ARI3A_HUMAN
ID ARI3A_HUMAN Reviewed; 593 AA.
AC Q99856; Q5I858; Q6P9C6; Q8IZA7; Q8N4Z3;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=AT-rich interactive domain-containing protein 3A;
DE Short=ARID domain-containing protein 3A;
DE AltName: Full=B-cell regulator of IgH transcription;
DE Short=Bright;
DE AltName: Full=Dead ringer-like protein 1;
DE AltName: Full=E2F-binding protein 1;
GN Name=ARID3A; Synonyms=DRIL1, DRIL3, DRX, E2FBP1;
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 [GENOMIC DNA / MRNA].
RX PubMed=9722953; DOI=10.1006/geno.1998.5259;
RA Kortschak R.D., Reimann H., Zimmer M., Eyre H.J., Saint R., Jenne D.E.;
RT "The human dead ringer/bright homolog, DRIL1: cDNA cloning, gene structure,
RT and mapping to D19S886, a marker on 19p13.3 that is strictly linked to the
RT Peutz-Jeghers syndrome.";
RL Genomics 51:288-292(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH E2F1, AND VARIANT SER-556.
RX PubMed=9780002; DOI=10.1038/sj.onc.1202163;
RA Suzuki M., Okuyama S., Okamoto S., Shirasuna K., Nakajima T., Hachiya T.,
RA Nojima H., Sekiya S., Oda K.;
RT "A novel E2F binding protein with Myc-type HLH motif stimulates E2F-
RT dependent transcription by forming a heterodimer.";
RL Oncogene 17:853-865(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RA Paulin Y.G., Frank R.T., Davy E.J.;
RT "Molecular cloning and immunologic characterization of DRIL3, a new bright-
RT like ARID protein expressed in both myeloid and lymphoid cells, shares
RT homology to E2FBP1/pRB family complexes.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS HIS-36; GLU-320 AND
RP SER-556.
RC TISSUE=Placenta;
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 FUNCTION.
RX PubMed=11812999; DOI=10.1038/ncb742;
RA Peeper D.S., Shvarts A., Brummelkamp T., Douma S., Koh E.Y., Daley G.Q.,
RA Bernards R.;
RT "A functional screen identifies hDRIL1 as an oncogene that rescues RAS-
RT induced senescence.";
RL Nat. Cell Biol. 4:148-153(2002).
RN [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=12692263;
RA Ma K., Araki K., Ichwan S.J.A., Suganuma T., Tamamori-Adachi M.,
RA Ikeda M.-A.;
RT "E2FBP1/DRIL1, an AT-rich interaction domain-family transcription factor,
RT is regulated by p53.";
RL Mol. Cancer Res. 1:438-444(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-81 AND SER-88, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP INTERACTION WITH GTF2I AND BTK, SUBUNIT, DNA-BINDING, AND MUTAGENESIS OF
RP TYR-325.
RX PubMed=16738337; DOI=10.1128/mcb.02009-05;
RA Rajaiya J., Nixon J.C., Ayers N., Desgranges Z.P., Roy A.L., Webb C.F.;
RT "Induction of immunoglobulin heavy-chain transcription through the
RT transcription factor Bright requires TFII-I.";
RL Mol. Cell. Biol. 26:4758-4768(2006).
RN [10]
RP INTERACTION WITH ARID3B, DNA-BINDING, SUBUNIT, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF LYS-461; GLY-527; TYR-530; GLY-532 AND LEU-534.
RX PubMed=17400556; DOI=10.1074/jbc.m700397200;
RA Kim D., Probst L., Das C., Tucker P.W.;
RT "REKLES is an ARID3-restricted multifunctional domain.";
RL J. Biol. Chem. 282:15768-15777(2007).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-81 AND SER-88, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-88; THR-98; SER-101
RP AND SER-119, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-81; SER-88; SER-119;
RP SER-353 AND SER-362, 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 [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-452 AND LYS-462, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-462, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-398; LYS-399 AND LYS-462, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [21]
RP STRUCTURE BY NMR OF 218-351.
