CC catalytic subunit (either SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B)
CC and at least SMARCE1, ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and
CC SMARCB1/SNF5/BAF47. Other subunits specific to each of the complexes
CC may also be present permitting several possible combinations
CC developmentally and tissue specific (PubMed:11734557, PubMed:22952240,
CC PubMed:26601204). Component of the BAF (SWI/SNF-A) complex, which
CC includes at least actin (ACTB), ARID1A/BAF250A, ARID1B/BAF250B,
CC SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B,
CC SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and
CC one or more SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C
CC (PubMed:18765789). In muscle cells, the BAF complex also contains DPF3.
CC Component of neural progenitors-specific chromatin remodeling complex
CC (npBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B,
CC 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 EBAFb complex, at least composed of
CC SMARCA4/BRG1/BAF190A, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A, SMARCE1/BAF57,
CC SMARCD1/BAF60A, SMARCD2/BAF60B, SMARCC1/BAF155, SMARCC2/BAF170,
CC ARID1B/BAF250B, MLLT1/ENL and actin (PubMed:12665591). Interacts
CC through its C-terminus with SMARCA2/BRM/BAF190B and
CC SMARCA4/BRG1/BAF190A (PubMed:12200431, PubMed:11988099,
CC PubMed:15170388). Interacts with SMARCC1/BAF155 (PubMed:15170388).
CC {ECO:0000250|UniProtKB:E9Q4N7, ECO:0000269|PubMed:11988099,
CC ECO:0000269|PubMed:12200431, ECO:0000269|PubMed:12665591,
CC ECO:0000269|PubMed:15170388, ECO:0000269|PubMed:18765789,
CC ECO:0000303|PubMed:12672490, ECO:0000303|PubMed:22952240,
CC ECO:0000303|PubMed:26601204}.
CC -!- INTERACTION:
CC Q8NFD5; P51531: SMARCA2; NbExp=3; IntAct=EBI-679921, EBI-679562;
CC Q8NFD5; P51532: SMARCA4; NbExp=3; IntAct=EBI-679921, EBI-302489;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355,
CC ECO:0000269|PubMed:11988099}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=4;
CC Name=5;
CC IsoId=Q8NFD5-5; Sequence=Displayed;
CC Name=1;
CC IsoId=Q8NFD5-1; Sequence=VSP_061510;
CC Name=2;
CC IsoId=Q8NFD5-2; Sequence=VSP_061511;
CC Name=3;
CC IsoId=Q8NFD5-3; Sequence=VSP_061512;
CC -!- TISSUE SPECIFICITY: Widely expressed with high levels in heart,
CC skeletal muscle and kidney. {ECO:0000269|PubMed:11988099,
CC ECO:0000269|PubMed:12200431, ECO:0000269|PubMed:12665591}.
CC -!- POLYMORPHISM: The poly-Gln region is polymorphic and the number of Gln
CC varies in the population (from 17 to 23).
CC -!- DISEASE: Coffin-Siris syndrome 1 (CSS1) [MIM:135900]: 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:22405089,
CC ECO:0000269|PubMed:22426308, ECO:0000269|PubMed:22426309}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: [Isoform 1]: Produced by alternative initiation at Met-
CC 84 of isoform 5. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG36928.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAL76077.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAN03447.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAN70985.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAN70985.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA69592.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
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DR EMBL; AL049820; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL162578; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355297; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591545; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJ001216; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Y08266; CAA69592.1; ALT_FRAME; mRNA.
DR EMBL; AF521671; AAN03447.1; ALT_FRAME; mRNA.
DR EMBL; AF253515; AAN70985.1; ALT_SEQ; mRNA.
DR EMBL; AF468300; AAL76077.1; ALT_INIT; mRNA.
DR EMBL; AF259792; AAG36928.1; ALT_INIT; mRNA.
DR EMBL; AB033061; BAA86549.1; -; mRNA.
DR RefSeq; NP_001333742.1; NM_001346813.1.
DR RefSeq; NP_059989.2; NM_017519.2.
DR RefSeq; NP_065783.3; NM_020732.3.
DR PDB; 2CXY; X-ray; 1.60 A; A=1124-1242.
DR PDB; 2EH9; X-ray; 2.00 A; A=1124-1242.
