ENL_HUMAN
ID ENL_HUMAN Reviewed; 559 AA.
AC Q03111; Q14768;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Protein ENL;
DE AltName: Full=YEATS domain-containing protein 1;
GN Name=MLLT1; Synonyms=ENL, LTG19, YEATS1;
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].
RX PubMed=1423624; DOI=10.1016/0092-8674(92)90602-9;
RA Tkachuk D.C., Kohler S., Cleary M.L.;
RT "Involvement of a homolog of Drosophila trithorax by 11q23 chromosomal
RT translocations in acute leukemias.";
RL Cell 71:691-700(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8378076;
RA Yamamoto K., Seto M., Komatsu H., Iida S., Akao Y., Kojima S., Kodera Y.,
RA Nakazawa S., Ariyoshi Y., Takahashi T., Ueda R.;
RT "Two distinct portions of LTG19/ENL at 19p13 are involved in t(11;19)
RT leukemia.";
RL Oncogene 8:2617-2625(1993).
RN [3]
RP CHARACTERIZATION.
RX PubMed=8080983;
RA Rubnitz J.E., Morrissey J., Savage P.A., Cleary M.L.;
RT "ENL, the gene fused with HRX in t(11;19) leukemias, encodes a nuclear
RT protein with transcriptional activation potential in lymphoid and myeloid
RT cells.";
RL Blood 84:1747-1752(1994).
RN [4]
RP IDENTIFICATION IN A SWI/SNF-LIKE EBAFB COMPLEX.
RX PubMed=12665591; DOI=10.1128/mcb.23.8.2942-2952.2003;
RA Nie Z., Yan Z., Chen E.H., Sechi S., Ling C., Zhou S., Xue Y., Yang D.,
RA Murray D., Kanakubo E., Cleary M.L., Wang W.;
RT "Novel SWI/SNF chromatin-remodeling complexes contain a mixed-lineage
RT leukemia chromosomal translocation partner.";
RL Mol. Cell. Biol. 23:2942-2952(2003).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292 AND SER-296, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND IDENTIFICATION BY
RP 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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [10]
RP FUNCTION, AND IDENTIFICATION IN THE SEC COMPLEX.
RX PubMed=20159561; DOI=10.1016/j.molcel.2010.01.026;
RA Lin C., Smith E.R., Takahashi H., Lai K.C., Martin-Brown S., Florens L.,
RA Washburn M.P., Conaway J.W., Conaway R.C., Shilatifard A.;
RT "AFF4, a component of the ELL/P-TEFb elongation complex and a shared
RT subunit of MLL chimeras, can link transcription elongation to leukemia.";
RL Mol. Cell 37:429-437(2010).
RN [11]
RP FUNCTION, AND IDENTIFICATION IN THE SEC COMPLEX.
RX PubMed=20471948; DOI=10.1016/j.molcel.2010.04.013;
RA He N., Liu M., Hsu J., Xue Y., Chou S., Burlingame A., Krogan N.J.,
RA Alber T., Zhou Q.;
RT "HIV-1 Tat and host AFF4 recruit two transcription elongation factors into
RT a bifunctional complex for coordinated activation of HIV-1 transcription.";
RL Mol. Cell 38:428-438(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292; SER-296; SER-359 AND
RP SER-361, 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 [13]
RP IDENTIFICATION IN THE SEC COMPLEX.
RX PubMed=22195968; DOI=10.1016/j.molcel.2011.12.008;
RA Smith E.R., Lin C., Garrett A.S., Thornton J., Mohaghegh N., Hu D.,
RA Jackson J., Saraf A., Swanson S.K., Seidel C., Florens L., Washburn M.P.,
RA Eissenberg J.C., Shilatifard A.;
RT "The little elongation complex regulates small nuclear RNA transcription.";
RL Mol. Cell 44:954-965(2011).
RN [14]
RP INTERACTION WITH ALKBH4.
RX PubMed=23145062; DOI=10.1371/journal.pone.0049045;
RA Bjornstad L.G., Meza T.J., Otterlei M., Olafsrud S.M., Meza-Zepeda L.A.,
RA Falnes P.O.;
RT "Human ALKBH4 interacts with proteins associated with transcription.";
RL PLoS ONE 7:E49045-E49045(2012).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [16]
RP IDENTIFICATION BY 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 [17]
RP FUNCTION, AND DOMAIN.
RX PubMed=27105114; DOI=10.1016/j.molcel.2016.03.028;
RA Li Y., Sabari B.R., Panchenko T., Wen H., Zhao D., Guan H., Wan L.,
RA Huang H., Tang Z., Zhao Y., Roeder R.G., Shi X., Allis C.D., Li H.;
RT "Molecular coupling of histone crotonylation and active transcription by
RT AF9 YEATS domain.";
RL Mol. Cell 62:181-193(2016).
