EZH2_XENTR
ID EZH2_XENTR Reviewed; 748 AA.
AC Q28D84;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 76.
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; ORFNames=TGas092f05.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula;
RG Sanger Xenopus tropicalis EST/cDNA 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; CR855647; CAJ83863.1; -; mRNA.
DR RefSeq; NP_001017293.1; NM_001017293.2.
DR AlphaFoldDB; Q28D84; -.
DR SMR; Q28D84; -.
DR GeneID; 550047; -.
DR KEGG; xtr:550047; -.
DR CTD; 2146; -.
DR Xenbase; XB-GENE-956215; ezh2.
DR InParanoid; Q28D84; -.
DR OrthoDB; 875190at2759; -.
DR Reactome; R-XTR-212300; PRC2 methylates histones and DNA.
DR Reactome; R-XTR-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-XTR-3214841; PKMTs methylate histone lysines.
DR Reactome; R-XTR-8943724; Regulation of PTEN gene transcription.
DR Proteomes; UP000008143; Chromosome 6.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000020146; Expressed in ovary and 44 other tissues.
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:0031507; P:heterochromatin assembly; IBA:GO_Central.
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 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..748
FT /note="Histone-lysine N-methyltransferase EZH2"
FT /id="PRO_0000345430"
FT DOMAIN 505..607
FT /note="CXC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00970"
FT DOMAIN 614..729
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 184..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..207
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 748 AA; 85630 MW; 0D6D3FDE6C329CD1 CRC64;
MGQTGKKSEK GPVCWRKRVK SEYMRLRQLK RFRRADEVKS MFNTNRQKIM ERTEILNQEW
KQRRIQPVHI MTTVSSLRGT RECSVTSDLD FPKQVIPLKT LTAVASVPIM YSWSPLQQNF
MVEDETVLHN IPYMGDEVLD QDGTFIEELI KNYDGKVHGD RECGFINDEI FVELVNALAQ
YSDYEDDEDG DDNQDDERDD TAKDQDDNME DQETQPLRKF PSDKIFEAIS SMFPDKGTLE
ELKEKYKELT EQQLPGALPP ECTPNIDGPN AKSVQREQSL HSFHTLFCRR CFKYDCFLHP
FHATPNTYKR KNNEAANDGK PCGPHCYQLL EGAREFAAAL TAERIKTPPK RPSGRRRGRL
PNNTSRPSTP TVNVLEAKDT DSDREAGTET GGESNDKEEE EKKDETSSSS EANSRCQTPI
KMKPNIEPPE NVEWSGAEAS LFRVLIGTYY DNFCAIARLI GTKTCRQVYE FRVKESSIIA
PVIAEDVDTP PRKKKRKHRL WAAHCRKIQL KKDGSSNHVY NYQPCDHPRQ PCDSSCPCVI
AQNFCEKFCQ CSSECQNRFP GCRCKAQCNT KQCPCYLAVR ECDPDLCLTC GAADHWDSKN
VSCKNCSIQR GSKKHLLLAP SDVAGWGIFI KDPVQKNEFI SEYCGEIISQ DEADRRGKVY
DKYMCSFLFN LNNDFVVDAT RKGNKIRFAN HSVNPNCYAK VMMVNGDHRI GIFAKRAIQT
GEELFFDYRY SQADALKYVG IEREMEIP