DR PDBsum; 2CXY; -.
DR PDBsum; 2EH9; -.
DR AlphaFoldDB; Q8NFD5; -.
DR SMR; Q8NFD5; -.
DR BioGRID; 121559; 134.
DR ComplexPortal; CPX-1205; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1206; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1210; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1211; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1213; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1215; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1217; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1218; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1220; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1221; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1223; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1224; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1227; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1228; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant.
DR CORUM; Q8NFD5; -.
DR IntAct; Q8NFD5; 90.
DR MINT; Q8NFD5; -.
DR STRING; 9606.ENSP00000344546; -.
DR GlyGen; Q8NFD5; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q8NFD5; -.
DR PhosphoSitePlus; Q8NFD5; -.
DR BioMuta; ARID1B; -.
DR DMDM; 73921720; -.
DR EPD; Q8NFD5; -.
DR jPOST; Q8NFD5; -.
DR MassIVE; Q8NFD5; -.
DR MaxQB; Q8NFD5; -.
DR PaxDb; Q8NFD5; -.
DR PeptideAtlas; Q8NFD5; -.
DR PRIDE; Q8NFD5; -.
DR ProteomicsDB; 73289; -. [Q8NFD5-1]
DR ProteomicsDB; 73290; -. [Q8NFD5-2]
DR ProteomicsDB; 73291; -. [Q8NFD5-3]
DR Antibodypedia; 19980; 171 antibodies from 27 providers.
DR DNASU; 57492; -.
DR Ensembl; ENST00000346085.10; ENSP00000344546.5; ENSG00000049618.24. [Q8NFD5-2]
DR Ensembl; ENST00000350026.10; ENSP00000055163.7; ENSG00000049618.24. [Q8NFD5-1]
DR Ensembl; ENST00000636930.2; ENSP00000490491.2; ENSG00000049618.24. [Q8NFD5-3]
DR GeneID; 57492; -.
DR KEGG; hsa:57492; -.
DR MANE-Select; ENST00000636930.2; ENSP00000490491.2; NM_001374828.1; NP_001361757.1. [Q8NFD5-3]
DR UCSC; uc003qqo.4; human. [Q8NFD5-5]
DR CTD; 57492; -.
DR DisGeNET; 57492; -.
DR GeneCards; ARID1B; -.
DR GeneReviews; ARID1B; -.
DR HGNC; HGNC:18040; ARID1B.
DR HPA; ENSG00000049618; Low tissue specificity.
DR MalaCards; ARID1B; -.
DR MIM; 135900; phenotype.
DR MIM; 614556; gene.
DR neXtProt; NX_Q8NFD5; -.
DR OpenTargets; ENSG00000049618; -.
DR Orphanet; 251056; 6q25 microdeletion syndrome.
DR Orphanet; 1465; Coffin-Siris syndrome.
DR PharmGKB; PA134909463; -.
DR VEuPathDB; HostDB:ENSG00000049618; -.
DR eggNOG; KOG2510; Eukaryota.
DR GeneTree; ENSGT00940000155634; -.
DR InParanoid; Q8NFD5; -.
DR OrthoDB; 256110at2759; -.
DR PhylomeDB; Q8NFD5; -.
DR TreeFam; TF320364; -.
DR PathwayCommons; Q8NFD5; -.
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; Q8NFD5; -.
DR SIGNOR; Q8NFD5; -.
DR BioGRID-ORCS; 57492; 38 hits in 1109 CRISPR screens.
DR ChiTaRS; ARID1B; human.
DR EvolutionaryTrace; Q8NFD5; -.
DR GeneWiki; ARID1B; -.
DR GenomeRNAi; 57492; -.
DR Pharos; Q8NFD5; Tbio.
DR PRO; PR:Q8NFD5; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q8NFD5; protein.
DR Bgee; ENSG00000049618; Expressed in bone marrow cell and 202 other tissues.
DR ExpressionAtlas; Q8NFD5; baseline and differential.
DR Genevisible; Q8NFD5; 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; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0071565; C:nBAF complex; IBA:GO_Central.
DR GO; GO:0071564; C:npBAF complex; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0016514; C:SWI/SNF complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:GDB.
