ID ARID2_HUMAN Reviewed; 1835 AA.
AC Q68CP9; Q15KG9; Q5EB51; Q645I3; Q6ZRY5; Q7Z3I5; Q86T28; Q96SJ6; Q9HCL5;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 27-MAR-2024, entry version 177.
DE RecName: Full=AT-rich interactive domain-containing protein 2 {ECO:0000305};
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|HGNC:HGNC:18037}; Synonyms=BAF200, KIAA1557;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH SRF,
RP SUBUNIT, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-1093, AND DNA-BINDING.
RX PubMed=15640446; DOI=10.1093/nar/gki145;
RA Patsialou A., Wilsker D., Moran E.;
RT "DNA-binding properties of ARID family proteins.";
RL Nucleic Acids Res. 33:66-80(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 28-1835 (ISOFORM 2), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 150-1835 (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 950-1835 (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 976-1835 (ISOFORM 1).
RC TISSUE=Testis;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1030-1835 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631; SER-635; THR-653;
RP SER-689; THR-692 AND SER-1496, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635; SER-689 AND SER-1496,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-631; SER-1300;
RP SER-1391 AND SER-1496, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-7; LYS-15; LYS-119; LYS-555;
RP LYS-1701; LYS-1716 AND LYS-1731, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [13]
RP REVIEW ON SWI/SNF CHROMATIN REMODELING COMPLEXES.
RX PubMed=12672490; DOI=10.1016/s0959-437x(03)00022-4;
RA Martens J.A., Winston F.;
RT "Recent advances in understanding chromatin remodeling by SWI/SNF
RT complexes.";
RL Curr. Opin. Genet. Dev. 13:136-142(2003).
RN [14]
RP IDENTIFICATION IN THE PBAF COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15985610; DOI=10.1101/gad.1323805;
RA Yan Z., Cui K., Murray D.M., Ling C., Xue Y., Gerstein A., Parsons R.,
RA Zhao K., Wang W.;
RT "PBAF chromatin-remodeling complex requires a novel specificity subunit,
RT BAF200, to regulate expression of selective interferon-responsive genes.";
RL Genes Dev. 19:1662-1667(2005).
RN [15]
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 [16]
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 [17]
RP INVOLVEMENT IN CSS6, AND VARIANTS CSS6 343-LEU--GLN-1835 DEL AND
RP 1440-GLN--GLN-1835 DEL.
RX PubMed=26238514; DOI=10.1007/s10048-015-0454-0;
RA Shang L., Cho M.T., Retterer K., Folk L., Humberson J., Rohena L.,
RA Sidhu A., Saliganan S., Iglesias A., Vitazka P., Juusola J.,
RA O'Donnell-Luria A.H., Shen Y., Chung W.K.;
RT "Mutations in ARID2 are associated with intellectual disabilities.";
RL Neurogenetics 16:307-314(2015).
RN [18]
RP INVOLVEMENT IN CSS6.
RX PubMed=28884947; DOI=10.1002/ajmg.a.38407;
RA Van Paemel R., De Bruyne P., van der Straaten S., D'hondt M., Fraenkel U.,
RA Dheedene A., Menten B., Callewaert B.;
RT "Confirmation of an ARID2 defect in SWI/SNF-related intellectual
RT disability.";
RL Am. J. Med. Genet. A 173:3104-3108(2017).
RN [19]
RP INVOLVEMENT IN CSS6.
RX PubMed=28124119; DOI=10.1007/s00439-017-1757-z;
RA Bramswig N.C., Caluseriu O., Luedecke H.J., Bolduc F.V., Noel N.C.,
RA Wieland T., Surowy H.M., Christen H.J., Engels H., Strom T.M.,
RA Wieczorek D.;
RT "Heterozygosity for ARID2 loss-of-function mutations in individuals with a
RT Coffin-Siris syndrome-like phenotype.";
RL Hum. Genet. 136:297-305(2017).
