GenomeNet

Database: UniProt/SWISS-PROT
Entry: SETB2_HUMAN
LinkDB: SETB2_HUMAN
Original site: SETB2_HUMAN 
ID   SETB2_HUMAN             Reviewed;         719 AA.
AC   Q96T68; Q5TC65; Q5TC66; Q5W0A7; Q659A7; Q86UD6; Q96AI6;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   20-DEC-2017, entry version 142.
DE   RecName: Full=Histone-lysine N-methyltransferase SETDB2;
DE            EC=2.1.1.43;
DE   AltName: Full=Chronic lymphocytic leukemia deletion region gene 8 protein;
DE   AltName: Full=Lysine N-methyltransferase 1F;
DE   AltName: Full=SET domain bifurcated 2;
GN   Name=SETDB2; Synonyms=C13orf4, CLLD8, KMT1F;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLY-117.
RX   PubMed=11306461;
RA   Mabuchi H., Fujii H., Calin G., Alder H., Negrini M., Rassenti L.,
RA   Kipps T.J., Bullrich F., Croce C.M.;
RT   "Cloning and characterization of CLLD6, CLLD7, and CLLD8, novel
RT   candidate genes for leukemogenesis at chromosome 13q14, a region
RT   commonly deleted in B-cell chronic lymphocytic leukemia.";
RL   Cancer Res. 61:2870-2877(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057823; DOI=10.1038/nature02379;
RA   Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA   Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
RA   Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA   Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA   Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA   Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
RA   Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA   Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA   Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA   Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA   Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA   Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA   Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA   King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA   Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA   Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA   Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
RA   Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA   Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA   Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA   Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA   Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
RT   "The DNA sequence and analysis of human chromosome 13.";
RL   Nature 428:522-528(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
RP   MET-473.
RC   TISSUE=Colon, and Testis;
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).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 332-719 (ISOFORM 3), AND
RP   VARIANT MET-473.
RC   TISSUE=Amygdala;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=20404330; DOI=10.1074/jbc.M109.052399;
RA   Falandry C., Fourel G., Galy V., Ristriani T., Horard B., Bensimon E.,
RA   Salles G., Gilson E., Magdinier F.;
RT   "CLLD8/KMT1F is a lysine methyltransferase that is important for
RT   chromosome segregation.";
RL   J. Biol. Chem. 285:20234-20241(2010).
RN   [6]
RP   VARIANTS GLY-117 AND MET-473.
RX   PubMed=12754510; DOI=10.1038/ng1166;
RA   Zhang Y., Leaves N.I., Anderson G.G., Ponting C.P., Broxholme J.,
RA   Holt R., Edser P., Bhattacharyya S., Dunham A., Adcock I.M.,
RA   Pulleyn L., Barnes P.J., Harper J.I., Abecasis G., Cardon L.,
RA   White M., Burton J., Matthews L., Mott R., Ross M., Cox R.,
RA   Moffatt M.F., Cookson W.O.C.M.;
RT   "Positional cloning of a quantitative trait locus on chromosome 13q14
RT   that influences immunoglobulin E levels and asthma.";
RL   Nat. Genet. 34:181-186(2003).
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.
CC       {ECO:0000269|PubMed:20404330}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
CC       S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC   -!- INTERACTION:
CC       Q8N8R7:ARL14EP; NbExp=3; IntAct=EBI-1222089, EBI-2807994;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20404330}.
CC       Chromosome {ECO:0000305|PubMed:20404330}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q96T68-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96T68-2; Sequence=VSP_008413;
CC         Note=No experimental confirmation available.;
CC       Name=3;
CC         IsoId=Q96T68-3; Sequence=VSP_024034;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Highest expression in heart,
CC       testis and ovary.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAH56265.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC       Sequence=CAI10818.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AF334407; AAK38373.1; -; mRNA.
DR   EMBL; AL139321; CAH71048.1; -; Genomic_DNA.
DR   EMBL; AL136218; CAH71048.1; JOINED; Genomic_DNA.
DR   EMBL; AL136218; CAI10817.1; -; Genomic_DNA.
DR   EMBL; AL139321; CAI10817.1; JOINED; Genomic_DNA.
