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AT-rich interactive domain-containing protein 1B (ARID domain-containing protein 1B) (BRG1-associated factor 250b) (BAF250B)

 ARI1B_MOUSE             Reviewed;        2244 AA.
E9Q4N7;
22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
05-APR-2011, sequence version 1.
23-MAY-2018, entry version 60.
RecName: Full=AT-rich interactive domain-containing protein 1B;
Short=ARID domain-containing protein 1B {ECO:0000305};
AltName: Full=BRG1-associated factor 250b {ECO:0000305};
Short=BAF250B {ECO:0000305};
Name=Arid1b {ECO:0000312|MGI:MGI:1926129};
Synonyms=Baf250b {ECO:0000305};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
FUNCTION OF THE NBAF AND NPBAF COMPLEXES, IDENTIFICATION BY MASS
SPECTROMETRY, AND IDENTIFICATION IN THE NBAF AND NPBAF COMPLEXES.
PubMed=17640523; DOI=10.1016/j.neuron.2007.06.019;
Lessard J., Wu J.I., Ranish J.A., Wan M., Winslow M.M., Staahl B.T.,
Wu H., Aebersold R., Graef I.A., Crabtree G.R.;
"An essential switch in subunit composition of a chromatin remodeling
complex during neural development.";
Neuron 55:201-215(2007).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1563, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Kidney, Lung, Pancreas, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[4]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-358 AND ARG-477, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Embryo;
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).
[5]
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).
[6]
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).
-!- 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 (PubMed:17640523). Binds DNA non-specifically.
{ECO:0000250|UniProtKB:Q8NFD5, ECO:0000269|PubMed:17640523,
ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}.
-!- SUBUNIT: Component of SWI/SNF chromatin remodeling complexes, in
some of which it can be mutually exclusive with ARID1B/BAF250B.
The canonical complex contains a catalytic subunit (either
SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B), and at least
SMARCE1, ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and
SMARCB1/SNF5/BAF47. Other subunits specific to each of the
complexes may also be present permitting several possible
combinations developmentally and tissue specific. 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 (By similarity). 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 (PubMed:17640523). Component
of a SWI/SNF-like EBAFb complex, at least composed of
SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, ACTL6A/BAF53A, SMARCE1/BAF57,
SMARCD1/BAF60A, SMARCD2/BAF60B, SMARCC1/BAF155, SMARCC2/BAF170,
ARID1B/BAF250B, MLLT1/ENL and actin. Interacts through its C-
terminus with SMARCA2/BRM/BAF190B and SMARCA4/BRG1/BAF190A.
Interacts with SMARCC1/BAF155 (By similarity).
{ECO:0000250|UniProtKB:Q8NFD5, ECO:0000269|PubMed:17640523,
ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}.
-!- INTERACTION:
Q3TKT4:Smarca4; NbExp=5; IntAct=EBI-6900614, EBI-1210244;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8NFD5,
ECO:0000255|PROSITE-ProRule:PRU00355}.
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EMBL; AC126929; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC132611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC166064; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS49929.1; -.
RefSeq; NP_001078824.1; NM_001085355.1.
UniGene; Mm.133401; -.
ProteinModelPortal; E9Q4N7; -.
IntAct; E9Q4N7; 3.
STRING; 10090.ENSMUSP00000111463; -.
MaxQB; E9Q4N7; -.
PaxDb; E9Q4N7; -.
PeptideAtlas; E9Q4N7; -.
PRIDE; E9Q4N7; -.
Ensembl; ENSMUST00000115797; ENSMUSP00000111463; ENSMUSG00000069729.
GeneID; 239985; -.
KEGG; mmu:239985; -.
UCSC; uc008aey.1; mouse.
CTD; 57492; -.
MGI; MGI:1926129; Arid1b.
eggNOG; KOG2510; Eukaryota.
eggNOG; ENOG410Y034; LUCA.
GeneTree; ENSGT00550000074575; -.
InParanoid; E9Q4N7; -.
KO; K11653; -.
OMA; PPYPGMN; -.
OrthoDB; EOG091G00GP; -.
TreeFam; TF320364; -.
Reactome; R-MMU-3214858; RMTs methylate histone arginines.
Reactome; R-MMU-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
ChiTaRS; Arid1b; mouse.
PRO; PR:E9Q4N7; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000069729; -.
ExpressionAtlas; E9Q4N7; baseline and differential.
Genevisible; E9Q4N7; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0071565; C:nBAF complex; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0016514; C:SWI/SNF complex; ISO:MGI.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0006338; P:chromatin remodeling; IC:MGI.
