ID E9Q6R4_MOUSE Unreviewed; 2243 AA.
AC E9Q6R4;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=AT rich interactive domain 1B (SWI-like) {ECO:0000313|Ensembl:ENSMUSP00000090398.5};
GN Name=Arid1b {ECO:0000313|Ensembl:ENSMUSP00000090398.5,
GN ECO:0000313|MGI:MGI:1926129};
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 {ECO:0000313|Ensembl:ENSMUSP00000090398.5, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0000313|Ensembl:ENSMUSP00000090398.5, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000090398.5,
RC ECO:0000313|Proteomes:UP000000589};
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 [2] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [3] {ECO:0007829|PubMed:24129315}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=24129315;
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 [4] {ECO:0000313|Ensembl:ENSMUSP00000090398.5}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000090398.5};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR SMR; E9Q6R4; -.
DR ComplexPortal; CPX-1234; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1235; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1238; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1239; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1242; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1243; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1246; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1247; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1254; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1255; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1258; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1259; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1263; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1264; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR iPTMnet; E9Q6R4; -.
DR EPD; E9Q6R4; -.
DR jPOST; E9Q6R4; -.
DR MaxQB; E9Q6R4; -.
DR ProteomicsDB; 363690; -.
DR Antibodypedia; 19980; 197 antibodies from 27 providers.
DR Ensembl; ENSMUST00000092723.11; ENSMUSP00000090398.5; ENSMUSG00000069729.15.
DR AGR; MGI:1926129; -.
DR MGI; MGI:1926129; Arid1b.
DR VEuPathDB; HostDB:ENSMUSG00000069729; -.
DR GeneTree; ENSGT00940000155634; -.
DR ChiTaRS; Arid1b; mouse.
DR Proteomes; UP000000589; Chromosome 17.
DR Bgee; ENSMUSG00000069729; Expressed in rostral migratory stream and 234 other cell types or tissues.
DR ExpressionAtlas; E9Q6R4; baseline and differential.
DR GO; GO:0140092; C:bBAF complex; NAS:ComplexPortal.
DR GO; GO:0035060; C:brahma complex; NAS:ComplexPortal.
DR GO; GO:0000785; C:chromatin; NAS:ComplexPortal.
DR GO; GO:0071565; C:nBAF complex; NAS:ComplexPortal.
DR GO; GO:0071564; C:npBAF complex; NAS:ComplexPortal.
DR GO; GO:0016514; C:SWI/SNF complex; NAS:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0006338; P:chromatin remodeling; NAS:ComplexPortal.
DR GO; GO:0045597; P:positive regulation of cell differentiation; NAS:ComplexPortal.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; NAS:ComplexPortal.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; NAS:ComplexPortal.
DR GO; GO:0045582; P:positive regulation of T cell differentiation; NAS:ComplexPortal.
DR GO; GO:0070316; P:regulation of G0 to G1 transition; NAS:ComplexPortal.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; NAS:ComplexPortal.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; NAS:ComplexPortal.
DR GO; GO:2000819; P:regulation of nucleotide-excision repair; NAS:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; NAS:ComplexPortal.
DR CDD; cd16877; ARID_ARID1B; 1.
DR Gene3D; 1.10.150.60; ARID DNA-binding domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR038040; ARID_ARID1B.
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 PANTHER; PTHR12656:SF11; AT-RICH INTERACTIVE DOMAIN-CONTAINING PROTEIN 1B; 1.
DR PANTHER; PTHR12656; BRG-1 ASSOCIATED FACTOR 250 BAF250; 1.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF12031; BAF250_C; 1.
DR SMART; SM01014; ARID; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SUPFAM; SSF46774; ARID-like; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR PROSITE; PS51011; ARID; 1.
