EZH1_PONAB
ID EZH1_PONAB Reviewed; 747 AA.
AC Q5RDS6;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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 -!- 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; CR857825; CAH90081.1; -; mRNA.
DR RefSeq; NP_001124996.1; NM_001131524.1.
DR AlphaFoldDB; Q5RDS6; -.
DR SMR; Q5RDS6; -.
DR STRING; 9601.ENSPPYP00000023752; -.
DR PRIDE; Q5RDS6; -.
DR GeneID; 100171872; -.
DR KEGG; pon:100171872; -.
DR CTD; 2145; -.
DR eggNOG; KOG1079; Eukaryota.
DR InParanoid; Q5RDS6; -.
DR Proteomes; UP000001595; Unplaced.
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:0006338; P:chromatin remodeling; IEA:InterPro.
DR GO; GO:0070734; P:histone H3-K27 methylation; IEA:InterPro.
DR CDD; cd00167; SANT; 1.
DR CDD; cd19217; SET_EZH1; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR026489; CXC_dom.
DR InterPro; IPR032926; EZH1.
DR InterPro; IPR045318; EZH1/2-like.
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; PTHR45747; 1.
DR PANTHER; PTHR45747:SF1; PTHR45747:SF1; 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 Chromatin regulator; Isopeptide bond; Methyltransferase; Nucleus;
KW Reference proteome; Repressor; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation.
FT CHAIN 1..747
FT /note="Histone-lysine N-methyltransferase EZH1"
FT /id="PRO_0000323740"
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 188..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 491..496
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 188..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"
SQ SEQUENCE 747 AA; 85253 MW; B3EC441B32D103D8 CRC64;
MEIPNPPTSK CITYWKRKVK SEYMRLRQLK RLQANMGAKA LYVANFAKVQ EKTQILNEEW
KKLRVQPVQS MKPVCGHPFL KKCTIESIFP GFASQHMLMR SLNTVALVPI MYSWSPLQQN
FMVEDETVLC NIPYMGDEVK EEDETFIEEL INNYDGKVHG EEEMIPGSVL ISDAVFLELV
DALNQYSDEE EEGHNDTSDG KQDDSKEDLP VTRKRKRHAI EGNKKSSKKQ FPNDMIFSAI
ASMFPENGVP DDMKERYREL TEMSDPNALP PQCTPNIDGP NAKSVQREQS LHSFHTLFCR
RCFKYDCFLH PFHATPNVYK RKNKEIKIEP EPCGTDCFLL LEGAKEYAML HNPRSKCSGR
RRRRHHIVSA SCSNASASAV 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
EELFLDYRYS QADALKYVGI ERETDVL
