GenomeNet

Database: UniProt
Entry: P70351
LinkDB: P70351
Original site: P70351 
ID   EZH1_MOUSE              Reviewed;         747 AA.
AC   P70351; A2A4K5; Q3TPR1; Q3U3V5; Q3UU02; Q8BR85; Q922L1; Q9R089;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   13-FEB-2019, entry version 152.
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=Enx2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=9214638; DOI=10.1093/emboj/16.11.3219;
RA   Laible G., Wolf A., Dorn R., Reuter G., Nislow C., Lebersorger A.,
RA   Popkin D., Pillus L., Jenuwein T.;
RT   "Mammalian homologues of the Polycomb-group gene Enhancer of zeste
RT   mediate gene silencing in Drosophila heterochromatin and at S.
RT   cerevisiae telomeres.";
RL   EMBO J. 16:3219-3232(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
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 [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   PubMed=10051331; DOI=10.1007/s003359900993;
RA   Laible G., Haynes A.R., Lebersorger A., O'Carroll D., Mattei M.-G.,
RA   Denny P., Brown S.D.M., Jenuwein T.;
RT   "The murine polycomb-group genes ezh1 and ezh2 map close to hox gene
RT   clusters on mouse chromosomes 11 and 6.";
RL   Mamm. Genome 10:311-314(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=ILS, and ISS;
RX   PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA   Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA   Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT   "High-throughput sequence identification of gene coding variants
RT   within alcohol-related QTLs.";
RL   Mamm. Genome 12:657-663(2001).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Aorta, Cerebellum, Corpora quadrigemina, Hippocampus, and Vein;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, IDENTIFICATION BY
RP   MASS SPECTROMETRY, AND IDENTIFICATION IN THE PRC2/EED-EZH1 COMPLEX.
RX   PubMed=19026780; DOI=10.1016/j.molcel.2008.10.016;
RA   Shen X., Liu Y., Hsu Y.-J., Fujiwara Y., Kim J., Mao X., Yuan G.-C.,
RA   Orkin S.H.;
RT   "EZH1 mediates methylation on histone H3 lysine 27 and complements
RT   EZH2 in maintaining stem cell identity and executing pluripotency.";
RL   Mol. Cell 32:491-502(2008).
RN   [10]
RP   IDENTIFICATION IN THE PRC2 COMPLEX.
RX   PubMed=20144788; DOI=10.1016/j.stem.2009.12.014;
RA   Walker E., Chang W.Y., Hunkapiller J., Cagney G., Garcha K.,
RA   Torchia J., Krogan N.J., Reiter J.F., Stanford W.L.;
RT   "Polycomb-like 2 associates with PRC2 and regulates transcriptional
RT   networks during mouse embryonic stem cell self-renewal and
RT   differentiation.";
RL   Cell Stem Cell 6:153-166(2010).
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:19026780}.
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:19026780};
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:19026780, ECO:0000269|PubMed:20144788}.
CC   -!- INTERACTION:
CC       Q62315:Jarid2; NbExp=4; IntAct=EBI-2531737, EBI-493592;
CC       Q02395:Mtf2; NbExp=3; IntAct=EBI-2531737, EBI-2531578;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Colocalizes with
CC       trimethylated 'Lys-27' of histone H3. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P70351-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P70351-2; Sequence=VSP_036388;
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in kidney, adrenal
CC       gland, testis and brain. {ECO:0000269|PubMed:9473645}.
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=AAH07135.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAL90764.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAL90765.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAA25018.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAE23827.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAE24446.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAE32680.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAE37674.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=EDL03899.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; U60453; AAC53279.1; -; mRNA.
DR   EMBL; AB004817; BAA25018.1; ALT_INIT; mRNA.
DR   EMBL; AF104360; AAD54021.1; -; Genomic_DNA.
DR   EMBL; AF483490; AAL90764.1; ALT_INIT; mRNA.
DR   EMBL; AF483491; AAL90765.1; ALT_INIT; mRNA.
DR   EMBL; AK045374; BAC32334.1; -; mRNA.
DR   EMBL; AK138942; BAE23827.1; ALT_INIT; mRNA.
DR   EMBL; AK140694; BAE24446.1; ALT_INIT; mRNA.
DR   EMBL; AK154565; BAE32680.1; ALT_INIT; mRNA.
DR   EMBL; AK164192; BAE37674.1; ALT_INIT; mRNA.
DR   EMBL; AL590969; CAM19569.1; -; Genomic_DNA.
DR   EMBL; AL590969; CAM19570.1; -; Genomic_DNA.
DR   EMBL; CH466677; EDL03899.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BC007135; AAH07135.1; ALT_INIT; mRNA.
DR   RefSeq; NP_031996.1; NM_007970.3.
DR   RefSeq; XP_006532241.1; XM_006532178.3. [P70351-1]
DR   UniGene; Mm.5027; -.
DR   ProteinModelPortal; P70351; -.
DR   BioGrid; 199563; 19.
DR   DIP; DIP-56992N; -.
DR   IntAct; P70351; 8.
DR   STRING; 10090.ENSMUSP00000102906; -.
DR   iPTMnet; P70351; -.
DR   PhosphoSitePlus; P70351; -.
DR   EPD; P70351; -.
DR   MaxQB; P70351; -.
DR   PaxDb; P70351; -.