PE 1: Evidence at protein level;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Proteomics identification {ECO:0007829|EPD:E9Q6R4,
KW ECO:0007829|MaxQB:E9Q6R4};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT DOMAIN 1060..1151
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1012..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1153..1260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1285..1324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1404..1571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1702..1775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1828..1866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1878..1898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..102
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..131
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..719
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1035
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1052
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1166..1198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1214..1254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1287..1324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1443..1468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1501..1530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1537..1569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1702..1719
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1720..1748
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1849..1866
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2243 AA; 237020 MW; AF09D60CABA0235B CRC64;
MAHSASAAAA ASSNSAQSGR SEAALKEGGS AAALSSSAAV AASSSSAGPG STMETGLLPN
HKLKAVGEAP AAPPHQQHHH HHAHHHHHHH AHHLHHLHHH HALQQQLNQF QQPQPPQPQQ
QQPPPPPQQQ HPTANNSLGG AGGGAPQPGP DMEQPQHGGA KDSVAGNQAD PQGQPLLSKP
GDEDDAPPKM GEPAGSRYEH PGLGAQQQPA PVAVPGGGGG PAAVSEFNNY YGSAAPASGG
PGGRAGPCFD QHGGQQSPGM GMMHSASAAA GAPSSMDPLQ NSHEGYPNSQ YNHYPGYSRP
GAGGGGGGGG GGGGSGGGGG GGGAGGAGGA AAAAAGAGAV AAAAAAAAAA AAAAGGGGGG
GYGSSSSGYG VLSSPRQQGG GMMMGPGGGG AASLSKAAAG AAAAAGGFQR FAGQNQHPSG
ATPTLNQLLT SPSPMMRSYG GSYPDYSSSS APPPPSQPQS QAAAGAAAGG QQAAAGMGLG
KDLGAQYAAA SPAWAAAQQR SHPAMSPGTP GPTMGRSQGS PMDPMVMKRP QLYGMGTHPH
SQPQQSSPYP GGSYGPPGAQ RYPLGMQGRA PGALGGLQYP QQQMPPQYGQ QAVSGYCQQG
QQPYYNQQPQ PSHLPPQAQY LQPAAAQSQQ RYQPQQDMSQ EGYGTRSQPP LAPGKSNHED
LNLIQQERPS SLPDLSGSID DLPTGTEATL SSAVSASGST SSQGDQSNPA QSPFSPHASP
HLSSIPGGPS PSPVGSPVGS NQSRSGPISP ASIPGSQMPP QPPGSQSESS SHPALSQSPM
PQERGFMTGT QRNPQMSQYG PQQTGPSMSP HPSPGGQMHP GISNFQQSNS SGTYGPQMSQ
YGPQGNYSRT PTYSGVPSAS YSGPGPGMGI NANNQMHGQG PAQPCGAMPL GRMPSAGMQN
RPFPGTMSSV TPSSPGMSQQ GGPGMGPPMP TVNRKAQEAA AAVMQAAANS AQSRQGSFPG
MNQSGLVASS SPYSQSMNNN SSLMSTQAQP YSMTPTMVNS STASMGLADM MSPSESKLSV
PLKADGKEEG VSQPESKSKK SSSSSTTGEK ITKVYELGNE PERKLWVDRY LTFMEERGSP
VSSLPAVGKK PLDLFRLYVC VKEIGGLAQV NKNKKWRELA TNLNVGTSSS AASSLKKQYI
QYLFAFECKT ERGEEPPPEV FSTGDSKKQP KLQPPSPANS GSLQGPQTPQ STGSNSMAEV
PGDLKPPTPA STPHGQMTPM QSGRSSTVSV HDPFSDVSDS AYPKRNSMTP NAPYQQGMGM
PDMMGRMPYE PNKDPFSGMR KVPGSSEPFM TQGQVPNSGM QDMYNQSPSG AMSNLGMGQR
QQFPYGTSYD RRHEAYGQQY PGQGPPTGQP PYGGHQPGLY PQQPNYKRHM DGMYGPPAKR
HEGDMYNMQY GSQQQEMYNQ YGGSYSGPDR RPIQGQYPYP YNRERMQGPG QMQPHGIPPQ
MMGGPMQSSS SEGPQQNMWA TRNDMPYPYQ SRQGPGGPAQ APPYPGMNRT DDMMVPEQRI
NHESQWPSHV SQRQPYMSSS ASMQPITRPP QSSYQTPPSL PNHISRAPSP ASFQRSLESR
MSPSKSPFLP TMKMQKVMPT VPTSQVTGPP PQPPPIRREI TFPPGSVEAS QPILKQRRKI
TSKDIVTPEA WRVMMSLKSG LLAESTWALD TINILLYDDS TVATFNLSQL SGFLELLVEY
FRKCLIDIFG ILMEYEVGDP SQKALDHRSG KKDDSQSLED DSGKEDDDAE CLVEEEEEEE
EEEEDSEKIE SEGKSSPALA APDASVDPKE TPKQASKFDK LPIKIVKKNK LFVVDRSDKL
GRVQEFSSGL LHWQLGGGDT TEHIQTHFES KMEIPPRRRP PPPLSSTGKK KELEGKGDSE
EQPEKSIIAT IDDVLSARPG ALPEDTNPGP QTDSGKFPFG IQQAKSHRNI RLLEDEPRSR
DETPLCTIAH WQDSLAKRCI CVSNIVRSLS FVPGNDAEMS KHPGLVLILG KLILLHHEHP
ERKRAPQTYE KEEDEDKGVA CSKDEWWWDC LEVLRDNTLV TLANISGQLD LSAYTESICL
PILDGLLHWM VCPSAEAQDP FPTVGPNSVL SPQRLVLETL CKLSIQDNNV DLILATPPFS
RQEKFYATLV RYVGDRKNPV CREMSMALLS NLAQGDTLAA RAIAVQKGSI GNLISFLEDG
VTMAQYQQSQ HNLMHMQPPP LEPPSVDMMC RAAKALLAMA RVDENRSEFL LHEGRLLDIS
ISAVLNSLVA SVICDVLFQI GQL
//
