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AT-rich interactive domain-containing protein 1B (ARID domain-containing protein 1B) (BRG1-associated factor 250b) (BAF250B) (BRG1-binding protein hELD/OSA1) (Osa homolog 2) (hOsa2) (p250R)

 ARI1B_HUMAN             Reviewed;        2236 AA.
Q8NFD5; Q5JRD1; Q5VYC4; Q8IZY8; Q8TEV0; Q8TF02; Q99491; Q9ULI5;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
30-AUG-2005, sequence version 2.
25-APR-2018, entry version 159.
RecName: Full=AT-rich interactive domain-containing protein 1B;
Short=ARID domain-containing protein 1B;
AltName: Full=BRG1-associated factor 250b;
Short=BAF250B;
AltName: Full=BRG1-binding protein hELD/OSA1;
AltName: Full=Osa homolog 2;
Short=hOsa2;
AltName: Full=p250R;
Name=ARID1B; Synonyms=BAF250B, DAN15, KIAA1235, OSA2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND IDENTIFICATION IN SWI/SNF
COMPLEXES.
TISSUE=Brain;
PubMed=11734557; DOI=10.1074/jbc.M108702200;
Kato H., Tjernberg A., Zhang W., Krutchinsky A.N., An W., Takeuchi T.,
Ohtsuki Y., Sugano S., de Bruijn D.R., Chait B.T., Roeder R.G.;
"SYT associates with human SNF/SWI complexes and the C-terminal region
of its fusion partner SSX1 targets histones.";
J. Biol. Chem. 277:5498-5505(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-515.
PubMed=9804814; DOI=10.1074/jbc.273.46.30466;
Mangel L., Ternes T., Schmitz B., Doerfler W.;
"New 5'-(CGG)-3' repeats in the human genome.";
J. Biol. Chem. 273:30466-30471(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 9-199.
PubMed=8896557; DOI=10.1038/ng1196-285;
Imbert G., Saudou F., Yvert G., Devys D., Trottier Y., Garnier J.-M.,
Weber C., Mandel J.-L., Cancel G., Abbas N., Duerr A., Didierjean O.,
Stevanin G., Agid Y., Brice A.;
"Cloning of the gene for spinocerebellar ataxia 2 reveals a locus with
high sensitivity to expanded CAG/glutamine repeats.";
Nat. Genet. 14:285-291(1996).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 72-2236 (ISOFORM 1), TISSUE SPECIFICITY,
INTERACTION WITH SMARCA2 AND SMARCA4, AND IDENTIFICATION IN A
SWI/SNF-LIKE COMPLEX WITH ARID1A.
PubMed=12200431; DOI=10.1074/jbc.M205961200;
Inoue H., Furukawa T., Giannakopoulos S., Zhou S., King D.S.,
Tanese N.;
"Largest subunits of the human SWI/SNF chromatin-remodeling complex
promote transcriptional activation by steroid hormone receptors.";
J. Biol. Chem. 277:41674-41685(2002).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 272-2236 (ISOFORM 1), TISSUE
SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION
IN A SWI/SNF-LIKE EBAFB COMPLEX.
PubMed=12665591; DOI=10.1128/MCB.23.8.2942-2952.2003;
Nie Z., Yan Z., Chen E.H., Sechi S., Ling C., Zhou S., Xue Y.,
Yang D., Murray D., Kanakubo E., Cleary M.L., Wang W.;
"Novel SWI/SNF chromatin-remodeling complexes contain a mixed-lineage
leukemia chromosomal translocation partner.";
Mol. Cell. Biol. 23:2942-2952(2003).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 491-2236 (ISOFORM 2), SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, INTERACTION WITH SMARCA4, IDENTIFICATION
IN A COMPLEX WITH SMARCA4 AND SMARCD1, AND IDENTIFICATION IN A
SWI/SNF-LIKE COMPLEX WITH ARID1A.
PubMed=11988099;
Hurlstone A.F., Olave I.A., Barker N., van Noort M., Clevers H.;
"Cloning and characterization of hELD/OSA1, a novel BRG1 interacting
protein.";
Biochem. J. 364:255-264(2002).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 705-2236 (ISOFORM 3).
TISSUE=Brain;
PubMed=10574462; DOI=10.1093/dnares/6.5.337;
Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XV.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:337-345(1999).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-516; SER-1555 AND
SER-1559, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1777, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1555 AND SER-1559, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1555 AND SER-1715, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[15]
INVOLVEMENT IN CSS1, AND VARIANTS ALA-11 INS; 45-ALA--ALA-47 DEL;
HIS-82; SER-246; 318-GLY-GLY-319 DEL; GLY-319 DEL; 327-GLY-GLY-328
DEL; 333-GLY--GLY-337 DEL; VAL-363; ALA-396; VAL-429; PRO-450 INS;
ASN-497; THR-531; GLU-876; LEU-980; ILE-1092; PRO-1249; GLU-1271;
ARG-1303; ASN-1321; SER-1411; LYS-1466; HIS-1506; MET-1573; SER-1659;
GLU-1733 DEL; ARG-1773; ASN-1851; ARG-1898; ARG-1954 AND ARG-2163.
PubMed=22405089; DOI=10.1016/j.ajhg.2012.02.007;
Hoyer J., Ekici A.B., Endele S., Popp B., Zweier C., Wiesener A.,
Wohlleber E., Dufke A., Rossier E., Petsch C., Zweier M., Gohring I.,
Zink A.M., Rappold G., Schrock E., Wieczorek D., Riess O., Engels H.,
Rauch A., Reis A.;
"Haploinsufficiency of ARID1B, a member of the SWI/SNF-a chromatin-
remodeling complex, is a frequent cause of intellectual disability.";
Am. J. Hum. Genet. 90:565-572(2012).