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:0000269|PubMed:16782067, 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:0000269|PubMed:15985610, ECO:0000269|PubMed:16782067,
CC ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}.
CC -!- INTERACTION:
CC Q68CP9; Q86U86: PBRM1; NbExp=5; IntAct=EBI-637818, EBI-637807;
CC Q68CP9; P51532: SMARCA4; NbExp=9; IntAct=EBI-637818, EBI-302489;
CC Q68CP9; Q12824: SMARCB1; NbExp=13; IntAct=EBI-637818, EBI-358419;
CC Q68CP9; Q969G3: SMARCE1; NbExp=5; IntAct=EBI-637818, EBI-455078;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q68CP9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q68CP9-3; Sequence=VSP_015230;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart.
CC {ECO:0000269|PubMed:16782067}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated in adult heart (at protein level).
CC {ECO:0000269|PubMed:16782067}.
CC -!- DISEASE: Coffin-Siris syndrome 6 (CSS6) [MIM:617808]: A form of Coffin-
CC Siris syndrome, a congenital multiple malformation syndrome with broad
CC phenotypic and genetic variability. Cardinal features are intellectual
CC disability, coarse facial features, hypertrichosis, and hypoplastic or
CC absent fifth digit nails or phalanges. Additional features include
CC malformations of the cardiac, gastrointestinal, genitourinary, and/or
CC central nervous systems. Sucking/feeding difficulties, poor growth,
CC ophthalmologic abnormalities, hearing impairment, and spinal anomalies
CC are common findings. Both autosomal dominant and autosomal recessive
CC inheritance patterns have been reported. CSS6 inheritance is autosomal
CC dominant. {ECO:0000269|PubMed:26238514, ECO:0000269|PubMed:28124119,
CC ECO:0000269|PubMed:28884947}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB55320.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC87171.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; DQ096628; AAZ74794.1; -; mRNA.
DR EMBL; AY727870; AAU20329.3; -; mRNA.
DR EMBL; AL832200; CAD91164.1; -; mRNA.
DR EMBL; BX537879; CAD97878.1; -; mRNA.
DR EMBL; CR749833; CAH18689.1; -; mRNA.
DR EMBL; AK027718; BAB55320.1; ALT_INIT; mRNA.
DR EMBL; AK127872; BAC87171.1; ALT_SEQ; mRNA.
DR EMBL; BC090062; AAH90062.1; -; mRNA.
DR EMBL; AB046777; BAB13383.1; -; mRNA.
DR CCDS; CCDS31783.1; -. [Q68CP9-1]
DR RefSeq; NP_001334768.1; NM_001347839.1.
DR RefSeq; NP_689854.2; NM_152641.3. [Q68CP9-1]
DR PDB; 7VDV; EM; 3.40 A; Q=1-689.
DR PDB; 7Y8R; EM; 4.40 A; L=1-1835.
DR PDBsum; 7VDV; -.
DR PDBsum; 7Y8R; -.
DR AlphaFoldDB; Q68CP9; -.
DR EMDB; EMD-31926; -.
DR EMDB; EMD-33684; -.
DR SMR; Q68CP9; -.
DR BioGRID; 128219; 142.
DR ComplexPortal; CPX-1196; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B variant.
DR ComplexPortal; CPX-1199; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A variant.
DR CORUM; Q68CP9; -.
DR DIP; DIP-33391N; -.
DR IntAct; Q68CP9; 79.
DR MINT; Q68CP9; -.
DR STRING; 9606.ENSP00000335044; -.
DR GlyCosmos; Q68CP9; 2 sites, 1 glycan.
DR GlyGen; Q68CP9; 16 sites, 1 O-linked glycan (16 sites).
DR iPTMnet; Q68CP9; -.
DR MetOSite; Q68CP9; -.
DR PhosphoSitePlus; Q68CP9; -.
DR SwissPalm; Q68CP9; -.
DR BioMuta; ARID2; -.
DR DMDM; 73921721; -.
