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   02-JUN-2021, entry version 164.
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=11; 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=AAU20329.2; Type=Miscellaneous discrepancy; Note=Differs from position 1094 onward for unknown reason.; Evidence={ECO:0000305};
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; AAU20329.2; ALT_TERM; 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   BioGRID; 128219; 55.
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; 36.
DR   MINT; Q68CP9; -.
DR   STRING; 9606.ENSP00000335044; -.
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; Q68CP9; -.
DR   PeptideAtlas; Q68CP9; -.
DR   PRIDE; Q68CP9; -.
DR   ProteomicsDB; 66011; -. [Q68CP9-1]
DR   ProteomicsDB; 66013; -. [Q68CP9-3]
DR   Antibodypedia; 25264; 128 antibodies.
DR   DNASU; 196528; -.
DR   Ensembl; ENST00000334344; ENSP00000335044; ENSG00000189079. [Q68CP9-1]
DR   GeneID; 196528; -.
DR   KEGG; hsa:196528; -.
DR   UCSC; uc001ros.2; human. [Q68CP9-1]
DR   CTD; 196528; -.
DR   DisGeNET; 196528; -.
DR   GeneCards; 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:ENSG00000189079.15; -.
DR   eggNOG; KOG2312; Eukaryota.
DR   eggNOG; KOG2744; Eukaryota.
DR   GeneTree; ENSGT00390000016138; -.
DR   HOGENOM; CLU_003714_0_0_1; -.
DR   InParanoid; Q68CP9; -.
DR   OMA; ICDWRNC; -.
DR   OrthoDB; 39440at2759; -.
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   SIGNOR; Q68CP9; -.
DR   BioGRID-ORCS; 196528; 216 hits in 1034 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 kidney and 211 other tissues.
DR   ExpressionAtlas; Q68CP9; baseline and differential.
DR   Genevisible; Q68CP9; HS.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
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: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:1905168; P:positive regulation of double-strand break repair via homologous recombination; IMP:CACAO.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
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; Alternative splicing; Chromatin regulator; Disease variant;
KW   DNA-binding; Isopeptide bond; Mental retardation; Metal-binding; Nucleus;
KW   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"
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
//