GenomeNet

Database: UniProt
Entry: Q92800
LinkDB: Q92800
Original site: Q92800 
ID   EZH1_HUMAN              Reviewed;         747 AA.
AC   Q92800; A6NCH6; B4DIJ1; B4DIZ7; B4DSS2; B4E3R7; O43287; Q14459;
AC   Q53XP3;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   13-FEB-2019, entry version 172.
DE   RecName: Full=Histone-lysine N-methyltransferase EZH1;
DE            EC=2.1.1.43;
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
RA   Ostermeyer E.A., Lynch E.D., King M.-C., Welcsh P.L.,
RA   Osborne-Lawrence S., Spillman M., Bowcock A.M., Collins F.S.,
RA   Weber B.L.;
RT   "Characterization of EZH1, a human homolog of Drosophila Enhancer of
RT   zeste 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-
RT   2/Enx-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.
RT   The complete sequences of 100 new cDNA clones from brain which can
RT   code for 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
RT   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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA   Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA   Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA   Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA   Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA   Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA   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
RT   the 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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RT   project: 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.,
RA   Allen T., Samson C., Ferri L., Narod S., Morgan K., Simard J.;
RT   "Generation of a transcription map at the HSD17B locus centromeric to
RT   BRCA1 at 17q21.";
RL   Genomics 28:530-542(1995).
RN   [10]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, IDENTIFICATION IN
RP   THE 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.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [12]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-327, AND IDENTIFICATION BY
RP   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-
RT   modification with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
CC   -!- FUNCTION: Polycomb group (PcG) protein. Catalytic subunit of the
CC       PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3,
CC       leading to transcriptional repression of the affected target gene.
CC       Able to mono-, di- and trimethylate 'Lys-27' of histone H3 to form
CC       H3K27me1, H3K27me2 and H3K27me3, respectively. Required for
CC       embryonic stem cell derivation and self-renewal, suggesting that
CC       it is involved in safeguarding embryonic stem cell identity.
CC       Compared to EZH2-containing complexes, it is less abundant in
CC       embryonic stem cells, has weak methyltransferase activity and
CC       plays a less critical role in forming H3K27me3, which is required
CC       for embryonic stem cell identity and proper differentiation.
CC       {ECO:0000269|PubMed:19026781}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
CC         Evidence={ECO:0000269|PubMed:19026781};
CC   -!- SUBUNIT: Component of the PRC2/EED-EZH1 complex, which includes
CC       EED, EZH1, SUZ12, RBBP4 and AEBP2. The PRC2/EED-EZH1 is less
CC       abundant than the PRC2/EED-EZH2 complex, has weak
CC       methyltransferase activity and compacts chromatin in the absence
CC       of the methyltransferase cofactor S-adenosyl-L-methionine (SAM).
CC       {ECO:0000269|PubMed:19026781}.
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         Note=No experimental confirmation available.;
CC       Name=3;
CC         IsoId=Q92800-3; Sequence=VSP_036387;
CC         Note=No experimental confirmation available.;
CC       Name=4;
CC         IsoId=Q92800-4; Sequence=VSP_036385;
CC         Note=No experimental confirmation available.;
CC       Name=5;
CC         IsoId=Q92800-5; Sequence=VSP_036384;
CC         Note=No experimental confirmation available.;
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. EZ subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA20842.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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   UniGene; Hs.194669; -.
DR   ProteinModelPortal; Q92800; -.
DR   BioGrid; 108445; 21.
DR   DIP; DIP-58580N; -.
DR   IntAct; Q92800; 13.
DR   STRING; 9606.ENSP00000404658; -.
DR   BindingDB; Q92800; -.
DR   ChEMBL; CHEMBL2189116; -.
DR   GuidetoPHARMACOLOGY; 2835; -.
DR   iPTMnet; Q92800; -.
DR   PhosphoSitePlus; Q92800; -.
DR   BioMuta; EZH1; -.
DR   DMDM; 3334182; -.
DR   EPD; Q92800; -.
DR   jPOST; Q92800; -.
DR   MaxQB; Q92800; -.
DR   PaxDb; Q92800; -.
DR   PeptideAtlas; Q92800; -.
DR   PRIDE; Q92800; -.
DR   ProteomicsDB; 75480; -.
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   DNASU; 2145; -.
DR   Ensembl; ENST00000428826; ENSP00000404658; ENSG00000108799. [Q92800-1]
DR   Ensembl; ENST00000585893; ENSP00000467871; ENSG00000108799. [Q92800-3]
DR   Ensembl; ENST00000590078; ENSP00000465220; ENSG00000108799. [Q92800-4]
DR   Ensembl; ENST00000592743; ENSP00000466924; ENSG00000108799. [Q92800-1]
DR   GeneID; 2145; -.
DR   KEGG; hsa:2145; -.
DR   UCSC; uc002iaz.4; human. [Q92800-1]
DR   CTD; 2145; -.