DR EPD; Q68CP9; -.
DR jPOST; Q68CP9; -.
DR MassIVE; Q68CP9; -.
DR MaxQB; Q68CP9; -.
DR PaxDb; 9606-ENSP00000335044; -.
DR PeptideAtlas; Q68CP9; -.
DR ProteomicsDB; 66011; -. [Q68CP9-1]
DR ProteomicsDB; 66013; -. [Q68CP9-3]
DR Pumba; Q68CP9; -.
DR Antibodypedia; 25264; 160 antibodies from 19 providers.
DR DNASU; 196528; -.
DR Ensembl; ENST00000334344.11; ENSP00000335044.6; ENSG00000189079.18. [Q68CP9-1]
DR GeneID; 196528; -.
DR KEGG; hsa:196528; -.
DR MANE-Select; ENST00000334344.11; ENSP00000335044.6; NM_152641.4; NP_689854.2.
DR UCSC; uc001ros.2; human. [Q68CP9-1]
DR AGR; HGNC:18037; -.
DR CTD; 196528; -.
DR DisGeNET; 196528; -.
DR GeneCards; ARID2; -.
DR GeneReviews; ARID2; -.
DR HGNC; HGNC:18037; ARID2.
DR HPA; ENSG00000189079; Low tissue specificity.
DR MalaCards; ARID2; -.
DR MIM; 609539; gene.
DR MIM; 617808; phenotype.
DR neXtProt; NX_Q68CP9; -.
DR OpenTargets; ENSG00000189079; -.
DR Orphanet; 1465; Coffin-Siris syndrome.
DR PharmGKB; PA134916396; -.
DR VEuPathDB; HostDB:ENSG00000189079; -.
DR eggNOG; KOG2312; Eukaryota.
DR eggNOG; KOG2744; Eukaryota.
DR GeneTree; ENSGT00390000016138; -.
DR HOGENOM; CLU_003714_0_0_1; -.
DR InParanoid; Q68CP9; -.
DR OMA; NGQKCME; -.
DR OrthoDB; 5001776at2759; -.
DR PhylomeDB; Q68CP9; -.
DR TreeFam; TF106406; -.
DR PathwayCommons; Q68CP9; -.
DR Reactome; R-HSA-3214858; RMTs methylate histone arginines.
DR Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR SignaLink; Q68CP9; -.
DR SIGNOR; Q68CP9; -.
DR BioGRID-ORCS; 196528; 240 hits in 1210 CRISPR screens.
DR ChiTaRS; ARID2; human.
DR GeneWiki; ARID2; -.
DR GenomeRNAi; 196528; -.
DR Pharos; Q68CP9; Tbio.
DR PRO; PR:Q68CP9; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q68CP9; Protein.
DR Bgee; ENSG00000189079; Expressed in sperm and 189 other cell types or tissues.
DR ExpressionAtlas; Q68CP9; baseline and differential.
DR Genevisible; Q68CP9; HS.
DR GO; GO:0000785; C:chromatin; NAS:ComplexPortal.
DR GO; GO:0000776; C:kinetochore; NAS:ComplexPortal.
DR GO; GO:0016363; C:nuclear matrix; NAS:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0016586; C:RSC-type complex; NAS:ComplexPortal.
DR GO; GO:0016514; C:SWI/SNF complex; IDA:BHF-UCL.
DR GO; GO:0003677; F:DNA binding; IDA:GDB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0006338; P:chromatin remodeling; NAS:ComplexPortal.
DR GO; GO:0060982; P:coronary artery morphogenesis; IEA:Ensembl.
DR GO; GO:0048568; P:embryonic organ development; IEA:Ensembl.
DR GO; GO:0003007; P:heart morphogenesis; IEA:Ensembl.
DR GO; GO:0042592; P:homeostatic process; IEA:Ensembl.
DR GO; GO:0030336; P:negative regulation of cell migration; IDA:BHF-UCL.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:BHF-UCL.