DR GO; GO:0003713; F:transcription coactivator activity; NAS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IC:ComplexPortal.
DR GO; GO:0045815; P:epigenetic maintenance of chromatin in transcription-competent conformation; NAS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
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:0045582; P:positive regulation of T cell differentiation; IC:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
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 InterPro; IPR038040; ARID1B.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR021906; BAF250/Osa.
DR InterPro; IPR033388; BAF250_C.
DR PANTHER; PTHR12656; PTHR12656; 2.
DR PANTHER; PTHR12656:SF11; PTHR12656:SF11; 2.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF12031; BAF250_C; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SUPFAM; SSF46774; SSF46774; 1.
DR PROSITE; PS51011; ARID; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative initiation; Alternative splicing;
KW Chromatin regulator; DNA-binding; Intellectual disability; Methylation;
KW Neurogenesis; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Triplet repeat expansion.
FT CHAIN 1..2319
FT /note="AT-rich interactive domain-containing protein 1B"
FT /id="PRO_0000200576"
FT DOMAIN 1136..1227
FT /note="ARID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..1062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1085..1129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1230..1334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1346..1443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1475..1647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1782..1852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1904..1941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1954..1973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 502..506
FT /note="LXXLL"
FT MOTIF 1441..1460
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:O14497"
FT MOTIF 2119..2123
FT /note="LXXLL"
FT COMPBIAS 165..188
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..828
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..854
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..887
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..957
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..996
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1022..1062
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1112..1128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1242..1274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1290..1332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1363..1397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1519..1534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1577..1605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1614..1645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1796..1825
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1925..1941
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 487
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:E9Q4N7"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 599
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 608