DR   PeptideAtlas; P70351; -.
DR   PRIDE; P70351; -.
DR   Ensembl; ENSMUST00000100417; ENSMUSP00000097984; ENSMUSG00000006920. [P70351-2]
DR   Ensembl; ENSMUST00000107284; ENSMUSP00000102905; ENSMUSG00000006920. [P70351-1]
DR   GeneID; 14055; -.
DR   KEGG; mmu:14055; -.
DR   UCSC; uc007lnw.3; mouse. [P70351-2]
DR   UCSC; uc011yfk.2; mouse. [P70351-1]
DR   CTD; 2145; -.
DR   MGI; MGI:1097695; Ezh1.
DR   eggNOG; KOG1079; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000156604; -.
DR   HOVERGEN; HBG002453; -.
DR   InParanoid; P70351; -.
DR   KO; K17451; -.
DR   OrthoDB; 875190at2759; -.
DR   PhylomeDB; P70351; -.
DR   TreeFam; TF314509; -.
DR   PRO; PR:P70351; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   Bgee; ENSMUSG00000006920; Expressed in 279 organ(s), highest expression level in ciliary body.
DR   ExpressionAtlas; P70351; baseline and differential.
DR   Genevisible; P70351; MM.
DR   GO; GO:0000781; C:chromosome, telomeric region; IGI:ARUK-UCL.
DR   GO; GO:0035098; C:ESC/E(Z) complex; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003682; F:chromatin binding; ISO:MGI.
DR   GO; GO:0046976; F:histone methyltransferase activity (H3-K27 specific); IDA:MGI.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:ARUK-UCL.
DR   GO; GO:0006338; P:chromatin remodeling; IDA:ARUK-UCL.
DR   GO; GO:0006348; P:chromatin silencing at telomere; IGI:ARUK-UCL.
DR   GO; GO:0006343; P:establishment of chromatin silencing; IDA:ARUK-UCL.
DR   GO; GO:0036333; P:hepatocyte homeostasis; IGI:MGI.
DR   GO; GO:0098532; P:histone H3-K27 trimethylation; IGI:MGI.
DR   GO; GO:0097421; P:liver regeneration; IGI:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:1904772; P:response to tetrachloromethane; IGI:MGI.
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_0000213991.
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:0000250|UniProtKB:Q92800}.
FT   VAR_SEQ     555    747       QNRFPGCRCKTQCNTKQCPCYLAVRECDPDLCLTCGASEHW
FT                                DCKVVSCKNCSIQRGLKKHLLLAPSDVAGWGTFIKESVQKN
FT                                EFISEYCGELISQDEADRRGKVYDKYMSSFLFNLNNDFVVD
FT                                ATRKGNKIRFANHSVNPNCYAKVVMVNGDHRIGIFAKRAIQ
FT                                AGEELFFDYRYSQADALKYVGIERETDVF -> KSTLLSPS
FT                                STQVVGLGVPRLFSPAP (in isoform 2).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_036388.
FT   CONFLICT     84     84       T -> A (in Ref. 5; BAE32680).
FT                                {ECO:0000305}.
FT   CONFLICT    446    446       H -> Y (in Ref. 2; AAD54021).
FT                                {ECO:0000305}.
FT   CONFLICT    452    452       N -> Y (in Ref. 2; AAD54021).
FT                                {ECO:0000305}.
SQ   SEQUENCE   747 AA;  85188 MW;  43CECFBDF3E49192 CRC64;
     MDIASPPTSK CITYWKRKVK SEYMRLRQLK RLQANMGAKA LYVANFAKVQ EKTQILNEEW
     KKLRVQPVQP MKPVSGHPFL KKCTIESIFP GFDSQDMLMR SLNTVALVPI MYSWSPLQQN
     FMVEDETVLC NIPYMGDEVK EEDETFIEEL INNYDGKVHG EEEMIPGSVL ISDAVFLELV
     DALNQYSDEE EDGHNDPSDG KQDDSKEDLP VTRKRKRHAI EGNKKSSKKQ FPNDMIFSAI
     ASMFPENGVP DDMKERYREL TEMSDPNALP PQCTPNIDGP NAKSVQREQS LHSFHTLFCR
     RCFKYDCFLH PFHATPNVYK RKNKEIKIEP EPCGTDCFLL LEGAKEYAML HNPRSKCSGR
     RRRRHPVVSA SCSNASASAM AETKEGDSDR DTGNDWASSS SEANSRCQTP TKQKASPAPA
     QLCVVEAPSE PVEWTGAEES LFRVFHGTYF NNFCSIARLL GTKTCKQVFQ FAVKESLILK
     LPTDELMNPA QKKKRKHRLW AAHCRKIQLK KDNNSTQVYN YQPCDHPDRP CDSTCPCIMT
     QNFCEKFCQC SPDCQNRFPG CRCKTQCNTK QCPCYLAVRE CDPDLCLTCG ASEHWDCKVV
     SCKNCSIQRG LKKHLLLAPS DVAGWGTFIK ESVQKNEFIS EYCGELISQD EADRRGKVYD
     KYMSSFLFNL NNDFVVDATR KGNKIRFANH SVNPNCYAKV VMVNGDHRIG IFAKRAIQAG
     EELFFDYRYS QADALKYVGI ERETDVF
//
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