DR GO; GO:0006337; P:nucleosome disassembly; IDA:BHF-UCL.
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:1905168; P:positive regulation of double-strand break repair via homologous recombination; IMP:CACAO.
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; cd16866; ARID_ARID2; 1.
DR Gene3D; 1.10.150.60; ARID DNA-binding domain; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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 PANTHER; PTHR22970; AT-RICH INTERACTIVE DOMAIN-CONTAINING PROTEIN 2; 1.
DR PANTHER; PTHR22970:SF14; AT-RICH INTERACTIVE DOMAIN-CONTAINING PROTEIN 2; 1.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF02257; RFX_DNA_binding; 1.
DR SMART; SM01014; ARID; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SUPFAM; SSF46774; ARID-like; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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 3D-structure; Acetylation; Alternative splicing; Chromatin regulator;
KW Disease variant; DNA-binding; Intellectual disability; 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:0007744|PubMed:22814378"
FT CHAIN 2..1835
FT /note="AT-rich interactive domain-containing protein 2"
FT /id="PRO_0000200577"
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 1632..1657
FT /note="C2H2-type"
FT REGION 819..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 962..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1266..1287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1295..1314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1321..1341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1488..1522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1572..1629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1703..1728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 313..317
FT /note="LXXLL"
FT COMPBIAS 1271..1286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1296..1314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1493..1512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1572..1591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1602..1625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1706..1728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 635
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 653
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 692
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1391
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1496
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT CROSSLNK 7
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 119
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 555
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1701
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1716
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1731
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1784..1835
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_015230"
FT VARIANT 343..1835
FT /note="Missing (in CSS6)"
