GenomeNet

Database: UniProt/SWISS-PROT
Entry: SUV92_HUMAN
LinkDB: SUV92_HUMAN
Original site: SUV92_HUMAN 
ID   SUV92_HUMAN             Reviewed;         410 AA.
AC   Q9H5I1; D3DRT4; Q5JSS4; Q5JSS5; Q6I9Y3; Q8ND06;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   15-NOV-2002, sequence version 2.
DT   20-JUN-2018, entry version 163.
DE   RecName: Full=Histone-lysine N-methyltransferase SUV39H2;
DE            EC=2.1.1.43;
DE   AltName: Full=Histone H3-K9 methyltransferase 2;
DE            Short=H3-K9-HMTase 2;
DE   AltName: Full=Lysine N-methyltransferase 1B;
DE   AltName: Full=Suppressor of variegation 3-9 homolog 2;
DE            Short=Su(var)3-9 homolog 2;
GN   Name=SUV39H2; Synonyms=KMT1B;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA   Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA   Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA   Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA   Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA   Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA   Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA   Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA   Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA   Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA   Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA   Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA   Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA   Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA   Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA   Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA   Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA   Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Bone marrow, and Muscle;
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 96-410.
RC   TISSUE=Testis;
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   [7]
RP   FUNCTION.
RX   PubMed=14765126; DOI=10.1038/sj.emboj.7600074;
RA   Ait-Si-Ali S., Guasconi V., Fritsch L., Yahi H., Sekhri R.,
RA   Naguibneva I., Robin P., Cabon F., Polesskaya A., Harel-Bellan A.;
RT   "A Suv39h-dependent mechanism for silencing S-phase genes in
RT   differentiating but not in cycling cells.";
RL   EMBO J. 23:605-615(2004).
RN   [8]
RP   INTERACTION WITH SMAD5.
RX   PubMed=15107829; DOI=10.1038/sj.onc.1207660;
RA   Frontelo P., Leader J.E., Yoo N., Potocki A.C., Crawford M., Kulik M.,
RA   Lechleider R.J.;
RT   "Suv39h histone methyltransferases interact with Smads and cooperate
RT   in BMP-induced repression.";
RL   Oncogene 23:5242-5251(2004).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384 AND SER-388, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381; SER-384 AND
RP   SER-388, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381; SER-384 AND
RP   SER-388, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 112-410 IN COMPLEX WITH
RP   S-ADENOSYL-L-METHIONINE AND ZINC IONS.
RX   PubMed=20084102; DOI=10.1371/journal.pone.0008570;
RA   Wu H., Min J., Lunin V.V., Antoshenko T., Dombrovski L., Zeng H.,
RA   Allali-Hassani A., Campagna-Slater V., Vedadi M., Arrowsmith C.H.,
RA   Plotnikov A.N., Schapira M.;
RT   "Structural biology of human H3K9 methyltransferases.";
RL   PLoS ONE 5:E8570-E8570(2010).
RN   [14]
RP   VARIANT [LARGE SCALE ANALYSIS] HIS-383.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Histone methyltransferase that specifically
CC       trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-
CC       9' as substrate. H3 'Lys-9' trimethylation represents a specific
CC       tag for epigenetic transcriptional repression by recruiting HP1
CC       (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly
CC       functions in heterochromatin regions, thereby playing a central
CC       role in the establishment of constitutive heterochromatin at
CC       pericentric and telomere regions. H3 'Lys-9' trimethylation is
CC       also required to direct DNA methylation at pericentric repeats.
CC       SUV39H1 is targeted to histone H3 via its interaction with RB1 and
CC       is involved in many processes, such as cell cycle regulation,
CC       transcriptional repression and regulation of telomere length. May
CC       participate in regulation of higher-order chromatin organization
CC       during spermatogenesis. Recruited by the large PER complex to the
CC       E-box elements of the circadian target genes such as PER2 itself
CC       or PER1, contributes to the conversion of local chromatin to a
CC       heterochromatin-like repressive state through H3 'Lys-9'
CC       trimethylation. {ECO:0000269|PubMed:14765126}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
CC       S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC       {ECO:0000255|PROSITE-ProRule:PRU00912}.
