HM20B_HUMAN
ID HM20B_HUMAN Reviewed; 317 AA.
AC Q9P0W2; A6NMS5; D6W616; Q6IBP8; Q8NBD5; Q9HD21; Q9Y491; Q9Y4A2;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1-related;
DE Short=SMARCE1-related protein;
DE AltName: Full=BRCA2-associated factor 35;
DE AltName: Full=HMG box-containing protein 20B;
DE AltName: Full=HMG domain-containing protein 2;
DE AltName: Full=HMG domain-containing protein HMGX2;
DE AltName: Full=Sox-like transcriptional factor;
DE AltName: Full=Structural DNA-binding protein BRAF35;
GN Name=HMG20B; Synonyms=BRAF35, HMGX2, HMGXB2, SMARCE1R;
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), AND TISSUE SPECIFICITY.
RX PubMed=10773667; DOI=10.1159/000015486;
RA Sumoy L., Carim-Todd L., Escarceller M., Nadal M., Gratacos M.,
RA Pujana M.A., Estivill X., Peral B.;
RT "HMG20A and HMG20B map to human chromosomes 15q24 and 19p13.3 and
RT constitute a distinct class of HMG-box genes with ubiquitous expression.";
RL Cytogenet. Cell Genet. 88:62-67(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH BRCA2, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11207365; DOI=10.1016/s0092-8674(01)00209-4;
RA Marmorstein L.Y., Kinev A.V., Chan G.K.T., Bochar D.A., Beniya H.,
RA Epstein J.A., Yen T.J., Shiekhattar R.;
RT "A human BRCA2 complex containing a structural DNA binding component
RT influences cell cycle progression.";
RL Cell 104:247-257(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11997092; DOI=10.1016/s0167-4781(01)00373-6;
RA Lee Y.M., Shin H., Choi W., Ahn S., Kim W.;
RT "Characterization of human SMARCE1r high-mobility-group protein.";
RL Biochim. Biophys. Acta 1574:269-276(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=12083779; DOI=10.1016/s0006-291x(02)00624-1;
RA Wang C., McCarty I.M., Balazs L., Li Y., Steiner M.S.;
RT "Cloning a cDNA encoding an alternatively spliced protein of BRCA2-
RT associated factor 35.";
RL Biochem. Biophys. Res. Commun. 295:129-135(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Cerebellum;
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pancreas, Placenta, Skin, and Uterus;
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 [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 97-317 (ISOFORM 1).
RC TISSUE=Heart;
RA Suzuki H., Schullery D., Shnyreva M.G., Ostrowski J., Denisenko O.,
RA Mochizuki S., Bomsztyk K.;
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 103-317 (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP IDENTIFICATION AS A COMPONENT OF A HISTONE DEACETYLASE COMPLEX, AND
RP MUTAGENESIS OF LYS-116.
RX PubMed=12032298; DOI=10.1073/pnas.112008599;
RA Hakimi M.-A., Bochar D.A., Chenoweth J., Lane W.S., Mandel G.,
RA Shiekhattar R.;
RT "A core-BRAF35 complex containing histone deacetylase mediates repression
RT of neuronal-specific genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:7420-7425(2002).
RN [12]
RP IDENTIFICATION IN THE BHC COMPLEX WITH GSE1; GTF2I; HDAC1; HDAC2; KDM1A;
RP PHF21A; RCOR1; ZMYM2; ZMYM3 AND ZNF217.
RX PubMed=12493763; DOI=10.1074/jbc.m208992200;
RA Hakimi M.-A., Dong Y., Lane W.S., Speicher D.W., Shiekhattar R.;
RT "A candidate X-linked mental retardation gene is a component of a new
RT family of histone deacetylase-containing complexes.";
RL J. Biol. Chem. 278:7234-7239(2003).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-31, AND IDENTIFICATION BY MASS
RP 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 [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-31, AND IDENTIFICATION BY MASS
RP 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).
CC -!- FUNCTION: Required for correct progression through G2 phase of the cell
CC cycle and entry into mitosis. Required for RCOR1/CoREST mediated
CC repression of neuronal specific gene promoters.
CC -!- SUBUNIT: Component of a BHC histone deacetylase complex that contains
CC HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST and PHF21A/BHC80. The
CC BHC complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I.
CC Interacts with the BRCA2 tumor suppressor protein. Interacts with DTNB
CC (By similarity). {ECO:0000250|UniProtKB:Q9Z104,
CC ECO:0000269|PubMed:11207365, ECO:0000269|PubMed:12493763}.