FT /evidence="ECO:0000269|PubMed:26238514"
FT /id="VAR_080566"
FT VARIANT 1440..1835
FT /note="Missing (in CSS6)"
FT /evidence="ECO:0000269|PubMed:26238514"
FT /id="VAR_080567"
FT CONFLICT 169
FT /note="L -> P (in Ref. 3; CAH18689)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="F -> L (in Ref. 3; CAD91164)"
FT /evidence="ECO:0000305"
FT CONFLICT 665
FT /note="T -> I (in Ref. 3; CAD91164)"
FT /evidence="ECO:0000305"
FT CONFLICT 801
FT /note="M -> T (in Ref. 1; AAZ74794)"
FT /evidence="ECO:0000305"
FT CONFLICT 825
FT /note="S -> P (in Ref. 3; CAH18689)"
FT /evidence="ECO:0000305"
FT CONFLICT 906
FT /note="V -> F (in Ref. 3; CAD91164)"
FT /evidence="ECO:0000305"
FT CONFLICT 956
FT /note="A -> V (in Ref. 3; CAD91164)"
FT /evidence="ECO:0000305"
FT CONFLICT 988
FT /note="M -> T (in Ref. 3; CAH18689)"
FT /evidence="ECO:0000305"
FT CONFLICT 989
FT /note="S -> P (in Ref. 3; CAD97878)"
FT /evidence="ECO:0000305"
FT CONFLICT 1035
FT /note="Q -> R (in Ref. 4; BAB55320)"
FT /evidence="ECO:0000305"
FT CONFLICT 1062
FT /note="Q -> R (in Ref. 3; CAH18689)"
FT /evidence="ECO:0000305"
FT CONFLICT 1204
FT /note="S -> G (in Ref. 3; CAD97878)"
FT /evidence="ECO:0000305"
FT CONFLICT 1292
FT /note="S -> N (in Ref. 3; CAD97878)"
FT /evidence="ECO:0000305"
FT CONFLICT 1460
FT /note="V -> A (in Ref. 3; CAD97878)"
FT /evidence="ECO:0000305"
FT CONFLICT 1543
FT /note="D -> G (in Ref. 3; CAD91164)"
FT /evidence="ECO:0000305"
FT CONFLICT 1543
FT /note="D -> N (in Ref. 4; BAC87171)"
FT /evidence="ECO:0000305"
FT CONFLICT 1647
FT /note="S -> P (in Ref. 3; CAD97878)"
FT /evidence="ECO:0000305"
FT CONFLICT 1700
FT /note="L -> S (in Ref. 3; CAD91164)"
FT /evidence="ECO:0000305"
FT HELIX 20..29
FT /evidence="ECO:0007829|PDB:7VDV"
FT TURN 47..52
FT /evidence="ECO:0007829|PDB:7VDV"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:7VDV"
FT HELIX 60..66
FT /evidence="ECO:0007829|PDB:7VDV"
FT HELIX 69..75
FT /evidence="ECO:0007829|PDB:7VDV"
FT HELIX 85..103
FT /evidence="ECO:0007829|PDB:7VDV"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:7VDV"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:7VDV"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:7VDV"
FT HELIX 141..146
FT /evidence="ECO:0007829|PDB:7VDV"
FT HELIX 159..167
FT /evidence="ECO:0007829|PDB:7VDV"
FT HELIX 170..184
FT /evidence="ECO:0007829|PDB:7VDV"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:7VDV"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:7VDV"
FT HELIX 199..207
FT /evidence="ECO:0007829|PDB:7VDV"
FT TURN 218..221
FT /evidence="ECO:0007829|PDB:7VDV"
FT HELIX 223..229
FT /evidence="ECO:0007829|PDB:7VDV"
FT HELIX 233..240
FT /evidence="ECO:0007829|PDB:7VDV"
FT HELIX 244..250
FT /evidence="ECO:0007829|PDB:7VDV"
FT HELIX 281..297
FT /evidence="ECO:0007829|PDB:7VDV"
FT HELIX 300..308
FT /evidence="ECO:0007829|PDB:7VDV"
FT HELIX 311..320
FT /evidence="ECO:0007829|PDB:7VDV"
FT HELIX 325..338
FT /evidence="ECO:0007829|PDB:7VDV"
FT TURN 339..341
FT /evidence="ECO:0007829|PDB:7VDV"
