GenomeNet

Database: UniProt/TrEMBL
Entry: B5DFE2_RAT
LinkDB: B5DFE2_RAT
Original site: B5DFE2_RAT 
ID   B5DFE2_RAT              Unreviewed;       746 AA.
AC   B5DFE2;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   23-MAY-2018, entry version 87.
DE   SubName: Full=Enhancer of zeste 2 polycomb repressive complex 2 subunit {ECO:0000313|Ensembl:ENSRNOP00000008149};
DE   SubName: Full=Ezh2 protein {ECO:0000313|EMBL:AAI69027.1};
DE   SubName: Full=Similar to Enhancer of zeste homolog 2 (ENX-1), isoform CRA_b {ECO:0000313|EMBL:EDM15557.1};
GN   Name=Ezh2 {ECO:0000313|EMBL:AAI69027.1,
GN   ECO:0000313|Ensembl:ENSRNOP00000008149, ECO:0000313|RGD:1595860};
GN   Synonyms=LOC312299 {ECO:0000313|EMBL:EDM15557.1};
GN   ORFNames=rCG_28121 {ECO:0000313|EMBL:EDM15557.1};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|EMBL:AAI69027.1};
RN   [1] {ECO:0000313|EMBL:AAI69027.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain {ECO:0000313|EMBL:AAI69027.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M.,
RA   Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S.,
RA   Feolo M., Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F.,
RA   Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J.,
RA   Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N.,
RA   Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B.,
RA   Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B.,
RA   Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S.,
RA   Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R.,
RA   Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L.,
RA   Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E.,
RA   Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D.,
RA   Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G.,
RA   Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J.,
RA   Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L.,
RA   Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D.,
RA   Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A.,
RA   Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S.,
RA   Makowski K.A., Bosak S., Malek J.;
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   [2] {ECO:0000313|Ensembl:ENSRNOP00000008149, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000008149,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
RA   Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
RA   Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
RA   Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
RA   Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
RA   Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
RA   Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
RA   Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
RA   Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
RA   D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
RA   Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
RA   Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
RA   Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
RA   Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
RA   Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
RA   Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
RA   Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
RA   Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
RA   Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
RA   Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
RA   Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
RA   Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
RA   Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
RA   Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
RA   Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
RA   Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
RA   Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
RA   Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
RA   Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
RA   Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
RA   Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
RA   Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
RA   Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
RA   Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
RA   Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into
RT   mammalian evolution.";
RL   Nature 428:493-521(2004).
RN   [3] {ECO:0000313|EMBL:EDM15557.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BN {ECO:0000313|EMBL:EDM15557.1};
RX   PubMed=15632090; DOI=10.1101/gr.2889405;
RA   Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M.,
RA   Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z.,
RA   Istrail S., Li P., Sutton G.;
RT   "Gene and alternative splicing annotation with AIR.";
RL   Genome Res. 15:54-66(2005).
RN   [4] {ECO:0000313|EMBL:EDM15557.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BN {ECO:0000313|EMBL:EDM15557.1};
RA   Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
RA   Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
RA   Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L.,
RA   Lu F., Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C.,
RA   Sutton G.G., Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000213|PubMed:22673903}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [6] {ECO:0000313|Ensembl:ENSRNOP00000008149}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000008149};
RG   Ensembl;
RL   Submitted (FEB-2012) to UniProtKB.
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DR   EMBL; AABR07060512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC169027; AAI69027.1; -; mRNA.
DR   EMBL; CH473959; EDM15557.1; -; Genomic_DNA.
DR   RefSeq; NP_001128451.1; NM_001134979.1.
DR   RefSeq; XP_006236465.1; XM_006236403.3.
DR   UniGene; Rn.9027; -.
DR   STRING; 10116.ENSRNOP00000008149; -.
DR   PRIDE; B5DFE2; -.
DR   Ensembl; ENSRNOT00000008149; ENSRNOP00000008149; ENSRNOG00000006048.
DR   GeneID; 312299; -.
DR   KEGG; rno:312299; -.
DR   CTD; 2146; -.
DR   RGD; 1595860; Ezh2.
DR   eggNOG; KOG1079; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00780000121845; -.
DR   HOGENOM; HOG000008176; -.
DR   HOVERGEN; HBG002453; -.
DR   KO; K11430; -.
DR   OMA; IKEAWIK; -.
DR   OrthoDB; EOG091G09L0; -.
DR   TreeFam; TF314509; -.
DR   Reactome; R-RNO-212300; PRC2 methylates histones and DNA.
DR   Reactome; R-RNO-2559580; Oxidative Stress Induced Senescence.
DR   Reactome; R-RNO-3214841; PKMTs methylate histone lysines.
DR   Reactome; R-RNO-8943724; Regulation of PTEN gene transcription.
DR   Reactome; R-RNO-8953750; Transcriptional Regulation by E2F6.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000006048; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR   GO; GO:0035098; C:ESC/E(Z) complex; IEA:Ensembl.
DR   GO; GO:0000790; C:nuclear chromatin; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IDA:RGD.
DR   GO; GO:0045120; C:pronucleus; IEA:Ensembl.
DR   GO; GO:0003682; F:chromatin binding; IDA:RGD.
DR   GO; GO:0031490; F:chromatin DNA binding; IEA:Ensembl.
