ID A0A2K5LHP0_CERAT Unreviewed; 366 AA.
AC A0A2K5LHP0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Histone-lysine N-methyltransferase SETD7 {ECO:0000256|ARBA:ARBA00020512, ECO:0000256|PIRNR:PIRNR037249};
DE EC=2.1.1.- {ECO:0000256|PIRNR:PIRNR037249};
DE AltName: Full=SET domain-containing protein 7 {ECO:0000256|ARBA:ARBA00030095, ECO:0000256|PIRNR:PIRNR037249};
GN Name=SETD7 {ECO:0000313|Ensembl:ENSCATP00000012446.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000012446.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000012446.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Histone methyltransferase that specifically monomethylates
CC 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag
CC for epigenetic transcriptional activation. Plays a central role in the
CC transcriptional activation of genes. {ECO:0000256|PIRNR:PIRNR037249}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:60264, Rhea:RHEA-COMP:15543, Rhea:RHEA-COMP:15547,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.364;
CC Evidence={ECO:0000256|ARBA:ARBA00023564};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6)-
CC methyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:51736, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13053,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929;
CC Evidence={ECO:0000256|ARBA:ARBA00034257};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51737;
CC Evidence={ECO:0000256|ARBA:ARBA00034257};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR037249}.
CC Chromosome {ECO:0000256|PIRNR:PIRNR037249}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. SET7 subfamily.
CC {ECO:0000256|PIRNR:PIRNR037249}.
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 RefSeq; XP_011904629.1; XM_012049239.1.
DR AlphaFoldDB; A0A2K5LHP0; -.
DR STRING; 9531.ENSCATP00000012446; -.
DR Ensembl; ENSCATT00000036576.1; ENSCATP00000012446.1; ENSCATG00000030383.1.
DR GeneID; 105580796; -.
DR KEGG; caty:105580796; -.
DR CTD; 80854; -.
DR GeneTree; ENSGT00390000004827; -.
DR OMA; RITHTEV; -.
DR OrthoDB; 5304435at2759; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000030383; Expressed in skeletal muscle tissue and 12 other cell types or tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0140945; F:histone H3K4 monomethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0002039; F:p53 binding; IEA:Ensembl.
DR GO; GO:0006974; P:DNA damage response; IEA:Ensembl.
DR GO; GO:0070828; P:heterochromatin organization; IEA:Ensembl.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd10530; SET_SETD7; 1.
DR Gene3D; 2.20.110.10; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 3.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR InterPro; IPR017155; Hist-Lys_N-MeTrfase_SETD7.
DR InterPro; IPR003409; MORN.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR044436; SETD7_SET.
DR PANTHER; PTHR46820; HISTONE-LYSINE N-METHYLTRANSFERASE SETD7; 1.
DR PANTHER; PTHR46820:SF1; HISTONE-LYSINE N-METHYLTRANSFERASE SETD7; 1.
DR Pfam; PF02493; MORN; 4.
DR Pfam; PF00856; SET; 1.
DR PIRSF; PIRSF037249; Histone_Lys_mtfrase_SET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82185; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS51577; SAM_MT43_SET7; 1.
DR PROSITE; PS50280; SET; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159, ECO:0000256|PIRNR:PIRNR037249};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW ECO:0000256|PIRNR:PIRNR037249}; Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|PIRNR:PIRNR037249};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR037249};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRNR:PIRNR037249};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR037249};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|PIRNR:PIRNR037249};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR037249}.
FT DOMAIN 214..336
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT BINDING 226..228
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR037249-1"
FT BINDING 296
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR037249-1"
FT BINDING 297
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR037249-1"
FT BINDING 356
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR037249-1"
FT SITE 245
FT /note="Histone H3K4 binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR037249-2"
FT SITE 256
FT /note="Histone H3K4 binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR037249-2"
FT SITE 266
FT /note="Histone H3K4 binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR037249-2"
FT SITE 317
FT /note="Histone H3K4 binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR037249-2"
FT SITE 335
FT /note="Histone H3K4 binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR037249-2"
SQ SEQUENCE 366 AA; 40703 MW; 9211907078E37CC8 CRC64;
MDSDDEMVEE AVEGHLDDDG LPHGFCTVTY SSTDRFEGNF VHGEKNGRGK FFFFDGSTLE
GYYVDDALQG QGVYTYEDGG VLQGTYVDGE LNGPAQEYDT DGRLIFKGQY KDNIRHGVCW
IYYPDGGSLV GEVNEDGEMT GEKIAYVYPD ERTALYGKFI DGEMIEGKLA TLMSTEEGRP
HFELLPGNSV YHFDKSTSSC ISTNALLPDP YESERVYVAE SLISSAGEGL FSKVAVGPNT
VMSFYNGVRI THQEVDSRDW ALNGNTLSLD EETVIDVPEP YNHVSKYCAS LGHKANHSFT
PNCIYDMFVH PRFGPIKCIR TLRAVEADEE LTVAYGYDHS PPGKSGPEAP EWYQVELKAF
QATQQK
//