CC   -!- SUBUNIT: Interacts with SMAD5. The large PER complex involved in
CC       the histone methylation is composed of at least PER2, CBX3,
CC       TRIM28, SUV39H1 and/or SUV39H2; CBX3 mediates the formation of the
CC       complex. {ECO:0000269|PubMed:15107829,
CC       ECO:0000269|PubMed:20084102}.
CC   -!- INTERACTION:
CC       Q8NEU8:APPL2; NbExp=4; IntAct=EBI-723127, EBI-741261;
CC       Q9BXL8:CDCA4; NbExp=2; IntAct=EBI-723127, EBI-1773949;
CC       V9HWG0:HEL25; NbExp=3; IntAct=EBI-723127, EBI-10183977;
CC       Q8N5Z5:KCTD17; NbExp=2; IntAct=EBI-723127, EBI-743960;
CC       Q8TBB5:KLHDC4; NbExp=2; IntAct=EBI-723127, EBI-8472352;
CC       Q9Y605:MRFAP1; NbExp=2; IntAct=EBI-723127, EBI-995714;
CC       P16333:NCK1; NbExp=2; IntAct=EBI-723127, EBI-389883;
CC       Q5T6S3:PHF19; NbExp=2; IntAct=EBI-723127, EBI-2339674;
CC       Q8ND90:PNMA1; NbExp=4; IntAct=EBI-723127, EBI-302345;
CC       Q9UDV6:ZNF212; NbExp=2; IntAct=EBI-723127, EBI-1640204;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome,
CC       centromere {ECO:0000250}. Note=Associates with centromeric
CC       constitutive heterochromatin. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=3;
CC         IsoId=Q9H5I1-1; Sequence=Displayed;
CC         Note=No experimental confirmation available.;
CC       Name=1;
CC         IsoId=Q9H5I1-2; Sequence=VSP_002209;
CC       Name=2;
CC         IsoId=Q9H5I1-3; Sequence=VSP_002210;
CC   -!- DOMAIN: Although the SET domain contains the active site of
CC       enzymatic activity, both pre-SET and post-SET domains are required
CC       for methyltransferase activity. The SET domain also participates
CC       in stable binding to heterochromatin (By similarity).
CC       {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. Suvar3-9 subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00912}.
DR   EMBL; AK027067; BAB15645.1; -; mRNA.
DR   EMBL; CR457372; CAG33653.1; -; mRNA.
DR   EMBL; AC069544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL360083; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471072; EAW86254.1; -; Genomic_DNA.
DR   EMBL; CH471072; EAW86253.1; -; Genomic_DNA.
DR   EMBL; CH471072; EAW86255.1; -; Genomic_DNA.
DR   EMBL; CH471072; EAW86256.1; -; Genomic_DNA.
DR   EMBL; BC007754; AAH07754.1; -; mRNA.
DR   EMBL; BC029360; AAH29360.1; -; mRNA.
DR   EMBL; AL834488; CAD39146.1; -; mRNA.
DR   CCDS; CCDS53493.1; -. [Q9H5I1-3]
DR   CCDS; CCDS53494.1; -. [Q9H5I1-1]
DR   CCDS; CCDS7104.1; -. [Q9H5I1-2]
DR   RefSeq; NP_001180353.1; NM_001193424.1. [Q9H5I1-1]
DR   RefSeq; NP_001180354.1; NM_001193425.1. [Q9H5I1-2]
DR   RefSeq; NP_001180355.1; NM_001193426.1. [Q9H5I1-3]
DR   RefSeq; NP_001180356.1; NM_001193427.1.
