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Histone-lysine N-methyltransferase EZH2 (EC 2.1.1.43) (Enhancer of zeste homolog 2)

 EZH2_MACFA              Reviewed;         746 AA.
Q4R381; Q4R780;
22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
19-JUL-2005, sequence version 1.
28-MAR-2018, entry version 74.
RecName: Full=Histone-lysine N-methyltransferase EZH2;
EC=2.1.1.43;
AltName: Full=Enhancer of zeste homolog 2;
Name=EZH2; ORFNames=QtsA-15957, QtsA-18821;
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
NCBI_TaxID=9541;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Testis;
International consortium for macaque cDNA sequencing and analysis;
"DNA sequences of macaque genes expressed in brain or testis and its
evolutionary implications.";
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Polycomb group (PcG) protein. Catalytic subunit of the
PRC2/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-
27' (H3K27me) of histone H3, leading to transcriptional repression
of the affected target gene. Able to mono-, di- and trimethylate
'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3,
respectively. Displays a preference for substrates with less
methylation, loses activity when progressively more methyl groups
are incorporated into H3K27, H3K27me0 > H3K27me1 > H3K27me2.
Compared to EZH1-containing complexes, it is more abundant in
embryonic stem cells and plays a major role in forming H3K27me3,
which is required for embryonic stem cell identity and proper
differentiation. The PRC2/EED-EZH2 complex may also serve as a
recruiting platform for DNA methyltransferases, thereby linking
two epigenetic repression systems. EZH2 can also methylate non-
histone proteins such as the transcription factor GATA4 and the
nuclear receptor RORA. Regulates the circadian clock via histone
methylation at the promoter of the circadian genes. Essential for
the CRY1/2-mediated repression of the CLOCK-ARNTL/BMAL1
transcriptional activation of PER1/2. Involved in the di and
trimethylation of 'Lys-27' of histone H3 on PER1/2 promoters which
is necessary for the CRY1/2 proteins to inhibit transcription.
{ECO:0000250|UniProtKB:Q15910, ECO:0000250|UniProtKB:Q61188}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
{ECO:0000250|UniProtKB:Q15910}.
-!- SUBUNIT: Component of the PRC2/EED-EZH2 complex, which includes
EED, EZH2, SUZ12, RBBP4 and RBBP7 and possibly AEBP2 (By
similarity). The minimum components required for methyltransferase
activity of the PRC2/EED-EZH2 complex are EED, EZH2 and SUZ12 (By
similarity). The PRC2 complex may also interact with DNMT1,
DNMT3A, DNMT3B and PHF1 via the EZH2 subunit and with SIRT1 via
the SUZ12 subunit (By similarity). Interacts with HDAC1 and HDAC2
(By similarity). Interacts with PRAME (By similarity). Interacts
with CDYL. Binds ATRX via the SET domain (Probable). Interacts
with ARNTL/BMAL1, CLOCK and CRY1 (By similarity). Interacts with
DNMT3L; the interaction is direct (By similarity).
{ECO:0000250|UniProtKB:Q15910, ECO:0000250|UniProtKB:Q61188,
ECO:0000305}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q4R381-1; Sequence=Displayed;
Name=2;
IsoId=Q4R381-2; Sequence=VSP_034951, VSP_034952;
Note=No experimental confirmation available.;
-!- PTM: Phosphorylated by AKT1 (By similarity). Phosphorylation by
AKT1 reduces methyltransferase activity. Phosphorylation at Thr-
345 by CDK1 and CDK2 promotes maintenance of H3K27me3 levels at
EZH2-target loci, thus leading to epigenetic gene silencing (By
similarity). {ECO:0000250}.
-!- PTM: Sumoylated. {ECO:0000250}.
-!- PTM: Glycosylated: O-GlcNAcylation at Ser-75 by OGT increases
stability of EZH2 and facilitates the formation of H3K27me3 by the
PRC2/EED-EZH2 complex. {ECO:0000250}.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. Histone-lysine methyltransferase
family. EZ subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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EMBL; AB168941; BAE01042.1; -; mRNA.
EMBL; AB179385; BAE02436.1; -; mRNA.
RefSeq; XP_005551149.1; XM_005551092.2.
UniGene; Mfa.2576; -.
ProteinModelPortal; Q4R381; -.
SMR; Q4R381; -.
PRIDE; Q4R381; -.
GeneID; 102146280; -.
KEGG; mcf:102146280; -.
CTD; 2146; -.
HOVERGEN; HBG002453; -.
KO; K11430; -.
GO; GO:0035098; C:ESC/E(Z) complex; ISS:UniProtKB.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0001047; F:core promoter binding; ISS:UniProtKB.
GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:UniProtKB-EC.
GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
GO; GO:0070734; P:histone H3-K27 methylation; ISS:UniProtKB.
GO; GO:0045814; P:negative regulation of gene expression, epigenetic; ISS:UniProtKB.
GO; GO:0048387; P:negative regulation of retinoic acid receptor signaling pathway; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISS:UniProtKB.
GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:UniProtKB.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISS:UniProtKB.
GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00167; SANT; 1.
InterPro; IPR026489; CXC_dom.
InterPro; IPR021654; EZH1/EZH2.
InterPro; IPR001005; SANT/Myb.
InterPro; IPR001214; SET_dom.
InterPro; IPR033467; Tesmin/TSO1-like_CXC.
Pfam; PF11616; EZH2_WD-Binding; 1.
Pfam; PF00856; SET; 1.
SMART; SM01114; CXC; 1.
SMART; SM00717; SANT; 2.
SMART; SM00317; SET; 1.
PROSITE; PS51633; CXC; 1.
PROSITE; PS50280; SET; 1.
2: Evidence at transcript level;
Alternative splicing; Biological rhythms; Chromatin regulator;
Glycoprotein; Isopeptide bond; Methyltransferase; Nucleus;
Phosphoprotein; Repressor; S-adenosyl-L-methionine; Transcription;
Transcription regulation; Transferase; Ubl conjugation.
CHAIN 1 746 Histone-lysine N-methyltransferase EZH2.
/FTId=PRO_0000345426.
DOMAIN 503 605 CXC. {ECO:0000255|PROSITE-
ProRule:PRU00970}.
DOMAIN 612 727 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
REGION 1 340 Interaction with DNMT1, DNMT3A and
DNMT3B. {ECO:0000250}.
REGION 39 68 Interaction with EED. {ECO:0000250}.
REGION 329 522 Interaction with CDYL. {ECO:0000250}.
COMPBIAS 183 209 Asp-rich.
COMPBIAS 523 588 Cys-rich.
MOD_RES 21 21 Phosphoserine; by PKB/AKT1.
{ECO:0000250|UniProtKB:Q15910}.
MOD_RES 76 76 Phosphoserine.
{ECO:0000250|UniProtKB:Q15910}.
MOD_RES 339 339 Phosphothreonine.
{ECO:0000250|UniProtKB:Q15910}.
MOD_RES 345 345 Phosphothreonine; by CDK1 and CDK2.
{ECO:0000250|UniProtKB:Q15910}.
MOD_RES 363 363 Phosphoserine.
{ECO:0000250|UniProtKB:Q15910}.
MOD_RES 366 366 Phosphoserine.
{ECO:0000250|UniProtKB:Q15910}.
MOD_RES 367 367 Phosphothreonine.
{ECO:0000250|UniProtKB:Q15910}.
MOD_RES 487 487 Phosphothreonine.
{ECO:0000250|UniProtKB:Q15910}.
CARBOHYD 75 75 O-linked (GlcNAc) serine. {ECO:0000250}.
CROSSLNK 634 634 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q15910}.
VAR_SEQ 74 82 Missing (in isoform 2).
{ECO:0000303|Ref.1}.
/FTId=VSP_034951.
VAR_SEQ 511 553 DGSSNHVYNYQPCDHPRQPCDSSCPCVIAQNFCEKFCQCSS
EC -> G (in isoform 2).
{ECO:0000303|Ref.1}.
/FTId=VSP_034952.
CONFLICT 305 305 A -> T (in Ref. 1; BAE01042).
{ECO:0000305}.
SEQUENCE 746 AA; 85333 MW; 16942199E6E75621 CRC64;
MGQTGKKSEK GPVCWRKRVK SEYMRLRQLK RFRRADEVKS MFSSNRQKIL ERTEILNQEW
KQRRIQPVHI LTSVSSLRGT RECSVTSDLD FPTQVIPLKT LNAVASVPIM YSWSPLQQNF
MVEDETVLHN IPYMGDEVLD QDGTFIEELI KNYDGKVHGD RECGFINDEI FVELVNALGQ
YNDDDDDDDG DDPEEREEKQ KDLEDHRDDK ESRPPRKFPS DKIFEAISSM FPDKGTAEEL
KEKYKELTEQ QLPGALPPEC TPNIDGPNAK SVQREQSLHS FHTLFCRRCF KYDCFLHPFH
ATPNAYKRKN TETALDNKPC GPQCYQHLEG AKEFAAALTA ERIKTPPKRP GGRRRGRLPN
NSSRPSTPTI NVLESKDTDS DREAGTETGG ENNDKEEEEK KDETSSSSEA NSRCQTPIKM
KPNIEPPENV EWSGAEASMF RVLIGTYYDN FCAIARLIGT KTCRQVYEFR VKESSIIAPA
PAEDVDTPPR KKKRKHRLWA AHCRKIQLKK DGSSNHVYNY QPCDHPRQPC DSSCPCVIAQ
NFCEKFCQCS SECQNRFPGC RCKAQCNTKQ CPCYLAVREC DPDLCLTCGA ADHWDSKNVS
CKNCSIQRGS KKHLLLAPSD VAGWGIFIKD PVQKNEFISE YCGEIISQDE ADRRGKVYDK
YMCSFLFNLN NDFVVDATRK GNKIRFANHS VNPNCYAKVM MVNGDHRIGI FAKRAIQTGE
ELFFDYRYSQ ADALKYVGIE REMEIP


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