ARI1A_MOUSE
ID ARI1A_MOUSE Reviewed; 2283 AA.
AC A2BH40; Q640Q1; Q925Q1;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=AT-rich interactive domain-containing protein 1A;
DE Short=ARID domain-containing protein 1A;
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 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;
GN Name=Arid1a; Synonyms=Baf250, Baf250a, Osa1, Smarcf1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING (ISOFORM 3),
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION OF THE NBAF AND NPBAF COMPLEXES, IDENTIFICATION BY MASS
RP SPECTROMETRY, IDENTIFICATION IN THE NBAF AND NPBAF COMPLEXES, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=17640523; DOI=10.1016/j.neuron.2007.06.019;
RA Lessard J., Wu J.I., Ranish J.A., Wan M., Winslow M.M., Staahl B.T., Wu H.,
RA Aebersold R., Graef I.A., Crabtree G.R.;
RT "An essential switch in subunit composition of a chromatin remodeling
RT complex during neural development.";
RL Neuron 55:201-215(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-697, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365; SER-384; SER-697;
RP SER-699; SER-703; SER-731; SER-765; SER-773 AND THR-1874, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-431 AND ARG-1277, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
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 [9]
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 [10]
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 [11]
RP INTERACTION WITH FOS; FOSB; FOSL1 AND FOSL2.
RX PubMed=29272704; DOI=10.1016/j.molcel.2017.11.026;
RA Vierbuchen T., Ling E., Cowley C.J., Couch C.H., Wang X., Harmin D.A.,
RA Roberts C.W.M., Greenberg M.E.;
RT "AP-1 Transcription Factors and the BAF Complex Mediate Signal-Dependent
RT Enhancer Selection.";
RL Mol. Cell 68:1067-1082.e12(2017).
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 (PubMed:22952240, PubMed:26601204).
CC Belongs to the neural progenitors-specific chromatin remodeling complex
CC (npBAF complex) and the neuron-specific chromatin remodeling complex
CC (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 (PubMed:17640523).
CC {ECO:0000250|UniProtKB:O14497, ECO:0000269|PubMed:17640523,
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. 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. Component of the BAF (SWI/SNF-A) complex, which includes at
CC least actin (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 (By similarity). In
CC muscle cells, the BAF complex also contains DPF3. Component of neural
CC progenitors-specific chromatin remodeling complex (npBAF complex)
CC composed of 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 PHF10/BAF45A, ACTL6A/BAF53A and actin. Component of neuron-specific
CC chromatin remodeling complex (nBAF complex) composed of at least,
CC ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C,
CC SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47,
CC SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B,
CC DPF3/BAF45C, ACTL6B/BAF53B and actin (PubMed:17640523). Component of a
CC SWI/SNF-like EBAFa complex, at least composed of SMARCA4/BRG1/BAF190A,
CC SMARCB1/BAF47/SNF5, ACTL6A/BAF53A, SMARCE1/BAF57, SMARCD1/BAF60A,
CC SMARCC1/BAF155, SMARCC2/BAF170, BAF250A and MLLT1/ENL. Interacts
CC through its C-terminus with SMARCA2/BRM/BAF190B and
CC SMARCA4/BRG1/BAF190A. Interacts with SMARCC1/BAF155 (By similarity).
CC Interacts with FOS (via bZIP domain and leucine-zipper region), FOSB
CC isoform 1 and 2, FOSL1 and FOSL2 (PubMed:29272704).
CC {ECO:0000250|UniProtKB:O14497, ECO:0000269|PubMed:17640523,
CC ECO:0000269|PubMed:29272704, ECO:0000303|PubMed:22952240,
CC ECO:0000303|PubMed:26601204}.