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:E9Q4N7"
FT MOD_RES 640
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1625
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1638
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1642
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1798
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1860
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..83
FT /note="Missing (in isoform 1)"
FT /id="VSP_061510"
FT VAR_SEQ 662
FT /note="Q -> QDSGDATWKETFWL (in isoform 2)"
FT /id="VSP_061511"
FT VAR_SEQ 1115
FT /note="K -> KDSYSSQGISQPPTPGNLPVPSPMSPSSASISSFHGDESDSISSPGW
FT PKTPSSP (in isoform 3)"
FT /id="VSP_061512"
FT VARIANT 94
FT /note="A -> AA"
FT /evidence="ECO:0000269|PubMed:22405089"
FT /id="VAR_067662"
FT VARIANT 128..130
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:22405089"
FT /id="VAR_067663"
FT VARIANT 165
FT /note="Q -> H"
FT /evidence="ECO:0000269|PubMed:22405089"
FT /id="VAR_067664"
FT VARIANT 329
FT /note="G -> S (in dbSNP:rs375160616)"
FT /evidence="ECO:0000269|PubMed:22405089"
FT /id="VAR_067665"
FT VARIANT 401..402
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:22405089"
FT /id="VAR_067666"
FT VARIANT 402
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:22405089"
FT /id="VAR_067667"
FT VARIANT 410..411
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:22405089"
FT /id="VAR_067668"
FT VARIANT 416..420
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:22405089"
FT /id="VAR_067669"
FT VARIANT 446
FT /note="A -> V (in dbSNP:rs748273011)"
FT /evidence="ECO:0000269|PubMed:22405089"
FT /id="VAR_067670"
FT VARIANT 479
FT /note="G -> A (in dbSNP:rs760718156)"
FT /evidence="ECO:0000269|PubMed:22405089"
FT /id="VAR_067671"
FT VARIANT 512
FT /note="M -> V (in dbSNP:rs199948752)"
FT /evidence="ECO:0000269|PubMed:22405089"
FT /id="VAR_067672"
FT VARIANT 533
FT /note="P -> PP"
FT /evidence="ECO:0000269|PubMed:22405089"
FT /id="VAR_067673"
FT VARIANT 571
FT /note="P -> R (found in a patient with autism; unknown
FT pathological significance; dbSNP:rs769085274)"
FT /evidence="ECO:0000269|PubMed:26637798"
FT /id="VAR_078697"
FT VARIANT 580
FT /note="S -> N (in dbSNP:rs764716697)"
FT /evidence="ECO:0000269|PubMed:22405089"
FT /id="VAR_067674"
FT VARIANT 614
FT /note="M -> T (in dbSNP:rs141260832)"
FT /evidence="ECO:0000269|PubMed:22405089"
FT /id="VAR_067675"
FT VARIANT 854
FT /note="S -> L (found in a patient with short stature;
FT unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:26376624"
FT /id="VAR_077456"
FT VARIANT 897
FT /note="G -> A (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036257"
FT VARIANT 959
FT /note="Q -> E (in dbSNP:rs138254872)"
FT /evidence="ECO:0000269|PubMed:22405089"
FT /id="VAR_067676"
FT VARIANT 1063
FT /note="Q -> L (in dbSNP:rs139620600)"
FT /evidence="ECO:0000269|PubMed:22405089"
FT /id="VAR_067677"
FT VARIANT 1175
FT /note="V -> I (in dbSNP:rs775526039)"
FT /evidence="ECO:0000269|PubMed:22405089"
FT /id="VAR_067678"
FT VARIANT 1332
FT /note="Q -> P (in dbSNP:rs768013849)"
FT /evidence="ECO:0000269|PubMed:22405089"
FT /id="VAR_067679"
FT VARIANT 1354
FT /note="G -> E (in dbSNP:rs149389876)"