RN [18]
RP FUNCTION.
RX PubMed=28241139; DOI=10.1038/nature21688;
RA Erb M.A., Scott T.G., Li B.E., Xie H., Paulk J., Seo H.S., Souza A.,
RA Roberts J.M., Dastjerdi S., Buckley D.L., Sanjana N.E., Shalem O.,
RA Nabet B., Zeid R., Offei-Addo N.K., Dhe-Paganon S., Zhang F., Orkin S.H.,
RA Winter G.E., Bradner J.E.;
RT "Transcription control by the ENL YEATS domain in acute leukaemia.";
RL Nature 543:270-274(2017).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-240; LYS-262 AND LYS-342, 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 [20]
RP ACTIVITY REGULATION.
RX PubMed=30374167; DOI=10.1038/s41589-018-0144-y;
RA Li X., Li X.M., Jiang Y., Liu Z., Cui Y., Fung K.Y., van der Beelen S.H.E.,
RA Tian G., Wan L., Shi X., Allis C.D., Li H., Li Y., Li X.D.;
RT "Structure-guided development of YEATS domain inhibitors by targeting pi-
RT pi-pi stacking.";
RL Nat. Chem. Biol. 14:1140-1149(2018).
RN [21] {ECO:0007744|PDB:5J9S}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1-148 IN COMPLEX WITH ACETYLATED
RP HISTONE, AND FUNCTION.
RX PubMed=28241141; DOI=10.1038/nature21687;
RA Wan L., Wen H., Li Y., Lyu J., Xi Y., Hoshii T., Joseph J.K., Wang X.,
RA Loh Y.E., Erb M.A., Souza A.L., Bradner J.E., Shen L., Li W., Li H.,
RA Allis C.D., Armstrong S.A., Shi X.;
RT "ENL links histone acetylation to oncogenic gene expression in acute
RT myeloid leukaemia.";
RL Nature 543:265-269(2017).
CC -!- FUNCTION: Chromatin reader component of the super elongation complex
CC (SEC), a complex required to increase the catalytic rate of RNA
CC polymerase II transcription by suppressing transient pausing by the
CC polymerase at multiple sites along the DNA (PubMed:20159561,
CC PubMed:20471948). Specifically recognizes and binds acetylated and
CC crotonylated histones, with a preference for histones that are
CC crotonylated (PubMed:27105114). Has a slightly higher affinity for
CC binding histone H3 crotonylated at 'Lys-27' (H3K27cr) than 'Lys-20'
CC (H3K9cr20) (PubMed:27105114). {ECO:0000269|PubMed:20159561,
CC ECO:0000269|PubMed:20471948, ECO:0000269|PubMed:27105114}.
CC -!- FUNCTION: Acts as a key chromatin reader in acute myeloid leukemia by
CC recognizing and binding to acetylated histones via its YEATS domain,
CC thereby regulating oncogenic gene transcription.
CC {ECO:0000269|PubMed:28241139, ECO:0000269|PubMed:28241141}.
CC -!- ACTIVITY REGULATION: Acylated lysine-binding is specifically inhibited
CC by the tripeptide XL-13m, carrying a 2-furancarbonyl side chain,
CC preventing recruitment to chromatin. {ECO:0000269|PubMed:30374167}.
CC -!- SUBUNIT: Component of the super elongation complex (SEC), at least
CC composed of EAF1, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb
CC complex and ELL (ELL, ELL2 or ELL3) (PubMed:20159561, PubMed:20471948,
CC PubMed:22195968). Interacts with ALKBH4 (PubMed:23145062). Component of
CC a SWI/SNF-like EBAFb complex, at least composed of
CC SMARCA4/BRG1/BAF190A, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A, SMARCE1/BAF57,
CC SMARCD1/BAF60A, SMARCD2/BAF60B, SMARCC1/BAF155, SMARCC2/BAF170,
CC ARID1B/BAF250B, MLLT1/ENL and actin (PubMed:12665591).
CC {ECO:0000269|PubMed:12665591, ECO:0000269|PubMed:20159561,
CC ECO:0000269|PubMed:20471948, ECO:0000269|PubMed:22195968,
CC ECO:0000269|PubMed:23145062}.
CC -!- INTERACTION:
CC Q03111; Q9UHB7: AFF4; NbExp=8; IntAct=EBI-1384215, EBI-395282;
CC Q03111; Q8TEK3: DOT1L; NbExp=6; IntAct=EBI-1384215, EBI-2619253;
CC Q03111; O95070: YIF1A; NbExp=3; IntAct=EBI-1384215, EBI-2799703;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DOMAIN: The YEATS domain specifically recognizes and binds acylated
CC histones, with a preference for histones that are crotonylated.
