SETMR_MOUSE
ID SETMR_MOUSE Reviewed; 309 AA.
AC Q80UJ9; E9QLD6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Histone-lysine N-methyltransferase SETMAR {ECO:0000305};
DE EC=2.1.1.357 {ECO:0000250|UniProtKB:Q53H47};
DE AltName: Full=SET domain without mariner transposase fusion protein {ECO:0000312|MGI:MGI:1921979};
GN Name=Setmar {ECO:0000312|MGI:MGI:1921979};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Histone methyltransferase that methylates 'Lys-4' and 'Lys-
CC 36' of histone H3, 2 specific tags for epigenetic transcriptional
CC activation. Specifically mediates dimethylation of H3 'Lys-36'.
CC {ECO:0000250|UniProtKB:Q53H47}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(36)-[histone H3] + 2 S-adenosyl-L-methionine = 2 H(+)
CC + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3] + 2 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60308, Rhea:RHEA-COMP:9785, Rhea:RHEA-
CC COMP:9787, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61976; EC=2.1.1.357;
CC Evidence={ECO:0000250|UniProtKB:Q53H47};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q53H47}.
CC Chromosome {ECO:0000250|UniProtKB:Q53H47}.
CC -!- DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that are
CC arranged in a triangular cluster; some of these Cys residues contribute
CC to the binding of two zinc ions within the cluster.
CC {ECO:0000250|UniProtKB:Q53H47}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR EMBL; AC153916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC045208; AAH45208.1; -; mRNA.
DR CCDS; CCDS51867.1; -.
DR RefSeq; NP_848478.2; NM_178391.4.
DR AlphaFoldDB; Q80UJ9; -.
DR SMR; Q80UJ9; -.
DR STRING; 10090.ENSMUSP00000048225; -.
DR iPTMnet; Q80UJ9; -.
DR PhosphoSitePlus; Q80UJ9; -.
DR EPD; Q80UJ9; -.
DR PaxDb; Q80UJ9; -.
DR PRIDE; Q80UJ9; -.
DR ProteomicsDB; 256971; -.
DR DNASU; 74729; -.
DR Ensembl; ENSMUST00000049246; ENSMUSP00000048225; ENSMUSG00000034639.
DR GeneID; 74729; -.
DR KEGG; mmu:74729; -.
DR UCSC; uc009dde.3; mouse.
DR CTD; 6419; -.
DR MGI; MGI:1921979; Setmar.
DR VEuPathDB; HostDB:ENSMUSG00000034639; -.
DR eggNOG; KOG1082; Eukaryota.
DR GeneTree; ENSGT00940000162663; -.
DR HOGENOM; CLU_020840_3_3_1; -.
DR InParanoid; Q80UJ9; -.
DR OMA; CEPNLFM; -.
DR OrthoDB; 753093at2759; -.
DR PhylomeDB; Q80UJ9; -.
DR TreeFam; TF316038; -.
DR BioGRID-ORCS; 74729; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q80UJ9; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q80UJ9; protein.
DR Bgee; ENSMUSG00000034639; Expressed in ear vesicle and 212 other tissues.
DR ExpressionAtlas; Q80UJ9; baseline and differential.
DR Genevisible; Q80UJ9; MM.
DR GO; GO:0000793; C:condensed chromosome; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0035861; C:site of double-strand break; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0044547; F:DNA topoisomerase binding; ISO:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0004519; F:endonuclease activity; ISO:MGI.
DR GO; GO:0042054; F:histone methyltransferase activity; IBA:GO_Central.
DR GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); ISS:UniProtKB.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0003697; F:single-stranded DNA binding; ISO:MGI.
DR GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0008283; P:cell population proliferation; ISO:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0000737; P:DNA catabolic process, endonucleolytic; ISO:MGI.
DR GO; GO:0000729; P:DNA double-strand break processing; ISO:MGI.
DR GO; GO:0015074; P:DNA integration; ISO:MGI.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; ISO:MGI.
DR GO; GO:0097676; P:histone H3-K36 dimethylation; ISO:MGI.
DR GO; GO:0010452; P:histone H3-K36 methylation; ISS:UniProtKB.
DR GO; GO:0051568; P:histone H3-K4 methylation; ISS:UniProtKB.
DR GO; GO:0016571; P:histone methylation; IBA:GO_Central.
DR GO; GO:0044774; P:mitotic DNA integrity checkpoint signaling; ISO:MGI.
DR GO; GO:2001251; P:negative regulation of chromosome organization; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:UniProt.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; ISO:MGI.
DR GO; GO:2000373; P:positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity; ISO:MGI.
DR GO; GO:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; ISO:MGI.
DR GO; GO:0031297; P:replication fork processing; ISO:MGI.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR007728; Pre-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR Pfam; PF05033; Pre-SET; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00468; PreSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50867; PRE_SET; 1.
DR PROSITE; PS50280; SET; 1.
PE 2: Evidence at transcript level;
KW Chromatin regulator; Chromosome; Metal-binding; Methyltransferase; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; Zinc.
FT CHAIN 1..309
FT /note="Histone-lysine N-methyltransferase SETMAR"
FT /id="PRO_0000259527"
FT DOMAIN 74..137
FT /note="Pre-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00157"
FT DOMAIN 140..264
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 284..300
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q53H47"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q53H47"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q53H47"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q53H47"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q53H47"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q53H47"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q53H47"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q53H47"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q53H47"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q53H47"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q53H47"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q53H47"
FT BINDING 150..152
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q53H47"
FT BINDING 193
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 221
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 224..225
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q53H47"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q53H47"
FT BINDING 288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q53H47"
FT BINDING 290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q53H47"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q53H47"
FT CONFLICT 103
FT /note="L -> F (in Ref. 2; AAH45208)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="S -> R (in Ref. 2; AAH45208)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 309 AA; 34417 MW; 38F60C1C5B13D80C CRC64;
MSAEGVEKLS LEIAASEEES VAPTEQQDVA CGLENLPVSL WPLGAEPRPK PFQYTPDHVA
GPGADIDPTQ ITFPGCACIE TPCVPGTCSC LRHENNYDDN LCLRDVGSEG KYAKPVFECN
VLCQCGMRCR NRVVQNGLHF LLQVFQTEKK GWGLRTLEFI PKGRFVCEYA GEVLGFSEVQ
RRIHLQTSHD SNYIIAVREH IYSGQIMETF VDPTYIGNIG RFLNHSCEPN LLMIPVRIDS
MVPKLALFAA KDILPGEELS YDYSGRFLNQ VSSKDKEKID CSPPRKPCYC GAQSCTTFLP
YDSSLYMAP