FT HELIX 349..360
FT /evidence="ECO:0007829|PDB:7VDV"
FT TURN 361..363
FT /evidence="ECO:0007829|PDB:7VDV"
FT STRAND 364..367
FT /evidence="ECO:0007829|PDB:7VDV"
FT HELIX 368..381
FT /evidence="ECO:0007829|PDB:7VDV"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:7VDV"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:7VDV"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:7VDV"
FT STRAND 397..399
FT /evidence="ECO:0007829|PDB:7VDV"
FT HELIX 400..405
FT /evidence="ECO:0007829|PDB:7VDV"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:7VDV"
FT HELIX 412..428
FT /evidence="ECO:0007829|PDB:7VDV"
FT HELIX 430..438
FT /evidence="ECO:0007829|PDB:7VDV"
FT HELIX 443..451
FT /evidence="ECO:0007829|PDB:7VDV"
FT HELIX 461..464
FT /evidence="ECO:0007829|PDB:7VDV"
FT STRAND 467..469
FT /evidence="ECO:0007829|PDB:7VDV"
FT STRAND 516..518
FT /evidence="ECO:0007829|PDB:7VDV"
SQ SEQUENCE 1835 AA; 197391 MW; F540A029FA2264D4 CRC64;
MANSTGKAPP DERRKGLAFL DELRQFHHSR GSPFKKIPAV GGKELDLHGL YTRVTTLGGF
AKVSEKNQWG EIVEEFNFPR SCSNAAFALK QYYLRYLEKY EKVHHFGEDD DEVPPGNPKP
QLPIGAIPSS YNYQQHSVSD YLRQSYGLSM DFNSPNDYNK LVLSLLSGLP NEVDFAINVC
TLLSNESKHV MQLEKDPKII TLLLANAGVF DDTLGSFSTV FGEEWKEKTD RDFVKFWKDI
VDDNEVRDLI SDRNKSHEGT SGEWIWESLF HPPRKLGIND IEGQRVLQIA VILRNLSFEE
GNVKLLAANR TCLRFLLLSA HSHFISLRQL GLDTLGNIAA ELLLDPVDFK TTHLMFHTVT
KCLMSRDRFL KMRGMEILGN LCKAEDNGVL ICEYVDQDSY REIICHLTLP DVLLVISTLE
VLYMLTEMGD VACTKIAKVE KSIDMLVCLV SMDIQMFGPD ALAAVKLIEH PSSSHQMLSE
IRPQAIEQVQ TQTHVASAPA SRAVVAQHVA PPPGIVEIDS EKFACQWLNA HFEVNPDCSV
SRAEMYSEYL STCSKLARGG ILTSTGFYKC LRTVFPNHTV KRVEDSSSNG QAHIHVVGVK
RRAIPLPIQM YYQQQPVSTS VVRVDSVPDV SPAPSPAGIP HGSQTIGNHF QRTPVANQSS
NLTATQMSFP VQGVHTVAQT VSRIPQNPSP HTHQQQNAPV TVIQSKAPIP CEVVKATVIQ
NSIPQTGVPV SIAVGGGPPQ SSVVQNHSTG PQPVTVVNSQ TLLHHPSVIP QQSPLHTVVP
GQIPSGTPVT VIQQAVPQSH MFGRVQNIPA CTSTVSQGQQ LITTSPQPVQ TSSQQTSAGS
QSQDTVIIAP PQYVTTSASN IVSATSVQNF QVATGQMVTI AGVPSPQASR VGFQNIAPKP
LPSQQVSSTV VQQPIQQPQQ PTQQSVVIVS QPAQQGQTYA PAIHQIVLAN PAALPAGQTV
QLTGQPNITP SSSPSPVPAT NNQVPTAMSS SSTPQSQGPP PTVSQMLSVK RQQQQQHSPA
PPPQQVQVQV QQPQQVQMQV QPQQSNAGVG QPASGESSLI KQLLLPKRGP STPGGKLILP
APQIPPPNNA RAPSPQVVYQ VASNQAAGFG VQGQTPAQQL LVGQQNVQLV PSAMPPSGGV
QTVPISNLQI LPGPLISNSP ATIFQGTSGN QVTITVVPNT SFAPATVSQG NATQLIAPAG
ITMSGTQTGV GLPVQTLPAT QASPAGQSSC TTATPPFKGD KIICQKEEEA KEATGLHVHE
RKIEVMENPS CRRGATNTSN GDTKENEMHV GSLLNGRKYS DSSLPPSNSG KIQSETNQCS
LISNGPSLEL GENGASGKQN SEQIDMQDIK SDLRKPLVNG ICDFDKGDGS HLSKNIPNHK
TSNHVGNGEI SPMEPQGTLD ITQQDTAKGD QLERISNGPV LTLGGSSVSS IQEASNAATQ
QFSGTDLLNG PLASSLNSDV PQQRPSVVVS PHSTTSVIQG HQIIAVPDSG SKVSHSPALS
SDVRSTNGTA ECKTVKRPAE DTDRETVAGI PNKVGVRIVT ISDPNNAGCS ATMVAVPAGA
DPSTVAKVAI ESAVQQKQQH PPTYVQNVVP QNTPMPPSPA VQVQGQPNSS QPSPFSGSSQ
PGDPMRKPGQ NFMCLWQSCK KWFQTPSQVF YHAATEHGGK DVYPGQCLWE GCEPFQRQRF
SFITHLQDKH CSKDALLAGL KQDEPGQAGS QKSSTKQPTV GGTSSTPRAQ KAIVNHPSAA
LMALRRGSRN LVFRDFTDEK EGPITKHIRL TAALILKNIG KYSECGRRLL KRHENNLSVL
AISNMEASST LAKCLYELNF TVQSKEQEKD SEMLQ
//
