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   27-MAR-2024, entry version 195.
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="https://atlasgeneticsoncology.org/gene/9/ENL";
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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   PDB; 7X88; X-ray; 2.25 A; A=1-148.
DR   PDB; 7X8B; X-ray; 2.30 A; A/C=1-148.
DR   PDB; 7X8F; X-ray; 2.44 A; A/C=1-148.
DR   PDB; 7X8G; X-ray; 1.91 A; A/C=1-148.
DR   PDB; 8PJI; X-ray; 1.70 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   PDBsum; 7X88; -.
DR   PDBsum; 7X8B; -.
DR   PDBsum; 7X8F; -.
DR   PDBsum; 7X8G; -.
DR   PDBsum; 8PJI; -.
DR   AlphaFoldDB; Q03111; -.
DR   SMR; Q03111; -.
DR   BioGRID; 110444; 125.
DR   CORUM; Q03111; -.
DR   IntAct; Q03111; 35.
DR   MINT; Q03111; -.
DR   STRING; 9606.ENSP00000252674; -.
DR   BindingDB; Q03111; -.
DR   ChEMBL; CHEMBL4295801; -.
DR   GuidetoPHARMACOLOGY; 3183; -.
DR   GlyCosmos; Q03111; 1 site, 1 glycan.
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; 9606-ENSP00000252674; -.
DR   PeptideAtlas; Q03111; -.
DR   ProteomicsDB; 58185; -.
DR   Pumba; Q03111; -.
DR   Antibodypedia; 11832; 157 antibodies from 25 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   AGR; HGNC:7134; -.
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; FEIQHFV; -.
DR   OrthoDB; 4267365at2759; -.
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; 41 hits in 1184 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 178 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0008023; C:transcription elongation factor complex; IDA:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0070577; F:lysine-acetylated histone binding; IBA:GO_Central.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IBA:GO_Central.
DR   CDD; cd16906; YEATS_AF-9_like; 1.
DR   Gene3D; 1.20.1270.290; -; 1.
DR   Gene3D; 2.60.40.1970; YEATS domain; 1.
DR   InterPro; IPR040930; AF-9_AHD.
DR   InterPro; IPR038704; YEAST_sf.
DR   InterPro; IPR005033; YEATS.
DR   PANTHER; PTHR47827; AHD DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR47827:SF4; PROTEIN ENL; 1.
DR   Pfam; PF17793; AHD; 1.
DR   Pfam; PF03366; YEATS; 1.
DR   PROSITE; PS51037; YEATS; 1.
DR   Genevisible; Q03111; HS.
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          109..112
FT                   /evidence="ECO:0007829|PDB:7E7C"
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
//