[16]
INVOLVEMENT IN CSS1.
PubMed=22426308; DOI=10.1038/ng.2219;
Tsurusaki Y., Okamoto N., Ohashi H., Kosho T., Imai Y., Hibi-Ko Y.,
Kaname T., Naritomi K., Kawame H., Wakui K., Fukushima Y., Homma T.,
Kato M., Hiraki Y., Yamagata T., Yano S., Mizuno S., Sakazume S.,
Ishii T., Nagai T., Shiina M., Ogata K., Ohta T., Niikawa N.,
Miyatake S., Okada I., Mizuguchi T., Doi H., Saitsu H., Miyake N.,
Matsumoto N.;
"Mutations affecting components of the SWI/SNF complex cause Coffin-
Siris syndrome.";
Nat. Genet. 44:376-378(2012).
[17]
INVOLVEMENT IN CSS1.
PubMed=22426309; DOI=10.1038/ng.2217;
Santen G.W., Aten E., Sun Y., Almomani R., Gilissen C., Nielsen M.,
Kant S.G., Snoeck I.N., Peeters E.A., Hilhorst-Hofstee Y.,
Wessels M.W., den Hollander N.S., Ruivenkamp C.A., van Ommen G.J.,
Breuning M.H., den Dunnen J.T., van Haeringen A., Kriek M.;
"Mutations in SWI/SNF chromatin remodeling complex gene ARID1B cause
Coffin-Siris syndrome.";
Nat. Genet. 44:379-380(2012).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502; SER-516; SER-1542;
SER-1555 AND SER-1559, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[20]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-557, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[21]
REVIEW ON SWI/SNF CHROMATIN REMODELING COMPLEXES.
PubMed=12672490; DOI=10.1016/S0959-437X(03)00022-4;
Martens J.A., Winston F.;
"Recent advances in understanding chromatin remodeling by SWI/SNF
complexes.";
Curr. Opin. Genet. Dev. 13:136-142(2003).
[22]
DNA-BINDING, IDENTIFICATION IN SWI/SNF COMPLEXES, AND INTERACTION WITH
SMARCA2; SMARCA4 AND SMARCC1.
PubMed=15170388; DOI=10.1042/BJ20040524;
Wang X., Nagl N.G., Wilsker D., Van Scoy M., Pacchione S., Yaciuk P.,
Dallas P.B., Moran E.;
"Two related ARID family proteins are alternative subunits of human
SWI/SNF complexes.";
Biochem. J. 383:319-325(2004).
[23]
DNA-BINDING.
PubMed=14982958; DOI=10.1093/nar/gkh277;
Wilsker D., Patsialou A., Zumbrun S.D., Kim S., Chen Y., Dallas P.B.,
Moran E.;
"The DNA-binding properties of the ARID-containing subunits of yeast
and mammalian SWI/SNF complexes.";
Nucleic Acids Res. 32:1345-1353(2004).
[24]
IDENTIFICATION IN THE BAF COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=18765789; DOI=10.1101/gad.471408;
Lange M., Kaynak B., Forster U.B., Toenjes M., Fischer J.J., Grimm C.,
Schlesinger J., Just S., Dunkel I., Krueger T., Mebus S., Lehrach H.,
Lurz R., Gobom J., Rottbauer W., Abdelilah-Seyfried S., Sperling S.;
"Regulation of muscle development by DPF3, a novel histone acetylation
and methylation reader of the BAF chromatin remodeling complex.";
Genes Dev. 22:2370-2384(2008).
[25]
REVIEW ON SWI/SNF CHROMATIN REMODELING COMPLEXES.
PubMed=22952240; DOI=10.1074/jbc.R111.309302;
Euskirchen G., Auerbach R.K., Snyder M.;
"SWI/SNF chromatin-remodeling factors: multiscale analyses and diverse
functions.";
J. Biol. Chem. 287:30897-30905(2012).
[26]
REVIEW ON SWI/SNF CHROMATIN REMODELING COMPLEXES.
PubMed=26601204; DOI=10.1126/sciadv.1500447;
Kadoch C., Crabtree G.R.;
"Mammalian SWI/SNF chromatin remodeling complexes and cancer:
Mechanistic insights gained from human genomics.";
Sci. Adv. 1:E1500447-E1500447(2015).
[27]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1041-1159.
RIKEN structural genomics initiative (RSGI);
"Crystal structure of the HBAF250B AT-rich interaction domain
(ARID).";
Submitted (OCT-2006) to the PDB data bank.
[28]
VARIANT [LARGE SCALE ANALYSIS] ALA-814.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[29]
VARIANTS LEU-771; ALA-1436; LEU-1563 AND TYR-1987.
PubMed=26376624; DOI=10.1186/s12864-015-1898-1;
Yu Y., Yao R., Wang L., Fan Y., Huang X., Hirschhorn J., Dauber A.,
Shen Y.;
"De novo mutations in ARID1B associated with both syndromic and non-
syndromic short stature.";
BMC Genomics 16:701-701(2015).
[30]
VARIANTS ARG-488 AND SER-1413.
PubMed=26637798; DOI=10.1016/j.neuron.2015.11.009;
D'Gama A.M., Pochareddy S., Li M., Jamuar S.S., Reiff R.E., Lam A.T.,
Sestan N., Walsh C.A.;
"Targeted DNA Sequencing from Autism Spectrum Disorder Brains
Implicates Multiple Genetic Mechanisms.";
Neuron 88:910-917(2015).