GO; GO:0097026; P:dendritic cell dendrite assembly; IMP:MGI.
GO; GO:0060996; P:dendritic spine development; IMP:MGI.
GO; GO:0007270; P:neuron-neuron synaptic transmission; IMP:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
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; IPR016024; ARM-type_fold.
InterPro; IPR021906; BAF250/Osa.
InterPro; IPR033388; BAF250_C.
PANTHER; PTHR12656; PTHR12656; 2.
PANTHER; PTHR12656:SF11; PTHR12656:SF11; 2.
Pfam; PF01388; ARID; 1.
Pfam; PF12031; BAF250_C; 1.
SMART; SM00501; BRIGHT; 1.
SUPFAM; SSF46774; SSF46774; 1.
SUPFAM; SSF48371; SSF48371; 1.
PROSITE; PS51011; ARID; 1.
1: Evidence at protein level;
Acetylation; Chromatin regulator; Coiled coil; Complete proteome;
DNA-binding; Methylation; Neurogenesis; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation.
CHAIN 1 2244 AT-rich interactive domain-containing
protein 1B.
/FTId=PRO_0000442428.
DOMAIN 1061 1152 ARID. {ECO:0000255|PROSITE-
ProRule:PRU00355}.
MOTIF 373 377 LXXLL. {ECO:0000250|UniProtKB:Q8NFD5}.
MOTIF 1366 1385 Nuclear localization signal.
{ECO:0000250|UniProtKB:O14497}.
MOTIF 2044 2048 LXXLL. {ECO:0000250|UniProtKB:Q8NFD5}.
COMPBIAS 23 49 His-rich. {ECO:0000255|PROSITE-
ProRule:PRU00009}.
COMPBIAS 52 78 Gln-rich. {ECO:0000255|PROSITE-
ProRule:PRU00006}.
COMPBIAS 61 103 Pro-rich. {ECO:0000255|PROSITE-
ProRule:PRU00015}.
COMPBIAS 87 355 Gly-rich. {ECO:0000255|PROSITE-
ProRule:PRU00008}.
COMPBIAS 272 445 Ala-rich. {ECO:0000255|PROSITE-
ProRule:PRU00001}.
COMPBIAS 898 1046 Ser-rich. {ECO:0000255|PROSITE-
ProRule:PRU00016}.
COMPBIAS 1726 1753 Glu-rich. {ECO:0000255|PROSITE-
ProRule:PRU00007}.
MOD_RES 358 358 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 454 454 Phosphoserine.
{ECO:0000250|UniProtKB:Q8NFD5}.
MOD_RES 468 468 Phosphoserine.
{ECO:0000250|UniProtKB:Q8NFD5}.
MOD_RES 477 477 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 509 509 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q8NFD5}.
MOD_RES 1550 1550 Phosphoserine.
{ECO:0000250|UniProtKB:Q8NFD5}.
MOD_RES 1563 1563 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1567 1567 Phosphoserine.
{ECO:0000250|UniProtKB:Q8NFD5}.
MOD_RES 1723 1723 Phosphoserine.
{ECO:0000250|UniProtKB:Q8NFD5}.
MOD_RES 1785 1785 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8NFD5}.
