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 03-AUG-2022, entry version 187.
DE RecName: Full=Histone-lysine N-methyltransferase SUV39H2;
DE EC=2.1.1.355;
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA 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., Naguibneva I.,
RA 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 in
RT 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., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381; SER-384 AND SER-388, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT 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 SER-388, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Histone methyltransferase that specifically trimethylates
CC 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. H3
CC 'Lys-9' trimethylation represents a specific tag for epigenetic
CC transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5)
CC proteins to methylated histones. Mainly functions in heterochromatin
CC regions, thereby playing a central role in the establishment of
CC constitutive heterochromatin at pericentric and telomere regions. H3
CC 'Lys-9' trimethylation is also required to direct DNA methylation at
CC pericentric repeats. SUV39H1 is targeted to histone H3 via its
CC interaction with RB1 and is involved in many processes, such as cell
CC cycle regulation, transcriptional repression and regulation of telomere
CC length. May participate in regulation of higher-order chromatin
CC organization during spermatogenesis. Recruited by the large PER complex
CC to the 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:
CC Reaction=L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60276, Rhea:RHEA-COMP:15538, Rhea:RHEA-
CC COMP:15546, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.355;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00912};
CC -!- SUBUNIT: Interacts with SMAD5. The large PER complex involved in the
CC histone methylation is composed of at least PER2, CBX3, TRIM28, SUV39H1
CC and/or SUV39H2; CBX3 mediates the formation of the complex.
CC {ECO:0000269|PubMed:15107829, ECO:0000269|PubMed:20084102}.
CC -!- INTERACTION:
CC Q9H5I1; Q8NEU8: APPL2; NbExp=6; IntAct=EBI-723127, EBI-741261;
CC Q9H5I1; Q9BXL8: CDCA4; NbExp=2; IntAct=EBI-723127, EBI-1773949;
CC Q9H5I1; V9HWG0: HEL25; NbExp=3; IntAct=EBI-723127, EBI-10183977;
CC Q9H5I1; Q8N5Z5: KCTD17; NbExp=2; IntAct=EBI-723127, EBI-743960;
CC Q9H5I1; Q8TBB5: KLHDC4; NbExp=2; IntAct=EBI-723127, EBI-8472352;
CC Q9H5I1; Q9Y605: MRFAP1; NbExp=2; IntAct=EBI-723127, EBI-995714;
CC Q9H5I1; P16333: NCK1; NbExp=2; IntAct=EBI-723127, EBI-389883;
CC Q9H5I1; Q5T6S3: PHF19; NbExp=2; IntAct=EBI-723127, EBI-2339674;
CC Q9H5I1; Q8ND90: PNMA1; NbExp=5; IntAct=EBI-723127, EBI-302345;
CC Q9H5I1; Q9UDV6: ZNF212; NbExp=2; IntAct=EBI-723127, EBI-1640204;
CC Q9H5I1-2; Q8NEU8: APPL2; NbExp=3; IntAct=EBI-11977575, EBI-741261;
CC Q9H5I1-2; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-11977575, EBI-5916454;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere
CC {ECO:0000250}. Note=Associates with centromeric constitutive
CC heterochromatin. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=3;
CC IsoId=Q9H5I1-1; Sequence=Displayed;
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 enzymatic
CC activity, both pre-SET and post-SET domains are required for
CC methyltransferase activity. The SET domain also participates in stable
CC binding to heterochromatin (By similarity). {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. Suvar3-9
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00912}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 PDB; 2R3A; X-ray; 2.00 A; A=112-410.
DR PDB; 6P0R; X-ray; 2.40 A; A/B=112-410.
DR PDBsum; 2R3A; -.
DR PDBsum; 6P0R; -.
DR AlphaFoldDB; Q9H5I1; -.
DR SMR; Q9H5I1; -.
DR BioGRID; 122838; 79.
DR IntAct; Q9H5I1; 66.
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 jPOST; Q9H5I1; -.
DR MassIVE; Q9H5I1; -.
DR MaxQB; Q9H5I1; -.
DR PaxDb; Q9H5I1; -.
DR PeptideAtlas; Q9H5I1; -.
DR PRIDE; Q9H5I1; -.
DR ProteomicsDB; 80906; -. [Q9H5I1-1]
DR ProteomicsDB; 80907; -. [Q9H5I1-2]
DR ProteomicsDB; 80908; -. [Q9H5I1-3]
DR Antibodypedia; 24975; 381 antibodies from 36 providers.
DR DNASU; 79723; -.
DR Ensembl; ENST00000313519.9; ENSP00000319208.5; ENSG00000152455.16. [Q9H5I1-2]
DR Ensembl; ENST00000354919.11; ENSP00000346997.6; ENSG00000152455.16. [Q9H5I1-1]
DR Ensembl; ENST00000378325.7; ENSP00000367576.3; ENSG00000152455.16. [Q9H5I1-3]
DR GeneID; 79723; -.
DR KEGG; hsa:79723; -.
DR MANE-Select; ENST00000354919.11; ENSP00000346997.6; NM_001193424.2; NP_001180353.1.