DR   EMBL; AL136218; CAI10818.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC017078; AAH17078.1; -; mRNA.
DR   EMBL; BC047434; AAH47434.1; -; mRNA.
DR   EMBL; AL831937; CAH56265.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS53868.1; -. [Q96T68-2]
DR   CCDS; CCDS9417.1; -. [Q96T68-1]
DR   RefSeq; NP_001153780.1; NM_001160308.2. [Q96T68-2]
DR   RefSeq; NP_114121.2; NM_031915.2. [Q96T68-1]
DR   UniGene; Hs.631789; -.
DR   PDB; 5TFP; X-ray; 2.00 A; A/B=1-64.
DR   PDBsum; 5TFP; -.
DR   ProteinModelPortal; Q96T68; -.
DR   SMR; Q96T68; -.
DR   BioGrid; 123768; 14.
DR   IntAct; Q96T68; 2.
DR   STRING; 9606.ENSP00000326477; -.
DR   iPTMnet; Q96T68; -.
DR   PhosphoSitePlus; Q96T68; -.
DR   BioMuta; SETDB2; -.
DR   DMDM; 143811459; -.
DR   PaxDb; Q96T68; -.
DR   PeptideAtlas; Q96T68; -.
DR   PRIDE; Q96T68; -.
DR   Ensembl; ENST00000317257; ENSP00000326477; ENSG00000136169. [Q96T68-2]
DR   Ensembl; ENST00000354234; ENSP00000346175; ENSG00000136169. [Q96T68-1]
DR   GeneID; 83852; -.
DR   KEGG; hsa:83852; -.
DR   UCSC; uc001vcz.4; human. [Q96T68-1]
DR   CTD; 83852; -.
DR   DisGeNET; 83852; -.
DR   EuPathDB; HostDB:ENSG00000136169.16; -.
DR   GeneCards; SETDB2; -.
DR   H-InvDB; HIX0011315; -.
DR   HGNC; HGNC:20263; SETDB2.
DR   HPA; CAB012190; -.
DR   HPA; HPA071677; -.
DR   MIM; 607865; gene.
DR   neXtProt; NX_Q96T68; -.
DR   OpenTargets; ENSG00000136169; -.
DR   PharmGKB; PA134956285; -.
DR   eggNOG; KOG1141; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00780000121845; -.
DR   HOVERGEN; HBG106688; -.
DR   InParanoid; Q96T68; -.
DR   KO; K18494; -.
DR   OMA; KCHFQRR; -.
DR   PhylomeDB; Q96T68; -.
DR   TreeFam; TF106411; -.
DR   Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
DR   ChiTaRS; SETDB2; human.
DR   GenomeRNAi; 83852; -.
DR   PRO; PR:Q96T68; -.
DR   Proteomes; UP000005640; Chromosome 13.
DR   Bgee; ENSG00000136169; -.
DR   CleanEx; HS_SETDB2; -.
DR   ExpressionAtlas; Q96T68; baseline and differential.
DR   Genevisible; Q96T68; HS.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0046974; F:histone methyltransferase activity (H3-K9 specific); IDA:UniProtKB.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; TAS:Reactome.
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; IMP:UniProtKB.
DR   GO; GO:0001947; P:heart looping; ISS:UniProtKB.
DR   GO; GO:0051567; P:histone H3-K9 methylation; IDA:UniProtKB.
DR   GO; GO:0070986; P:left/right axis specification; ISS:UniProtKB.
DR   GO; GO:0000278; P:mitotic cell cycle; IMP: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   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell cycle; Cell division;
KW   Chromatin regulator; Chromosome; Complete proteome;
KW   Developmental protein; Metal-binding; Methyltransferase; Mitosis;
KW   Nucleus; Polymorphism; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase; Zinc.
FT   CHAIN         1    719       Histone-lysine N-methyltransferase
FT                                SETDB2.
FT                                /FTId=PRO_0000186088.
FT   DOMAIN      157    229       MBD. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00338}.
FT   DOMAIN      291    364       Pre-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00157}.