RX PubMed=20455271; DOI=10.1002/prot.22718;
RA Liu G., Huang Y.J., Xiao R., Wang D., Acton T.B., Montelione G.T.;
RT "Solution NMR structure of the ARID domain of human AT-rich interactive
RT domain-containing protein 3A: a human cancer protein interaction network
RT target.";
RL Proteins 78:2170-2175(2010).
CC -!- FUNCTION: Transcription factor which may be involved in the control of
CC cell cycle progression by the RB1/E2F1 pathway and in B-cell
CC differentiation. {ECO:0000269|PubMed:11812999,
CC ECO:0000269|PubMed:12692263}.
CC -!- SUBUNIT: Homodimer. Heterodimer with ARID3B. Interacts with E2F1.
CC Interacts with GTF2I and BTK. {ECO:0000269|PubMed:16738337,
CC ECO:0000269|PubMed:17400556, ECO:0000269|PubMed:9780002}.
CC -!- INTERACTION:
CC Q99856; X5D778: ANKRD11; NbExp=3; IntAct=EBI-5458244, EBI-17183751;
CC Q99856; Q06187: BTK; NbExp=3; IntAct=EBI-5458244, EBI-624835;
CC Q99856; Q15323: KRT31; NbExp=3; IntAct=EBI-5458244, EBI-948001;
CC Q99856; O15479: MAGEB2; NbExp=3; IntAct=EBI-5458244, EBI-1057615;
CC Q99856; O15481: MAGEB4; NbExp=3; IntAct=EBI-5458244, EBI-751857;
CC Q99856; Q9UBU8-2: MORF4L1; NbExp=3; IntAct=EBI-5458244, EBI-10288852;
CC Q99856; Q15014: MORF4L2; NbExp=3; IntAct=EBI-5458244, EBI-399257;
CC Q99856; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-5458244, EBI-945833;
CC Q99856; Q6BDI9: REP15; NbExp=3; IntAct=EBI-5458244, EBI-12048237;
CC Q99856; O60220: TIMM8A; NbExp=3; IntAct=EBI-5458244, EBI-1049822;
CC Q99856; Q5I0X7: TTC32; NbExp=3; IntAct=EBI-5458244, EBI-8636434;
CC Q99856; P23025: XPA; NbExp=3; IntAct=EBI-5458244, EBI-295222;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355,
CC ECO:0000269|PubMed:17400556}. Cytoplasm {ECO:0000269|PubMed:17400556}.
CC Note=Shuttles between nucleus and cytoplasm.
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest expression in
CC skeletal muscle, thalamus, and colon.
CC -!- INDUCTION: By p53/TP53 following DNA damage.
CC {ECO:0000269|PubMed:12692263}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAW30734.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U88047; AAC32888.1; -; mRNA.
DR EMBL; AF039850; AAC69994.1; -; Genomic_DNA.
DR EMBL; AF039844; AAC69994.1; JOINED; Genomic_DNA.
DR EMBL; AF039845; AAC69994.1; JOINED; Genomic_DNA.
DR EMBL; AF039846; AAC69994.1; JOINED; Genomic_DNA.
DR EMBL; AF039847; AAC69994.1; JOINED; Genomic_DNA.
DR EMBL; AF039848; AAC69994.1; JOINED; Genomic_DNA.
DR EMBL; AF039849; AAC69994.1; JOINED; Genomic_DNA.
DR EMBL; AY152547; AAN74028.1; -; mRNA.
DR EMBL; AY845638; AAW30734.1; ALT_FRAME; mRNA.
DR EMBL; AC005391; AAC28918.1; -; Genomic_DNA.
DR EMBL; AC005379; AAC28499.1; -; Genomic_DNA.
DR EMBL; BC033163; AAH33163.1; -; mRNA.
DR EMBL; BC060828; AAH60828.1; -; mRNA.
DR CCDS; CCDS12050.1; -.
DR RefSeq; NP_005215.1; NM_005224.2.
DR RefSeq; XP_005259570.1; XM_005259513.4.
DR RefSeq; XP_005259571.1; XM_005259514.4.
DR RefSeq; XP_016881934.1; XM_017026445.1.