-!- FUNCTION: Involved in transcriptional activation and repression of
select genes by chromatin remodeling (alteration of DNA-nucleosome
topology). Component of SWI/SNF chromatin remodeling complexes
that carry out key enzymatic activities, changing chromatin
structure by altering DNA-histone contacts within a nucleosome in
an ATP-dependent manner. Belongs to the neural progenitors-
specific chromatin remodeling complex (npBAF complex) and the
neuron-specific chromatin remodeling complex (nBAF complex).
During neural development a switch from a stem/progenitor to a
postmitotic chromatin remodeling mechanism occurs as neurons exit
the cell cycle and become committed to their adult state. The
transition from proliferating neural stem/progenitor cells to
postmitotic neurons requires a switch in subunit composition of
the npBAF and nBAF complexes. As neural progenitors exit mitosis
and differentiate into neurons, npBAF complexes which contain
ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous
alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits
in neuron-specific complexes (nBAF). The npBAF complex is
essential for the self-renewal/proliferative capacity of the
multipotent neural stem cells. The nBAF complex along with CREST
plays a role regulating the activity of genes essential for
dendrite growth (By similarity). Binds DNA non-specifically
(PubMed:14982958, PubMed:15170388). {ECO:0000250|UniProtKB:E9Q4N7,
ECO:0000269|PubMed:14982958, ECO:0000269|PubMed:15170388,
ECO:0000303|PubMed:12672490, ECO:0000303|PubMed:22952240,
ECO:0000303|PubMed:26601204}.
-!- SUBUNIT: Component of SWI/SNF chromatin remodeling complexes, in
some of which it can be mutually exclusive with ARID1B/BAF250B
(PubMed:12672490, PubMed:22952240, PubMed:26601204,
PubMed:12200431, PubMed:11988099, PubMed:15170388). The canonical
complex contains a catalytic subunit (either SMARCA4/BRG1/BAF190A
or SMARCA2/BRM/BAF190B) and at least SMARCE1, ACTL6A/BAF53,
SMARCC1/BAF155, SMARCC2/BAF170, and SMARCB1/SNF5/BAF47. Other
subunits specific to each of the complexes may also be present
permitting several possible combinations developmentally and
tissue specific (PubMed:11734557, PubMed:22952240,
PubMed:26601204). Component of the BAF (SWI/SNF-A) complex, which
includes at least actin (ACTB), ARID1A/BAF250A, ARID1B/BAF250B,
SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B,
SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1,
and one or more SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C
(PubMed:18765789). In muscle cells, the BAF complex also contains
DPF3. Component of neural progenitors-specific chromatin
remodeling complex (npBAF complex) composed of at least,
ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C,
SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47,
SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, PHF10/BAF45A,
ACTL6A/BAF53A and actin. Component of neuron-specific chromatin
remodeling complex (nBAF complex) composed of at least,
ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C,
SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47,
SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B,
DPF3/BAF45C, ACTL6B/BAF53B and actin (By similarity). Component of
a SWI/SNF-like EBAFb complex, at least composed of
SMARCA4/BRG1/BAF190A, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A,
SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B, SMARCC1/BAF155,
SMARCC2/BAF170, ARID1B/BAF250B, MLLT1/ENL and actin
(PubMed:12665591). Interacts through its C-terminus with
SMARCA2/BRM/BAF190B and SMARCA4/BRG1/BAF190A (PubMed:12200431,
PubMed:11988099, PubMed:15170388). Interacts with SMARCC1/BAF155
(PubMed:15170388). {ECO:0000250|UniProtKB:E9Q4N7,
ECO:0000269|PubMed:11988099, ECO:0000269|PubMed:12200431,
ECO:0000269|PubMed:12665591, ECO:0000269|PubMed:15170388,
ECO:0000269|PubMed:18765789, ECO:0000303|PubMed:12672490,
ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}.
-!- INTERACTION:
P51531:SMARCA2; NbExp=3; IntAct=EBI-679921, EBI-679562;
P51532:SMARCA4; NbExp=3; IntAct=EBI-679921, EBI-302489;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00355, ECO:0000269|PubMed:11988099}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q8NFD5-1; Sequence=Displayed;
Name=2;
IsoId=Q8NFD5-2; Sequence=VSP_015226;
Name=3;
IsoId=Q8NFD5-3; Sequence=VSP_015227;
Name=4;
IsoId=Q8NFD5-4; Sequence=VSP_040800;
-!- TISSUE SPECIFICITY: Widely expressed with high levels in heart,
skeletal muscle and kidney. {ECO:0000269|PubMed:11988099,
ECO:0000269|PubMed:12200431, ECO:0000269|PubMed:12665591}.
-!- POLYMORPHISM: The poly-Gln region is polymorphic and the number of
Gln varies in the population (from 17 to 23).
-!- DISEASE: Coffin-Siris syndrome 1 (CSS1) [MIM:135900]: A form of
Coffin-Siris syndrome, a congenital multiple malformation syndrome
with broad phenotypic and genetic variability. Cardinal features
are intellectual disability, coarse facial features,
hypertrichosis, and hypoplastic or absent fifth digit nails or
phalanges. Additional features include malformations of the
cardiac, gastrointestinal, genitourinary, and/or central nervous
systems. Sucking/feeding difficulties, poor growth, ophthalmologic
abnormalities, hearing impairment, and spinal anomalies are common
findings. Both autosomal dominant and autosomal recessive
inheritance patterns have been reported.