FT   DOMAIN      367    694       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   REGION      377    379       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION      651    652       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   METAL       293    293       Zinc 1. {ECO:0000250}.
FT   METAL       293    293       Zinc 2. {ECO:0000250}.
FT   METAL       295    295       Zinc 1. {ECO:0000250}.
FT   METAL       299    299       Zinc 1. {ECO:0000250}.
FT   METAL       299    299       Zinc 3. {ECO:0000250}.
FT   METAL       305    305       Zinc 1. {ECO:0000250}.
FT   METAL       307    307       Zinc 2. {ECO:0000250}.
FT   METAL       345    345       Zinc 2. {ECO:0000250}.
FT   METAL       345    345       Zinc 3. {ECO:0000250}.
FT   METAL       349    349       Zinc 2. {ECO:0000250}.
FT   METAL       351    351       Zinc 3. {ECO:0000250}.
FT   METAL       356    356       Zinc 3. {ECO:0000250}.
FT   METAL       654    654       Zinc 4. {ECO:0000250}.
FT   METAL       707    707       Zinc 4. {ECO:0000250}.
FT   METAL       709    709       Zinc 4. {ECO:0000250}.
FT   METAL       714    714       Zinc 4. {ECO:0000250}.
FT   BINDING     418    418       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING     648    648       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   VAR_SEQ      70     81       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_008413.
FT   VAR_SEQ     523    523       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:17974005}.
FT                                /FTId=VSP_024034.
FT   VARIANT     117    117       E -> G (in dbSNP:rs7998427).
FT                                {ECO:0000269|PubMed:11306461,
FT                                ECO:0000269|PubMed:12754510}.
FT                                /FTId=VAR_031282.
FT   VARIANT     473    473       V -> M (in dbSNP:rs2057413).
FT                                {ECO:0000269|PubMed:12754510,
FT                                ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:17974005}.
FT                                /FTId=VAR_016976.
FT   HELIX         8     17       {ECO:0000244|PDB:5TFP}.
FT   HELIX        21     40       {ECO:0000244|PDB:5TFP}.
FT   HELIX        46     60       {ECO:0000244|PDB:5TFP}.
FT   TURN         61     63       {ECO:0000244|PDB:5TFP}.
SQ   SEQUENCE   719 AA;  81894 MW;  01CD2CFE5C1D9067 CRC64;
     MGEKNGDAKT FWMELEDDGK VDFIFEQVQN VLQSLKQKIK DGSATNKEYI QAMILVNEAT
     IINSSTSIKG ASQKEVNAQS SDPMPVTQKE QENKSNAFPS TSCENSFPED CTFLTTENKE
     ILSLEDKVVD FREKDSSSNL SYQSHDCSGA CLMKMPLNLK GENPLQLPIK CHFQRRHAKT
     NSHSSALHVS YKTPCGRSLR NVEEVFRYLL ETECNFLFTD NFSFNTYVQL ARNYPKQKEV
     VSDVDISNGV ESVPISFCNE IDSRKLPQFK YRKTVWPRAY NLTNFSSMFT DSCDCSEGCI
     DITKCACLQL TARNAKTSPL SSDKITTGYK YKRLQRQIPT GIYECSLLCK CNRQLCQNRV
     VQHGPQVRLQ VFKTEQKGWG VRCLDDIDRG TFVCIYSGRL LSRANTEKSY GIDENGRDEN
     TMKNIFSKKR KLEVACSDCE VEVLPLGLET HPRTAKTEKC PPKFSNNPKE LTVETKYDNI
     SRIQYHSVIR DPESKTAIFQ HNGKKMEFVS SESVTPEDND GFKPPREHLN SKTKGAQKDS
     SSNHVDEFED NLLIESDVID ITKYREETPP RSRCNQATTL DNQNIKKAIE VQIQKPQEGR
     STACQRQQVF CDEELLSETK NTSSDSLTKF NKGNVFLLDA TKEGNVGRFL NHSCCPNLLV
     QNVFVETHNR NFPLVAFFTN RYVKARTELT WDYGYEAGTV PEKEIFCQCG VNKCRKKIL
//
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