EZH1_HUMAN
ID EZH1_HUMAN Reviewed; 747 AA.
AC Q92800; A6NCH6; B4DIJ1; B4DIZ7; B4DSS2; B4E3R7; O43287; Q14459; Q53XP3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Histone-lysine N-methyltransferase EZH1;
DE EC=2.1.1.356 {ECO:0000269|PubMed:19026781};
DE AltName: Full=ENX-2;
DE AltName: Full=Enhancer of zeste homolog 1;
GN Name=EZH1; Synonyms=KIAA0388;
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).
RX PubMed=8921387; DOI=10.1006/geno.1996.0537;
RA Abel K.J., Brody L.C., Valdes J.M., Erdos M.R., McKinley D.R.,
RA Castilla L.H., Merajver S.D., Couch F.J., Friedman L.S., Ostermeyer E.A.,
RA Lynch E.D., King M.-C., Welcsh P.L., Osborne-Lawrence S., Spillman M.,
RA Bowcock A.M., Collins F.S., Weber B.L.;
RT "Characterization of EZH1, a human homolog of Drosophila Enhancer of zeste
RT near BRCA1.";
RL Genomics 37:161-171(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9473645; DOI=10.1016/s0167-4781(97)00156-5;
RA Ogawa M., Hiraoka Y., Taniguchi K., Aiso S.;
RT "Cloning and expression of a human/mouse Polycomb group gene, ENX-2/Enx-
RT 2.";
RL Biochim. Biophys. Acta 1395:151-158(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 5).
RC TISSUE=Brain, Hippocampus, and Uterus;
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=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 434-538.
RX PubMed=7490091; DOI=10.1006/geno.1995.1185;
RA Rommens J.M., Durocher F., McArthur J., Tonin P., Leblanc J.-F., Allen T.,
RA Samson C., Ferri L., Narod S., Morgan K., Simard J.;
RT "Generation of a transcription map at the HSD17B locus centromeric to BRCA1
RT at 17q21.";
RL Genomics 28:530-542(1995).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, IDENTIFICATION IN THE
RP PRC2/EED-EZH1 COMPLEX, AND MUTAGENESIS OF HIS-690.
RX PubMed=19026781; DOI=10.1016/j.molcel.2008.11.004;
RA Margueron R., Li G., Sarma K., Blais A., Zavadil J., Woodcock C.L.,
RA Dynlacht B.D., Reinberg D.;
RT "Ezh1 and Ezh2 maintain repressive chromatin through different
RT mechanisms.";
RL Mol. Cell 32:503-518(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-327, 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).
RN [13]
RP INTERACTION WITH EZHIP.
RX PubMed=31451685; DOI=10.1038/s41467-019-11800-x;
RA Ragazzini R., Perez-Palacios R., Baymaz I.H., Diop S., Ancelin K.,
RA Zielinski D., Michaud A., Givelet M., Borsos M., Aflaki S., Legoix P.,
RA Jansen P.W.T.C., Servant N., Torres-Padilla M.E., Bourc'his D., Fouchet P.,
RA Vermeulen M., Margueron R.;
RT "EZHIP constrains Polycomb Repressive Complex 2 activity in germ cells.";
RL Nat. Commun. 10:3858-3858(2019).
CC -!- FUNCTION: Polycomb group (PcG) protein. Catalytic subunit of the
CC PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading
CC to transcriptional repression of the affected target gene. Able to
CC mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1,
CC H3K27me2 and H3K27me3, respectively. Required for embryonic stem cell
CC derivation and self-renewal, suggesting that it is involved in
CC safeguarding embryonic stem cell identity. Compared to EZH2-containing
CC complexes, it is less abundant in embryonic stem cells, has weak
CC methyltransferase activity and plays a less critical role in forming
CC H3K27me3, which is required for embryonic stem cell identity and proper
CC differentiation. {ECO:0000269|PubMed:19026781}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+)
CC + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60292, Rhea:RHEA-COMP:15535, Rhea:RHEA-
CC COMP:15548, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.356;
CC Evidence={ECO:0000269|PubMed:19026781};
CC -!- SUBUNIT: Component of the PRC2/EED-EZH1 complex, which includes EED,
CC EZH1, SUZ12, RBBP4 and AEBP2 (PubMed:19026781). The PRC2/EED-EZH1 is
CC less abundant than the PRC2/EED-EZH2 complex, has weak
CC methyltransferase activity and compacts chromatin in the absence of the
CC methyltransferase cofactor S-adenosyl-L-methionine (SAM)
CC (PubMed:19026781). Interacts with EZHIP; the interaction blocks EZH1
CC methyltransferase activity (PubMed:31451685).
