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Showing Protein Histone-lysine N-methyltransferase SUV39H1 (HMDBP00422)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 2 metabolites
Identification
HMDB Protein ID HMDBP00422
Secondary Accession Numbers
  • 5659
Name Histone-lysine N-methyltransferase SUV39H1
Synonyms
  1. H3-K9-HMTase 1
  2. Histone H3-K9 methyltransferase 1
  3. Lysine N-methyltransferase 1A
  4. Position-effect variegation 3-9 homolog
  5. Su(var)3-9 homolog 1
  6. Suppressor of variegation 3-9 homolog 1
Gene Name SUV39H1
Protein Type Unknown
Biological Properties
General Function Involved in chromatin binding
Specific Function Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. Also weakly methylates histone H1 (in vitro). H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as repression of MYOD1-stimulated differentiation, regulation of the control switch for exiting the cell cycle and entering differentiation, repression by the PML-RARA fusion protein, BMP-induced repression, repression of switch recombination to IgA and regulation of telomere length. Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus.
Pathways
  • Lysine degradation
Reactions
S-Adenosylmethionine + L-lysine-[histone] → S-Adenosylhomocysteine + N(6)-methyl-L-lysine-[histone] details
Protein lysine + S-Adenosylmethionine → Protein N6-methyl-L-lysine + S-Adenosylhomocysteine details
S-Adenosylmethionine + Protein N6-methyl-L-lysine → S-Adenosylhomocysteine + Protein N6,N6-dimethyl-L-lysine details
S-Adenosylmethionine + Protein N6,N6-dimethyl-L-lysine → S-Adenosylhomocysteine + Protein N6,N6,N6-trimethyl-L-lysine details
GO Classification
Biological Process
cell cycle
rRNA processing
virus-host interaction
cell differentiation
transcription, DNA-dependent
chromatin silencing at rDNA
Cellular Component
chromosome, centromeric region
condensed nuclear chromosome
chromatin silencing complex
rDNA heterochromatin
Component
organelle
membrane-bounded organelle
intracellular membrane-bounded organelle
nucleus
organelle part
intracellular organelle part
chromosomal part
chromatin
Function
ion binding
cation binding
metal ion binding
binding
catalytic activity
transition metal ion binding
zinc ion binding
transferase activity
protein methyltransferase activity
protein-lysine n-methyltransferase activity
histone-lysine n-methyltransferase activity
chromatin binding
transferase activity, transferring one-carbon groups
methyltransferase activity
Molecular Function
histone methyltransferase activity (H3-K9 specific)
zinc ion binding
chromatin binding
Process
cellular process
cellular component organization at cellular level
organelle organization
chromosome organization
chromatin organization
chromatin modification
chromatin assembly or disassembly
Cellular Location
  1. Nucleus
  2. Chromosome
  3. centromere
Gene Properties
Chromosome Location X
Locus Xp11.23
SNPs SUV39H1
Gene Sequence 
>1239 bp
ATGGCGGAAAATTTAAAAGGCTGCAGCGTGTGTTGCAAGTCTTCTTGGAATCAGCTGCAG
GACCTGTGCCGCCTGGCCAAGCTCTCCTGCCCTGCCCTCGGTATCTCTAAGAGGAACCTC
TATGACTTTGAAGTCGAGTACCTGTGCGATTACAAGAAGATCCGCGAACAGGAATATTAC
CTGGTGAAATGGCGTGGATATCCAGACTCAGAGAGCACCTGGGAGCCACGGCAGAATCTC
AAGTGTGTGCGTATCCTCAAGCAGTTCCACAAGGACTTAGAAAGGGAGCTGCTCCGGCGG
CACCACCGGTCAAAGACCCCCCGGCACCTGGACCCAAGCTTGGCCAACTACCTGGTGCAG
AAGGCCAAGCAGAGGCGGGCGCTCCGTCGCTGGGAGCAGGAGCTCAATGCCAAGCGCAGC
