GenomeNet

Database: UniProt
Entry: Q8C267
LinkDB: Q8C267
Original site: Q8C267 
ID   SETB2_MOUSE             Reviewed;         713 AA.
AC   Q8C267;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   13-FEB-2019, entry version 118.
DE   RecName: Full=Histone-lysine N-methyltransferase SETDB2;
DE            EC=2.1.1.43;
DE   AltName: Full=SET domain bifurcated 2;
GN   Name=Setdb2; Synonyms=Gm293;
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 MRNA] (ISOFORM 2).
RC   STRAIN=NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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).
CC   -!- FUNCTION: Histone methyltransferase involved in left-right axis
CC       specification in early development and mitosis. Specifically
CC       trimethylates 'Lys-9' of histone H3 (H3K9me3). H3K9me3 is a
CC       specific tag for epigenetic transcriptional repression that
CC       recruits HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated
CC       histones. Contributes to H3K9me3 in both the interspersed
CC       repetitive elements and centromere-associated repeats. Plays a
CC       role in chromosome condensation and segregation during mitosis (By
CC       similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8C267-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C267-2; Sequence=VSP_024063, VSP_024064, VSP_024065;
CC         Note=No experimental confirmation available.;
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}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
DR   EMBL; AK089197; BAC40789.1; -; mRNA.
DR   EMBL; AC114007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   UniGene; Mm.205022; -.
DR   ProteinModelPortal; Q8C267; -.
DR   SMR; Q8C267; -.
DR   STRING; 10090.ENSMUSP00000093450; -.
DR   PhosphoSitePlus; Q8C267; -.
DR   PaxDb; Q8C267; -.
DR   PRIDE; Q8C267; -.
DR   Ensembl; ENSMUST00000095775; ENSMUSP00000093450; ENSMUSG00000071350. [Q8C267-1]
DR   Ensembl; ENSMUST00000111253; ENSMUSP00000106884; ENSMUSG00000071350. [Q8C267-2]
DR   UCSC; uc007uei.1; mouse. [Q8C267-1]
DR   UCSC; uc007uej.1; mouse. [Q8C267-2]
DR   MGI; MGI:2685139; Setdb2.
DR   eggNOG; KOG1141; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000158209; -.
DR   HOGENOM; HOG000060314; -.
DR   HOVERGEN; HBG106688; -.
DR   InParanoid; Q8C267; -.
DR   PhylomeDB; Q8C267; -.
DR   TreeFam; TF106411; -.
DR   Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR   PRO; PR:Q8C267; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   Bgee; ENSMUSG00000071350; Expressed in 208 organ(s), highest expression level in oocyte.
DR   ExpressionAtlas; Q8C267; baseline and differential.
DR   Genevisible; Q8C267; MM.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0046974; F:histone methyltransferase activity (H3-K9 specific); ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR   GO; GO:0001947; P:heart looping; ISS:UniProtKB.
DR   GO; GO:0051567; P:histone H3-K9 methylation; ISS:UniProtKB.
DR   GO; GO:0070986; P:left/right axis specification; ISS:UniProtKB.
DR   GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   InterPro; IPR016177; DNA-bd_dom_sf.
DR   InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR   InterPro; IPR007728; Pre-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF01429; MBD; 1.
DR   Pfam; PF05033; Pre-SET; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00391; MBD; 1.
DR   SMART; SM00468; PreSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF54171; SSF54171; 1.
DR   PROSITE; PS50982; MBD; 1.
DR   PROSITE; PS50867; PRE_SET; 1.
DR   PROSITE; PS50280; SET; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell cycle; Cell division; Chromatin regulator;
KW   Chromosome; Complete proteome; Developmental protein; Metal-binding;
KW   Methyltransferase; Mitosis; Nucleus; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase; Zinc.
FT   CHAIN         1    713       Histone-lysine N-methyltransferase
FT                                SETDB2.
FT                                /FTId=PRO_0000281824.
FT   DOMAIN      161    233       MBD. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00338}.
FT   DOMAIN      294    367       Pre-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00157}.
FT   DOMAIN      370    688       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   REGION      380    382       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION      645    646       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   METAL       296    296       Zinc 1. {ECO:0000250}.
FT   METAL       296    296       Zinc 2. {ECO:0000250}.
FT   METAL       298    298       Zinc 1. {ECO:0000250}.
FT   METAL       302    302       Zinc 1. {ECO:0000250}.
FT   METAL       302    302       Zinc 3. {ECO:0000250}.
FT   METAL       308    308       Zinc 1. {ECO:0000250}.
FT   METAL       310    310       Zinc 2. {ECO:0000250}.
FT   METAL       348    348       Zinc 2. {ECO:0000250}.
FT   METAL       348    348       Zinc 3. {ECO:0000250}.
FT   METAL       352    352       Zinc 2. {ECO:0000250}.
FT   METAL       354    354       Zinc 3. {ECO:0000250}.
FT   METAL       359    359       Zinc 3. {ECO:0000250}.
FT   METAL       648    648       Zinc 4. {ECO:0000250}.
FT   METAL       701    701       Zinc 4. {ECO:0000250}.
FT   METAL       703    703       Zinc 4. {ECO:0000250}.
FT   METAL       708    708       Zinc 4. {ECO:0000250}.
FT   BINDING     642    642       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   VAR_SEQ      70     86       GMFITYSNPEVNTHRSN -> D (in isoform 2).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_024063.
FT   VAR_SEQ     119    156       SPGKKVFLPVKNKADNLVKKEAPLHISFHRHICSRTCL ->
FT                                YVYVIRVSAPSVCCLLNIPKSLTPFIKFNSRCLCLLVN
FT                                (in isoform 2).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_024064.
FT   VAR_SEQ     157    713       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_024065.
SQ   SEQUENCE   713 AA;  80636 MW;  C4E750F01ED4231A CRC64;
     MEEKNGDAKT FWMELQDDGK VDLMFEKTQN VLHSLKQKIK DGSATNGDYV QAMNLVNEAT
     LSNTQTLEKG MFITYSNPEV NTHRSNHTPV TQSEQENKSS AVPSASCDNS CPKGCTIPSP
     GKKVFLPVKN KADNLVKKEA PLHISFHRHI CSRTCLMETP LSLKGENPLQ LPIRCHFQRR
     HAKTNSHSSA LHVNYKTPCG RNLRNMEEVF HYLLETECNF LFTDNFSFNT YVQLTRNHPK
     QNEVVSDVDI SNGVESVSIP FCNEIDNSKL PRFKYRNTVW PRIYHLNFSN MFSDSCDCSE
     GCIDIKKCAC LQLTAKNAKA CPLSSDGECA GYKYKRLQRL IPTGIYECNL LCKCNKQMCQ
     NRVIQHGVRV RLQVFKSEKK GWGVRCLDDI DKGTFVCIYS GRLLRRATPE KTNIGENGRE
     QQHIVKNSFS KKRKLEVVCS DCDAHCDSPK AEDCPPKLSG DLKEPAVEMN HRNISRTQHH
     SVIRRTKSKT TVFHYSEKNM GFVCSDSAAP EDKNGFKPAQ EHVNSEARRA HEDLSSNPAG
     DSEDTQLTES DVIDITASRE DSAPAYRCKH ATIVDRKDTK QVLEVPGKKS QEEEPAASQS
     QQALCDEELP SERTKIPSAS LMQLSKESLF LLDASKEGNV GRFLNHSCCP NLWVQNVFVE
     THDRNFPLVA FFTNRYVKAR TELTWDYGYE AGATPAKEIL CQCGFNKCRK KLI
//
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