CC -!- INTERACTION:
CC Q9P0W2; Q86V38: ATN1; NbExp=3; IntAct=EBI-713401, EBI-11954292;
CC Q9P0W2; P51587: BRCA2; NbExp=8; IntAct=EBI-713401, EBI-79792;
CC Q9P0W2; Q9NWQ9: C14orf119; NbExp=3; IntAct=EBI-713401, EBI-725606;
CC Q9P0W2; Q68D86: CCDC102B; NbExp=6; IntAct=EBI-713401, EBI-10171570;
CC Q9P0W2; Q96JN2-2: CCDC136; NbExp=3; IntAct=EBI-713401, EBI-10171416;
CC Q9P0W2; P02489: CRYAA; NbExp=3; IntAct=EBI-713401, EBI-6875961;
CC Q9P0W2; P30040: ERP29; NbExp=6; IntAct=EBI-713401, EBI-946830;
CC Q9P0W2; Q9NP66: HMG20A; NbExp=6; IntAct=EBI-713401, EBI-740641;
CC Q9P0W2; P42858: HTT; NbExp=3; IntAct=EBI-713401, EBI-466029;
CC Q9P0W2; Q92876: KLK6; NbExp=3; IntAct=EBI-713401, EBI-2432309;
CC Q9P0W2; P19012: KRT15; NbExp=3; IntAct=EBI-713401, EBI-739566;
CC Q9P0W2; O76015: KRT38; NbExp=6; IntAct=EBI-713401, EBI-1047263;
CC Q9P0W2; P61970: NUTF2; NbExp=3; IntAct=EBI-713401, EBI-591778;
CC Q9P0W2; O75928-2: PIAS2; NbExp=5; IntAct=EBI-713401, EBI-348567;
CC Q9P0W2; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-713401, EBI-1105153;
CC Q9P0W2; O75971-2: SNAPC5; NbExp=3; IntAct=EBI-713401, EBI-12004298;
CC Q9P0W2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-713401, EBI-5235340;
CC Q9P0W2; Q8N0S2: SYCE1; NbExp=3; IntAct=EBI-713401, EBI-6872807;
CC Q9P0W2; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-713401, EBI-1105213;
CC Q9P0W2; Q86WV8: TSC1; NbExp=3; IntAct=EBI-713401, EBI-12806590;
CC Q9P0W2; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-713401, EBI-739895;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Localized to condensed
CC chromosomes in mitosis in conjunction with BRCA2.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9P0W2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P0W2-2; Sequence=VSP_037131;
CC Name=3;
CC IsoId=Q9P0W2-3; Sequence=VSP_037132;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in adult tissues.
CC {ECO:0000269|PubMed:10773667, ECO:0000269|PubMed:11997092}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC26860.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAC26860.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH21585.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF146223; AAF66707.1; -; mRNA.
DR EMBL; AL355709; CAB90809.2; -; mRNA.
DR EMBL; AF331191; AAG60060.1; -; mRNA.
DR EMBL; AF288679; AAG01174.1; -; mRNA.
DR EMBL; AF072165; AAF76253.1; -; mRNA.
DR EMBL; AK090733; BAC03510.1; -; mRNA.
DR EMBL; AC005786; AAC62837.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69306.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69307.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69308.1; -; Genomic_DNA.
DR EMBL; BC002552; AAH02552.1; -; mRNA.
DR EMBL; BC003505; AAH03505.2; -; mRNA.
DR EMBL; BC004408; AAH04408.2; -; mRNA.
DR EMBL; BC021585; AAH21585.1; ALT_INIT; mRNA.
DR EMBL; AF072836; AAC26860.1; ALT_SEQ; mRNA.
DR EMBL; CR456754; CAG33035.1; -; mRNA.
DR CCDS; CCDS45919.1; -. [Q9P0W2-1]
DR RefSeq; NP_006330.2; NM_006339.2. [Q9P0W2-1]
DR AlphaFoldDB; Q9P0W2; -.
DR SMR; Q9P0W2; -.
DR BioGRID; 115642; 74.
DR CORUM; Q9P0W2; -.
DR IntAct; Q9P0W2; 62.
DR MINT; Q9P0W2; -.
DR STRING; 9606.ENSP00000328269; -.
DR GlyGen; Q9P0W2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9P0W2; -.
DR PhosphoSitePlus; Q9P0W2; -.
DR BioMuta; HMG20B; -.
DR EPD; Q9P0W2; -.
DR jPOST; Q9P0W2; -.
DR MassIVE; Q9P0W2; -.
DR MaxQB; Q9P0W2; -.