CC {ECO:0000269|PubMed:27105114}.
CC -!- DISEASE: Note=A chromosomal aberration involving MLLT1 is associated
CC with acute leukemias. Translocation t(11;19)(q23;p13.3) with
CC KMT2A/MLL1. The result is a rogue activator protein.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ENLID9.html";
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DR EMBL; L04285; AAA58457.1; -; mRNA.
DR EMBL; D14539; BAA03406.1; -; mRNA.
DR CCDS; CCDS12160.1; -.
DR PIR; B44265; B44265.
DR RefSeq; NP_005925.2; NM_005934.3.
DR PDB; 5J9S; X-ray; 2.70 A; A=1-148.
DR PDB; 6HPW; X-ray; 1.90 A; A=1-148.
DR PDB; 6HPX; X-ray; 2.30 A; A=1-148.
DR PDB; 6HPY; X-ray; 2.00 A; A=1-148.
DR PDB; 6HPZ; X-ray; 2.30 A; A=1-148.
DR PDB; 6HQ0; X-ray; 1.81 A; A=1-148.
DR PDB; 6HT0; X-ray; 1.80 A; A=1-148.
DR PDB; 6HT1; X-ray; 2.10 A; A=1-148.
DR PDB; 6T1I; X-ray; 1.80 A; A=1-148.
DR PDB; 6T1J; X-ray; 1.97 A; A=1-148.
DR PDB; 6T1L; X-ray; 2.00 A; A=1-148.
DR PDB; 6T1M; X-ray; 1.85 A; A=1-148.
DR PDB; 6T1N; X-ray; 1.95 A; A=1-148.
DR PDB; 6T1O; X-ray; 1.90 A; A=1-148.
DR PDB; 7B0T; X-ray; 2.05 A; A=1-148.
DR PDB; 7B10; X-ray; 1.92 A; A=1-148.
DR PDB; 7E74; X-ray; 2.90 A; A/B/C/D=1-148.
DR PDB; 7E7A; X-ray; 2.64 A; A/B/C/D=1-148.
DR PDB; 7E7C; X-ray; 1.84 A; A=1-148.
DR PDBsum; 5J9S; -.
DR PDBsum; 6HPW; -.
DR PDBsum; 6HPX; -.
DR PDBsum; 6HPY; -.
DR PDBsum; 6HPZ; -.
DR PDBsum; 6HQ0; -.
DR PDBsum; 6HT0; -.
DR PDBsum; 6HT1; -.
DR PDBsum; 6T1I; -.
DR PDBsum; 6T1J; -.
DR PDBsum; 6T1L; -.
DR PDBsum; 6T1M; -.
DR PDBsum; 6T1N; -.
DR PDBsum; 6T1O; -.
DR PDBsum; 7B0T; -.
DR PDBsum; 7B10; -.
DR PDBsum; 7E74; -.
DR PDBsum; 7E7A; -.
DR PDBsum; 7E7C; -.
DR AlphaFoldDB; Q03111; -.
DR SMR; Q03111; -.
DR BioGRID; 110444; 95.
DR CORUM; Q03111; -.
DR IntAct; Q03111; 34.
DR STRING; 9606.ENSP00000252674; -.
DR BindingDB; Q03111; -.
DR ChEMBL; CHEMBL4295801; -.
DR GuidetoPHARMACOLOGY; 3183; -.
DR GlyGen; Q03111; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q03111; -.
DR PhosphoSitePlus; Q03111; -.
DR BioMuta; MLLT1; -.
DR DMDM; 116241350; -.
DR EPD; Q03111; -.
DR jPOST; Q03111; -.
DR MassIVE; Q03111; -.
DR MaxQB; Q03111; -.
DR PaxDb; Q03111; -.
DR PeptideAtlas; Q03111; -.
DR PRIDE; Q03111; -.
DR ProteomicsDB; 58185; -.
DR Antibodypedia; 11832; 141 antibodies from 24 providers.
DR DNASU; 4298; -.
DR Ensembl; ENST00000252674.9; ENSP00000252674.6; ENSG00000130382.9.
DR GeneID; 4298; -.
DR KEGG; hsa:4298; -.
DR MANE-Select; ENST00000252674.9; ENSP00000252674.6; NM_005934.4; NP_005925.2.
DR UCSC; uc002mek.4; human.
DR CTD; 4298; -.
DR DisGeNET; 4298; -.
DR GeneCards; MLLT1; -.
DR HGNC; HGNC:7134; MLLT1.
DR HPA; ENSG00000130382; Low tissue specificity.
DR MIM; 159556; gene.
DR neXtProt; NX_Q03111; -.
DR OpenTargets; ENSG00000130382; -.
