GenomeNet

Database: UniProt
Entry: Q9ZSM8
LinkDB: Q9ZSM8
Original site: Q9ZSM8 
ID   EZA1_ARATH              Reviewed;         856 AA.
AC   Q9ZSM8; O04246;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   16-JAN-2019, entry version 150.
DE   RecName: Full=Histone-lysine N-methyltransferase EZA1;
DE            EC=2.1.1.43;
DE   AltName: Full=CURLY LEAF-like 1;
DE   AltName: Full=Protein SET DOMAIN GROUP 10;
DE   AltName: Full=Protein SWINGER;
GN   Name=EZA1; Synonyms=SDG10, SET10, SWN; OrderedLocusNames=At4g02020;
GN   ORFNames=T10M13.3;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Bilodeau P., Luo M., Dennis E.S., Peacock W.J., Chaudhury A.M.;
RT   "EZA1, a novel polycomb group gene from Arabidopsis thaliana.";
RL   Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:769-777(1999).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18854416; DOI=10.1073/pnas.0808687105;
RA   De Lucia F., Crevillen P., Jones A.M.E., Greb T., Dean C.;
RT   "A PHD-polycomb repressive complex 2 triggers the epigenetic silencing
RT   of FLC during vernalization.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:16831-16836(2008).
RN   [6]
RP   INTERACTION WITH TAF13.
RX   PubMed=23506837; DOI=10.1016/j.ydbio.2013.03.005;
RA   Lindner M., Simonini S., Kooiker M., Gagliardini V., Somssich M.,
RA   Hohenstatt M., Simon R., Grossniklaus U., Kater M.M.;
RT   "TAF13 interacts with PRC2 members and is essential for Arabidopsis
RT   seed development.";
RL   Dev. Biol. 379:28-37(2013).
CC   -!- FUNCTION: Polycomb group (PcG) protein. Catalytic subunit of some
CC       PcG multiprotein complex, which methylates 'Lys-27' of histone H3,
CC       leading to transcriptional repression of the affected target
CC       genes. PcG proteins act by forming multiprotein complexes, which
CC       are required to maintain the transcriptionally repressive state of
CC       homeotic genes throughout development. PcG proteins are not
CC       required to initiate repression, but to maintain it during later
CC       stages of development (By similarity). {ECO:0000250}.
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:0000255|PROSITE-ProRule:PRU00909};
CC   -!- SUBUNIT: Component of the plant homeodomain / polycomb repressive
CC       complex 2 (PHD-PRC2) large complex during prolonged cold, composed
CC       of core PRC2 components (VRN2, EZA1, FIE and MSI1), and three
CC       related PHD finger proteins (VIL1, VIL2 and VIN3) that mediates
CC       histone H3 trimethylation on 'Lys-27' H3K27me3. Interacts with
CC       TAF13. {ECO:0000269|PubMed:18854416, ECO:0000269|PubMed:23506837}.
CC   -!- INTERACTION:
CC       Q8W5B1:VRN2; NbExp=3; IntAct=EBI-1102047, EBI-2128880;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. EZ subfamily. {ECO:0000255|PROSITE-ProRule:PRU00909}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC78694.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB80695.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AF100163; AAD09108.1; -; mRNA.
DR   EMBL; AF001308; AAC78694.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161493; CAB80695.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE82112.1; -; Genomic_DNA.
DR   EMBL; AY057477; AAL09711.1; -; mRNA.
DR   EMBL; AY090293; AAL90954.1; -; mRNA.
DR   PIR; T01503; T01503.
DR   PIR; T52415; T52415.
DR   RefSeq; NP_567221.1; NM_116433.3.
DR   UniGene; At.3858; -.
DR   ProteinModelPortal; Q9ZSM8; -.
DR   BioGrid; 13454; 5.
DR   DIP; DIP-35029N; -.
DR   IntAct; Q9ZSM8; 7.
DR   STRING; 3702.AT4G02020.1; -.
DR   iPTMnet; Q9ZSM8; -.
DR   PaxDb; Q9ZSM8; -.
DR   PRIDE; Q9ZSM8; -.
DR   EnsemblPlants; AT4G02020.1; AT4G02020.1; AT4G02020.
DR   GeneID; 828165; -.
DR   Gramene; AT4G02020.1; AT4G02020.1; AT4G02020.
DR   KEGG; ath:AT4G02020; -.
DR   Araport; AT4G02020; -.