DR UCSC; uc001ing.4; human. [Q9H5I1-1]
DR CTD; 79723; -.
DR DisGeNET; 79723; -.
DR GeneCards; SUV39H2; -.
DR HGNC; HGNC:17287; SUV39H2.
DR HPA; ENSG00000152455; Tissue enriched (testis).
DR MIM; 606503; gene.
DR neXtProt; NX_Q9H5I1; -.
DR OpenTargets; ENSG00000152455; -.
DR PharmGKB; PA134868807; -.
DR VEuPathDB; HostDB:ENSG00000152455; -.
DR eggNOG; KOG1082; Eukaryota.
DR GeneTree; ENSGT00940000156788; -.
DR HOGENOM; CLU_020840_8_0_1; -.
DR InParanoid; Q9H5I1; -.
DR OMA; CCRGYLN; -.
DR OrthoDB; 753093at2759; -.
DR PhylomeDB; Q9H5I1; -.
DR TreeFam; TF106452; -.
DR BioCyc; MetaCyc:HS07820-MON; -.
DR PathwayCommons; Q9H5I1; -.
DR Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
DR SignaLink; Q9H5I1; -.
DR BioGRID-ORCS; 79723; 14 hits in 1091 CRISPR screens.
DR ChiTaRS; SUV39H2; human.
DR EvolutionaryTrace; Q9H5I1; -.
DR GeneWiki; SUV39H2; -.
DR GenomeRNAi; 79723; -.
DR Pharos; Q9H5I1; Tchem.
DR PRO; PR:Q9H5I1; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9H5I1; protein.
DR Bgee; ENSG00000152455; Expressed in sperm and 133 other tissues.
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:0005634; C:nucleus; IBA:GO_Central.
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 cis-regulatory region 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:0006325; P:chromatin organization; 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:0034968; P:histone lysine methylation; IBA:GO_Central.
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 DisProt; DP02654; -.
DR Gene3D; 2.170.270.10; -; 1.
DR IDEAL; IID00498; -.
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 InterPro; IPR046341; SET_dom_sf.
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 SUPFAM; SSF82199; SSF82199; 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; Differentiation;
KW Metal-binding; Methyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase; Zinc.
FT CHAIN 1..410
FT /note="Histone-lysine N-methyltransferase SUV39H2"
FT /id="PRO_0000186059"
FT DOMAIN 47..105
FT /note="Chromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 189..247
FT /note="Pre-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00157"
FT DOMAIN 250..373
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 394..410
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20084102,
FT ECO:0007744|PDB:2R3A"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20084102,
FT ECO:0007744|PDB:2R3A"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20084102,
FT ECO:0007744|PDB:2R3A"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20084102,
FT ECO:0007744|PDB:2R3A"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:20084102,
FT ECO:0007744|PDB:2R3A"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20084102,
FT ECO:0007744|PDB:2R3A"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20084102,
FT ECO:0007744|PDB:2R3A"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20084102,
FT ECO:0007744|PDB:2R3A"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:20084102,
FT ECO:0007744|PDB:2R3A"
FT BINDING 233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20084102,
FT ECO:0007744|PDB:2R3A"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:20084102,
FT ECO:0007744|PDB:2R3A"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:20084102,
FT ECO:0007744|PDB:2R3A"
FT BINDING 261..263
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:20084102,
FT ECO:0007744|PDB:2R3A"
FT BINDING 330..331
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:20084102,
FT ECO:0007744|PDB:2R3A"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:20084102,
FT ECO:0007744|PDB:2R3A"
FT BINDING 372
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 398
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:20084102,
FT ECO:0007744|PDB:2R3A"
FT BINDING 399
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:20084102,
FT ECO:0007744|PDB:2R3A"
FT BINDING 400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:20084102,
FT ECO:0007744|PDB:2R3A"
FT BINDING 405
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:20084102,
FT ECO:0007744|PDB:2R3A"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..60
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_002209"
FT VAR_SEQ 104..283
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_002210"
FT VARIANT 383
FT /note="D -> H (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036344"
FT HELIX 125..147
FT /evidence="ECO:0007829|PDB:2R3A"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:2R3A"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:2R3A"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:2R3A"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:2R3A"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:2R3A"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:6P0R"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:2R3A"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:2R3A"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:2R3A"
FT STRAND 263..269
FT /evidence="ECO:0007829|PDB:2R3A"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:2R3A"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:2R3A"
FT HELIX 287..295
FT /evidence="ECO:0007829|PDB:2R3A"
FT HELIX 299..303
FT /evidence="ECO:0007829|PDB:2R3A"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:2R3A"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:6P0R"
FT STRAND 313..318
FT /evidence="ECO:0007829|PDB:2R3A"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:2R3A"
FT HELIX 325..328
FT /evidence="ECO:0007829|PDB:2R3A"
FT STRAND 336..345
FT /evidence="ECO:0007829|PDB:2R3A"
FT STRAND 353..360
FT /evidence="ECO:0007829|PDB:2R3A"
FT STRAND 367..370
FT /evidence="ECO:0007829|PDB:2R3A"
FT HELIX 372..374
FT /evidence="ECO:0007829|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
