ARID2_MOUSE
ID ARID2_MOUSE Reviewed; 1828 AA.
AC E9Q7E2;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=AT-rich interactive domain-containing protein 2;
DE Short=ARID domain-containing protein 2 {ECO:0000305};
DE AltName: Full=BRG1-associated factor 200 {ECO:0000305};
DE Short=BAF200 {ECO:0000305};
DE AltName: Full=Zinc finger protein with activation potential {ECO:0000305};
DE AltName: Full=Zipzap/p200 {ECO:0000303|PubMed:16782067};
GN Name=Arid2 {ECO:0000312|MGI:MGI:1924294}; Synonyms=Baf200 {ECO:0000305};
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 [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 [2]
RP TISSUE SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=16782067; DOI=10.1016/j.bbrc.2006.05.211;
RA Zhang X., Azhar G., Zhong Y., Wei J.Y.;
RT "Zipzap/p200 is a novel zinc finger protein contributing to cardiac gene
RT regulation.";
RL Biochem. Biophys. Res. Commun. 346:794-801(2006).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [4]
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 [5]
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).
CC -!- FUNCTION: Involved in transcriptional activation and repression of
CC select genes by chromatin remodeling (alteration of DNA-nucleosome
CC topology). Required for the stability of the SWI/SNF chromatin
CC remodeling complex SWI/SNF-B (PBAF). May be involved in targeting the
CC complex to different genes. May be involved in regulating
CC transcriptional activation of cardiac genes.
CC {ECO:0000250|UniProtKB:Q68CP9, ECO:0000303|PubMed:22952240,
CC ECO:0000303|PubMed:26601204}.
CC -!- SUBUNIT: Component of the SWI/SNF-B (PBAF) chromatin remodeling
CC complex, at least composed of SMARCA4/BRG1, SMARCB1/BAF47/SNF5,
CC ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCE1/BAF57, SMARCD1/BAF60A,
CC SMARCD2/BAF60B, perhaps SMARCD3/BAF60C, SMARCC1/BAF155, SMARCC2/BAF170,
CC PBRM1/BAF180, ARID2/BAF200 and actin. Interacts with SRF. Forms
CC complexes with SRF and SRF cofactors MYOCD, NKX2-5 and SRFBP1.
CC {ECO:0000250|UniProtKB:Q68CP9, ECO:0000303|PubMed:22952240,
CC ECO:0000303|PubMed:26601204}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355,
CC ECO:0000255|PROSITE-ProRule:PRU00858}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, expressed in heart,
CC liver and kidney. {ECO:0000269|PubMed:16782067}.
CC -!- SIMILARITY: Belongs to the RFX family. {ECO:0000255|PROSITE-
CC ProRule:PRU00858}.
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DR EMBL; AC133578; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS37185.2; -.
DR RefSeq; NP_780460.3; NM_175251.4.
DR AlphaFoldDB; E9Q7E2; -.
DR ComplexPortal; CPX-1248; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A variant.
DR ComplexPortal; CPX-1250; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B variant.
DR CORUM; E9Q7E2; -.
DR STRING; 10090.ENSMUSP00000093969; -.
DR iPTMnet; E9Q7E2; -.
DR PhosphoSitePlus; E9Q7E2; -.
DR EPD; E9Q7E2; -.
DR MaxQB; E9Q7E2; -.
DR PaxDb; E9Q7E2; -.
DR PeptideAtlas; E9Q7E2; -.
DR PRIDE; E9Q7E2; -.
DR ProteomicsDB; 277289; -.
DR Antibodypedia; 25264; 142 antibodies from 19 providers.
DR Ensembl; ENSMUST00000096250; ENSMUSP00000093969; ENSMUSG00000033237.
DR GeneID; 77044; -.
DR KEGG; mmu:77044; -.
DR UCSC; uc007xkd.2; mouse.
DR CTD; 196528; -.
DR MGI; MGI:1924294; Arid2.
DR VEuPathDB; HostDB:ENSMUSG00000033237; -.
DR eggNOG; KOG2312; Eukaryota.