SEQUENCE 2244 AA; 237795 MW; 51AA79A5AE8B30A9 CRC64;
METGLLPNHK LKAVGEAPAA PPHQQHHHHH AHHHHHHHAH HLHHLHHHHA LQQQLNQFQQ
PQPPQPQQQQ PPPPPQQQHP TANNSLGGAG GGAPQPGPDM EQPQHGGAKD SVAGNQADPQ
GQPLLSKPGD EDDAPPKMGE PAGSRYEHPG LGAQQQPAPV AVPGGGGGPA AVSEFNNYYG
SAAPASGGPG GRAGPCFDQH GGQQSPGMGM MHSASAAAGA PSSMDPLQNS HEGYPNSQYN
HYPGYSRPGA GGGGGGGGGG GGSGGGGGGG GAGGAGGAAA AAAGAGAVAA AAAAAAAAAA
AAGGGGGGGY GSSSSGYGVL SSPRQQGGGM MMGPGGGGAA SLSKAAAGAA AAAGGFQRFA
GQNQHPSGAT PTLNQLLTSP SPMMRSYGGS YPDYSSSSAP PPPSQPQSQA AAGAAAGGQQ
AAAGMGLGKD LGAQYAAASP AWAAAQQRSH PAMSPGTPGP TMGRSQGSPM DPMVMKRPQL
YGMGTHPHSQ PQQSSPYPGG SYGPPGAQRY PLGMQGRAPG ALGGLQYPQQ QMPPQYGQQA
VSGYCQQGQQ PYYNQQPQPS HLPPQAQYLQ PAAAQSQQRY QPQQDMSQEG YGTRSQPPLA
PGKSNHEDLN LIQQERPSSL PDLSGSIDDL PTGTEATLSS AVSASGSTSS QGDQSNPAQS
PFSPHASPHL SSIPGGPSPS PVGSPVGSNQ SRSGPISPAS IPGSQMPPQP PGSQSESSSH
PALSQSPMPQ ERGFMTGTQR NPQMSQYGPQ QTGPSMSPHP SPGGQMHPGI SNFQQSNSSG
TYGPQMSQYG PQGNYSRTPT YSGVPSASYS GPGPGMGINA NNQMHGQGPA QPCGAMPLGR
MPSAGMQNRP FPGTMSSVTP SSPGMSQQGG PGMGPPMPTV NRKAQEAAAA VMQAAANSAQ
SRQGSFPGMN QSGLVASSSP YSQSMNNNSS LMSTQAQPYS MTPTMVNSST ASMGLADMMS
PSESKLSVPL KADGKEEGVS QPESKSKDSY GSQGISQPPT PGNLPVPSPM SPSSASISSF
HGDESDSISS PGWPKTPSSP KSSSSSTTGE KITKVYELGN EPERKLWVDR YLTFMEERGS
PVSSLPAVGK KPLDLFRLYV CVKEIGGLAQ VNKNKKWREL ATNLNVGTSS SAASSLKKQY
IQYLFAFECK TERGEEPPPE VFSTGDSKKQ PKLQPPSPAN SGSLQGPQTP QSTGSNSMAE
VPGDLKPPTP ASTPHGQMTP MQSGRSSTVS VHDPFSDVSD SAYPKRNSMT PNAPYQQGMG
MPDMMGRMPY EPNKDPFSGM RKVPGSSEPF MTQGQVPNSG MQDMYNQSPS GAMSNLGMGQ
RQQFPYGTSY DRRHEAYGQQ YPGQGPPTGQ PPYGGHQPGL YPQQPNYKRH MDGMYGPPAK
RHEGDMYNMQ YGSQQQEMYN QYGGSYSGPD RRPIQGQYPY PYNRERMQGP GQMQPHGIPP
QMMGGPMQSS SSEGPQQNMW ATRNDMPYPY QSRQGPGGPA QAPPYPGMNR TDDMMVPEQR
INHESQWPSH VSQRQPYMSS SASMQPITRP PQSSYQTPPS LPNHISRAPS PASFQRSLES
RMSPSKSPFL PTMKMQKVMP TVPTSQVTGP PPQPPPIRRE ITFPPGSVEA SQPILKQRRK
ITSKDIVTPE AWRVMMSLKS GLLAESTWAL DTINILLYDD STVATFNLSQ LSGFLELLVE
YFRKCLIDIF GILMEYEVGD PSQKALDHRS GKKDDSQSLE DDSGKEDDDA ECLVEEEEEE
EEEEEDSEKI ESEGKSSPAL AAPDASVDPK ETPKQASKFD KLPIKIVKKN KLFVVDRSDK
LGRVQEFSSG LLHWQLGGGD TTEHIQTHFE SKMEIPPRRR PPPPLSSTGK KKELEGKGDS
EEQPEKSIIA TIDDVLSARP GALPEDTNPG PQTDSGKFPF GIQQAKSHRN IRLLEDEPRS
RDETPLCTIA HWQDSLAKRC ICVSNIVRSL SFVPGNDAEM SKHPGLVLIL GKLILLHHEH
PERKRAPQTY EKEEDEDKGV ACSKDEWWWD CLEVLRDNTL VTLANISGQL DLSAYTESIC
LPILDGLLHW MVCPSAEAQD PFPTVGPNSV LSPQRLVLET LCKLSIQDNN VDLILATPPF
SRQEKFYATL VRYVGDRKNP VCREMSMALL SNLAQGDTLA ARAIAVQKGS IGNLISFLED
GVTMAQYQQS QHNLMHMQPP PLEPPSVDMM CRAAKALLAM ARVDENRSEF LLHEGRLLDI
SISAVLNSLV ASVICDVLFQ IGQL


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