{ECO:0000269|PubMed:22405089, ECO:0000269|PubMed:22426308,
ECO:0000269|PubMed:22426309}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- CAUTION: It is uncertain whether Met-1 or Met-59 is the initiator.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAL76077.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAN70985.1; Type=Frameshift; Positions=857, 863; Evidence={ECO:0000305};
Sequence=CAA69592.1; Type=Frameshift; Positions=132; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AF259792; AAG36928.1; -; mRNA.
EMBL; AL355297; CAH71534.1; -; Genomic_DNA.
EMBL; AL049820; CAH71534.1; JOINED; Genomic_DNA.
EMBL; AL162578; CAH71534.1; JOINED; Genomic_DNA.
EMBL; AL591545; CAH71534.1; JOINED; Genomic_DNA.
EMBL; AL049820; CAI42308.1; -; Genomic_DNA.
EMBL; AL162578; CAI42308.1; JOINED; Genomic_DNA.
EMBL; AL355297; CAI42308.1; JOINED; Genomic_DNA.
EMBL; AL591545; CAI42308.1; JOINED; Genomic_DNA.
EMBL; AL162578; CAI40014.1; -; Genomic_DNA.
EMBL; AL049820; CAI40014.1; JOINED; Genomic_DNA.
EMBL; AL355297; CAI40014.1; JOINED; Genomic_DNA.
EMBL; AL591545; CAI40014.1; JOINED; Genomic_DNA.
EMBL; AL591545; CAI40666.1; -; Genomic_DNA.
EMBL; AL049820; CAI40666.1; JOINED; Genomic_DNA.
EMBL; AL162578; CAI40666.1; JOINED; Genomic_DNA.
EMBL; AL355297; CAI40666.1; JOINED; Genomic_DNA.
EMBL; AL049820; CAI42305.1; -; Genomic_DNA.
EMBL; AL591545; CAI42305.1; JOINED; Genomic_DNA.
EMBL; AL591545; CAI40664.1; -; Genomic_DNA.
EMBL; AL049820; CAI40664.1; JOINED; Genomic_DNA.
EMBL; AJ001216; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Y08266; CAA69592.1; ALT_FRAME; mRNA.
EMBL; AF521671; AAN03447.1; -; mRNA.
EMBL; AF253515; AAN70985.1; ALT_SEQ; mRNA.
EMBL; AF468300; AAL76077.1; ALT_INIT; mRNA.
EMBL; AB033061; BAA86549.1; -; mRNA.
CCDS; CCDS5251.2; -. [Q8NFD5-1]
CCDS; CCDS55072.1; -. [Q8NFD5-2]
RefSeq; NP_001333742.1; NM_001346813.1. [Q8NFD5-3]
RefSeq; NP_059989.2; NM_017519.2. [Q8NFD5-1]
RefSeq; NP_065783.3; NM_020732.3. [Q8NFD5-2]
UniGene; Hs.291587; -.
UniGene; Hs.744461; -.
PDB; 2CXY; X-ray; 1.60 A; A=1041-1159.
PDB; 2EH9; X-ray; 2.00 A; A=1041-1159.
PDBsum; 2CXY; -.
PDBsum; 2EH9; -.
ProteinModelPortal; Q8NFD5; -.
SMR; Q8NFD5; -.
BioGrid; 121559; 45.
CORUM; Q8NFD5; -.
IntAct; Q8NFD5; 15.
MINT; Q8NFD5; -.
STRING; 9606.ENSP00000344546; -.
iPTMnet; Q8NFD5; -.
PhosphoSitePlus; Q8NFD5; -.
BioMuta; ARID1B; -.
DMDM; 73921720; -.
EPD; Q8NFD5; -.
MaxQB; Q8NFD5; -.
PaxDb; Q8NFD5; -.
PeptideAtlas; Q8NFD5; -.
PRIDE; Q8NFD5; -.
Ensembl; ENST00000346085; ENSP00000344546; ENSG00000049618. [Q8NFD5-2]
Ensembl; ENST00000350026; ENSP00000055163; ENSG00000049618. [Q8NFD5-1]
Ensembl; ENST00000636930; ENSP00000490491; ENSG00000049618. [Q8NFD5-3]
Ensembl; ENST00000637810; ENSP00000489636; ENSG00000049618. [Q8NFD5-4]
GeneID; 57492; -.
KEGG; hsa:57492; -.
UCSC; uc003qqo.4; human. [Q8NFD5-1]
CTD; 57492; -.
DisGeNET; 57492; -.
EuPathDB; HostDB:ENSG00000049618.21; -.
GeneCards; ARID1B; -.
GeneReviews; ARID1B; -.
H-InvDB; HIX0006320; -.
H-InvDB; HIX0165033; -.
HGNC; HGNC:18040; ARID1B.
HPA; HPA016511; -.
HPA; HPA075291; -.
MalaCards; ARID1B; -.
MIM; 135900; phenotype.
MIM; 614556; gene.
neXtProt; NX_Q8NFD5; -.
OpenTargets; ENSG00000049618; -.
Orphanet; 251056; 6q25 microdeletion syndrome.
Orphanet; 1465; Coffin-Siris syndrome.
Orphanet; 3051; intellectual disability - sparse hair - brachydactyly.
PharmGKB; PA134909463; -.
eggNOG; KOG2510; Eukaryota.
eggNOG; ENOG410Y034; LUCA.
GeneTree; ENSGT00550000074575; -.
HOVERGEN; HBG058196; -.
