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EZH2_DANRE
ID   EZH2_DANRE              Reviewed;         760 AA.
AC   Q08BS4;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Histone-lysine N-methyltransferase EZH2;
DE            EC=2.1.1.356 {ECO:0000250|UniProtKB:Q15910};
DE   AltName: Full=Enhancer of zeste homolog 2;
GN   Name=ezh2; Synonyms=zgc:152758;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Polycomb group (PcG) protein. Catalytic subunit of the
CC       prc2/eed-ezh2 complex, which methylates 'Lys-9' and 'Lys-27' of histone
CC       H3, leading to transcriptional repression of the affected target gene.
CC       May regulate the circadian clock via histone methylation at the
CC       promoter of the circadian genes. {ECO:0000250|UniProtKB:Q61188}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+)
CC         + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:60292, Rhea:RHEA-COMP:15535, Rhea:RHEA-
CC         COMP:15548, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.356;
CC         Evidence={ECO:0000250|UniProtKB:Q15910};
CC   -!- SUBUNIT: Component of the prc2/eed-ezh2 complex.
CC       {ECO:0000250|UniProtKB:Q15910}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15910}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC       superfamily. Histone-lysine methyltransferase family. EZ subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR   EMBL; BC124588; AAI24589.1; -; mRNA.
DR   RefSeq; NP_001070747.1; NM_001077279.1.
DR   AlphaFoldDB; Q08BS4; -.
DR   SMR; Q08BS4; -.
DR   STRING; 7955.ENSDARP00000023693; -.
DR   PaxDb; Q08BS4; -.
DR   GeneID; 768133; -.
DR   KEGG; dre:768133; -.
DR   CTD; 2146; -.
DR   ZFIN; ZDB-GENE-041111-259; ezh2.
DR   eggNOG; KOG1079; Eukaryota.
DR   InParanoid; Q08BS4; -.
DR   OrthoDB; 875190at2759; -.
DR   PhylomeDB; Q08BS4; -.
DR   Reactome; R-DRE-212300; PRC2 methylates histones and DNA.
DR   Reactome; R-DRE-2559580; Oxidative Stress Induced Senescence.
DR   Reactome; R-DRE-3214841; PKMTs methylate histone lysines.
DR   Reactome; R-DRE-8943724; Regulation of PTEN gene transcription.
DR   Reactome; R-DRE-8953750; Transcriptional Regulation by E2F6.
DR   PRO; PR:Q08BS4; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0035098; C:ESC/E(Z) complex; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0046976; F:histone methyltransferase activity (H3-K27 specific); IBA:GO_Central.
DR   GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR   GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR   GO; GO:0048565; P:digestive tract development; IMP:ZFIN.
DR   GO; GO:0031101; P:fin regeneration; IMP:ZFIN.
DR   GO; GO:0007507; P:heart development; IMP:ZFIN.
DR   GO; GO:0031507; P:heterochromatin assembly; IBA:GO_Central.
DR   GO; GO:0070734; P:histone H3-K27 methylation; IMP:ZFIN.
DR   GO; GO:0098532; P:histone H3-K27 trimethylation; IBA:GO_Central.
DR   GO; GO:0045814; P:negative regulation of gene expression, epigenetic; ISS:UniProtKB.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR   GO; GO:0001894; P:tissue homeostasis; IMP:ZFIN.
DR   CDD; cd00167; SANT; 1.
DR   CDD; cd19218; SET_EZH2; 1.
DR   Gene3D; 2.170.270.10; -; 1.
DR   InterPro; IPR026489; CXC_dom.
DR   InterPro; IPR045318; EZH1/2-like.
DR   InterPro; IPR021654; EZH1/EZH2.
DR   InterPro; IPR044439; EZH2_SET.
DR   InterPro; IPR041343; PRC2_HTH_1.
DR   InterPro; IPR041355; Pre-SET_CXC.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR033467; Tesmin/TSO1-like_CXC.
DR   PANTHER; PTHR45747; PTHR45747; 1.
DR   Pfam; PF11616; EZH2_WD-Binding; 1.
DR   Pfam; PF18118; PRC2_HTH_1; 1.
DR   Pfam; PF18264; preSET_CXC; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM01114; CXC; 1.
DR   SMART; SM00717; SANT; 2.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF82199; SSF82199; 1.
DR   PROSITE; PS51633; CXC; 1.
DR   PROSITE; PS50280; SET; 1.
PE   2: Evidence at transcript level;
KW   Biological rhythms; Chromatin regulator; Methyltransferase; Nucleus;
KW   Reference proteome; Repressor; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN           1..760
FT                   /note="Histone-lysine N-methyltransferase EZH2"
FT                   /id="PRO_0000345427"
FT   DOMAIN          517..619
FT                   /note="CXC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00970"
FT   DOMAIN          626..741
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   REGION          208..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          356..444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..389
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        390..421
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   760 AA;  87145 MW;  E04C67897A59905F CRC64;
     MGLTGRKSEK GPVCWRRRVK SEYMRLRQLK RFRRADEVKS MFSSNRQKIL ERTDILNQEW
     KLRRIQPVHI MTPVSSLRGT RECTVDSGFS EFSRQVIPLK TLNAVASVPV MYSWSPLQQN
     FMVEDETVLH NIPYMGDEIL DQDGTFIEEL IKNYDGKVHG DRECGFINDE IFVELVNALN
     QYSDNEEDDE EDDHHDYKFE KMDLCDGKDD AEDHKEQLSS ESHNNDGSKK FPSDKIFEAI
     SSMFPDKGST EELKEKYKEL TEQQLPGALP PECTPNIDGP NAKSVQREQS LHSFHTLFCR
     RCFKYDCFLH PFQATPNTYK RKNMENLVDS KPCGIYCYMY MVQDGMVREY PAGVVPERAK
     TPSKRSTGRR RGRLPNSNSR PSTPTVNSET KDTDSDREGG ADGNDSNDKD DDDKKDETTS
     SSEANSRCQT PVKLKLSSEP PENVDWSGAE ASLFRVLIGT YYDNFCAIAR LIGTKTCRQV
     YEFRVKESSI IARAPAVDEN TPQRKKKRKH RLWATHCRKI QLKKDGSSNH VYNYQPCDHP
     RQPCDSSCPC VTAQNFCEKF CQCSSECQNR FPGCRCKAQC NTKQCPCYLA VRECDPDLCL
     TCGAAEHWDS KNVSCKNCSI QRGAKKHLLL APSDVAGWGI FIKEPVQKNE FISEYCGEII
     SQDEADRRGK VYDKYMCSFL FNLNNDFVVD ATRKGNKIRF ANHSVNPNCY AKVMMVNGDH
     RIGIFAKRAI QTGEELFFDY RYSQADALKY VGIEREMEIP
 
 
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