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Database: UniProt
Entry: Q5RDS6
LinkDB: Q5RDS6
Original site: Q5RDS6 
ID   EZH1_PONAB              Reviewed;         747 AA.
AC   Q5RDS6;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   16-JAN-2019, entry version 88.
DE   RecName: Full=Histone-lysine N-methyltransferase EZH1;
DE            EC=2.1.1.43;
DE   AltName: Full=Enhancer of zeste homolog 1;
GN   Name=EZH1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By
CC       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   -!- 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       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Colocalizes with
CC       trimethylated 'Lys-27' of histone H3. {ECO:0000250}.
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}.
DR   EMBL; CR857825; CAH90081.1; -; mRNA.
DR   RefSeq; NP_001124996.1; NM_001131524.1.
DR   ProteinModelPortal; Q5RDS6; -.
DR   STRING; 9601.ENSPPYP00000023752; -.
DR   PRIDE; Q5RDS6; -.
DR   GeneID; 100171872; -.
DR   KEGG; pon:100171872; -.
DR   CTD; 2145; -.
DR   eggNOG; KOG1079; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   HOVERGEN; HBG002453; -.
DR   InParanoid; Q5RDS6; -.
DR   KO; K17451; -.
DR   OrthoDB; 875190at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0035098; C:ESC/E(Z) complex; ISS:UniProtKB.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0070734; P:histone H3-K27 methylation; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Chromatin regulator; Complete proteome; Isopeptide bond;
KW   Methyltransferase; Nucleus; Reference proteome; Repressor;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Ubl conjugation.
FT   CHAIN         1    747       Histone-lysine N-methyltransferase EZH1.
FT                                /FTId=PRO_0000323740.
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    605       Cys-rich.
FT   CROSSLNK    327    327       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q92800}.
SQ   SEQUENCE   747 AA;  85253 MW;  B3EC441B32D103D8 CRC64;
     MEIPNPPTSK CITYWKRKVK SEYMRLRQLK RLQANMGAKA LYVANFAKVQ EKTQILNEEW
     KKLRVQPVQS MKPVCGHPFL 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
     EELFLDYRYS QADALKYVGI ERETDVL
//
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