DR   RefSeq; NP_078946.1; NM_024670.3. [Q9H5I1-2]
DR   RefSeq; XP_006717566.1; XM_006717503.3. [Q9H5I1-2]
DR   RefSeq; XP_011517964.1; XM_011519662.2. [Q9H5I1-2]
DR   RefSeq; XP_016872126.1; XM_017016637.1. [Q9H5I1-2]
DR   UniGene; Hs.554883; -.
DR   PDB; 2R3A; X-ray; 2.00 A; A=112-410.
DR   PDBsum; 2R3A; -.
DR   ProteinModelPortal; Q9H5I1; -.
DR   SMR; Q9H5I1; -.
DR   BioGrid; 122838; 51.
DR   IntAct; Q9H5I1; 58.
DR   MINT; Q9H5I1; -.
DR   STRING; 9606.ENSP00000346997; -.
DR   BindingDB; Q9H5I1; -.
DR   ChEMBL; CHEMBL1795177; -.
DR   iPTMnet; Q9H5I1; -.
DR   PhosphoSitePlus; Q9H5I1; -.
DR   BioMuta; SUV39H2; -.
DR   DMDM; 25091325; -.
DR   EPD; Q9H5I1; -.
DR   MaxQB; Q9H5I1; -.
DR   PaxDb; Q9H5I1; -.
DR   PeptideAtlas; Q9H5I1; -.
DR   PRIDE; Q9H5I1; -.
DR   ProteomicsDB; 80906; -.
DR   ProteomicsDB; 80907; -. [Q9H5I1-2]
DR   ProteomicsDB; 80908; -. [Q9H5I1-3]
DR   DNASU; 79723; -.
DR   Ensembl; ENST00000313519; ENSP00000319208; ENSG00000152455. [Q9H5I1-2]
DR   Ensembl; ENST00000354919; ENSP00000346997; ENSG00000152455. [Q9H5I1-1]
DR   Ensembl; ENST00000378325; ENSP00000367576; ENSG00000152455. [Q9H5I1-3]
DR   GeneID; 79723; -.
DR   KEGG; hsa:79723; -.
DR   UCSC; uc001ing.4; human. [Q9H5I1-1]
DR   CTD; 79723; -.
DR   DisGeNET; 79723; -.
DR   EuPathDB; HostDB:ENSG00000152455.15; -.
DR   GeneCards; SUV39H2; -.
DR   HGNC; HGNC:17287; SUV39H2.
DR   HPA; HPA045901; -.
DR   HPA; HPA057554; -.
DR   MIM; 606503; gene.
DR   neXtProt; NX_Q9H5I1; -.
DR   OpenTargets; ENSG00000152455; -.
DR   PharmGKB; PA134868807; -.
DR   eggNOG; KOG1082; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00780000121845; -.
DR   HOGENOM; HOG000231244; -.
DR   HOVERGEN; HBG055621; -.
DR   InParanoid; Q9H5I1; -.
DR   KO; K11419; -.
DR   OMA; AWCVPCL; -.
DR   OrthoDB; EOG091G0Y4N; -.
DR   PhylomeDB; Q9H5I1; -.
DR   TreeFam; TF106452; -.
DR   Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
DR   ChiTaRS; SUV39H2; human.
DR   EvolutionaryTrace; Q9H5I1; -.
DR   GeneWiki; SUV39H2; -.
DR   GenomeRNAi; 79723; -.
DR   PRO; PR:Q9H5I1; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   Bgee; ENSG00000152455; -.
DR   CleanEx; HS_SUV39H2; -.
DR   ExpressionAtlas; Q9H5I1; baseline and differential.
DR   Genevisible; Q9H5I1; HS.
DR   GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
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:1904047; F:S-adenosyl-L-methionine binding; IDA:UniProtKB.
DR   GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0071456; P:cellular response to hypoxia; IDA:MGI.
DR   GO; GO:0006333; P:chromatin assembly or disassembly; IMP:UniProtKB.
DR   GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
DR   GO; GO:0036123; P:histone H3-K9 dimethylation; ISS:UniProtKB.
