SETD6_RAT
ID SETD6_RAT Reviewed; 474 AA.
AC D3ZSK5;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=N-lysine methyltransferase SETD6;
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q8TBK2};
DE AltName: Full=SET domain-containing protein 6;
GN Name=Setd6;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Protein-lysine N-methyltransferase. Monomethylates 'Lys-310'
CC of the RELA subunit of NF-kappa-B complex, leading to down-regulation
CC of NF-kappa-B transcription factor activity. Monomethylates 'Lys-8' of
CC H2AZ (H2AZK8me1) (By similarity). Required for the maintenance of
CC embryonic stem cell self-renewal (By similarity). Methylates PAK4.
CC {ECO:0000250|UniProtKB:Q8TBK2, ECO:0000250|UniProtKB:Q9CWY3}.
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:0000250|UniProtKB:Q8TBK2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51737;
CC Evidence={ECO:0000250|UniProtKB:Q8TBK2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(8)-[histone H2AZ] + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyl-L-lysyl(8)-[histone H2AZ] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:67808, Rhea:RHEA-COMP:17357, Rhea:RHEA-COMP:17358,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929;
CC Evidence={ECO:0000250|UniProtKB:Q8TBK2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67809;
CC Evidence={ECO:0000250|UniProtKB:Q8TBK2};
CC -!- SUBUNIT: Monomer, homodimer and homotrimer; these structures are
CC stabilized in the presence of S-adenosyl-L-methionine (SAM).
CC {ECO:0000250|UniProtKB:Q8TBK2}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8TBK2}.
CC -!- PTM: Automethylated. {ECO:0000250|UniProtKB:Q8TBK2}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. SETD6 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR EMBL; CH474006; EDL87271.1; -; Genomic_DNA.
DR RefSeq; NP_001099637.1; NM_001106167.1.
DR AlphaFoldDB; D3ZSK5; -.
DR SMR; D3ZSK5; -.
DR STRING; 10116.ENSRNOP00000016626; -.
DR PaxDb; D3ZSK5; -.
DR PeptideAtlas; D3ZSK5; -.
DR PRIDE; D3ZSK5; -.
DR Ensembl; ENSRNOT00000016626; ENSRNOP00000016626; ENSRNOG00000012447.
DR GeneID; 291844; -.
DR KEGG; rno:291844; -.
DR UCSC; RGD:1560538; rat.
DR CTD; 79918; -.
DR RGD; 1560538; Setd6.
DR eggNOG; KOG1338; Eukaryota.
DR GeneTree; ENSGT00940000153577; -.
DR HOGENOM; CLU_017135_2_0_1; -.
DR InParanoid; D3ZSK5; -.
DR OMA; EYSADYL; -.
DR OrthoDB; 490654at2759; -.
DR PhylomeDB; D3ZSK5; -.
DR TreeFam; TF106399; -.
DR Reactome; R-RNO-3214841; PKMTs methylate histone lysines.
DR PRO; PR:D3ZSK5; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Proteomes; UP000234681; Chromosome 19.
DR Bgee; ENSRNOG00000012447; Expressed in liver and 20 other tissues.
DR Genevisible; D3ZSK5; RN.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0051059; F:NF-kappaB binding; ISO:RGD.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; ISS:UniProtKB.
DR GO; GO:0034968; P:histone lysine methylation; ISS:UniProtKB.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0018026; P:peptidyl-lysine monomethylation; ISS:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0048863; P:stem cell differentiation; ISS:UniProtKB.
DR GO; GO:0019827; P:stem cell population maintenance; ISS:UniProtKB.
DR CDD; cd19178; SET_SETD6; 1.
DR Gene3D; 3.90.1420.10; -; 1.
DR InterPro; IPR011383; N-lys_methylase_SETD6.
DR InterPro; IPR015353; Rubisco_LSMT_subst-bd.
DR InterPro; IPR036464; Rubisco_LSMT_subst-bd_sf.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR044430; SETD6_SET.
DR Pfam; PF09273; Rubis-subs-bind; 1.
DR Pfam; PF00856; SET; 1.
DR PIRSF; PIRSF011771; RMS1_SET; 1.
DR SUPFAM; SSF81822; SSF81822; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50280; SET; 1.
PE 3: Inferred from homology;
KW Methylation; Methyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..474
FT /note="N-lysine methyltransferase SETD6"
FT /id="PRO_0000405841"
FT DOMAIN 63..287
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 74..76
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TBK2"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8TBK2"
FT BINDING 224
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TBK2"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8TBK2"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8TBK2"
FT BINDING 252..253
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TBK2"
FT BINDING 298
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TBK2"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CWY3"
FT MOD_RES 64
FT /note="N6-methylated lysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q8TBK2"
FT MOD_RES 180
FT /note="N6-methylated lysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q8TBK2"
FT MOD_RES 373
FT /note="N6-methylated lysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q8TBK2"
SQ SEQUENCE 474 AA; 53362 MW; 1673696BC0D7EF40 CRC64;
MAAPAKRARV SDASPLAAPC PVPRAAARVP LPLPAGPSGH EPESDAVAGF LRWCTRVGLE
LSPKVLVSRQ GTVAGYGMVA RESVQPGELL FAVPRSALLS PHTCSISDLL ERERGALQSL
SGWVPLLLAL LHELQAPASP WSPYFALWPE LGRLEHPMFW PEEERLRLLK GTGVPEAVEK
DLVNIRSEYY SIVLPFMEAH SDLFSPTVRS LELYRQLVAL VMAYSFQEPL EEEEDEKEPN
SPLMVPAADI LNHIANHNAN LEYSAEYLRM VATQPILKGH EIFNTYGQMA NWQLIHMYGF
AEPYPNNTDD TADIQMVAVR EAALQGTEDE TERLLLCERW DFLCKQELVG EEGAFVIGRE
EVLTEEELAT TLKVLCMPAE EFRDYKERAG WGEEETEDGS LAITNIPKLQ ESWKRLLRDS
VLLTLQTYAT DLKTEQDLLS NKEVYAKLSW REQQALQVRY GQKMILHRLL ELTS