DR   DisGeNET; 2145; -.
DR   EuPathDB; HostDB:ENSG00000108799.12; -.
DR   GeneCards; EZH1; -.
DR   HGNC; HGNC:3526; EZH1.
DR   HPA; HPA005478; -.
DR   HPA; HPA077684; -.
DR   MIM; 601674; gene.
DR   neXtProt; NX_Q92800; -.
DR   OpenTargets; ENSG00000108799; -.
DR   PharmGKB; PA27938; -.
DR   eggNOG; KOG1079; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000156604; -.
DR   HOVERGEN; HBG002453; -.
DR   InParanoid; Q92800; -.
DR   KO; K17451; -.
DR   OMA; RRRHHMV; -.
DR   OrthoDB; 875190at2759; -.
DR   PhylomeDB; Q92800; -.
DR   TreeFam; TF314509; -.
DR   ChiTaRS; EZH1; human.
DR   GeneWiki; EZH1; -.
DR   GenomeRNAi; 2145; -.
DR   PRO; PR:Q92800; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   Bgee; ENSG00000108799; Expressed in 234 organ(s), highest expression level in right hemisphere of cerebellum.
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:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0003682; F:chromatin binding; TAS:ProtInc.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISM:NTNU_SB.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:UniProtKB-EC.
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:0006348; P:chromatin silencing at telomere; ISS:ARUK-UCL.
DR   GO; GO:0006343; P:establishment of chromatin silencing; ISS:ARUK-UCL.
DR   GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR   GO; GO:0070734; P:histone H3-K27 methylation; IEA:InterPro.
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   CDD; cd00167; SANT; 1.
DR   InterPro; IPR026489; CXC_dom.
DR   InterPro; IPR032926; EZH1.
DR   InterPro; IPR021654; EZH1/EZH2.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR033467; Tesmin/TSO1-like_CXC.
DR   PANTHER; PTHR22884:SF333; PTHR22884:SF333; 1.
DR   Pfam; PF11616; EZH2_WD-Binding; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM01114; CXC; 1.
DR   SMART; SM00717; SANT; 2.
DR   SMART; SM00317; SET; 1.
DR   PROSITE; PS51633; CXC; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chromatin regulator; Complete proteome;
KW   Isopeptide bond; Methyltransferase; Nucleus; Reference proteome;
KW   Repressor; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase; Ubl conjugation.
FT   CHAIN         1    747       Histone-lysine N-methyltransferase EZH1.
FT                                /FTId=PRO_0000213990.
FT   DOMAIN      504    606       CXC. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00970}.
FT   DOMAIN      613    728       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   MOTIF       491    496       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   COMPBIAS    524    606       Cys-rich.
FT   CROSSLNK    327    327       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   VAR_SEQ       1    162       MEIPNPPTSKCITYWKRKVKSEYMRLRQLKRLQANMGAKAL
FT                                YVANFAKVQEKTQILNEEWKKLRVQPVQSMKPVSGHPFLKK
FT                                CTIESIFPGFASQHMLMRSLNTVALVPIMYSWSPLQQNFMV
FT                                EDETVLCNIPYMGDEVKEEDETFIEELINNYDGKVHGEE
FT                                -> MEEASCPTCSVNEACEWTPFSQK (in isoform
FT                                5). {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_036384.
FT   VAR_SEQ       1     70       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_036385.
FT   VAR_SEQ       1      1       M -> MEDYSKM (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_036386.
FT   VAR_SEQ      83    122       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_036387.
FT   MUTAGEN     690    690       H->A: Loss of methyltransferase activity.
FT                                {ECO:0000269|PubMed:19026781}.
FT   CONFLICT     24     24       M -> I (in Ref. 5; BAG58503).
FT                                {ECO:0000305}.
FT   CONFLICT    353    353       P -> S (in Ref. 2; BAA25019).
FT                                {ECO:0000305}.
FT   CONFLICT    389    389       D -> Y (in Ref. 5; BAG65579).
FT                                {ECO:0000305}.
FT   CONFLICT    488    488       N -> Y (in Ref. 1; AAC50778).
FT                                {ECO:0000305}.
FT   CONFLICT    532    535       DSTC -> EAL (in Ref. 2; BAA25019).
FT                                {ECO:0000305}.
FT   CONFLICT    591    602       ASEHWDCKVVSC -> PQSTGTARWFPV (in Ref. 2;
FT                                BAA25019). {ECO:0000305}.
FT   CONFLICT    631    631       E -> K (in Ref. 5; BAG61734).
FT                                {ECO:0000305}.
FT   CONFLICT    697    697       Y -> C (in Ref. 5; BAG58659).
FT                                {ECO:0000305}.
FT   CONFLICT    700    747       VVMVNGDHRIGIFAKRAIQAGEELFFDYRYSQADALKYVGI
FT                                ERETDVL -> GESQ (in Ref. 2; BAA25019).
FT                                {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
//
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