FT /evidence="ECO:0000269|PubMed:22405089"
FT /id="VAR_067680"
FT VARIANT 1386
FT /note="G -> R (in dbSNP:rs199674889)"
FT /evidence="ECO:0000269|PubMed:22405089"
FT /id="VAR_067681"
FT VARIANT 1404
FT /note="S -> N (in dbSNP:rs142808724)"
FT /evidence="ECO:0000269|PubMed:22405089"
FT /id="VAR_067682"
FT VARIANT 1494
FT /note="P -> S"
FT /evidence="ECO:0000269|PubMed:22405089"
FT /id="VAR_067683"
FT VARIANT 1496
FT /note="P -> S (found in a patient with autism; unknown
FT pathological significance; dbSNP:rs1051017338)"
FT /evidence="ECO:0000269|PubMed:26637798"
FT /id="VAR_078698"
FT VARIANT 1519
FT /note="G -> A (probable disease-associated variant found in
FT a patient with short stature; de novo mutation)"
FT /evidence="ECO:0000269|PubMed:26376624"
FT /id="VAR_077457"
FT VARIANT 1549
FT /note="Q -> K"
FT /evidence="ECO:0000269|PubMed:22405089"
FT /id="VAR_067684"
FT VARIANT 1589
FT /note="R -> H (in dbSNP:rs1449208173)"
FT /evidence="ECO:0000269|PubMed:22405089"
FT /id="VAR_067685"
FT VARIANT 1646
FT /note="P -> L (found in a patient with short stature;
FT unknown pathological significance; dbSNP:rs1455506883)"
FT /evidence="ECO:0000269|PubMed:26376624"
FT /id="VAR_077458"
FT VARIANT 1656
FT /note="T -> M (in dbSNP:rs777745107)"
FT /evidence="ECO:0000269|PubMed:22405089"
FT /id="VAR_067686"
FT VARIANT 1742
FT /note="N -> S (in dbSNP:rs140177120)"
FT /evidence="ECO:0000269|PubMed:22405089"
FT /id="VAR_067687"
FT VARIANT 1816
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:22405089"
FT /id="VAR_067688"
FT VARIANT 1856
FT /note="K -> R (in dbSNP:rs574141489)"
FT /evidence="ECO:0000269|PubMed:22405089"
FT /id="VAR_067689"
FT VARIANT 1934
FT /note="D -> N (in dbSNP:rs200305796)"
FT /evidence="ECO:0000269|PubMed:22405089"
FT /id="VAR_067690"
FT VARIANT 1981
FT /note="K -> R (in dbSNP:rs758204258)"
FT /evidence="ECO:0000269|PubMed:22405089"
FT /id="VAR_067691"
FT VARIANT 2037
FT /note="K -> R (in dbSNP:rs756220726)"
FT /evidence="ECO:0000269|PubMed:22405089"
FT /id="VAR_067692"
FT VARIANT 2070
FT /note="D -> Y (probable disease-associated variant found in
FT a patient with short stature; de novo mutation)"
FT /evidence="ECO:0000269|PubMed:26376624"
FT /id="VAR_077459"
FT VARIANT 2246
FT /note="Q -> R"
FT /evidence="ECO:0000269|PubMed:22405089"
FT /id="VAR_067693"
FT CONFLICT 353
FT /note="S -> N (in Ref. 5; AAN70985)"
FT /evidence="ECO:0000305"
FT CONFLICT 417..419
FT /note="AGA -> SRS (in Ref. 4; AAN03447)"
FT /evidence="ECO:0000305"
FT CONFLICT 529
FT /note="P -> A (in Ref. 5; AAN70985)"
FT /evidence="ECO:0000305"
FT CONFLICT 770
FT /note="V -> A (in Ref. 6; AAL76077)"
FT /evidence="ECO:0000305"
FT CONFLICT 987
FT /note="T -> P (in Ref. 6; AAL76077)"
FT /evidence="ECO:0000305"
FT CONFLICT 1284
FT /note="T -> I (in Ref. 7; AAG36928)"
FT /evidence="ECO:0000305"
FT CONFLICT 1422
FT /note="P -> S (in Ref. 5; AAN70985)"
FT /evidence="ECO:0000305"
FT CONFLICT 1515
FT /note="P -> L (in Ref. 8; BAA86549)"
FT /evidence="ECO:0000305"
FT CONFLICT 1617
FT /note="P -> S (in Ref. 5; AAN70985)"
FT /evidence="ECO:0000305"
FT CONFLICT 1796
FT /note="D -> N (in Ref. 6; AAL76077)"
FT /evidence="ECO:0000305"
FT CONFLICT 2279