CC -!- INTERACTION:
CC A2BH40; O35845: Smarca4; NbExp=2; IntAct=EBI-371499, EBI-371515;
CC A2BH40; Q3TKT4: Smarca4; NbExp=7; IntAct=EBI-371499, EBI-1210244;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=A2BH40-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2BH40-2; Sequence=VSP_038737, VSP_038739;
CC Name=3;
CC IsoId=A2BH40-3; Sequence=VSP_038740;
CC Name=4;
CC IsoId=A2BH40-4; Sequence=VSP_038737, VSP_038738, VSP_038739;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at high levels in the
CC testis. {ECO:0000269|PubMed:11318604}.
CC -!- DEVELOPMENTAL STAGE: Expressed ubiquitously throughout the developing
CC spinal cord, brain and other embryonic tissues at 10.5 dpc-16.5 dpc. In
CC the earlier stages at 9.5 dpc and 10.5 dpc, is fairly ubiquitous though
CC with clearly elevated expression in the progress zone and lateral
CC mesoderm of limb buds, optic and otic vesicle, neural tube, and brain.
CC Later on at 11.5 dpc and 12.5 dpc, expression becomes more restricted
CC and is confined to the interdigital area of limbs, dorsal
CC mes/metencephalon, neocortex, and neural tube. Expression is seen in
CC the eye lens from 10.5 dpc until 12.5 dpc.
CC {ECO:0000269|PubMed:11318604, ECO:0000269|PubMed:17640523}.
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DR EMBL; AF268912; AAK54504.1; -; mRNA.
DR EMBL; BX537327; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR751606; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR925752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC082554; AAH82554.1; -; mRNA.
DR CCDS; CCDS38908.1; -. [A2BH40-1]
DR CCDS; CCDS89836.1; -. [A2BH40-4]
DR RefSeq; NP_001074288.1; NM_001080819.1. [A2BH40-1]
DR RefSeq; XP_006539390.1; XM_006539327.3. [A2BH40-2]
DR AlphaFoldDB; A2BH40; -.
DR BMRB; A2BH40; -.
DR SMR; A2BH40; -.
DR BioGRID; 220298; 40.
DR ComplexPortal; CPX-1232; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1233; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1236; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1237; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1240; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1241; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1244; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1245; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1251; Embryonic stem cell-specific SWI/SNF ATP-dependent chromatin remodeling complex.
DR ComplexPortal; CPX-1252; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1253; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1256; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1257; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1261; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1262; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
DR DIP; DIP-58952N; -.
DR IntAct; A2BH40; 21.
DR MINT; A2BH40; -.
DR STRING; 10090.ENSMUSP00000122354; -.
DR GlyConnect; 2144; 1 N-Linked glycan (1 site).
DR GlyGen; A2BH40; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; A2BH40; -.
DR PhosphoSitePlus; A2BH40; -.
DR SwissPalm; A2BH40; -.
DR EPD; A2BH40; -.
DR jPOST; A2BH40; -.
DR MaxQB; A2BH40; -.
DR PaxDb; A2BH40; -.
DR PeptideAtlas; A2BH40; -.
DR PRIDE; A2BH40; -.
DR ProteomicsDB; 283266; -. [A2BH40-1]
DR ProteomicsDB; 283267; -. [A2BH40-2]
DR ProteomicsDB; 283268; -. [A2BH40-3]
DR ProteomicsDB; 283269; -. [A2BH40-4]
DR Antibodypedia; 1691; 238 antibodies from 34 providers.
DR Ensembl; ENSMUST00000008024; ENSMUSP00000008024; ENSMUSG00000007880. [A2BH40-4]
DR Ensembl; ENSMUST00000105897; ENSMUSP00000101517; ENSMUSG00000007880. [A2BH40-1]
DR GeneID; 93760; -.
DR KEGG; mmu:93760; -.
DR UCSC; uc008vdh.1; mouse. [A2BH40-1]
DR UCSC; uc008vdj.1; mouse. [A2BH40-4]
DR CTD; 8289; -.
DR MGI; MGI:1935147; Arid1a.
DR VEuPathDB; HostDB:ENSMUSG00000007880; -.
DR eggNOG; KOG2510; Eukaryota.
