ID A0A2K5X1R4_MACFA Unreviewed; 695 AA.
AC A0A2K5X1R4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Histone-lysine N-methyltransferase EZH2 {ECO:0000256|ARBA:ARBA00024111};
DE EC=2.1.1.356 {ECO:0000256|ARBA:ARBA00012186};
GN Name=EZH2 {ECO:0000313|Ensembl:ENSMFAP00000043392.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000043392.1, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000043392.1, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000043392.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000090};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR RefSeq; XP_005551149.1; XM_005551092.2.
DR AlphaFoldDB; A0A2K5X1R4; -.
DR SMR; A0A2K5X1R4; -.
DR Ensembl; ENSMFAT00000017682.2; ENSMFAP00000043392.1; ENSMFAG00000040192.2.
DR VEuPathDB; HostDB:ENSMFAG00000040192; -.
DR GeneTree; ENSGT00940000155013; -.
DR OrthoDB; 902834at2759; -.
DR Proteomes; UP000233100; Chromosome 3.
DR Bgee; ENSMFAG00000040192; Expressed in thymus and 13 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0140951; F:histone H3K27 trimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR CDD; cd00167; SANT; 1.
DR CDD; cd19218; SET_EZH2; 1.
DR Gene3D; 1.20.58.1880; -; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR InterPro; IPR026489; CXC_dom.
DR InterPro; IPR045318; EZH1/2-like.
DR InterPro; IPR048358; EZH1/2_MCSS.
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; HISTONE-LYSINE N-METHYLTRANSFERASE E(Z); 1.
DR PANTHER; PTHR45747:SF3; HISTONE-LYSINE N-METHYLTRANSFERASE EZH2; 1.
DR Pfam; PF21358; Ezh2_MCSS; 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; SET domain; 1.
DR PROSITE; PS51633; CXC; 1.
DR PROSITE; PS50280; SET; 1.
PE 4: Predicted;
KW Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000233100};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 454..554
FT /note="CXC"
FT /evidence="ECO:0000259|PROSITE:PS51633"
FT DOMAIN 561..676
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 171..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..186
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 695 AA; 79621 MW; 9DEAFE0755468660 CRC64;
MGQTGKKSEK GPVCWRKRVK SEYMRLRQLK RFRRADEVKS MFSSNRQKIL ERTEILNQEW
KQRRIQPVHI LTSCSVTSDL DFPTQVIPLK TLNAVASVPI MYSWSPLQQN FMVEDETVLH
NIPYMGDEVL DQDGTFIEEL IKNYDGKVHG DRECGFINDE IFVELVNALG QYNDDDDDDD
GDDPEEREEK QKDLEDHRDD KESRPPRKFP SDKIFEAISS MFPDKGTAEE LKEKYKELTE
QQLPGALPPE CTPNIDGPNA KSVQREQSLH SFHTLFCRRC FKYDCFLHPF HATPNTYKRK
NTETALDNKP CGPQCYQHLE GAKEFAAALT AERIKTPPKR PGGRRRGRLP NNSSRPSTPT
INVLESKDTD SDREAGTETG GENNDKEEEE KKDETSSSSE ANSRCQTPIK MKPNIEPPEN
VEWSGAEASM FRVLIGTYYD NFCAIARLIG TKTCRQVYEF RVKESSIIAP APAEDVDTPP
RKKKRKHRLW AAHCRKIQLK KGQNRFPGCR CKAQCNTKQC PCYLAVRECD PDLCLTCGAA
DHWDSKNVSC KNCSIQRGSK KHLLLAPSDV AGWGIFIKDP VQKNEFISEY CGEIISQDEA
DRRGKVYDKY MCSFLFNLNN DFVVDATRKG NKIRFANHSV NPNCYAKVMM VNGDHRIGIF
AKRAIQTGEE LFFDYRYSQA DALKYVGIER EMEIP
//