FT /note="D -> N (in Ref. 7; AAG36928)"
FT /evidence="ECO:0000305"
FT HELIX 1046..1049
FT /evidence="ECO:0007829|PDB:2CXY"
FT HELIX 1056..1070
FT /evidence="ECO:0007829|PDB:2CXY"
FT HELIX 1087..1097
FT /evidence="ECO:0007829|PDB:2CXY"
FT HELIX 1100..1106
FT /evidence="ECO:0007829|PDB:2CXY"
FT HELIX 1109..1115
FT /evidence="ECO:0007829|PDB:2CXY"
FT HELIX 1122..1135
FT /evidence="ECO:0007829|PDB:2CXY"
FT HELIX 1137..1145
FT /evidence="ECO:0007829|PDB:2CXY"
FT INIT_MET Q8NFD5-1:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES Q8NFD5-1:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
SQ SEQUENCE 2319 AA; 243943 MW; 0267747AF33071BF CRC64;
MAARAAAAAA AAAARARARA GSGERRAPPG PRPAPGARDL EAGARGAAAA AAAPGPMLGG
GGDGGGGLNS VHHHPLLPRH ELNMAHNAGA AAAAGTHSAK SGGSEAALKE GGSAAALSSS
SSSSAAAAAA SSSSSSGPGS AMETGLLPNH KLKTVGEAPA APPHQQHHHH HHAHHHHHHA
HHLHHHHALQ QQLNQFQQQQ QQQQQQQQQQ QQQQHPISNN NSLGGAGGGA PQPGPDMEQP
QHGGAKDSAA GGQADPPGPP LLSKPGDEDD APPKMGEPAG GRYEHPGLGA LGTQQPPVAV
PGGGGGPAAV PEFNNYYGSA APASGGPGGR AGPCFDQHGG QQSPGMGMMH SASAAAAGAP
GSMDPLQNSH EGYPNSQCNH YPGYSRPGAG GGGGGGGGGG GGSGGGGGGG GAGAGGAGAG
AVAAAAAAAA AAAGGGGGGG YGGSSAGYGV LSSPRQQGGG MMMGPGGGGA ASLSKAAAGS
AAGGFQRFAG QNQHPSGATP TLNQLLTSPS PMMRSYGGSY PEYSSPSAPP PPPSQPQSQA
AAAGAAAGGQ QAAAGMGLGK DMGAQYAAAS PAWAAAQQRS HPAMSPGTPG PTMGRSQGSP
MDPMVMKRPQ LYGMGSNPHS QPQQSSPYPG GSYGPPGPQR YPIGIQGRTP GAMAGMQYPQ
QQMPPQYGQQ GVSGYCQQGQ QPYYSQQPQP PHLPPQAQYL PSQSQQRYQP QQDMSQEGYG
TRSQPPLAPG KPNHEDLNLI QQERPSSLPD LSGSIDDLPT GTEATLSSAV SASGSTSSQG
DQSNPAQSPF SPHASPHLSS IPGGPSPSPV GSPVGSNQSR SGPISPASIP GSQMPPQPPG
SQSESSSHPA LSQSPMPQER GFMAGTQRNP QMAQYGPQQT GPSMSPHPSP GGQMHAGISS
FQQSNSSGTY GPQMSQYGPQ GNYSRPPAYS GVPSASYSGP GPGMGISANN QMHGQGPSQP
CGAVPLGRMP SAGMQNRPFP GNMSSMTPSS PGMSQQGGPG MGPPMPTVNR KAQEAAAAVM
QAAANSAQSR QGSFPGMNQS GLMASSSPYS QPMNNSSSLM NTQAPPYSMA PAMVNSSAAS
VGLADMMSPG ESKLPLPLKA DGKEEGTPQP ESKSKKSSSS TTTGEKITKV YELGNEPERK
LWVDRYLTFM EERGSPVSSL PAVGKKPLDL FRLYVCVKEI GGLAQVNKNK KWRELATNLN
VGTSSSAASS LKKQYIQYLF AFECKIERGE EPPPEVFSTG DTKKQPKLQP PSPANSGSLQ
GPQTPQSTGS NSMAEVPGDL KPPTPASTPH GQMTPMQGGR SSTISVHDPF SDVSDSSFPK
RNSMTPNAPY QQGMSMPDVM GRMPYEPNKD PFGGMRKVPG SSEPFMTQGQ MPNSSMQDMY
NQSPSGAMSN LGMGQRQQFP YGASYDRRHE PYGQQYPGQG PPSGQPPYGG HQPGLYPQQP
NYKRHMDGMY GPPAKRHEGD MYNMQYSSQQ QEMYNQYGGS YSGPDRRPIQ GQYPYPYSRE
RMQGPGQIQT HGIPPQMMGG PLQSSSSEGP QQNMWAARND MPYPYQNRQG PGGPTQAPPY
PGMNRTDDMM VPDQRINHES QWPSHVSQRQ PYMSSSASMQ PITRPPQPSY QTPPSLPNHI
SRAPSPASFQ RSLENRMSPS KSPFLPSMKM QKVMPTVPTS QVTGPPPQPP PIRREITFPP
GSVEASQPVL KQRRKITSKD IVTPEAWRVM MSLKSGLLAE STWALDTINI LLYDDSTVAT
FNLSQLSGFL ELLVEYFRKC LIDIFGILME YEVGDPSQKA LDHNAARKDD SQSLADDSGK
EEEDAECIDD DEEDEEDEEE DSEKTESDEK SSIALTAPDA AADPKEKPKQ ASKFDKLPIK
IVKKNNLFVV DRSDKLGRVQ EFNSGLLHWQ LGGGDTTEHI QTHFESKMEI PPRRRPPPPL
SSAGRKKEQE GKGDSEEQQE KSIIATIDDV LSARPGALPE DANPGPQTES SKFPFGIQQA
KSHRNIKLLE DEPRSRDETP LCTIAHWQDS LAKRCICVSN IVRSLSFVPG NDAEMSKHPG
LVLILGKLIL LHHEHPERKR APQTYEKEED EDKGVACSKD EWWWDCLEVL RDNTLVTLAN
ISGQLDLSAY TESICLPILD GLLHWMVCPS AEAQDPFPTV GPNSVLSPQR LVLETLCKLS
IQDNNVDLIL ATPPFSRQEK FYATLVRYVG DRKNPVCREM SMALLSNLAQ GDALAARAIA
VQKGSIGNLI SFLEDGVTMA QYQQSQHNLM HMQPPPLEPP SVDMMCRAAK ALLAMARVDE
NRSEFLLHEG RLLDISISAV LNSLVASVIC DVLFQIGQL
