SUV39H1

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SUV39H1
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases SUV39H1, H3-K9-HMTase 1, KMT1A, MG44, SUV39H, suppressor of variegation 3-9 homolog 1
External IDs MGI: 1099440 HomoloGene: 2388 GeneCards: SUV39H1
RNA expression pattern
PBB GE SUV39H1 218619 s at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_003173
NM_001282166

NM_001290716
NM_011514

RefSeq (protein)

NP_001269095
NP_003164

NP_001277645.1
NP_035644.1
NP_001277645
NP_035644

Location (UCSC) Chr X: 48.7 – 48.71 Mb Chr X: 8.06 – 8.07 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

Histone-lysine N-methyltransferase SUV39H1 is an enzyme that in humans is encoded by the SUV39H1 gene.[3]

Function[edit]

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.[4]

Interactions[edit]

SUV39H1 has been shown to interact with:

References[edit]

  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ a b 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 1171278Freely accessible. PMID 10202156. 
  4. ^ "Entrez Gene: SUV39H1 suppressor of variegation 3-9 homolog 1 (Drosophila)". 
  5. ^ a b 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 139799Freely accessible. PMID 12242305. 
  6. ^ a b 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. 
  7. ^ 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. 
  8. ^ 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 154218Freely accessible. PMID 12711675. 
  9. ^ a b c 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 99834Freely accessible. PMID 11788710. 
  10. ^ 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. 
  11. ^ 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. 
  12. ^ 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 99795Freely accessible. PMID 11533237. 
  13. ^ 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 85941Freely accessible. PMID 10848615. 

Further reading[edit]