CATCTGGGACGCATCACTGTAGAGAATGAGGTGGACCTGGACGGCCCTCCGCGGGCCTTC
GTGTACATCAATGAGTACCGTGTTGGTGAGGGCATCACCCTCAACCAGGTGGCTGTGGGC
TGCGAGTGCCAGGACTGTCTGTGGGCACCCACTGGAGGCTGCTGCCCGGGGGCGTCACTG
CACAAGTTTGCCTACAATGACCAGGGCCAGGTGCGGCTTCGAGCCGGGCTGCCCATCTAC
GAGTGCAACTCCCGCTGCCGCTGCGGCTATGACTGCCCAAATCGTGTGGTACAGAAGGGT
ATCCGATATGACCTCTGCATCTTCCGGACGGATGATGGGCGTGGCTGGGGCGTCCGCACC
CTGGAGAAGATTCGCAAGAACAGCTTCGTCATGGAGTACGTGGGAGAGATCATTACCTCA
GAGGAGGCAGAGCGGCGGGGCCAGATCTACGACCGTCAGGGCGCCACCTACCTCTTTGAC
CTGGACTACGTGGAGGACGTGTACACCGTGGATGCCGCCTACTATGGCAACATCTCCCAC
TTTGTCAACCACAGTTGTGACCCCAACCTGCAGGTGTACAACGTCTTCATAGACAACCTT
GACGAGCGGCTGCCCCGCATCGCTTTCTTTGCCACAAGAACCATCCGGGCAGGCGAGGAG
CTCACCTTTGATTACAACATGCAAGTGGACCCCGTGGACATGGAGAGCACCCGCATGGAC
TCCAACTTTGGCCTGGCTGGGCTCCCTGGCTCCCCTAAGAAGCGGGTCCGTATTGAATGC
AAGTGTGGGACTGAGTCCTGCCGCAAATACCTCTTCTAG
Protein Properties
Number of Residues 412
Molecular Weight 47907.065
Theoretical pI 8.024
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>Histone-lysine N-methyltransferase SUV39H1
MAENLKGCSVCCKSSWNQLQDLCRLAKLSCPALGISKRNLYDFEVEYLCDYKKIREQEYY
LVKWRGYPDSESTWEPRQNLKCVRILKQFHKDLERELLRRHHRSKTPRHLDPSLANYLVQ
KAKQRRALRRWEQELNAKRSHLGRITVENEVDLDGPPRAFVYINEYRVGEGITLNQVAVG
CECQDCLWAPTGGCCPGASLHKFAYNDQGQVRLRAGLPIYECNSRCRCGYDCPNRVVQKG
IRYDLCIFRTDDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFD
LDYVEDVYTVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIRAGEE
LTFDYNMQVDPVDMESTRMDSNFGLAGLPGSPKKRVRIECKCGTESCRKYLF
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID O43463
UniProtKB/Swiss-Prot Entry Name SUV91_HUMAN
PDB IDs
GenBank Gene ID AF019968
GeneCard ID SUV39H1
GenAtlas ID SUV39H1
HGNC ID HGNC:11479
References
General References
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  4. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [PubMed:19690332 ]
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  6. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed:17924679 ]
  7. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
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  10. Aagaard L, Laible G, Selenko P, Schmid M, Dorn R, Schotta G, Kuhfittig S, Wolf A, Lebersorger A, Singh PB, Reuter G, Jenuwein T: Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31. EMBO J. 1999 Apr 1;18(7):1923-38. [PubMed:10202156 ]
  11. Aagaard L, Schmid M, Warburton P, Jenuwein T: Mitotic phosphorylation of SUV39H1, a novel component of active centromeres, coincides with transient accumulation at mammalian centromeres. J Cell Sci. 2000 Mar;113 ( Pt 5):817-29. [PubMed:10671371 ]
  12. Rea S, Eisenhaber F, O'Carroll D, Strahl BD, Sun ZW, Schmid M, Opravil S, Mechtler K, Ponting CP, Allis CD, Jenuwein T: Regulation of chromatin structure by site-specific histone H3 methyltransferases. Nature. 2000 Aug 10;406(6796):593-9. [PubMed:10949293 ]
  13. Firestein R, Cui X, Huie P, Cleary ML: Set domain-dependent regulation of transcriptional silencing and growth control by SUV39H1, a mammalian ortholog of Drosophila Su(var)3-9. Mol Cell Biol. 2000 Jul;20(13):4900-9. [PubMed:10848615 ]
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  16. Fujita N, Watanabe S, Ichimura T, Tsuruzoe S, Shinkai Y, Tachibana M, Chiba T, Nakao M: Methyl-CpG binding domain 1 (MBD1) interacts with the Suv39h1-HP1 heterochromatic complex for DNA methylation-based transcriptional repression. J Biol Chem. 2003 Jun 27;278(26):24132-8. Epub 2003 Apr 23. [PubMed:12711603 ]