DR   GO; GO:0046976; F:histone methyltransferase activity (H3-K27 specific); IEA:Ensembl.
DR   GO; GO:0070878; F:primary miRNA binding; IEA:Ensembl.
DR   GO; GO:1990841; F:promoter-specific chromatin binding; IEA:Ensembl.
DR   GO; GO:0043021; F:ribonucleoprotein complex binding; IEA:Ensembl.
DR   GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0044212; F:transcription regulatory region DNA binding; IMP:RGD.
DR   GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; IEA:Ensembl.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
DR   GO; GO:0035984; P:cellular response to trichostatin A; IEA:Ensembl.
DR   GO; GO:0021695; P:cerebellar cortex development; IEA:Ensembl.
DR   GO; GO:0006306; P:DNA methylation; IEA:Ensembl.
DR   GO; GO:0070314; P:G1 to G0 transition; IEA:Ensembl.
DR   GO; GO:0036333; P:hepatocyte homeostasis; IEA:Ensembl.
DR   GO; GO:0021766; P:hippocampus development; IEP:RGD.
DR   GO; GO:0070734; P:histone H3-K27 methylation; IMP:RGD.
DR   GO; GO:0098532; P:histone H3-K27 trimethylation; IEA:Ensembl.
DR   GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
DR   GO; GO:0043433; P:negative regulation of DNA binding transcription factor activity; IEA:Ensembl.
DR   GO; GO:0045605; P:negative regulation of epidermal cell differentiation; IEA:Ensembl.
DR   GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0010629; P:negative regulation of gene expression; IMP:RGD.
DR   GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IEA:Ensembl.
DR   GO; GO:0048387; P:negative regulation of retinoic acid receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0051154; P:negative regulation of striated muscle cell differentiation; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:RGD.
DR   GO; GO:0034244; P:negative regulation of transcription elongation from RNA polymerase II promoter; IEA:Ensembl.
DR   GO; GO:1900006; P:positive regulation of dendrite development; IMP:RGD.
DR   GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IEA:Ensembl.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; IEA:Ensembl.
DR   GO; GO:0043406; P:positive regulation of MAP kinase activity; IEA:Ensembl.
DR   GO; GO:0071168; P:protein localization to chromatin; IEA:Ensembl.
DR   GO; GO:0042127; P:regulation of cell proliferation; IEA:Ensembl.
DR   GO; GO:0042752; P:regulation of circadian rhythm; IEA:Ensembl.
DR   GO; GO:0014013; P:regulation of gliogenesis; IEA:Ensembl.
DR   GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR   GO; GO:1904772; P:response to tetrachloromethane; IEA:Ensembl.
DR   GO; GO:0014834; P:skeletal muscle satellite cell maintenance involved in skeletal muscle regeneration; IEA:Ensembl.
DR   CDD; cd00167; SANT; 1.
DR   InterPro; IPR026489; CXC_dom.
DR   InterPro; IPR021654; EZH1/EZH2.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR033467; Tesmin/TSO1-like_CXC.
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   Complete proteome {ECO:0000313|Proteomes:UP000002494};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494}.
FT   DOMAIN      503    605       CXC. {ECO:0000259|PROSITE:PS51633}.
FT   DOMAIN      612    727       SET. {ECO:0000259|PROSITE:PS50280}.
SQ   SEQUENCE   746 AA;  85251 MW;  E71777E1E49ABAA3 CRC64;
     MGQTGKKSEK GPVCWRKRVK SEYMRLRQLK RFRRADEVKT MFSSNRQKIL ERTETLNQEW
     KQRRIQPVHI MTSVSSLRGT RECSVTSDLD FPAQVIPLKT LNAVASVPIM YSWSPLQQNF
     MVEDETVLHN IPYMGDEVLD QDGTFIEELI KNYDGKVHGD RECGFINDEI FVELVNALGQ
     YNDDDDDDDG DDPDEREEKQ KDLDDSRDDK ETCPPRKFPA DKIFEAISSM FPDKGTAEEL
     KEKYKELTEQ QLPGALPPEC TPNIDGPNAK SVQREQSLHS FHTLFCRRCF KYDCFLHPFH
     ATPNTYKRKN TETALDNKPC GPQCYQHLEG AKEFAAALTA ERIKTPPKRP GGRRRGRLPN
     NSSRPSTPTI SVLESKDTDS DREAGTETGG ENNDKEEEEK KDETSSSSEA NSRCQTPIKM
     KPNIEPPENV EWSGAEASMF RVLIGTYYDN FCAIARLIGT KTCRQVYEFR VKESSIIAPV
     PTEDVDTPPR KKKRKHRLWA AHCRKIQLKK DGSSNHVYNY QPCDHPRQPC DSSCPCVIAQ
     NFCEKFCQCS SECQNRFPGC RCKAQCNTKQ CPCYLAVREC DPDLCLTCGA ADHWDSKNVS
     CKNCSIQRGS KKHLLLAPSD VAGWGIFIKD PVQKNEFISE YCGEIISQDE ADRRGKVYDK
     YMCSFLFNLN NDFVVDATRK GNKIRFANHS VNPNCYAKVM MVNGDHRIGI FAKRAIQTGE
     ELFFDYRYSQ ADALKYVGIE REMEIP
//
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