EZH2B_XENLA
ID EZH2B_XENLA Reviewed; 748 AA.
AC Q4V863;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 82.
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-B;
GN Name=ezh2-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2005) 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; BC097526; AAH97526.1; -; mRNA.
DR RefSeq; NP_001167506.1; NM_001174035.1.
DR AlphaFoldDB; Q4V863; -.
DR SMR; Q4V863; -.
DR DNASU; 100381148; -.
DR GeneID; 100381148; -.
DR KEGG; xla:100381148; -.
DR CTD; 100381148; -.
DR Xenbase; XB-GENE-6252001; ezh2.S.
DR OrthoDB; 875190at2759; -.
DR Proteomes; UP000186698; Chromosome 6S.
DR Bgee; 100381148; Expressed in gastrula and 17 other tissues.
DR GO; GO:0035098; C:ESC/E(Z) complex; ISS:UniProtKB.
DR GO; GO:0046976; F:histone methyltransferase activity (H3-K27 specific); IEA:UniProtKB-EC.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR GO; GO:0070734; P:histone H3-K27 methylation; IEA:InterPro.
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; 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_0000345429"
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 183..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..204
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..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 748 AA; 85742 MW; BD6B17AF6B7B2A6A CRC64;
MGQTGKKSEK GAVCWRKRVK SEYMRLRQLK RFRRADEVKS MFNTNRQKIM ERTEILNQEW
KQRRIQPVHI MTTVSSLRGT RECFVTSDLD FPKQVIPLKT LTAVASMPIM YSWSPLQQNF
MVEDETVLHN IPYMGDEVLD QDGTFIEELI KNYDGKVHGD RECGFINDEI FVELVNALAQ
YSDYEDDEDG EDNQDDERDD ITKDQDDNME EKETLPLRKF PSDKIFEAIS SVFPDKGTSE
ELKEKYKELT EQQLPGALPP ECTPNIDGSN AKSVQREQSL HSFHTLFCRR CFKYDCFLHP
FHATPNTYKR KNNEAANDGK LCGPYCYQLL EGAREFAAAL TAEIIKTPPK RPSGRRRGRL
PNNSSRPSTP TVNVLEAKDT DSDREAGTET GGESNDKEEE EKKDETDSSS EANSRCQTPI
KMKPNIEPPE NVEWSGAEAS LFRVLIGTYY DNFCAIARLI STKTCRQVYE FRVKESSIIA
PVIAEDVDTP PRKKKRKHRL WAAHCRKIQL KKDGSSNHVY NYQPCDHPRQ PCDSSCPCVI
AQNFCEKFCQ CSSDCQNRFP GCRCKAQCNT KQCPCYLAVR ECDPDLCLTC GAADHWDSKN
VSCKNCSIQR GSKKHLLLAP SDVAGWGIYI KDPVQKNEFI SEYCGEIISQ DEADRRGKVY
DKYMCSFLFN LNNDFVVDAT RKGNKIRFAN HSLNPNCYAK VMMVNGDHRI GIFAKRAIQT
GEELFFDYRY SQADALKYVG IEREMEIP
