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Title: Suv39h1  
Author: World Heritage Encyclopedia
Language: English
Subject: HDAC9, HDAC3, Retinoblastoma protein
Publisher: World Heritage Encyclopedia


Suppressor of variegation 3-9 homolog 1 (Drosophila)
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols  ; H3-K9-HMTase 1; KMT1A; MG44; SUV39H
External IDs ChEMBL: GeneCards:
EC number
RNA expression pattern
Species Human Mouse
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search

Histone-lysine N-methyltransferase SUV39H1 is an [2]


SUV39H1 has been shown to interact with HDAC9,[3] HDAC1,[4] Histone deacetylase 2,[4] Retinoblastoma protein,[5][6] CBX5,[3][7][8] HDAC3,[4] DNMT3A,[9] MBD1,[7] RUNX1,[10] SBF1[11] and CBX1.[1]


  1. ^ 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.  
  2. ^ "Entrez Gene: SUV39H1 suppressor of variegation 3-9 homolog 1 (Drosophila)". 
  3. ^ a b Zhang, Chun Li; McKinsey Timothy A; Olson Eric N (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. (United States) 22 (20): 7302–12.  
  4. ^ a b c Vaute, Olivier; Nicolas Estelle; Vandel Laurence; Trouche Didier (January 2002). "Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases". Nucleic Acids Res. (England) 30 (2): 475–81.  
  5. ^ Nielsen, S J; Schneider R, Bauer U M, Bannister A J, Morrison A, O'Carroll D, Firestein R, Cleary M, Jenuwein T, Herrera R E, Kouzarides T (August 2001). "Rb targets histone H3 methylation and HP1 to promoters".  
  6. ^ 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. (United States) 21 (19): 6484–94.  
  7. ^ a b Fujita, Naoyuki; Watanabe Sugiko; Ichimura Takaya; Tsuruzoe Shu; Shinkai Yoichi; Tachibana Makoto; Chiba Tsutomu; Nakao Mitsuyoshi (June 2003). "Methyl-CpG binding domain 1 (MBD1) interacts with the Suv39h1-HP1 heterochromatic complex for DNA methylation-based transcriptional repression". J. Biol. Chem. (United States) 278 (26): 24132–8.  
  8. ^ Rual, Jean-François; Venkatesan Kavitha, Hao Tong, Hirozane-Kishikawa Tomoko, Dricot Amélie, Li Ning, Berriz Gabriel F, Gibbons Francis D, Dreze Matija, Ayivi-Guedehoussou Nono, Klitgord Niels, Simon Christophe, Boxem Mike, Milstein Stuart, Rosenberg Jennifer, Goldberg Debra S, Zhang Lan V, Wong Sharyl L, Franklin Giovanni, Li Siming, Albala Joanna S, Lim Janghoo, Fraughton Carlene, Llamosas Estelle, Cevik Sebiha, Bex Camille, Lamesch Philippe, Sikorski Robert S, Vandenhaute Jean, Zoghbi Huda Y, Smolyar Alex, Bosak Stephanie, Sequerra Reynaldo, Doucette-Stamm Lynn, Cusick Michael E, Hill David E, Roth Frederick P, Vidal Marc (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network".  
  9. ^ Fuks, François; Hurd Paul J; Deplus Rachel; Kouzarides Tony (May 2003). "The DNA methyltransferases associate with HP1 and the SUV39H1 histone methyltransferase". Nucleic Acids Res. (England) 31 (9): 2305–12.  
  10. ^ Chakraborty, Soumen; Sinha Kislay Kumar; Senyuk Vitalyi; Nucifora Giuseppina (August 2003). "SUV39H1 interacts with AML1 and abrogates AML1 transactivity. AML1 is methylated in vivo". Oncogene (England) 22 (34): 5229–37.  
  11. ^ Firestein, R; Cui X; Huie P; Cleary M L (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. (UNITED STATES) 20 (13): 4900–9.  

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