InParanoid; Q8NFD5; -.
KO; K11653; -.
OMA; PPYPGMN; -.
OrthoDB; EOG091G00GP; -.
PhylomeDB; Q8NFD5; -.
TreeFam; TF320364; -.
Reactome; R-HSA-3214858; RMTs methylate histone arginines.
Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
SIGNOR; Q8NFD5; -.
ChiTaRS; ARID1B; human.
EvolutionaryTrace; Q8NFD5; -.
GeneWiki; ARID1B; -.
GenomeRNAi; 57492; -.
PRO; PR:Q8NFD5; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000049618; -.
CleanEx; HS_ARID1B; -.
ExpressionAtlas; Q8NFD5; baseline and differential.
Genevisible; Q8NFD5; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0071565; C:nBAF complex; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0016514; C:SWI/SNF complex; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:GDB.
GO; GO:0003713; F:transcription coactivator activity; NAS:UniProtKB.
GO; GO:1904385; P:cellular response to angiotensin; IEA:Ensembl.
GO; GO:0048096; P:chromatin-mediated maintenance of transcription; NAS:UniProtKB.
GO; GO:0097026; P:dendritic cell dendrite assembly; IEA:Ensembl.
GO; GO:0060996; P:dendritic spine development; IEA:Ensembl.
GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
GO; GO:0007270; P:neuron-neuron synaptic transmission; IEA:Ensembl.
GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.10.150.60; -; 1.
InterPro; IPR038040; ARID1B.
InterPro; IPR001606; ARID_dom.
InterPro; IPR036431; ARID_dom_sf.
InterPro; IPR021906; BAF250/Osa.
InterPro; IPR033388; BAF250_C.
PANTHER; PTHR12656; PTHR12656; 3.
PANTHER; PTHR12656:SF11; PTHR12656:SF11; 3.
Pfam; PF01388; ARID; 1.
Pfam; PF12031; BAF250_C; 1.
SMART; SM00501; BRIGHT; 1.
SUPFAM; SSF46774; SSF46774; 1.
PROSITE; PS51011; ARID; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Chromatin regulator;
Complete proteome; DNA-binding; Mental retardation; Methylation;
Neurogenesis; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Transcription; Transcription regulation;
Triplet repeat expansion.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
CHAIN 2 2236 AT-rich interactive domain-containing
protein 1B.
/FTId=PRO_0000200576.
DOMAIN 1053 1144 ARID. {ECO:0000255|PROSITE-
ProRule:PRU00355}.
MOTIF 419 423 LXXLL.
MOTIF 1358 1377 Nuclear localization signal.
{ECO:0000250|UniProtKB:O14497}.
MOTIF 2036 2040 LXXLL.
COMPBIAS 2 47 Ala-rich.
COMPBIAS 35 57 Ser-rich.
COMPBIAS 81 104 His-rich.
COMPBIAS 107 131 Gln-rich.
COMPBIAS 114 131 Poly-Gln.
COMPBIAS 141 401 Gly-rich.
COMPBIAS 329 493 Ala-rich.
COMPBIAS 574 633 Gln-rich.
COMPBIAS 684 771 Ser-rich.
COMPBIAS 932 935 Poly-Ala.
COMPBIAS 1034 1037 Poly-Ser.
COMPBIAS 1441 1444 Poly-Ser.
COMPBIAS 1459 1597 Pro-rich.
COMPBIAS 1833 1836 Poly-Pro.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 404 404 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:E9Q4N7}.
MOD_RES 502 502 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 516 516 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 525 525 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:E9Q4N7}.
MOD_RES 557 557 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1542 1542 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1555 1555 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1559 1559 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1715 1715 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1777 1777 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VAR_SEQ 1 750 Missing (in isoform 4).
{ECO:0000303|PubMed:11734557}.
/FTId=VSP_040800.
VAR_SEQ 579 579 Q -> QDSGDATWKETFWL (in isoform 2).
{ECO:0000303|PubMed:11988099}.
/FTId=VSP_015226.
VAR_SEQ 1032 1032 K -> KDSYSSQGISQPPTPGNLPVPSPMSPSSASISSFHG
DESDSISSPGWPKTPSSP (in isoform 3).
{ECO:0000303|PubMed:10574462}.
/FTId=VSP_015227.
VARIANT 11 11 A -> AA. {ECO:0000269|PubMed:22405089}.
/FTId=VAR_067662.
VARIANT 45 47 Missing. {ECO:0000269|PubMed:22405089}.
/FTId=VAR_067663.
VARIANT 82 82 Q -> H. {ECO:0000269|PubMed:22405089}.
/FTId=VAR_067664.
VARIANT 246 246 G -> S (in dbSNP:rs375160616).
{ECO:0000269|PubMed:22405089}.
/FTId=VAR_067665.
VARIANT 318 319 Missing. {ECO:0000269|PubMed:22405089}.
/FTId=VAR_067666.
VARIANT 319 319 Missing. {ECO:0000269|PubMed:22405089}.
/FTId=VAR_067667.
VARIANT 327 328 Missing. {ECO:0000269|PubMed:22405089}.
/FTId=VAR_067668.
VARIANT 333 337 Missing. {ECO:0000269|PubMed:22405089}.
/FTId=VAR_067669.
VARIANT 363 363 A -> V (in dbSNP:rs748273011).
{ECO:0000269|PubMed:22405089}.
/FTId=VAR_067670.
VARIANT 396 396 G -> A (in dbSNP:rs760718156).
{ECO:0000269|PubMed:22405089}.
/FTId=VAR_067671.