DR   TAIR; locus:2132178; AT4G02020.
DR   eggNOG; KOG1079; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   HOGENOM; HOG000083511; -.
DR   InParanoid; Q9ZSM8; -.
DR   KO; K11430; -.
DR   OrthoDB; 875190at2759; -.
DR   PhylomeDB; Q9ZSM8; -.
DR   Reactome; R-ATH-212300; PRC2 methylates histones and DNA.
DR   Reactome; R-ATH-2559580; Oxidative Stress Induced Senescence.
DR   Reactome; R-ATH-8953750; Transcriptional Regulation by E2F6.
DR   PRO; PR:Q9ZSM8; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9ZSM8; baseline and differential.
DR   Genevisible; Q9ZSM8; AT.
DR   GO; GO:0005677; C:chromatin silencing complex; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0031519; C:PcG protein complex; IEA:InterPro.
DR   GO; GO:0009506; C:plasmodesma; IDA:TAIR.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003727; F:single-stranded RNA binding; IDA:TAIR.
DR   GO; GO:0006349; P:regulation of gene expression by genetic imprinting; IMP:TAIR.
DR   CDD; cd00167; SANT; 1.
DR   InterPro; IPR026489; CXC_dom.
DR   InterPro; IPR025778; Hist-Lys_N-MeTrfase_EZ.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR033467; Tesmin/TSO1-like_CXC.
DR   PANTHER; PTHR22884:SF237; PTHR22884:SF237; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM01114; CXC; 1.
DR   SMART; SM00717; SANT; 1.
DR   SMART; SM00317; SET; 1.
DR   PROSITE; PS51633; CXC; 1.
DR   PROSITE; PS51576; SAM_MT43_EZ; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Complete proteome; Methyltransferase; Nucleus;
KW   Reference proteome; Repressor; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN         1    856       Histone-lysine N-methyltransferase EZA1.
FT                                /FTId=PRO_0000213996.
FT   DOMAIN      489    539       SANT.
FT   DOMAIN      594    693       CXC. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00970}.
FT   DOMAIN      707    822       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   COMPBIAS     17     33       Asp/Glu-rich (acidic).
FT   COMPBIAS    605    680       Cys-rich.
SQ   SEQUENCE   856 AA;  95396 MW;  DD4B099C936F197C CRC64;
     MVTDDSNSSG RIKSHVDDDD DGEEEEDRLE GLENRLSELK RKIQGERVRS IKEKFEANRK
     KVDAHVSPFS SAASSRATAE DNGNSNMLSS RMRMPLCKLN GFSHGVGDRD YVPTKDVISA
     SVKLPIAERI PPYTTWIFLD RNQRMAEDQS VVGRRQIYYE QHGGETLICS DSEEEPEPEE
     EKREFSEGED SIIWLIGQEY GMGEEVQDAL CQLLSVDASD ILERYNELKL KDKQNTEEFS
     NSGFKLGISL EKGLGAALDS FDNLFCRRCL VFDCRLHGCS QPLISASEKQ PYWSDYEGDR
     KPCSKHCYLQ LKAVREVPET CSNFASKAEE KASEEECSKA VSSDVPHAAA SGVSLQVEKT
     DIGIKNVDSS SGVEQEHGIR GKREVPILKD SNDLPNLSNK KQKTAASDTK MSFVNSVPSL
     DQALDSTKGD QGGTTDNKVN RDSEADAKEV GEPIPDNSVH DGGSSICQPH HGSGNGAIII
     AEMSETSRPS TEWNPIEKDL YLKGVEIFGR NSCLIARNLL SGLKTCLDVS NYMRENEVSV
     FRRSSTPNLL LDDGRTDPGN DNDEVPPRTR LFRRKGKTRK LKYSTKSAGH PSVWKRIAGG
     KNQSCKQYTP CGCLSMCGKD CPCLTNETCC EKYCGCSKSC KNRFRGCHCA KSQCRSRQCP
     CFAAGRECDP DVCRNCWVSC GDGSLGEAPR RGEGQCGNMR LLLRQQQRIL LGKSDVAGWG
     AFLKNSVSKN EYLGEYTGEL ISHHEADKRG KIYDRANSSF LFDLNDQYVL DAQRKGDKLK
     FANHSAKPNC YAKVMFVAGD HRVGIFANER IEASEELFYD YRYGPDQAPV WARKPEGSKK
     DDSAITHRRA RKHQSH
//
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