SUV39H1

Suppressor of variegation 3-9 homolog 1 (Drosophila)
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 3MTS​
Identifiers
Symbols	SUV39H1 ; H3-K9-HMTase 1; KMT1A; MG44; SUV39H
External IDs	OMIM: 300254 MGI: 1099440 HomoloGene: 2388 ChEMBL: 1795118 GeneCards: SUV39H1 Gene
EC number	2.1.1.43
Gene ontology Molecular function • transcription regulatory region sequence-specific DNA binding • RNA polymerase II regulatory region sequence-specific DNA binding • chromatin binding • protein binding • zinc ion binding • S-adenosylmethionine-dependent methyltransferase activity • histone-lysine N-methyltransferase activity • histone methyltransferase activity • histone methyltransferase activity (H3-K9 specific) • protein N-terminus binding Cellular component • chromosome, centromeric region • heterochromatin • condensed nuclear chromosome • nucleus • nuclear lamina • nucleoplasm • chromatin silencing complex • rDNA heterochromatin Biological process • negative regulation of transcription from RNA polymerase II promoter • chromatin silencing at rDNA • response to amphetamine • chromatin organization • transcription, DNA-templated • rRNA processing • cellular response to DNA damage stimulus • cell cycle • gene expression • viral process • cell differentiation • response to nutrient levels • histone H3-K9 dimethylation • histone H3-K9 trimethylation • regulation of gene expression, epigenetic • negative regulation of circadian rhythm • negative regulation of gene expression, epigenetic • negative regulation of transcription, DNA-templated • rhythmic process • cellular response to hypoxia Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	6839	20937
Ensembl	ENSG00000101945	ENSMUSG00000039231
UniProt	O43463	O54864
RefSeq (mRNA)	NM_001282166	NM_001290716
RefSeq (protein)	NP_001269095	NP_001277645
Location (UCSC)	Chr X: 48.7 – 48.71 Mb	Chr X: 8.06 – 8.07 Mb
PubMed search

Histone-lysine N-methyltransferase SUV39H1 is an enzyme that in humans is encoded by the SUV39H1 gene.^[1]

Function

This gene is a member of the suppressor of variegation 3-9 homolog family and encodes a protein with a chromodomain and a C-terminal SET domain. This nuclear protein moves to the centromeres during mitosis and functions as a histone methyltransferase, methylating Lys-9 of histone H3. Overall, it plays a vital role in heterochromatin organization, chromosome segregation, and mitotic progression.^[2]

Interactions

SUV39H1 has been shown to interact with:

• CBX1,^[1]
• CBX5,^[3][4][5]
• DNMT3A,^[6]
• HDAC1,^[7]
• HDAC3,^[7]
• HDAC9,^[3]
• Histone deacetylase 2,^[7]
• MBD1,^[4]
• RUNX1,^[8]
• Retinoblastoma protein,^[9][10] and
• SBF1.^[11]

References

1. Aagaard L, Laible G, Selenko P, Schmid M, Dorn R, Schotta G, Kuhfittig S, Wolf A, Lebersorger A, Singh PB, Reuter G, Jenuwein T (June 1999). "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. 18 (7): 1923–38. doi:10.1093/emboj/18.7.1923. PMC 1171278. PMID 10202156.
2. "Entrez Gene: SUV39H1 suppressor of variegation 3-9 homolog 1 (Drosophila)".
3. Zhang CL, McKinsey TA, Olson EN (October 2002). "Association of class II histone deacetylases with heterochromatin protein 1: potential role for histone methylation in control of muscle differentiation". Mol. Cell. Biol. 22 (20): 7302–12. doi:10.1128/mcb.22.20.7302-7312.2002. PMC 139799. PMID 12242305.
4. Fujita N, Watanabe S, Ichimura T, Tsuruzoe S, Shinkai Y, Tachibana M, Chiba T, Nakao M (June 2003). "Methyl-CpG binding domain 1 (MBD1) interacts with the Suv39h1-HP1 heterochromatic complex for DNA methylation-based transcriptional repression". J. Biol. Chem. 278 (26): 24132–8. doi:10.1074/jbc.M302283200. PMID 12711603.
5. Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
6. Fuks F, Hurd PJ, Deplus R, Kouzarides T (May 2003). "The DNA methyltransferases associate with HP1 and the SUV39H1 histone methyltransferase". Nucleic Acids Res. 31 (9): 2305–12. doi:10.1093/nar/gkg332. PMC 154218. PMID 12711675.
7. Vaute O, Nicolas E, Vandel L, Trouche D (January 2002). "Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases". Nucleic Acids Res. 30 (2): 475–81. doi:10.1093/nar/30.2.475. PMC 99834. PMID 11788710.
8. Chakraborty S, Sinha KK, Senyuk V, Nucifora G (August 2003). "SUV39H1 interacts with AML1 and abrogates AML1 transactivity. AML1 is methylated in vivo". Oncogene 22 (34): 5229–37. doi:10.1038/sj.onc.1206600. PMID 12917624.
9. Nielsen SJ, Schneider R, Bauer UM, Bannister AJ, Morrison A, O'Carroll D, Firestein R, Cleary M, Jenuwein T, Herrera RE, Kouzarides T (August 2001). "Rb targets histone H3 methylation and HP1 to promoters". Nature 412 (6846): 561–5. doi:10.1038/35087620. PMID 11484059.
10. Vandel L, Nicolas E, Vaute O, Ferreira R, Ait-Si-Ali S, Trouche D (October 2001). "Transcriptional repression by the retinoblastoma protein through the recruitment of a histone methyltransferase". Mol. Cell. Biol. 21 (19): 6484–94. doi:10.1128/mcb.21.19.6484-6494.2001. PMC 99795. PMID 11533237.
11. Firestein R, Cui X, Huie P, Cleary ML (July 2000). "Set domain-dependent regulation of transcriptional silencing and growth control by SUV39H1, a mammalian ortholog of Drosophila Su(var)3-9". Mol. Cell. Biol. 20 (13): 4900–9. doi:10.1128/mcb.20.13.4900-4909.2000. PMC 85941. PMID 10848615.