DR GeneTree; ENSGT00940000155194; -.
DR HOGENOM; CLU_000974_1_1_1; -.
DR InParanoid; A2BH40; -.
DR OMA; CRPIDMD; -.
DR OrthoDB; 256110at2759; -.
DR PhylomeDB; A2BH40; -.
DR Reactome; R-MMU-3214858; RMTs methylate histone arginines.
DR Reactome; R-MMU-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR BioGRID-ORCS; 93760; 10 hits in 84 CRISPR screens.
DR ChiTaRS; Arid1a; mouse.
DR PRO; PR:A2BH40; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A2BH40; protein.
DR Bgee; ENSMUSG00000007880; Expressed in animal zygote and 279 other tissues.
DR ExpressionAtlas; A2BH40; baseline and differential.
DR Genevisible; A2BH40; MM.
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:MGI.
DR GO; GO:0071565; C:nBAF complex; IDA:UniProtKB.
DR GO; GO:0071564; C:npBAF complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0016514; C:SWI/SNF complex; IDA:MGI.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0016922; F:nuclear receptor binding; ISO:MGI.
DR GO; GO:0031491; F:nucleosome binding; IDA:MGI.
DR GO; GO:0030521; P:androgen receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0003205; P:cardiac chamber development; IMP:MGI.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; IMP:MGI.
DR GO; GO:0006325; P:chromatin organization; IPI:MGI.
DR GO; GO:0006338; P:chromatin remodeling; IMP:MGI.
DR GO; GO:0007566; P:embryo implantation; IMP:MGI.
DR GO; GO:0030900; P:forebrain development; IMP:MGI.
DR GO; GO:0001704; P:formation of primary germ layer; IMP:MGI.
DR GO; GO:0007369; P:gastrulation; IMP:MGI.
DR GO; GO:0042921; P:glucocorticoid receptor signaling pathway; ISO:MGI.
DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR GO; GO:0006337; P:nucleosome disassembly; ISO:MGI.
DR GO; GO:0003408; P:optic cup formation involved in camera-type eye development; IMP:MGI.
DR GO; GO:0060674; P:placenta blood vessel development; IMP:MGI.
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; ISS: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 GO; GO:0019827; P:stem cell population maintenance; IMP:MGI.
DR GO; GO:1901998; P:toxin transport; IMP:MGI.
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 Acetylation; Alternative splicing; Chromatin regulator; DNA-binding;
KW Methylation; Neurogenesis; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O14497"
FT CHAIN 2..2283
FT /note="AT-rich interactive domain-containing protein 1A"
FT /id="PRO_0000391619"
FT DOMAIN 1018..1109
FT /note="ARID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT REGION 1..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 979..1006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1114..1484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1539..1636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1757..1782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1872..1904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1917..1941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 296..300
FT /note="LXXLL"
FT MOTIF 1369..1388
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:O14497"
FT MOTIF 1710..1714
FT /note="LXXLL"
FT MOTIF 1965..1969
FT /note="LXXLL"
FT MOTIF 2083..2087