VARIANT 429 429 M -> V (in dbSNP:rs199948752).
{ECO:0000269|PubMed:22405089}.
/FTId=VAR_067672.
VARIANT 450 450 P -> PP. {ECO:0000269|PubMed:22405089}.
/FTId=VAR_067673.
VARIANT 488 488 P -> R (found in a patient with autism;
unknown pathological significance;
dbSNP:rs769085274).
{ECO:0000269|PubMed:26637798}.
/FTId=VAR_078697.
VARIANT 497 497 S -> N (in dbSNP:rs764716697).
{ECO:0000269|PubMed:22405089}.
/FTId=VAR_067674.
VARIANT 531 531 M -> T (in dbSNP:rs141260832).
{ECO:0000269|PubMed:22405089}.
/FTId=VAR_067675.
VARIANT 771 771 S -> L (found in a patient with short
stature; unknown pathological
significance).
{ECO:0000269|PubMed:26376624}.
/FTId=VAR_077456.
VARIANT 814 814 G -> A (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036257.
VARIANT 876 876 Q -> E (in dbSNP:rs138254872).
{ECO:0000269|PubMed:22405089}.
/FTId=VAR_067676.
VARIANT 980 980 Q -> L (in dbSNP:rs139620600).
{ECO:0000269|PubMed:22405089}.
/FTId=VAR_067677.
VARIANT 1092 1092 V -> I (in dbSNP:rs775526039).
{ECO:0000269|PubMed:22405089}.
/FTId=VAR_067678.
VARIANT 1249 1249 Q -> P (in dbSNP:rs768013849).
{ECO:0000269|PubMed:22405089}.
/FTId=VAR_067679.
VARIANT 1271 1271 G -> E (in dbSNP:rs149389876).
{ECO:0000269|PubMed:22405089}.
/FTId=VAR_067680.
VARIANT 1303 1303 G -> R (in dbSNP:rs199674889).
{ECO:0000269|PubMed:22405089}.
/FTId=VAR_067681.
VARIANT 1321 1321 S -> N (in dbSNP:rs142808724).
{ECO:0000269|PubMed:22405089}.
/FTId=VAR_067682.
VARIANT 1411 1411 P -> S. {ECO:0000269|PubMed:22405089}.
/FTId=VAR_067683.
VARIANT 1413 1413 P -> S (found in a patient with autism;
unknown pathological significance;
dbSNP:rs1051017338).
{ECO:0000269|PubMed:26637798}.
/FTId=VAR_078698.
VARIANT 1436 1436 G -> A (probable disease-associated
mutation found in a patient with short
stature; de novo mutation).
{ECO:0000269|PubMed:26376624}.
/FTId=VAR_077457.
VARIANT 1466 1466 Q -> K. {ECO:0000269|PubMed:22405089}.
/FTId=VAR_067684.
VARIANT 1506 1506 R -> H. {ECO:0000269|PubMed:22405089}.
/FTId=VAR_067685.
VARIANT 1563 1563 P -> L (found in a patient with short
stature; unknown pathological
significance).
{ECO:0000269|PubMed:26376624}.
/FTId=VAR_077458.
VARIANT 1573 1573 T -> M (in dbSNP:rs777745107).
{ECO:0000269|PubMed:22405089}.
/FTId=VAR_067686.
VARIANT 1659 1659 N -> S (in dbSNP:rs140177120).
{ECO:0000269|PubMed:22405089}.
/FTId=VAR_067687.
VARIANT 1733 1733 Missing. {ECO:0000269|PubMed:22405089}.
/FTId=VAR_067688.
VARIANT 1773 1773 K -> R (in dbSNP:rs574141489).
{ECO:0000269|PubMed:22405089}.
/FTId=VAR_067689.
VARIANT 1851 1851 D -> N (in dbSNP:rs200305796).
{ECO:0000269|PubMed:22405089}.
/FTId=VAR_067690.
VARIANT 1898 1898 K -> R (in dbSNP:rs758204258).
{ECO:0000269|PubMed:22405089}.
/FTId=VAR_067691.
VARIANT 1954 1954 K -> R (in dbSNP:rs756220726).
{ECO:0000269|PubMed:22405089}.
/FTId=VAR_067692.
VARIANT 1987 1987 D -> Y (probable disease-associated
mutation found in a patient with short
stature; de novo mutation).
{ECO:0000269|PubMed:26376624}.
/FTId=VAR_077459.
VARIANT 2163 2163 Q -> R. {ECO:0000269|PubMed:22405089}.
/FTId=VAR_067693.
CONFLICT 334 336 AGA -> SRS (in Ref. 5; AAN03447).
{ECO:0000305}.
CONFLICT 446 446 P -> A (in Ref. 6; AAN70985).
{ECO:0000305}.
CONFLICT 687 687 V -> A (in Ref. 7; AAL76077).
{ECO:0000305}.
CONFLICT 904 904 T -> P (in Ref. 7; AAL76077).
{ECO:0000305}.
CONFLICT 1201 1201 T -> I (in Ref. 1; AAG36928).
{ECO:0000305}.
CONFLICT 1339 1339 P -> S (in Ref. 6; AAN70985).
{ECO:0000305}.
CONFLICT 1432 1432 P -> L (in Ref. 8; BAA86549).
{ECO:0000305}.
CONFLICT 1534 1534 P -> S (in Ref. 6; AAN70985).
{ECO:0000305}.
CONFLICT 1713 1713 D -> N (in Ref. 7; AAL76077).
{ECO:0000305}.