DR   GO; GO:0036124; P:histone H3-K9 trimethylation; ISS:UniProtKB.
DR   GO; GO:0042754; P:negative regulation of circadian rhythm; ISS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   CDD; cd00024; CHROMO; 1.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR023779; Chromodomain_CS.
DR   InterPro; IPR011381; Histone_H3-K9_MeTrfase.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR007728; Pre-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF00385; Chromo; 1.
DR   Pfam; PF05033; Pre-SET; 1.
DR   Pfam; PF00856; SET; 1.
DR   PIRSF; PIRSF009343; SUV39_SET; 1.
DR   SMART; SM00298; CHROMO; 1.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00468; PreSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF54160; SSF54160; 1.
DR   PROSITE; PS00598; CHROMO_1; 1.
DR   PROSITE; PS50013; CHROMO_2; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50867; PRE_SET; 1.
DR   PROSITE; PS51579; SAM_MT43_SUVAR39_3; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Biological rhythms; Cell cycle;
KW   Centromere; Chromatin regulator; Chromosome; Complete proteome;
KW   Differentiation; Metal-binding; Methyltransferase; Nucleus;
KW   Phosphoprotein; Polymorphism; Reference proteome; Repressor;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Zinc.
FT   CHAIN         1    410       Histone-lysine N-methyltransferase
FT                                SUV39H2.
FT                                /FTId=PRO_0000186059.
FT   DOMAIN       47    105       Chromo. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00053}.
FT   DOMAIN      189    247       Pre-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00157}.
FT   DOMAIN      250    373       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN      394    410       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   REGION      261    263       S-adenosyl-L-methionine binding.
FT                                {ECO:0000244|PDB:2R3A,
FT                                ECO:0000269|PubMed:20084102}.
FT   REGION      330    331       S-adenosyl-L-methionine binding.
FT                                {ECO:0000244|PDB:2R3A,
FT                                ECO:0000269|PubMed:20084102}.
FT   METAL       191    191       Zinc 1. {ECO:0000244|PDB:2R3A,
FT                                ECO:0000269|PubMed:20084102}.
FT   METAL       191    191       Zinc 2. {ECO:0000244|PDB:2R3A,
FT                                ECO:0000269|PubMed:20084102}.
FT   METAL       193    193       Zinc 1. {ECO:0000244|PDB:2R3A,
FT                                ECO:0000269|PubMed:20084102}.
FT   METAL       196    196       Zinc 1. {ECO:0000244|PDB:2R3A,
FT                                ECO:0000269|PubMed:20084102}.
FT   METAL       196    196       Zinc 3. {ECO:0000244|PDB:2R3A,
FT                                ECO:0000269|PubMed:20084102}.
FT   METAL       201    201       Zinc 1. {ECO:0000244|PDB:2R3A,
FT                                ECO:0000269|PubMed:20084102}.
FT   METAL       202    202       Zinc 2. {ECO:0000244|PDB:2R3A,
FT                                ECO:0000269|PubMed:20084102}.
FT   METAL       229    229       Zinc 2. {ECO:0000244|PDB:2R3A,
FT                                ECO:0000269|PubMed:20084102}.
FT   METAL       229    229       Zinc 3. {ECO:0000244|PDB:2R3A,
FT                                ECO:0000269|PubMed:20084102}.
FT   METAL       233    233       Zinc 2. {ECO:0000244|PDB:2R3A,
FT                                ECO:0000269|PubMed:20084102}.
FT   METAL       235    235       Zinc 3. {ECO:0000244|PDB:2R3A,
FT                                ECO:0000269|PubMed:20084102}.
FT   METAL       239    239       Zinc 3. {ECO:0000244|PDB:2R3A,
FT                                ECO:0000269|PubMed:20084102}.
FT   METAL       333    333       Zinc 4. {ECO:0000244|PDB:2R3A,
FT                                ECO:0000269|PubMed:20084102}.
