ID EZH1_BOVIN Reviewed; 747 AA.
AC A7E2Z2;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=Histone-lysine N-methyltransferase EZH1;
DE EC=2.1.1.356 {ECO:0000250|UniProtKB:Q92800};
DE AltName: Full=Enhancer of zeste homolog 1;
GN Name=EZH1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Polycomb group (PcG) protein. Catalytic subunit of the
CC PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading
CC to transcriptional repression of the affected target gene. Able to
CC mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1,
CC H3K27me2 and H3K27me3, respectively. Required for embryonic stem cell
CC derivation and self-renewal, suggesting that it is involved in
CC safeguarding embryonic stem cell identity. Compared to EZH2-containing
CC complexes, it is less abundant in embryonic stem cells, has weak
CC methyltransferase activity and plays a less critical role in forming
CC H3K27me3, which is required for embryonic stem cell identity and proper
CC differentiation. {ECO:0000250|UniProtKB:Q92800}.
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:Q92800};
CC -!- SUBUNIT: Component of the PRC2/EED-EZH1 complex, which includes EED,
CC EZH1, SUZ12, RBBP4 and AEBP2. The PRC2/EED-EZH1 is less abundant than
CC the PRC2/EED-EZH2 complex, has weak methyltransferase activity and
CC compacts chromatin in the absence of the methyltransferase cofactor S-
CC adenosyl-L-methionine (SAM). Interacts with EZHIP; the interaction
CC blocks EZH1 methyltransferase activity. {ECO:0000250|UniProtKB:Q92800}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92800}.
CC Note=Colocalizes with trimethylated 'Lys-27' of histone H3.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A7E2Z2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A7E2Z2-2; Sequence=VSP_036369;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC151626; AAI51627.1; -; mRNA.
DR RefSeq; NP_001095621.1; NM_001102151.2. [A7E2Z2-2]
DR RefSeq; XP_005220793.1; XM_005220736.3. [A7E2Z2-1]
DR RefSeq; XP_015314321.1; XM_015458835.1.
DR AlphaFoldDB; A7E2Z2; -.
DR SMR; A7E2Z2; -.
DR STRING; 9913.ENSBTAP00000063661; -.
DR PaxDb; 9913-ENSBTAP00000029222; -.
DR Ensembl; ENSBTAT00000029222.5; ENSBTAP00000029222.4; ENSBTAG00000021918.5. [A7E2Z2-2]
DR GeneID; 533087; -.
DR KEGG; bta:533087; -.
DR CTD; 2145; -.
DR VEuPathDB; HostDB:ENSBTAG00000021918; -.
DR eggNOG; KOG1079; Eukaryota.
DR GeneTree; ENSGT00940000156604; -.
DR HOGENOM; CLU_011342_0_0_1; -.
DR InParanoid; A7E2Z2; -.
DR OrthoDB; 902834at2759; -.
DR TreeFam; TF314509; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000021918; Expressed in neutrophil and 104 other cell types or tissues.
DR ExpressionAtlas; A7E2Z2; baseline and differential.
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 H3K27 methyltransferase activity; IBA:GO_Central.
DR GO; GO:0140951; F:histone H3K27 trimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0031507; P:heterochromatin formation; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd00167; SANT; 1.
DR CDD; cd19217; SET_EZH1; 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; IPR044438; EZH1_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:SF1; HISTONE-LYSINE N-METHYLTRANSFERASE EZH1; 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 2: Evidence at transcript level;
KW Alternative splicing; Chromatin regulator; Isopeptide bond;
KW Methyltransferase; Nucleus; Reference proteome; Repressor;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase; Ubl conjugation.
FT CHAIN 1..747
FT /note="Histone-lysine N-methyltransferase EZH1"
FT /id="PRO_0000363956"
FT DOMAIN 504..606
FT /note="CXC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00970"
FT DOMAIN 613..728
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 186..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 327
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92800"
FT VAR_SEQ 700..747
FT /note="VVMVNGDHRIGIFAKRAIQAGEELFFDYRYSQADALKYVGIERETDVL ->
FT AKITDLKA (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_036369"
SQ SEQUENCE 747 AA; 85285 MW; A40D3D08F63CA155 CRC64;
MDIPNPPTSK CITYWKRKVK SEYMRLRQLK RLQANMGAKA LYVANFAKVQ EKTQILNEEW
KKLRVQPVQL MKPVSGHPFL KKCTIESIFP GFASQHMLMR SLNTVALVPI MYSWSPLQQN
FMVEDETVLC NIPYMGDEVK EEDETFIEEL INNYDGKVHG EEEMIPGSVL ISDAVFLELV
DALNQYSDED EEGHNDTSDG KQDDSKEDLP VTRKRKRHAI EGSKKSSKKQ FPNDMIFSAI
ASMFPENGVP DDMKERYREL TEMSDPNALP PQCTPNIDGP NAKSVQREQS LHSFHTLFCR
RCFKYDCFLH PFHATPNVYK RKNKEIKIEP EPCGTDCFLL LEGAKEYAML HNPRSKCSGR
RRRRHHVVNA SCSNTSASAV AETKEGDSDR DTGNDWASSS SEANSRCQTP TKQKASPAPP
QLCVVEAPSE PVEWTGAEES LFRVFHGTYF NNFCSIARLL GTKTCKQVFQ FAVKESLILK
LPTDELMNPS QKKKRKHRLW AAHCRKIQLK KDNSSTQVYN YQPCDHPDRP CDSTCPCIMT
QNFCEKFCQC NPDCQNRFPG CRCKTQCNTK QCPCYLAVRE CDPDLCLTCG ASEHWDCKVV
SCKNCSIQRG LKKHLLLAPS DVAGWGTFIK ESVQKNEFIS EYCGELISQD EADRRGKVYD
KYMSSFLFNL NNDFVVDATR KGNKIRFANH SVNPNCYAKV VMVNGDHRIG IFAKRAIQAG
EELFFDYRYS QADALKYVGI ERETDVL
//