DR PharmGKB; PA30848; -.
DR VEuPathDB; HostDB:ENSG00000130382; -.
DR eggNOG; KOG3149; Eukaryota.
DR GeneTree; ENSGT00940000158800; -.
DR HOGENOM; CLU_036086_0_0_1; -.
DR InParanoid; Q03111; -.
DR OMA; NDAQELK; -.
DR OrthoDB; 727038at2759; -.
DR PhylomeDB; Q03111; -.
DR TreeFam; TF314586; -.
DR PathwayCommons; Q03111; -.
DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
DR SignaLink; Q03111; -.
DR SIGNOR; Q03111; -.
DR BioGRID-ORCS; 4298; 37 hits in 1091 CRISPR screens.
DR ChiTaRS; MLLT1; human.
DR GeneWiki; MLLT1; -.
DR GenomeRNAi; 4298; -.
DR Pharos; Q03111; Tchem.
DR PRO; PR:Q03111; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q03111; protein.
DR Bgee; ENSG00000130382; Expressed in cardiac muscle of right atrium and 176 other tissues.
DR Genevisible; Q03111; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0032783; C:super elongation complex; IBA:GO_Central.
DR GO; GO:0008023; C:transcription elongation factor complex; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 2.60.40.1970; -; 1.
DR InterPro; IPR040930; AF-9_AHD.
DR InterPro; IPR038704; YEAST_sf.
DR InterPro; IPR005033; YEATS.
DR PANTHER; PTHR23195; PTHR23195; 1.
DR Pfam; PF17793; AHD; 1.
DR Pfam; PF03366; YEATS; 1.
DR PROSITE; PS51037; YEATS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Chromosomal rearrangement;
KW Isopeptide bond; Nucleus; Phosphoprotein; Proto-oncogene;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..559
FT /note="Protein ENL"
FT /id="PRO_0000215938"
FT DOMAIN 1..138
FT /note="YEATS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00376"
FT REGION 56..58
FT /note="Acylated histone binding"
FT /evidence="ECO:0000269|PubMed:28241141,
FT ECO:0007744|PDB:5J9S"
FT REGION 78..80
FT /note="Acylated histone binding"
FT /evidence="ECO:0000269|PubMed:28241141,
FT ECO:0007744|PDB:5J9S"
FT REGION 147..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..284
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..470
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 103
FT /note="Acylated histone binding"
FT /evidence="ECO:0000269|PubMed:28241141,
FT ECO:0007744|PDB:5J9S"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CROSSLNK 240
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 262
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 342
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 269..270
FT /note="KG -> NP (in Ref. 1; AAA58457)"
FT /evidence="ECO:0000305"
FT STRAND 6..19
FT /evidence="ECO:0007829|PDB:6HT0"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:6HT0"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:6HT0"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:6HT0"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:6HT0"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:6HT0"
FT STRAND 71..79
FT /evidence="ECO:0007829|PDB:6HT0"
FT STRAND 81..90
FT /evidence="ECO:0007829|PDB:6HT0"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:6HT0"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:6HT0"
FT STRAND 114..126
FT /evidence="ECO:0007829|PDB:6HT0"
FT HELIX 129..137
FT /evidence="ECO:0007829|PDB:6HT0"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:6HT0"
SQ SEQUENCE 559 AA; 62056 MW; A8480BA0F8742173 CRC64;
MDNQCTVQVR LELGHRAQLR KKPTTEGFTH DWMVFVRGPE QCDIQHFVEK VVFWLHDSFP
KPRRVCKEPP YKVEESGYAG FIMPIEVHFK NKEEPRKVCF TYDLFLNLEG NPPVNHLRCE
KLTFNNPTTE FRYKLLRAGG VMVMPEGADT VSRPSPDYPM LPTIPLSAFS DPKKTKPSHG
SKDANKESSK TSKPHKVTKE HRERPRKDSE SKSSSKELER EQAKSSKDTS RKLGEGRLPK
EEKAPPPKAA FKEPKMALKE TKLESTSPKG GPPPPPPPPP RASSKRPATA DSPKPSAKKQ
KKSSSKGSRS APGTSPRTSS SSSFSDKKPA KDKSSTRGEK VKAESEPREA KKALEVEESN
SEDEASFKSE SAQSSPSNSS SSSDSSSDSD FEPSQNHSQG PLRSMVEDLQ SEESDEDDSS
SGEEAAGKTN PGRDSRLSFS DSESDNSADS SLPSREPPPP QKPPPPNSKV SGRRSPESCS
KPEKILKKGT YDKAYTDELV ELHRRLMALR ERNVLQQIVN LIEETGHFNV TNTTFDFDLF
SLDETTVRKL QSCLEAVAT