CC {ECO:0000269|PubMed:19026781, ECO:0000269|PubMed:31451685}.
CC -!- INTERACTION:
CC Q92800; O75530: EED; NbExp=4; IntAct=EBI-8830732, EBI-923794;
CC Q92800-2; O75530-2: EED; NbExp=3; IntAct=EBI-12322467, EBI-11132357;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19026781}.
CC Note=Colocalizes with trimethylated 'Lys-27' of histone H3.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q92800-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92800-2; Sequence=VSP_036386;
CC Name=3;
CC IsoId=Q92800-3; Sequence=VSP_036387;
CC Name=4;
CC IsoId=Q92800-4; Sequence=VSP_036385;
CC Name=5;
CC IsoId=Q92800-5; Sequence=VSP_036384;
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. EZ subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20842.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U50315; AAC50778.1; -; mRNA.
DR EMBL; AB004818; BAA25019.1; -; mRNA.
DR EMBL; AB002386; BAA20842.2; ALT_INIT; mRNA.
DR EMBL; BT009782; AAP88784.1; -; mRNA.
DR EMBL; AK304835; BAG65579.1; -; mRNA.
DR EMBL; AK295626; BAG58503.1; -; mRNA.
DR EMBL; AK295853; BAG58659.1; -; mRNA.
DR EMBL; AK299887; BAG61734.1; -; mRNA.
DR EMBL; AC100793; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471152; EAW60870.1; -; Genomic_DNA.
DR EMBL; BC015882; AAH15882.1; -; mRNA.
DR EMBL; L38934; AAB59574.1; -; mRNA.
DR CCDS; CCDS32659.1; -. [Q92800-1]
DR CCDS; CCDS82129.1; -. [Q92800-3]
DR RefSeq; NP_001308008.1; NM_001321079.1. [Q92800-2]
DR RefSeq; NP_001308010.1; NM_001321081.1.
DR RefSeq; NP_001308011.1; NM_001321082.1. [Q92800-3]
DR RefSeq; NP_001982.2; NM_001991.4. [Q92800-1]
DR PDB; 7KSO; EM; 3.90 A; A=1-747.
DR PDB; 7KSR; EM; 4.10 A; A=1-747.
DR PDB; 7KTP; EM; 4.80 A; A=1-747.
DR PDBsum; 7KSO; -.
DR PDBsum; 7KSR; -.
DR PDBsum; 7KTP; -.
DR AlphaFoldDB; Q92800; -.
DR SMR; Q92800; -.
DR BioGRID; 108445; 85.
DR DIP; DIP-58580N; -.
DR IntAct; Q92800; 15.
DR MINT; Q92800; -.
DR STRING; 9606.ENSP00000404658; -.
DR BindingDB; Q92800; -.
DR ChEMBL; CHEMBL2189116; -.
DR DrugBank; DB12887; Tazemetostat.
DR DrugCentral; Q92800; -.
DR GuidetoPHARMACOLOGY; 2835; -.
DR iPTMnet; Q92800; -.
DR PhosphoSitePlus; Q92800; -.
DR BioMuta; EZH1; -.
DR DMDM; 3334182; -.
DR EPD; Q92800; -.
DR jPOST; Q92800; -.
DR MassIVE; Q92800; -.
DR MaxQB; Q92800; -.
DR PaxDb; Q92800; -.
DR PeptideAtlas; Q92800; -.
DR PRIDE; Q92800; -.
DR ProteomicsDB; 75480; -. [Q92800-1]
DR ProteomicsDB; 75481; -. [Q92800-2]
DR ProteomicsDB; 75482; -. [Q92800-3]
DR ProteomicsDB; 75483; -. [Q92800-4]
DR ProteomicsDB; 75484; -. [Q92800-5]
DR TopDownProteomics; Q92800-5; -. [Q92800-5]
DR Antibodypedia; 1432; 417 antibodies from 38 providers.