DR PDB; 2KK0; NMR; -; A=218-351.
DR PDB; 4LJX; X-ray; 2.21 A; A/B=216-351.
DR PDBsum; 2KK0; -.
DR PDBsum; 4LJX; -.
DR AlphaFoldDB; Q99856; -.
DR BMRB; Q99856; -.
DR SMR; Q99856; -.
DR BioGRID; 108154; 103.
DR IntAct; Q99856; 73.
DR MINT; Q99856; -.
DR STRING; 9606.ENSP00000263620; -.
DR GlyGen; Q99856; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q99856; -.
DR MetOSite; Q99856; -.
DR PhosphoSitePlus; Q99856; -.
DR SwissPalm; Q99856; -.
DR BioMuta; ARID3A; -.
DR DMDM; 12230034; -.
DR EPD; Q99856; -.
DR jPOST; Q99856; -.
DR MassIVE; Q99856; -.
DR MaxQB; Q99856; -.
DR PaxDb; Q99856; -.
DR PeptideAtlas; Q99856; -.
DR PRIDE; Q99856; -.
DR ProteomicsDB; 78506; -.
DR ABCD; Q99856; 2 sequenced antibodies.
DR Antibodypedia; 1435; 285 antibodies from 33 providers.
DR DNASU; 1820; -.
DR Ensembl; ENST00000263620.8; ENSP00000263620.2; ENSG00000116017.11.
DR GeneID; 1820; -.
DR KEGG; hsa:1820; -.
DR MANE-Select; ENST00000263620.8; ENSP00000263620.2; NM_005224.3; NP_005215.1.
DR UCSC; uc002lql.4; human.
DR CTD; 1820; -.
DR DisGeNET; 1820; -.
DR GeneCards; ARID3A; -.
DR HGNC; HGNC:3031; ARID3A.
DR HPA; ENSG00000116017; Tissue enhanced (placenta, testis).
DR MIM; 603265; gene.
DR neXtProt; NX_Q99856; -.
DR OpenTargets; ENSG00000116017; -.
DR PharmGKB; PA27485; -.
DR VEuPathDB; HostDB:ENSG00000116017; -.
DR eggNOG; KOG2744; Eukaryota.
DR GeneTree; ENSGT00940000160899; -.
DR HOGENOM; CLU_026952_3_0_1; -.
DR InParanoid; Q99856; -.
DR OMA; MKPKWEE; -.
DR OrthoDB; 1347369at2759; -.
DR PhylomeDB; Q99856; -.
DR TreeFam; TF320364; -.
DR PathwayCommons; Q99856; -.
DR Reactome; R-HSA-6804116; TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest.
DR SignaLink; Q99856; -.
DR SIGNOR; Q99856; -.
DR BioGRID-ORCS; 1820; 175 hits in 1104 CRISPR screens.
DR ChiTaRS; ARID3A; human.
DR EvolutionaryTrace; Q99856; -.
DR GeneWiki; ARID3A; -.
DR GenomeRNAi; 1820; -.
DR Pharos; Q99856; Tbio.
DR PRO; PR:Q99856; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q99856; protein.
DR Bgee; ENSG00000116017; Expressed in monocyte and 112 other tissues.
DR ExpressionAtlas; Q99856; baseline and differential.
DR Genevisible; Q99856; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0045121; C:membrane raft; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.150.60; -; 1.
DR InterPro; IPR045147; ARI3A/B/C.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR023334; REKLES_domain.
DR PANTHER; PTHR15348; PTHR15348; 1.