DR eggNOG; KOG2744; Eukaryota.
DR GeneTree; ENSGT00390000016138; -.
DR HOGENOM; CLU_003714_0_0_1; -.
DR InParanoid; E9Q7E2; -.
DR OMA; HTAYHAI; -.
DR OrthoDB; 39440at2759; -.
DR PhylomeDB; E9Q7E2; -.
DR TreeFam; TF106406; -.
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; 77044; 12 hits in 77 CRISPR screens.
DR ChiTaRS; Arid2; mouse.
DR PRO; PR:E9Q7E2; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; E9Q7E2; protein.
DR Bgee; ENSMUSG00000033237; Expressed in rostral migratory stream and 259 other tissues.
DR ExpressionAtlas; E9Q7E2; baseline and differential.
DR Genevisible; E9Q7E2; MM.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0000776; C:kinetochore; IC:ComplexPortal.
DR GO; GO:0016363; C:nuclear matrix; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0016586; C:RSC-type complex; IC:ComplexPortal.
DR GO; GO:0016514; C:SWI/SNF complex; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; IMP:MGI.
DR GO; GO:0006338; P:chromatin remodeling; IC:ComplexPortal.
DR GO; GO:0072359; P:circulatory system development; IMP:MGI.
DR GO; GO:0060982; P:coronary artery morphogenesis; IMP:MGI.
DR GO; GO:0048568; P:embryonic organ development; IMP:MGI.
DR GO; GO:0003007; P:heart morphogenesis; IMP:MGI.
DR GO; GO:0042592; P:homeostatic process; IMP:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0006337; P:nucleosome disassembly; ISO: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:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISO:MGI.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IC:ComplexPortal.
DR GO; GO:0045582; P:positive regulation of T cell differentiation; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
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; IC:ComplexPortal.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.150.60; -; 1.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003150; DNA-bd_RFX.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF02257; RFX_DNA_binding; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SUPFAM; SSF46774; SSF46774; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51526; RFX_DBD; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromatin regulator; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q68CP9"
FT CHAIN 2..1828
FT /note="AT-rich interactive domain-containing protein 2"
FT /id="PRO_0000442429"
FT DOMAIN 13..105
FT /note="ARID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT DNA_BIND 524..603
FT /note="RFX-type winged-helix"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00858"
FT ZN_FING 1626..1651
FT /note="C2H2-type"
FT /evidence="ECO:0000250|UniProtKB:Q68CP9"
FT REGION 824..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 962..1028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1245..1339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1360..1462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1483..1503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1566..1618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1697..1726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 313..317
FT /note="LXXLL"
FT /evidence="ECO:0000250|UniProtKB:Q68CP9"
FT COMPBIAS 982..1028