DR DNASU; 2145; -.
DR Ensembl; ENST00000428826.7; ENSP00000404658.1; ENSG00000108799.13. [Q92800-1]
DR Ensembl; ENST00000585893.5; ENSP00000467871.1; ENSG00000108799.13. [Q92800-3]
DR Ensembl; ENST00000590078.5; ENSP00000465220.1; ENSG00000108799.13. [Q92800-4]
DR Ensembl; ENST00000592743.5; ENSP00000466924.1; ENSG00000108799.13. [Q92800-1]
DR GeneID; 2145; -.
DR KEGG; hsa:2145; -.
DR MANE-Select; ENST00000428826.7; ENSP00000404658.1; NM_001991.5; NP_001982.2.
DR UCSC; uc002iaz.4; human. [Q92800-1]
DR CTD; 2145; -.
DR DisGeNET; 2145; -.
DR GeneCards; EZH1; -.
DR HGNC; HGNC:3526; EZH1.
DR HPA; ENSG00000108799; Tissue enhanced (retina).
DR MIM; 601674; gene.
DR neXtProt; NX_Q92800; -.
DR OpenTargets; ENSG00000108799; -.
DR PharmGKB; PA27938; -.
DR VEuPathDB; HostDB:ENSG00000108799; -.
DR eggNOG; KOG1079; Eukaryota.
DR GeneTree; ENSGT00940000156604; -.
DR HOGENOM; CLU_011342_0_0_1; -.
DR InParanoid; Q92800; -.
DR OMA; HAMEGNK; -.
DR OrthoDB; 875190at2759; -.
DR PhylomeDB; Q92800; -.
DR TreeFam; TF314509; -.
DR BioCyc; MetaCyc:HS03158-MON; -.
DR PathwayCommons; Q92800; -.
DR SignaLink; Q92800; -.
DR BioGRID-ORCS; 2145; 24 hits in 1100 CRISPR screens.
DR ChiTaRS; EZH1; human.
DR GeneWiki; EZH1; -.
DR GenomeRNAi; 2145; -.
DR Pharos; Q92800; Tchem.
DR PRO; PR:Q92800; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q92800; protein.
DR Bgee; ENSG00000108799; Expressed in cerebellar hemisphere and 202 other tissues.
DR ExpressionAtlas; Q92800; baseline and differential.
DR Genevisible; Q92800; HS.
DR GO; GO:0000781; C:chromosome, telomeric region; ISS:ARUK-UCL.
DR GO; GO:0035098; C:ESC/E(Z) complex; IDA:UniProtKB.
DR GO; GO:0000792; C:heterochromatin; ISS:ARUK-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0046976; F:histone methyltransferase activity (H3-K27 specific); IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:ARUK-UCL.
DR GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
DR GO; GO:0006338; P:chromatin remodeling; ISS:ARUK-UCL.
DR GO; GO:0031507; P:heterochromatin assembly; ISS:ARUK-UCL.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0098532; P:histone H3-K27 trimethylation; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:ARUK-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; ISS:ARUK-UCL.
DR CDD; cd00167; SANT; 1.
DR CDD; cd19217; SET_EZH1; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR026489; CXC_dom.
DR InterPro; IPR032926; EZH1.
DR InterPro; IPR045318; EZH1/2-like.
DR InterPro; IPR021654; EZH1/EZH2.
DR InterPro; IPR044438; EZH1_SET.
DR InterPro; IPR041343; PRC2_HTH_1.
DR InterPro; IPR041355; Pre-SET_CXC.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR033467; Tesmin/TSO1-like_CXC.
DR PANTHER; PTHR45747; PTHR45747; 1.
DR PANTHER; PTHR45747:SF1; PTHR45747:SF1; 1.
DR Pfam; PF11616; EZH2_WD-Binding; 1.
DR Pfam; PF18118; PRC2_HTH_1; 1.
DR Pfam; PF18264; preSET_CXC; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM01114; CXC; 1.
DR SMART; SM00717; SANT; 2.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS51633; CXC; 1.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromatin regulator; Isopeptide bond;
KW Methyltransferase; Nucleus; Reference proteome; Repressor;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase; Ubl conjugation.