FT   METAL       398    398       Zinc 4. {ECO:0000244|PDB:2R3A,
FT                                ECO:0000269|PubMed:20084102}.
FT   METAL       400    400       Zinc 4. {ECO:0000244|PDB:2R3A,
FT                                ECO:0000269|PubMed:20084102}.
FT   METAL       405    405       Zinc 4. {ECO:0000244|PDB:2R3A,
FT                                ECO:0000269|PubMed:20084102}.
FT   BINDING     372    372       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING     399    399       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000244|PDB:2R3A,
FT                                ECO:0000269|PubMed:20084102}.
FT   MOD_RES     381    381       Phosphoserine.
FT                                {ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES     384    384       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES     388    388       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   VAR_SEQ       1     60       Missing (in isoform 1).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|Ref.2}.
FT                                /FTId=VSP_002209.
FT   VAR_SEQ     104    283       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_002210.
FT   VARIANT     383    383       D -> H (in a breast cancer sample;
FT                                somatic mutation).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_036344.
FT   HELIX       125    147       {ECO:0000244|PDB:2R3A}.
FT   STRAND      150    152       {ECO:0000244|PDB:2R3A}.
FT   STRAND      154    157       {ECO:0000244|PDB:2R3A}.
FT   STRAND      159    161       {ECO:0000244|PDB:2R3A}.
FT   TURN        196    198       {ECO:0000244|PDB:2R3A}.
FT   HELIX       202    205       {ECO:0000244|PDB:2R3A}.
FT   HELIX       244    246       {ECO:0000244|PDB:2R3A}.
FT   STRAND      252    256       {ECO:0000244|PDB:2R3A}.
FT   STRAND      258    260       {ECO:0000244|PDB:2R3A}.
FT   STRAND      263    269       {ECO:0000244|PDB:2R3A}.
FT   STRAND      276    280       {ECO:0000244|PDB:2R3A}.
FT   STRAND      283    286       {ECO:0000244|PDB:2R3A}.
FT   HELIX       287    295       {ECO:0000244|PDB:2R3A}.
FT   HELIX       299    303       {ECO:0000244|PDB:2R3A}.
FT   STRAND      305    307       {ECO:0000244|PDB:2R3A}.
FT   STRAND      313    318       {ECO:0000244|PDB:2R3A}.
FT   STRAND      320    323       {ECO:0000244|PDB:2R3A}.
FT   HELIX       325    328       {ECO:0000244|PDB:2R3A}.
FT   STRAND      336    345       {ECO:0000244|PDB:2R3A}.
FT   STRAND      353    360       {ECO:0000244|PDB:2R3A}.
FT   STRAND      367    370       {ECO:0000244|PDB:2R3A}.
FT   HELIX       372    374       {ECO:0000244|PDB:2R3A}.
SQ   SEQUENCE   410 AA;  46682 MW;  ED8BBF80AE838C69 CRC64;
     MAAVGAEARG AWCVPCLVSL DTLQELCRKE KLTCKSIGIT KRNLNNYEVE YLCDYKVVKD
     MEYYLVKWKG WPDSTNTWEP LQNLKCPLLL QQFSNDKHNY LSQVKKGKAI TPKDNNKTLK
     PAIAEYIVKK AKQRIALQRW QDELNRRKNH KGMIFVENTV DLEGPPSDFY YINEYKPAPG
     ISLVNEATFG CSCTDCFFQK CCPAEAGVLL AYNKNQQIKI PPGTPIYECN SRCQCGPDCP
     NRIVQKGTQY SLCIFRTSNG RGWGVKTLVK IKRMSFVMEY VGEVITSEEA ERRGQFYDNK
     GITYLFDLDY ESDEFTVDAA RYGNVSHFVN HSCDPNLQVF NVFIDNLDTR LPRIALFSTR
     TINAGEELTF DYQMKGSGDI SSDSIDHSPA KKRVRTVCKC GAVTCRGYLN
//
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