CONFLICT 2196 2196 D -> N (in Ref. 1; AAG36928).
{ECO:0000305}.
HELIX 1046 1049 {ECO:0000244|PDB:2CXY}.
HELIX 1056 1070 {ECO:0000244|PDB:2CXY}.
HELIX 1087 1097 {ECO:0000244|PDB:2CXY}.
HELIX 1100 1106 {ECO:0000244|PDB:2CXY}.
HELIX 1109 1115 {ECO:0000244|PDB:2CXY}.
HELIX 1122 1135 {ECO:0000244|PDB:2CXY}.
HELIX 1137 1145 {ECO:0000244|PDB:2CXY}.
SEQUENCE 2236 AA; 236123 MW; 4538B4747606C918 CRC64;
MAHNAGAAAA AGTHSAKSGG SEAALKEGGS AAALSSSSSS SAAAAAASSS SSSGPGSAME
TGLLPNHKLK TVGEAPAAPP HQQHHHHHHA HHHHHHAHHL HHHHALQQQL NQFQQQQQQQ
QQQQQQQQQQ QHPISNNNSL GGAGGGAPQP GPDMEQPQHG GAKDSAAGGQ ADPPGPPLLS
KPGDEDDAPP KMGEPAGGRY EHPGLGALGT QQPPVAVPGG GGGPAAVPEF NNYYGSAAPA
SGGPGGRAGP CFDQHGGQQS PGMGMMHSAS AAAAGAPGSM DPLQNSHEGY PNSQCNHYPG
YSRPGAGGGG GGGGGGGGGS GGGGGGGGAG AGGAGAGAVA AAAAAAAAAA GGGGGGGYGG
SSAGYGVLSS PRQQGGGMMM GPGGGGAASL SKAAAGSAAG GFQRFAGQNQ HPSGATPTLN
QLLTSPSPMM RSYGGSYPEY SSPSAPPPPP SQPQSQAAAA GAAAGGQQAA AGMGLGKDMG
AQYAAASPAW AAAQQRSHPA MSPGTPGPTM GRSQGSPMDP MVMKRPQLYG MGSNPHSQPQ
QSSPYPGGSY GPPGPQRYPI GIQGRTPGAM AGMQYPQQQM PPQYGQQGVS GYCQQGQQPY
YSQQPQPPHL PPQAQYLPSQ SQQRYQPQQD MSQEGYGTRS QPPLAPGKPN HEDLNLIQQE
RPSSLPDLSG SIDDLPTGTE ATLSSAVSAS GSTSSQGDQS NPAQSPFSPH ASPHLSSIPG
GPSPSPVGSP VGSNQSRSGP ISPASIPGSQ MPPQPPGSQS ESSSHPALSQ SPMPQERGFM
AGTQRNPQMA QYGPQQTGPS MSPHPSPGGQ MHAGISSFQQ SNSSGTYGPQ MSQYGPQGNY
SRPPAYSGVP SASYSGPGPG MGISANNQMH GQGPSQPCGA VPLGRMPSAG MQNRPFPGNM
SSMTPSSPGM SQQGGPGMGP PMPTVNRKAQ EAAAAVMQAA ANSAQSRQGS FPGMNQSGLM
ASSSPYSQPM NNSSSLMNTQ APPYSMAPAM VNSSAASVGL ADMMSPGESK LPLPLKADGK
EEGTPQPESK SKKSSSSTTT GEKITKVYEL GNEPERKLWV DRYLTFMEER GSPVSSLPAV
GKKPLDLFRL YVCVKEIGGL AQVNKNKKWR ELATNLNVGT SSSAASSLKK QYIQYLFAFE
CKIERGEEPP PEVFSTGDTK KQPKLQPPSP ANSGSLQGPQ TPQSTGSNSM AEVPGDLKPP
TPASTPHGQM TPMQGGRSST ISVHDPFSDV SDSSFPKRNS MTPNAPYQQG MSMPDVMGRM
PYEPNKDPFG GMRKVPGSSE PFMTQGQMPN SSMQDMYNQS PSGAMSNLGM GQRQQFPYGA
SYDRRHEPYG QQYPGQGPPS GQPPYGGHQP GLYPQQPNYK RHMDGMYGPP AKRHEGDMYN
MQYSSQQQEM YNQYGGSYSG PDRRPIQGQY PYPYSRERMQ GPGQIQTHGI PPQMMGGPLQ
SSSSEGPQQN MWAARNDMPY PYQNRQGPGG PTQAPPYPGM NRTDDMMVPD QRINHESQWP
SHVSQRQPYM SSSASMQPIT RPPQPSYQTP PSLPNHISRA PSPASFQRSL ENRMSPSKSP
FLPSMKMQKV MPTVPTSQVT GPPPQPPPIR REITFPPGSV EASQPVLKQR RKITSKDIVT
PEAWRVMMSL KSGLLAESTW ALDTINILLY DDSTVATFNL SQLSGFLELL VEYFRKCLID
IFGILMEYEV GDPSQKALDH NAARKDDSQS LADDSGKEEE DAECIDDDEE DEEDEEEDSE
KTESDEKSSI ALTAPDAAAD PKEKPKQASK FDKLPIKIVK KNNLFVVDRS DKLGRVQEFN
SGLLHWQLGG GDTTEHIQTH FESKMEIPPR RRPPPPLSSA GRKKEQEGKG DSEEQQEKSI
IATIDDVLSA RPGALPEDAN PGPQTESSKF PFGIQQAKSH RNIKLLEDEP RSRDETPLCT
IAHWQDSLAK RCICVSNIVR SLSFVPGNDA EMSKHPGLVL ILGKLILLHH EHPERKRAPQ
TYEKEEDEDK GVACSKDEWW WDCLEVLRDN TLVTLANISG QLDLSAYTES ICLPILDGLL
HWMVCPSAEA QDPFPTVGPN SVLSPQRLVL ETLCKLSIQD NNVDLILATP PFSRQEKFYA
TLVRYVGDRK NPVCREMSMA LLSNLAQGDA LAARAIAVQK GSIGNLISFL EDGVTMAQYQ
QSQHNLMHMQ PPPLEPPSVD MMCRAAKALL AMARVDENRS EFLLHEGRLL DISISAVLNS
LVASVICDVL FQIGQL


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18-003-44091 AT-rich interactive domain-containing protein 3B - ARID domain-containing protein 3B; Bright-like; Bright and dead ringer protein Polyclonal 0.05 mg Aff Pur
20-372-60127 AT rich interactive domain 1A (SWI- like) (ARID1A). transcript variant 1. mRNA - Mouse monoclonal anti-human ARID1A antibody; ARID domain-containing protein 1A; SWI_SNF-related. matrix-associated. act 0.1 mg
EIAAB38780 ATP-dependent helicase SMARCA4,BAF190A,BAF190A,BRG1,BRG1-associated factor 190A,Homo sapiens,Human,Mitotic growth and transcription activator,Protein brahma homolog 1,Protein BRG-1,SMARCA4,SNF2B,SNF2-