DR PaxDb; Q9P0W2; -.
DR PeptideAtlas; Q9P0W2; -.
DR PRIDE; Q9P0W2; -.
DR ProteomicsDB; 83610; -. [Q9P0W2-1]
DR ProteomicsDB; 83611; -. [Q9P0W2-2]
DR ProteomicsDB; 83612; -. [Q9P0W2-3]
DR Antibodypedia; 23254; 309 antibodies from 34 providers.
DR DNASU; 10362; -.
DR Ensembl; ENST00000333651.11; ENSP00000328269.6; ENSG00000064961.19. [Q9P0W2-1]
DR GeneID; 10362; -.
DR KEGG; hsa:10362; -.
DR MANE-Select; ENST00000333651.11; ENSP00000328269.6; NM_006339.3; NP_006330.2.
DR UCSC; uc002lya.4; human. [Q9P0W2-1]
DR CTD; 10362; -.
DR DisGeNET; 10362; -.
DR GeneCards; HMG20B; -.
DR HGNC; HGNC:5002; HMG20B.
DR HPA; ENSG00000064961; Low tissue specificity.
DR MIM; 605535; gene.
DR neXtProt; NX_Q9P0W2; -.
DR OpenTargets; ENSG00000064961; -.
DR PharmGKB; PA29332; -.
DR VEuPathDB; HostDB:ENSG00000064961; -.
DR eggNOG; KOG0381; Eukaryota.
DR GeneTree; ENSGT00940000161213; -.
DR InParanoid; Q9P0W2; -.
DR OMA; NIDRYMH; -.
DR OrthoDB; 1458939at2759; -.
DR PhylomeDB; Q9P0W2; -.
DR TreeFam; TF106440; -.
DR PathwayCommons; Q9P0W2; -.
DR Reactome; R-HSA-3214815; HDACs deacetylate histones.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; Q9P0W2; -.
DR SIGNOR; Q9P0W2; -.
DR BioGRID-ORCS; 10362; 13 hits in 1103 CRISPR screens.
DR ChiTaRS; HMG20B; human.
DR GeneWiki; HMG20B; -.
DR GenomeRNAi; 10362; -.
DR Pharos; Q9P0W2; Tbio.
DR PRO; PR:Q9P0W2; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9P0W2; protein.
DR Bgee; ENSG00000064961; Expressed in lower esophagus muscularis layer and 178 other tissues.
DR ExpressionAtlas; Q9P0W2; baseline and differential.
DR Genevisible; Q9P0W2; HS.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0033234; P:negative regulation of protein sumoylation; IEA:Ensembl.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0016925; P:protein sumoylation; IEA:Ensembl.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
DR Gene3D; 1.10.30.10; -; 1.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR Pfam; PF00505; HMG_box; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Chromatin regulator; Chromosome;
KW Coiled coil; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..317
FT /note="SWI/SNF-related matrix-associated actin-dependent
FT regulator of chromatin subfamily E member 1-related"
FT /id="PRO_0000048575"
FT DNA_BIND 70..138
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 190..257
FT /evidence="ECO:0000255"
FT COMPBIAS 35..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 31
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..102
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12083779"
FT /id="VSP_037131"
FT VAR_SEQ 83..106
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037132"
FT MUTAGEN 116
FT /note="K->I: Loss of DNA binding activity of the BHC
FT histone deacetylase complex."
FT /evidence="ECO:0000269|PubMed:12032298"
FT CONFLICT 11..12
FT /note="AA -> SS (in Ref. 3; AAG01174)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="G -> D (in Ref. 10; CAG33035)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="H -> Q (in Ref. 9; AAC26860)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="G -> D (in Ref. 5; BAC03510)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 317 AA; 35813 MW; ADFCF71C47F8CD2D CRC64;
MSHGPKQPGA AAAPAGGKAP GQHGGFVVTV KQERGEGPRA GEKGSHEEEP VKKRGWPKGK
KRKKILPNGP KAPVTGYVRF LNERREQIRT RHPDLPFPEI TKMLGAEWSK LQPTEKQRYL
DEAEREKQQY MKELRAYQQS EAYKMCTEKI QEKKIKKEDS SSGLMNTLLN GHKGGDCDGF
STFDVPIFTE EFLDQNKARE AELRRLRKMN VAFEEQNAVL QRHTQSMSSA RERLEQELAL
EERRTLALQQ QLQAVRQALT ASFASLPVPG TGETPTLGTL DFYMARLHGA IERDPAQHEK
LIVRIKEILA QVASEHL