FT /note="LXXLL"
FT COMPBIAS 203..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1128..1158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1174..1190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1306..1373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1395..1440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1468..1482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1551..1591
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1767..1782
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O14497"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14497"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14497"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14497"
FT MOD_RES 287
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O14497"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14497"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 431
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14497"
FT MOD_RES 697
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 699
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 703
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 731
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 765
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 773
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14497"
FT MOD_RES 1236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14497"
FT MOD_RES 1277
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1605
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14497"
FT MOD_RES 1613
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O14497"
FT MOD_RES 1874
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1886
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O14497"
FT MOD_RES 1903
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O14497"
FT MOD_RES 1927
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14497"
FT MOD_RES 1942
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14497"
FT VAR_SEQ 1..385
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11318604,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_038737"
FT VAR_SEQ 1181
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038738"
FT VAR_SEQ 1336
FT /note="Q -> QQQQQR (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11318604,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_038739"
FT VAR_SEQ 1367..1583
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_038740"
FT CONFLICT 697
FT /note="S -> F (in Ref. 1; AAK54504)"
FT /evidence="ECO:0000305"
FT CONFLICT 750
FT /note="D -> E (in Ref. 1; AAK54504)"
FT /evidence="ECO:0000305"
FT CONFLICT 758
FT /note="P -> S (in Ref. 1; AAK54504)"
FT /evidence="ECO:0000305"
FT CONFLICT 833
FT /note="M -> I (in Ref. 1; AAK54504)"
FT /evidence="ECO:0000305"
FT CONFLICT 1011
FT /note="K -> Q (in Ref. 1; AAK54504)"
FT /evidence="ECO:0000305"
FT CONFLICT 1148
FT /note="P -> H (in Ref. 1; AAK54504)"
FT /evidence="ECO:0000305"
FT CONFLICT 1181..1182
FT /note="SR -> G (in Ref. 1; AAK54504)"
FT /evidence="ECO:0000305"
FT CONFLICT 1635
FT /note="M -> I (in Ref. 1; AAK54504)"
FT /evidence="ECO:0000305"
FT CONFLICT 1755