26-522 ARID3C is a member of the ARID (AT-rich interaction domain) family of proteins. The ARID domain is a helix-turn-helix motif-based DNA-binding domain. ARID family members have roles in embryonic patter 0.05 mg
EIAAB38781 ATP-dependent helicase SMARCA4,BAF190A,Baf190a,Brg1,BRG1-associated factor 190A,Protein brahma homolog 1,Rat,Rattus norvegicus,Smarca4,Snf2b,SNF2-beta,Snf2l4,SWI_SNF-related matrix-associated actin-de
EIAAB38778 ATP-dependent helicase SMARCA4,BAF190A,BAF190A,Bos taurus,Bovine,BRG1,BRG1-associated factor 190A,Protein brahma homolog 1,SMARCA4,SNF2B,SNF2-beta,SNF2L4,SWI_SNF-related matrix-associated actin-depend
EIAAB38779 ATP-dependent helicase SMARCA4,BAF190A,Baf190a,Brg1,BRG1-associated factor 190A,Mouse,Mus musculus,Protein brahma homolog 1,Smarca4,Snf2b,SNF2-beta,Snf2l4,SWI_SNF-related matrix-associated actin-depen
25-803 This gene is a member of the PAR6 family and encodes a protein with a PSD95_Discs-large_ZO1 (PDZ) domain, an OPR domain and a semi-Cdc42_Rac interactive binding (CRIB) domain. This cytoplasmic protein 0.05 mg
60157 IgG,AT rich interactive domain 2 (ARID, RFX_like) (ARID2) 0.1 mg
GWB-FD34A2 AT rich interactive domain 2 (ARID RFX-like) (ARID2), Antibody
ARID3B ARID2 Gene AT rich interactive domain 2 (ARID, RFX-like)
25-203 LIM domain only 6 is a three LIM domain-containing protein. The LIM domain is a cysteine-rich sequence motif that binds zinc atoms to form a specific protein-binding interface for protein-protein inte 0.05 mg
28-082 LIM domain only 6 is a three LIM domain-containing protein. The LIM domain is a cysteine-rich sequence motif that binds zinc atoms to form a specific protein-binding interface for protein-protein inte 0.05 mg
27-597 LHX3 is a member a large protein family which carry the LIM domain, a unique cysteine-rich zinc-binding domain. The encoded protein is a transcription factor that is required for pituitary development 0.1 mg
27-596 LHX3 is a member a large protein family which carry the LIM domain, a unique cysteine-rich zinc-binding domain. The encoded protein is a transcription factor that is required for pituitary development 0.05 mg
27-913 LHX3 encodes a member a large protein family which carry the LIM domain, a unique cysteine-rich zinc-binding domain. The encoded protein is a transcription factor that is required for pituitary develo 0.1 mg
28-043 ARID3B is a member of the ARID (AT-rich interaction domain) family of DNA-binding proteins. The protein is homologous with two proteins that bind to the retinoblastoma gene product, and also with the 0.1 mg
28-946 ARID3B is a member of the ARID (AT-rich interaction domain) family of DNA-binding proteins. The protein is homologous with two proteins that bind to the retinoblastoma gene product, and also with the 0.05 mg
18-003-44039 LIM domain-binding protein 1 - Nuclear LIM interactor; Carboxyl-terminal LIM domain-binding protein 2; CLIM-2; LIM domain-binding factor CLIM2; hLdb1 Polyclonal 0.05 mg Aff Pur
31-212 LHX2 is a protein belonging to a large protein family, members of which carry the LIM domain, a unique cysteine-rich zinc-binding domain. The encoded protein may function as a transcriptional regulato 0.1 mg
EIAAB38239 Homo sapiens,Human,P1725,SH3 domain-binding glutamic acid-rich-like protein 3,SH3 domain-binding protein 1,SH3BGRL3,SH3BP-1
EIAAB38236 FASH3,Fovea-associated SH3 domain-binding protein,Homo sapiens,Human,SH3 domain-binding glutamic acid-rich-like protein 2,SH3BGRL2


 

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