DR Pfam; PF01388; ARID; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SUPFAM; SSF46774; SSF46774; 1.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51486; REKLES; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..593
FT /note="AT-rich interactive domain-containing protein 3A"
FT /id="PRO_0000200578"
FT DOMAIN 238..330
FT /note="ARID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT DOMAIN 444..541
FT /note="REKLES"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00819"
FT REGION 14..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..156
FT /note="Acidic"
FT REGION 445..488
FT /note="Important for nuclear localization"
FT /evidence="ECO:0000250"
FT REGION 490..513
FT /note="Homodimerization"
FT REGION 497..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..557
FT /note="Important for cytoplasmic localization"
FT /evidence="ECO:0000250"
FT REGION 539..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..159
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 98
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 398
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 399
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 452
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT CROSSLNK 462
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT VARIANT 36
FT /note="P -> H (in dbSNP:rs17857499)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_033203"
FT VARIANT 320
FT /note="K -> E (in dbSNP:rs17857501)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_033204"
FT VARIANT 556
FT /note="G -> S (in dbSNP:rs1051505)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9780002"
FT /id="VAR_033205"
FT MUTAGEN 325
FT /note="Y->A: Abolishes DNA-binding."
FT /evidence="ECO:0000269|PubMed:16738337"
FT MUTAGEN 461
FT /note="K->A: Abolishes nuclear targeting."
FT /evidence="ECO:0000269|PubMed:17400556"
FT MUTAGEN 527
FT /note="G->A,P: Impairs DNA-binding but not self-
FT association."
FT /evidence="ECO:0000269|PubMed:17400556"
FT MUTAGEN 530
FT /note="Y->A: Impairs DNA-binding but not self-association."
FT /evidence="ECO:0000269|PubMed:17400556"
FT MUTAGEN 530
FT /note="Y->F: No effect on DNA-binding."
FT /evidence="ECO:0000269|PubMed:17400556"
FT MUTAGEN 532
FT /note="G->A: Impairs DNA-binding."
FT /evidence="ECO:0000269|PubMed:17400556"
FT MUTAGEN 534
FT /note="L->A: Impairs DNA-binding."
FT /evidence="ECO:0000269|PubMed:17400556"
FT CONFLICT 423
FT /note="V -> S (in Ref. 2; AAN74028)"
FT /evidence="ECO:0000305"
FT HELIX 225..228
FT /evidence="ECO:0007829|PDB:4LJX"
FT HELIX 230..233
FT /evidence="ECO:0007829|PDB:4LJX"
FT HELIX 239..255
FT /evidence="ECO:0007829|PDB:4LJX"
FT HELIX 272..281
FT /evidence="ECO:0007829|PDB:4LJX"
FT HELIX 285..291
FT /evidence="ECO:0007829|PDB:4LJX"
FT HELIX 294..300
FT /evidence="ECO:0007829|PDB:4LJX"
FT HELIX 310..321
FT /evidence="ECO:0007829|PDB:4LJX"
FT HELIX 323..329
FT /evidence="ECO:0007829|PDB:4LJX"
FT HELIX 335..343
FT /evidence="ECO:0007829|PDB:4LJX"
SQ SEQUENCE 593 AA; 62889 MW; 4D09131E168A2880 CRC64;
MKLQAVMETL LQRQQRARQE LEARQQLPPD PPAAPPGRAR AAPDEDREPE SARMQRAQMA
ALAAMRAAAA GLGHPASPGG SEDGPPGSEE EDAAREGTPG SPGRGREGPG EEHFEDMASD
EDMKPKWEEE EMEEDLGEDE EEEEEDYEDE EEEEDEEGLG PPGPASLGTT ALFPRKAQPP
QAFRGDGVPR VLGGQERPGP GPAHPGGAAH VAPQLQPPDH GDWTYEEQFK QLYELDGDPK
RKEFLDDLFS FMQKRGTPVN RIPIMAKQVL DLFMLYVLVT EKGGLVEVIN KKLWREITKG
LNLPTSITSA AFTLRTQYMK YLYPYECEKR GLSNPNELQA AIDSNRREGR RQSFGGSLFA
YSPGGAHGML SSPKLPVSSL GLAASTNGSS ITPAPKIKKE EDSAIPITVP GRLPVSLAGH
PVVAAQAAAV QAAAAQAAVA AQAAALEQLR EKLESAEPPE KKMALVADEQ QRLMQRALQQ
NFLAMAAQLP MSIRINSQAS ESRQDSAVNL TGTNGSNSIS MSVEINGIMY TGVLFAQPPA
PTPTSAPNKG GGGGGGSSSN AGGRGGNTGT SGGQAGPAGL STPSTSTSNN SLP
