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Database: UniProt
Entry: Q80UJ9
LinkDB: Q80UJ9
Original site: Q80UJ9 
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   13-FEB-2019, entry version 104.
DE   RecName: Full=Histone-lysine N-methyltransferase SETMAR {ECO:0000305};
DE            EC=2.1.1.43 {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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the 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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Histone methyltransferase that methylates 'Lys-4' and
CC       'Lys-36' of histone H3, 2 specific tags for epigenetic
CC       transcriptional activation. Specifically mediates dimethylation of
CC       H3 'Lys-36'. {ECO:0000250|UniProtKB:Q53H47}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
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
CC       are arranged in a triangular cluster; some of these Cys residues
CC       contribute 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
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
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   UniGene; Mm.56539; -.
DR   ProteinModelPortal; Q80UJ9; -.
DR   SMR; Q80UJ9; -.
DR   STRING; 10090.ENSMUSP00000048225; -.
DR   iPTMnet; Q80UJ9; -.
DR   PhosphoSitePlus; Q80UJ9; -.
DR   PaxDb; Q80UJ9; -.
DR   PRIDE; Q80UJ9; -.
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   eggNOG; KOG1082; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000162663; -.
DR   HOGENOM; HOG000020052; -.
DR   HOVERGEN; HBG093940; -.
DR   InParanoid; Q80UJ9; -.
DR   KO; K11433; -.
DR   OMA; YDSSLYC; -.
DR   OrthoDB; 753093at2759; -.
DR   TreeFam; TF316038; -.
DR   PRO; PR:Q80UJ9; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   Bgee; ENSMUSG00000034639; Expressed in 239 organ(s), highest expression level in ear vesicle.
DR   ExpressionAtlas; Q80UJ9; baseline and differential.
DR   Genevisible; Q80UJ9; MM.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0010452; P:histone H3-K36 methylation; ISS:UniProtKB.
DR   GO; GO:0051568; P:histone H3-K4 methylation; ISS:UniProtKB.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR007728; Pre-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF05033; Pre-SET; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00468; PreSET; 1.
DR   SMART; SM00317; SET; 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; Complete proteome; Metal-binding;
KW   Methyltransferase; Nucleus; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase; Zinc.
FT   CHAIN         1    309       Histone-lysine N-methyltransferase
FT                                SETMAR.
FT                                /FTId=PRO_0000259527.
FT   DOMAIN       74    137       Pre-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00157}.
FT   DOMAIN      140    264       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN      284    300       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   REGION      150    152       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250|UniProtKB:Q53H47}.
FT   REGION      224    225       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250|UniProtKB:Q53H47}.
FT   METAL        76     76       Zinc 1. {ECO:0000250|UniProtKB:Q53H47}.
FT   METAL        76     76       Zinc 2. {ECO:0000250|UniProtKB:Q53H47}.
FT   METAL        78     78       Zinc 1. {ECO:0000250|UniProtKB:Q53H47}.
FT   METAL        83     83       Zinc 1. {ECO:0000250|UniProtKB:Q53H47}.
FT   METAL        83     83       Zinc 3. {ECO:0000250|UniProtKB:Q53H47}.
FT   METAL        88     88       Zinc 1. {ECO:0000250|UniProtKB:Q53H47}.
FT   METAL        90     90       Zinc 2. {ECO:0000250|UniProtKB:Q53H47}.
FT   METAL       119    119       Zinc 2. {ECO:0000250|UniProtKB:Q53H47}.
FT   METAL       119    119       Zinc 3. {ECO:0000250|UniProtKB:Q53H47}.
FT   METAL       123    123       Zinc 2. {ECO:0000250|UniProtKB:Q53H47}.
FT   METAL       125    125       Zinc 3. {ECO:0000250|UniProtKB:Q53H47}.
FT   METAL       129    129       Zinc 3. {ECO:0000250|UniProtKB:Q53H47}.
FT   METAL       227    227       Zinc 4. {ECO:0000250|UniProtKB:Q53H47}.
FT   METAL       288    288       Zinc 4. {ECO:0000250|UniProtKB:Q53H47}.
FT   METAL       290    290       Zinc 4. {ECO:0000250|UniProtKB:Q53H47}.
FT   METAL       295    295       Zinc 4. {ECO:0000250|UniProtKB:Q53H47}.
FT   BINDING     193    193       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING     221    221       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   CONFLICT    103    103       L -> F (in Ref. 2; AAH45208).
FT                                {ECO:0000305}.
FT   CONFLICT    273    273       S -> R (in Ref. 2; AAH45208).
FT                                {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
//
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