EZH2A_XENLA
ID EZH2A_XENLA Reviewed; 748 AA.
AC Q98SM3; Q5XH80;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, 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-A;
GN Name=ezh2-a; Synonyms=xez;
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 [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=11287189; DOI=10.1016/s0925-4773(01)00304-5;
RA Barnett M.W., Seville R.A., Nijjar S., Old R.W., Jones E.A.;
RT "Xenopus Enhancer of Zeste (XEZ); an anteriorly restricted polycomb gene
RT with a role in neural patterning.";
RL Mech. Dev. 102:157-167(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Polycomb group (PcG) protein (By similarity). Catalytic
CC subunit of the prc2/eed-ezh2 complex, which methylates 'Lys-9' and
CC 'Lys-27' of histone H3, leading to transcriptional repression of the
CC affected target gene (By similarity). May repress transcription of the
CC egr2 and en2 genes. May regulate the circadian clock via histone
CC methylation at the promoter of the circadian genes (By similarity).
CC {ECO:0000250|UniProtKB:Q61188, ECO:0000269|PubMed:11287189}.
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 -!- DEVELOPMENTAL STAGE: Does not appear to be maternally expressed.
CC Zygotic expression begins at late blastula, increases at mid and late
CC gastrula, and peaks in the early neurula. Expression is restricted to
CC the anterior nervous system. {ECO:0000269|PubMed:11287189}.
CC -!- INDUCTION: Induced by inhibition of BMP signaling.
CC {ECO:0000269|PubMed:11287189}.
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; AF351126; AAK30208.1; -; mRNA.
DR EMBL; BC084193; AAH84193.1; -; mRNA.
DR RefSeq; NP_001083886.1; NM_001090417.1.
DR RefSeq; XP_018121884.1; XM_018266395.1.
DR AlphaFoldDB; Q98SM3; -.
DR SMR; Q98SM3; -.
DR BioGRID; 100499; 6.
DR PRIDE; Q98SM3; -.
DR GeneID; 399174; -.
DR KEGG; xla:399174; -.
DR CTD; 399174; -.
DR Xenbase; XB-GENE-956220; ezh2.L.
DR OrthoDB; 875190at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 399174; Expressed in gastrula and 19 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; 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_0000345428"
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..220
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..204
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..220
FT /note="Basic and 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"
FT CONFLICT 25
FT /note="A -> R (in Ref. 2; AAH84193)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="K -> R (in Ref. 2; AAH84193)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="P -> R (in Ref. 2; AAH84193)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 748 AA; 85383 MW; 8618F615B348C46C CRC64;
MGQTGKKSEK GPVCWRKRVK SEYMALRQLK KFRRADEVKS MFNTNRQKIM ERTEILNQEW
KQRRIQPVHI MTTVSSLRGT RECSVTSDLD FPKQVIPLKT LTAVASVPIM YSWSPLQQNF
MVEDETVLHN IPYMGDEVLD QDGTFIEELI KNYDGKVHGD RECGFINDEI FVELVNALAQ
YSDYEDDEDG DDNQDDEQDD TAKDQDDNME DKETQPLRKF PSDKIFEAIS SMFPDKGTSE
ELKEKYKELT EQQLPGALPP ECTPNIDGPN AKSVQREQSL HSFHTLFCRP CFKYDCFLHP
FHATPNTYKR KNNEAANDGK PCGPHCYQLL EGAREFAAAL TAERIKTPPK RPSGRRRGRL
PNNTSRPSTP TVNVSEAKDT DSDREAGTET GGESNDKEEE EKKDETSSSS EANSRCQTPI
KMKPNIEPPE NVEWSGAEAS LFRVLIGTYY DNFCAIARLI GTKTCRQVYE FRVKESSIIS
PVIAEDVDTP PRKKKRKHRL WAAHCRKIQL KKDGSSNHVY NYQPCDHPRQ PCDSSCPCVI
AQNFCEKFCQ CSSECQNRFP GCRCKAQCNT KQCPCYLAVR ECDPDLCLTC GAADHWDSKN
VSCKNCSIQR GSKKHLLLAP SDVAGWGIFI NDTVQKNEFI SEYCGEIISQ DEADRRGKVY
DKYMCSFLFN LNNDFVVDAT RKGNKIRFAN HSVNPNCYAK VMMVNGDHRI GIFAKRAIQT
GEELFFDYRY SQADALKYVG IEREMEIP