  17. Sewalt RG, Lachner M, Vargas M, Hamer KM, den Blaauwen JL, Hendrix T, Melcher M, Schweizer D, Jenuwein T, Otte AP: Selective interactions between vertebrate polycomb homologs and the SUV39H1 histone lysine methyltransferase suggest that histone H3-K9 methylation contributes to chromosomal targeting of Polycomb group proteins. Mol Cell Biol. 2002 Aug;22(15):5539-53. [PubMed:12101246 ]
  18. Chakraborty S, Sinha KK, Senyuk V, Nucifora G: SUV39H1 interacts with AML1 and abrogates AML1 transactivity. AML1 is methylated in vivo. Oncogene. 2003 Aug 14;22(34):5229-37. [PubMed:12917624 ]
  19. Macaluso M, Cinti C, Russo G, Russo A, Giordano A: pRb2/p130-E2F4/5-HDAC1-SUV39H1-p300 and pRb2/p130-E2F4/5-HDAC1-SUV39H1-DNMT1 multimolecular complexes mediate the transcription of estrogen receptor-alpha in breast cancer. Oncogene. 2003 Jun 5;22(23):3511-7. [PubMed:12789259 ]
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  21. Frontelo P, Leader JE, Yoo N, Potocki AC, Crawford M, Kulik M, Lechleider RJ: Suv39h histone methyltransferases interact with Smads and cooperate in BMP-induced repression. Oncogene. 2004 Jul 1;23(30):5242-51. [PubMed:15107829 ]
  22. Krouwels IM, Wiesmeijer K, Abraham TE, Molenaar C, Verwoerd NP, Tanke HJ, Dirks RW: A glue for heterochromatin maintenance: stable SUV39H1 binding to heterochromatin is reinforced by the SET domain. J Cell Biol. 2005 Aug 15;170(4):537-49. [PubMed:16103223 ]
  23. Bradley SP, Kaminski DA, Peters AH, Jenuwein T, Stavnezer J: The histone methyltransferase Suv39h1 increases class switch recombination specifically to IgA. J Immunol. 2006 Jul 15;177(2):1179-88. [PubMed:16818776 ]
  24. Chin HG, Patnaik D, Esteve PO, Jacobsen SE, Pradhan S: Catalytic properties and kinetic mechanism of human recombinant Lys-9 histone H3 methyltransferase SUV39H1: participation of the chromodomain in enzymatic catalysis. Biochemistry. 2006 Mar 14;45(10):3272-84. [PubMed:16519522 ]
  25. Mal AK: Histone methyltransferase Suv39h1 represses MyoD-stimulated myogenic differentiation. EMBO J. 2006 Jul 26;25(14):3323-34. Epub 2006 Jul 13. [PubMed:16858404 ]
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  27. Reed-Inderbitzin E, Moreno-Miralles I, Vanden-Eynden SK, Xie J, Lutterbach B, Durst-Goodwin KL, Luce KS, Irvin BJ, Cleary ML, Brandt SJ, Hiebert SW: RUNX1 associates with histone deacetylases and SUV39H1 to repress transcription. Oncogene. 2006 Sep 21;25(42):5777-86. Epub 2006 May 1. [PubMed:16652147 ]
  28. Kamoi K, Yamamoto K, Misawa A, Miyake A, Ishida T, Tanaka Y, Mochizuki M, Watanabe T: SUV39H1 interacts with HTLV-1 Tax and abrogates Tax transactivation of HTLV-1 LTR. Retrovirology. 2006 Jan 13;3:5. [PubMed:16409643 ]
  29. Murayama A, Ohmori K, Fujimura A, Minami H, Yasuzawa-Tanaka K, Kuroda T, Oie S, Daitoku H, Okuwaki M, Nagata K, Fukamizu A, Kimura K, Shimizu T, Yanagisawa J: Epigenetic control of rDNA loci in response to intracellular energy status. Cell. 2008 May 16;133(4):627-39. doi: 10.1016/j.cell.2008.03.030. [PubMed:18485871 ]
  30. Li Z, Chen L, Kabra N, Wang C, Fang J, Chen J: Inhibition of SUV39H1 methyltransferase activity by DBC1. J Biol Chem. 2009 Apr 17;284(16):10361-6. doi: 10.1074/jbc.M900956200. Epub 2009 Feb 13. [PubMed:19218236 ]