FT /note="Y -> S (in Ref. 1; AAK54504)"
FT /evidence="ECO:0000305"
FT CONFLICT 1795
FT /note="S -> P (in Ref. 1; AAK54504)"
FT /evidence="ECO:0000305"
FT CONFLICT 1799
FT /note="N -> S (in Ref. 1; AAK54504)"
FT /evidence="ECO:0000305"
FT CONFLICT 1929
FT /note="E -> D (in Ref. 1; AAK54504)"
FT /evidence="ECO:0000305"
FT CONFLICT 1956
FT /note="E -> D (in Ref. 1; AAK54504)"
FT /evidence="ECO:0000305"
FT CONFLICT 1974
FT /note="S -> P (in Ref. 1; AAK54504)"
FT /evidence="ECO:0000305"
FT CONFLICT 2233
FT /note="A -> P (in Ref. 1; AAK54504)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2283 AA; 242092 MW; 0F14BB1372CC4268 CRC64;
MAAQVAPAAA SSLGNPPPPP SELKKAEQQQ REEAGGEAAA AAAERGEMKA AAGQESEGPA
VGPPQPLGKE LQDGAESNGG GGGGGAGSGG GPGAEPDLKN SNGNAGPRPA LNNNLPEPPG
GGGGGGSSSS DGVGAPPHSA AAALPPPAYG FGQAYGRSPS AVAAAAAAVF HQQHGGQQSP
GLAALQSGGG GGLEPYAGPQ QNSHDHGFPN HQYNSYYPNR SAYPPPPQAY ALSSPRGGTP
GSGAAAAAGS KPPPSSSASA SSSSSSFAQQ RFGAMGGGGP SAAGGGTPQP TATPTLNQLL
TSPSSARGYQ GYPGGDYGGG PQDGGAGKGP ADMASQCWGA AAAAAAAAAA VSGGAQQRSH
HAPMSPGSSG GGGQPLARTP QSSSPMDQMG KMRPQPYGGT NPYSQQQGPP SGPQQGHGYP
GQPYGSQTPQ RYPMTMQGRA QSAMGSLSYA QQIPPYGQQG PSAYGQQGQT PYYNQQSPHP
QQQPPYAQQP PSQTPHAQPS YQQQPQTQQP QLQSSQPPYS QQPSQPPHQQ SPTPYPSQQS
TTQQHPQSQP PYSQPQAQSP YQQQQPQQPA SSSLSQQAAY PQPQPQQSQQ TAYSQQRFPP
PQELSQDSFG SQASSAPSMT SSKGGQEDMN LSLQSRPSSL PDLSGSIDDL PMGTEGALSP
GVSTSGISSS QGEQSNPAQS PFSPHTSPHL PGIRGPSPSP VGSPASVAQS RSGPLSPAAV
PGNQMPPRPP SGQSDSIMHP SMNQSSIAQD RGYMQRNPQM PQYTSPQPGS ALSPRQPSGG
QMHSGVGSYQ QNSMGSYGPQ GSQYGPQGGY PRQPNYNALP NANYPNAGMA GSMNPMGAGG
QMHGQPGIPP YGTLPPGRMA HASMGNRPYG PNMANMPPQV GSGMCPPPGG MNRKTQESAV
AMHVAANSIQ NRPPGYPNMN QGGMMGTGPP YGQGINSMAG MINPQGPPYP MGGTMANNSA
GMAASPEMMG LGDVKLTPAT KMNNKADGTP KTESKSKKSS SSTTTNEKIT KLYELGGEPE
RKMWVDRYLA FTEEKAMGMT NLPAVGRKPL DLYRLYVSVK EIGGLTQVNK NKKWRELATN
LNVGTSSSAA SSLKKQYIQC LYAFECKIER GEDPPPDIFA AADSKKSQPK IQPPSPAGSG
SMQGPQTPQS TSSSMAEGGD LKPPTPASTP HSQIPPLPGM SRSNSVGIQD AFPDGSDPTF
QKRNSMTPNP GYQPSMNTSD MMGRMSYEPN KDPYGSMRKA PGSDPFMSSG QGPNGGMGDP
YSRAAGPGLG SVAMGPRQHY PYGGPYDRVR TEPGIGPEGN MGTGAPQPNL MPSTPDSGMY
SPSRYPPQQQ QQQQQQHDSY GNQFSTQGTP SSSPFPSQQT TMYQQQQQNY KRPMDGTYGP
PAKRHEGEMY SVPYSAGQGQ PQQQQLPAAQ SQPASQPQAA QPSPQQDVYN QYSNAYPASA
TAATDRRPAG GPQNQFPFQF GRDRVSAPPG SSAQQNMPPQ MMGGPIQASA EVAQQGTMWQ
GRNDMTYNYA NRQNTGSATQ GPAYHGVNRT DEMLHTDQRA NHEGPWPSHG TRQPPYGPSA
PVPPMTRPPP SNYQPPPSMP NHIPQVSSPA PLPRPMENRT SPSKSPFLHS GMKMQKAGPP
VPASHIAPTP VQPPMIRRDI TFPPGSVEAT QPVLKQRRRL TMKDIGTPEA WRVMMSLKSG
LLAESTWALD TINILLYDDN SIMTFNLSQL PGLLELLVEY FRRCLIEIFG ILKEYEVGDP
GQRTLLDPGR FTKVYSPAHT EEEEEEHLDP KLEEEEEEGV GNDEEMAFLG KDKPSSENNE
EKLVSKFDKL PVKIVQRNDP FVVDCSDKLG RVQEFDSGLL HWRIGGGDTT EHIQTHFESK
IELLPSRPYV PCPTPPRKHL TTVEGTPGTT EQEGPPPDGL PEKRITATMD DMLSTRSSTL
TDEGAKSAEA TKESSKFPFG ISPAQSHRNI KILEDEPHSK DETPLCTLLD WQDSLAKRCV
CVSNTIRSLS FVPGNDFEMS KHPGLLLILG KLILLHHKHP ERKQAPLTYE KEEEQDQGVS
CDKVEWWWDC LEMLRENTLV TLANISGQLD LSPYPESICL PVLDGLLHWA VCPSAEAQDP
FSTLGPNAVL SPQRLVLETL SKLSIQDNNV DLILATPPFS RLEKLYSTMV RFLSDRKNPV
CREMAVVLLA NLAQGDSLAA RAIAVQKGSI GNLLGFLEDS LAATQFQQSQ ASLLHMQNPP
FEPTSVDMMR RAARALLALA KVDENHSEFT LYESRLLDIS VSPLMNSLVS QVICDVLFLI
GQS