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1245..1262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1264..1321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1368..1405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1415..1462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1488..1503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1566..1585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1596..1618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1700..1718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q68CP9"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68CP9"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68CP9"
FT MOD_RES 635
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68CP9"
FT MOD_RES 653
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q68CP9"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68CP9"
FT MOD_RES 692
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q68CP9"
FT MOD_RES 1294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68CP9"
FT MOD_RES 1385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68CP9"
FT MOD_RES 1491
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68CP9"
FT CROSSLNK 7
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q68CP9"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q68CP9"
FT CROSSLNK 119
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q68CP9"
FT CROSSLNK 555
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q68CP9"
FT CROSSLNK 1695
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q68CP9"
FT CROSSLNK 1710
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q68CP9"
FT CROSSLNK 1725
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q68CP9"
SQ SEQUENCE 1828 AA; 195988 MW; 1BC23646CFA2F68D CRC64;
MANSTGKAPP DERRKGLAFL DELRQFHHSR GSPFKKIPAV GGKELDLHGL YTRVTTLGGF
AKVSEKNQWG EIVEEFNFPR SCSNAAFALK QYYLRYLEKY EKVHHFGEDD DEVPPGNPKP
QLPIGAIPSS YNYQQHSVSD YLRQSYGLSM DFNSPNDYNK LVLSLLSGLP NEVDFAINVC
TLLSNESKHV MQLEKDPKII TLLLANAGVF DDTLGSFSSV FGEEWREKTD RDFVKFWKDI
VDDNEVRDLI SDRNKAHEDT PGEWIWESLF HPPRKLGIND IEGQRVLQIA VILRNLSFEE
SNVKLLAANR TCLRFLLLSA HSHFISLRQL GLDTLGNIAA ELLLDPVDFR TTHLMFHTVT
KCLMSRDRFL KMRGMEILGN LCKAEDNGVL ICEYVDQDSY REIICHLTLP DVLLVTSTLE
VLYMLTEMGD VACTKIAKVE KSIDVLVCLV SMDAQMFGPD ALAAVKLIEH PSSSHQVLSE
IRPQAIEQVQ TQTHIASGPA SRAVVAQHAA PPPGIVEIDS EKFACQWLNA HFEVNPDCSV
SRAEMYSEYL STCSKLARGG ILTSTGFYKC LRTVFPNHTV KRVEDSTSSG QAHIHVIGVK
RRALPLPIQM YYQQQPISTP VVRVDAVADL SPTPSPAGIP HGPQAAGNHF QRTPVTNQSS
NLTATQMSFP VQGIHTVAQT VSRIPPNPSV HTHQQQNSPV TVIQNKAPIP CEVVKATVIQ
NSVPQTAVPV SISVGGAPAQ NSVGQNHSAG PQPVTVVNSQ TLLHHPSVMP QPSPLHTVVP
GQVPSGTPVT VIQQTVPQSR MFGRVQSIPA CTSTVSQGQQ LITTSPQPMH TSSQQTAAGS
QPQDTVIIAP PQYVTTSASN IVSATSVQNF QVATGQVVTI AGVPSPQPSR VGFQNIAPKP
LPSQQVSPSV VQQPIQQPQQ PAQQSVVIVS QPAQQGQAYA PAIHQIVLAN PAALPAGQTV
QLTGQPNITP SSSPSPVPPT NNQVPTAMSS SSTLQSQGPP PTVSQMLSVK RQQQQQHSPA
APAQQVQVQV QQPQQVQVQV QPQQPSAGVG QPAPNESSLI KQLLLPKRGP STPGGKLILP
APQIPPPNNA RAPSPQVVYQ VANNQAAGFG VQGQTPAQQL LVGQQNVQLV QSAMPPAGGV
QTVPISNLQI LPGPLISNSP ATIFQGTSGN QVTITVVPNT SFATATVSQG NAAQLIAPAG
LSMSGAQASA GLQVQTLPAG QSACTTAPLP FKGDKIICQK EEEAKEATGL HVHERKIEVM
ENPSCRRGTT NTSNGDTSES ELQVGSLLNG RKYSDSSLPP SNSGKLQSET SQCSLISNGP
SLELGENGAP GKQNSEPVDM QDVKGDLKKA LVNGICDFDK GDGSHLSKNI PNHKTSNHVG
NGEISPVEPQ GTSGATQQDT AKGDQLERVS NGPVLTLGGS PSTSSMQEAP SVATPPLSGT
DLPNGPLASS LNSDVPQQRP SVVVSPHSTA PVIQGHQVIA VPHSGPRVTP SALSSDARST
NGTAECKTVK RPAEDNDRDT VPGIPNKVGV RIVTISDPNN AGCSATMVAV PAGADPSTVA
KVAIESAAQQ KQQHPPTYMQ SVAPQNTPMP PSPAVQVQGQ PSSSQPSPVS ASSQHADPVR
KPGQNFMCLW QSCKKWFQTP SQVFYHAATE HGGKDVYPGQ CLWEGCEPFQ RQRFSFITHL
QDKHCSKDAL LAGLKQDEPG QVANQKSSTK QPTVGGTGSA PRAQKAIASH PSAALMALRR
GSRNLVFRDF TDEKEGPITK HIRLTAALIL KNIGKYSECG RRLLKRHENN LSVLAISNME
ASSTLAKCLY ELNFTVQSKE QEKDSEML
