SETD6_BOVIN
ID SETD6_BOVIN Reviewed; 450 AA.
AC E1BI64; A5D7G4;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 71.
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 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 GENOMIC DNA].
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2007) 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=E1BI64-1; Sequence=Displayed;
CC Name=2;
CC IsoId=E1BI64-2; Sequence=VSP_040723;
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; AAFC03050240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC140545; AAI40546.1; -; mRNA.
DR RefSeq; NP_001091571.1; NM_001098102.1.
DR RefSeq; XP_005218752.1; XM_005218695.3. [E1BI64-1]
DR AlphaFoldDB; E1BI64; -.
DR SMR; E1BI64; -.
DR STRING; 9913.ENSBTAP00000027690; -.
DR PaxDb; E1BI64; -.
DR PRIDE; E1BI64; -.
DR GeneID; 539651; -.
DR KEGG; bta:539651; -.
DR CTD; 79918; -.
DR eggNOG; KOG1338; Eukaryota.
DR HOGENOM; CLU_017135_2_0_1; -.
DR InParanoid; E1BI64; -.
DR OrthoDB; 490654at2759; -.
DR TreeFam; TF106399; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Alternative splicing; Methylation; Methyltransferase; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..450
FT /note="N-lysine methyltransferase SETD6"
FT /id="PRO_0000405840"
FT DOMAIN 39..263
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 50..52
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TBK2"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8TBK2"
FT BINDING 200
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TBK2"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8TBK2"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8TBK2"
FT BINDING 228..229
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TBK2"
FT BINDING 274
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TBK2"
FT MOD_RES 40
FT /note="N6-methylated lysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q8TBK2"
FT MOD_RES 156
FT /note="N6-methylated lysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q8TBK2"
FT MOD_RES 349
FT /note="N6-methylated lysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q8TBK2"
FT VAR_SEQ 135..179
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_040723"
FT CONFLICT 181
FT /note="S -> C (in Ref. 2; AAI40546)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 450 AA; 51097 MW; 6AA72F595E16D25F CRC64;
MATQAKRRRV AGPAGSDDDP APVASFLSWC QRVGLELSPK VAVSRQGTVA GYGMVARESV
QPGELLFAVP RAALLSQHTC SISGVLERER GALQSQSGWV PLLLALLHEM QAPASPWSPY
FALWPELGRL QHPMFWPEEE RRRLLQGTGV PEAVEKDLVN IRSEYYSIVL PFMDAHPDLF
SPRVRSLELY RQLVALVMAY SFQEPLEEEE DEKEPNSPLM VPAADILNHL ANHNANLEYS
PTCLRMVAIQ PIPKGHEIFN TYGQMANWQL IHMYGFAEPY PDNTNDTADI QMVTVREAAL
QGTKVEAERL LLYERWDFLC KLEMVGEEGA FVIGREEVLT EEELATTLKV LCMPAEEFRA
FKDQNGWEDD KSEEDSLTIT DIPKLKASWR QLLRDSVLLT LQTYATDLKT EQDLLSNKEV
YAALSWREQQ ALQVRYGQKM ILHRLLELTR
