ID:SUV92_HUMAN DESCRIPTION: RecName: Full=Histone-lysine N-methyltransferase SUV39H2; EC=22.214.171.124; AltName: Full=Histone H3-K9 methyltransferase 2; Short=H3-K9-HMTase 2; AltName: Full=Lysine N-methyltransferase 1B; AltName: Full=Suppressor of variegation 3-9 homolog 2; Short=Su(var)3-9 homolog 2; FUNCTION: Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys- 9' as substrate. 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 cell cycle regulation, transcriptional repression and regulation of telomere length. May participate in regulation of higher-order chromatin organization during spermatogenesis. CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]. SUBUNIT: Interacts with SMAD5. INTERACTION: P16333:NCK1; NbExp=2; IntAct=EBI-723127, EBI-389883; SUBCELLULAR LOCATION: Nucleus (By similarity). Chromosome, centromere (By similarity). Note=Associates with centromeric constitutive heterochromatin (By similarity). DOMAIN: Although the SET domain contains the active site of enzymatic activity, both pre-SET and post-SET domains are required for methyltransferase activity. The SET domain also participates to stable binding to heterochromatin (By similarity). SIMILARITY: Belongs to the histone-lysine methyltransferase family. Suvar3-9 subfamily. SIMILARITY: Contains 1 chromo domain. SIMILARITY: Contains 1 post-SET domain. SIMILARITY: Contains 1 pre-SET domain. SIMILARITY: Contains 1 SET domain.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q9H5I1
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.