Further reading

• Schotta G, Ebert A, Reuter G (2003). "SU(VAR)3-9 is a conserved key function in heterochromatic gene silencing". Genetica 117 (2-3): 149–58. doi:10.1023/A:1022923508198. PMID 12723694.
• Hijmans EM, Voorhoeve PM, Beijersbergen RL, van 't Veer LJ, Bernards R (1995). "E2F-5, a new E2F family member that interacts with p130 in vivo". Mol. Cell. Biol. 15 (6): 3082–9. PMC 230539. PMID 7760804.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Aagaard L, Schmid M, Warburton P, Jenuwein T (2000). "Mitotic phosphorylation of SUV39H1, a novel component of active centromeres, coincides with transient accumulation at mammalian centromeres". J. Cell. Sci. 113 ( Pt 5) (5): 817–29. PMID 10671371.
• Melcher M, Schmid M, Aagaard L, Selenko P, Laible G, Jenuwein T (2000). "Structure-function analysis of SUV39H1 reveals a dominant role in heterochromatin organization, chromosome segregation, and mitotic progression". Mol. Cell. Biol. 20 (10): 3728–41. doi:10.1128/MCB.20.10.3728-3741.2000. PMC 85674. PMID 10779362.
• Firestein R, Cui X, Huie P, Cleary ML (2000). "Set domain-dependent regulation of transcriptional silencing and growth control by SUV39H1, a mammalian ortholog of Drosophila Su(var)3-9". Mol. Cell. Biol. 20 (13): 4900–9. doi:10.1128/MCB.20.13.4900-4909.2000. PMC 85941. PMID 10848615.
• Fraser ME, James MN, Bridger WA, Wolodko WT (2000). "Phosphorylated and dephosphorylated structures of pig heart, GTP-specific succinyl-CoA synthetase". J. Mol. Biol. 299 (5): 1325–39. doi:10.1006/jmbi.2000.3807. PMID 10873456.
• Rea S, Eisenhaber F, O'Carroll D, Strahl BD, Sun ZW, Schmid M, Opravil S, Mechtler K, Ponting CP, Allis CD, Jenuwein T (2000). "Regulation of chromatin structure by site-specific histone H3 methyltransferases". Nature 406 (6796): 593–9. doi:10.1038/35020506. PMID 10949293.
• Lachner M, O'Carroll D, Rea S, Mechtler K, Jenuwein T (2001). "Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins". Nature 410 (6824): 116–20. doi:10.1038/35065132. PMID 11242053.
• Vandel L, Trouche D (2001). "Physical association between the histone acetyl transferase CBP and a histone methyl transferase". EMBO Rep. 2 (1): 21–6. doi:10.1093/embo-reports/kve002. PMC 1083799. PMID 11252719.
• Nielsen SJ, Schneider R, Bauer UM, Bannister AJ, Morrison A, O'Carroll D, Firestein R, Cleary M, Jenuwein T, Herrera RE, Kouzarides T (2001). "Rb targets histone H3 methylation and HP1 to promoters". Nature 412 (6846): 561–5. doi:10.1038/35087620. PMID 11484059.
• Vandel L, Nicolas E, Vaute O, Ferreira R, Ait-Si-Ali S, Trouche D (2001). "Transcriptional repression by the retinoblastoma protein through the recruitment of a histone methyltransferase". Mol. Cell. Biol. 21 (19): 6484–94. doi:10.1128/MCB.21.19.6484-6494.2001. PMC 99795. PMID 11533237.
• Vaute O, Nicolas E, Vandel L, Trouche D (2002). "Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases". Nucleic Acids Res. 30 (2): 475–81. doi:10.1093/nar/30.2.475. PMC 99834. PMID 11788710.
• Schotta G, Ebert A, Krauss V, Fischer A, Hoffmann J, Rea S, Jenuwein T, Dorn R, Reuter G (2002). "Central role of Drosophila SU(VAR)3-9 in histone H3-K9 methylation and heterochromatic gene silencing". EMBO J. 21 (5): 1121–31. doi:10.1093/emboj/21.5.1121. PMC 125909. PMID 11867540.
• Sewalt RG, Lachner M, Vargas M, Hamer KM, den Blaauwen JL, Hendrix T, Melcher M, Schweizer D, Jenuwein T, Otte AP (2002). "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. 22 (15): 5539–53. doi:10.1128/MCB.22.15.5539-5553.2002. PMC 133945. PMID 12101246.
• Zhang CL, McKinsey TA, Olson EN (2002). "Association of class II histone deacetylases with heterochromatin protein 1: potential role for histone methylation in control of muscle differentiation". Mol. Cell. Biol. 22 (20): 7302–12. doi:10.1128/MCB.22.20.7302-7312.2002. PMC 139799. PMID 12242305.
• Yamamoto K, Sonoda M (2003). "Self-interaction of heterochromatin protein 1 is required for direct binding to histone methyltransferase, SUV39H1". Biochem. Biophys. Res. Commun. 301 (2): 287–92. doi:10.1016/S0006-291X(02)03021-8. PMID 12565857.