FT CHAIN 1..747
FT /note="Histone-lysine N-methyltransferase EZH1"
FT /id="PRO_0000213990"
FT DOMAIN 504..606
FT /note="CXC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00970"
FT DOMAIN 613..728
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 188..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 491..496
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 188..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 327
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..162
FT /note="MEIPNPPTSKCITYWKRKVKSEYMRLRQLKRLQANMGAKALYVANFAKVQEK
FT TQILNEEWKKLRVQPVQSMKPVSGHPFLKKCTIESIFPGFASQHMLMRSLNTVALVPIM
FT YSWSPLQQNFMVEDETVLCNIPYMGDEVKEEDETFIEELINNYDGKVHGEE -> MEEA
FT SCPTCSVNEACEWTPFSQK (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036384"
FT VAR_SEQ 1..70
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036385"
FT VAR_SEQ 1
FT /note="M -> MEDYSKM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036386"
FT VAR_SEQ 83..122
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036387"
FT MUTAGEN 690
FT /note="H->A: Loss of methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:19026781"
FT CONFLICT 24
FT /note="M -> I (in Ref. 5; BAG58503)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="P -> S (in Ref. 2; BAA25019)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="D -> Y (in Ref. 5; BAG65579)"
FT /evidence="ECO:0000305"
FT CONFLICT 488
FT /note="N -> Y (in Ref. 1; AAC50778)"
FT /evidence="ECO:0000305"
FT CONFLICT 532..535
FT /note="DSTC -> EAL (in Ref. 2; BAA25019)"
FT /evidence="ECO:0000305"
FT CONFLICT 591..602
FT /note="ASEHWDCKVVSC -> PQSTGTARWFPV (in Ref. 2; BAA25019)"
FT /evidence="ECO:0000305"
FT CONFLICT 631
FT /note="E -> K (in Ref. 5; BAG61734)"
FT /evidence="ECO:0000305"
FT CONFLICT 697
FT /note="Y -> C (in Ref. 5; BAG58659)"
FT /evidence="ECO:0000305"
FT CONFLICT 700..747
FT /note="VVMVNGDHRIGIFAKRAIQAGEELFFDYRYSQADALKYVGIERETDVL ->
FT GESQ (in Ref. 2; BAA25019)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 747 AA; 85271 MW; 7CFC52269CDA011B CRC64;
MEIPNPPTSK CITYWKRKVK SEYMRLRQLK RLQANMGAKA LYVANFAKVQ EKTQILNEEW
KKLRVQPVQS MKPVSGHPFL KKCTIESIFP GFASQHMLMR SLNTVALVPI MYSWSPLQQN
FMVEDETVLC NIPYMGDEVK EEDETFIEEL INNYDGKVHG EEEMIPGSVL ISDAVFLELV
DALNQYSDEE EEGHNDTSDG KQDDSKEDLP VTRKRKRHAI EGNKKSSKKQ FPNDMIFSAI
ASMFPENGVP DDMKERYREL TEMSDPNALP PQCTPNIDGP NAKSVQREQS LHSFHTLFCR
RCFKYDCFLH PFHATPNVYK RKNKEIKIEP EPCGTDCFLL LEGAKEYAML HNPRSKCSGR
RRRRHHIVSA SCSNASASAV AETKEGDSDR DTGNDWASSS SEANSRCQTP TKQKASPAPP
QLCVVEAPSE PVEWTGAEES LFRVFHGTYF NNFCSIARLL GTKTCKQVFQ FAVKESLILK
LPTDELMNPS QKKKRKHRLW AAHCRKIQLK KDNSSTQVYN YQPCDHPDRP CDSTCPCIMT
QNFCEKFCQC NPDCQNRFPG CRCKTQCNTK QCPCYLAVRE CDPDLCLTCG ASEHWDCKVV
SCKNCSIQRG LKKHLLLAPS DVAGWGTFIK ESVQKNEFIS EYCGELISQD EADRRGKVYD
KYMSSFLFNL NNDFVVDATR KGNKIRFANH SVNPNCYAKV VMVNGDHRIG IFAKRAIQAG
EELFFDYRYS QADALKYVGI ERETDVL
