SUV420H1

Suppressor of variegation 4-20 homolog 1 (Drosophila)
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 3S8P​
Identifiers
Symbols	SUV420H1 ; CGI-85; CGI85; KMT5B
External IDs	OMIM: 610881 MGI: 2444557 HomoloGene: 32351 GeneCards: SUV420H1 Gene
EC number	2.1.1.43
Gene ontology Molecular function • histone-lysine N-methyltransferase activity • histone methyltransferase activity (H4-K20 specific) Cellular component • condensed nuclear chromosome, centromeric region Biological process • transcription, DNA-templated • regulation of transcription, DNA-templated • muscle organ development • histone H4-K20 trimethylation Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	51111	225888
Ensembl	ENSG00000110066	ENSMUSG00000045098
UniProt	Q4FZB7	Q3U8K7
RefSeq (mRNA)	NM_001300907	NM_001167884
RefSeq (protein)	NP_001287836	NP_001161356
Location (UCSC)	Chr 11: 68.15 – 68.21 Mb	Chr 19: 3.77 – 3.82 Mb
PubMed search

Histone-lysine N-methyltransferase SUV420H1 is an enzyme that in humans is encoded by the SUV420H1 gene.^[1][2][3] The enzyme along with WHSC1 is responsible for dimethylation of lysine 20 on histone 4 in mouse and humans.^[4][5]

This gene encodes a protein that contains a SET domain. SET domains appear to be protein-protein interaction domains that mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). The function of this gene has not been determined. Two alternatively spliced transcript variants have been found for this gene.^[3]

References

1. Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W (Aug 2000). "Identification of Novel Human Genes Evolutionarily Conserved in Caenorhabditis elegans by Comparative Proteomics". Genome Res 10 (5): 703–13. doi:10.1101/gr.10.5.703. PMC 310876. PMID 10810093.
2. Twells RC, Metzker ML, Brown SD, Cox R, Garey C, Hammond H, Hey PJ, Levy E, Nakagawa Y, Philips MS, Todd JA, Hess JF (Jun 2001). "The sequence and gene characterization of a 400-kb candidate region for IDDM4 on chromosome 11q13". Genomics 72 (3): 231–42. doi:10.1006/geno.2000.6492. PMID 11401438.
3. "Entrez Gene: SUV420H1 suppressor of variegation 4-20 homolog 1 (Drosophila)".
4. http://www.ncbi.nlm.nih.gov/pubmed/18676810
5. http://www.ncbi.nlm.nih.gov/pubmed/21293379

Further reading

• 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.
• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (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.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Tryndyak VP, Kovalchuk O, Pogribny IP (2006). "Loss of DNA methylation and histone H4 lysine 20 trimethylation in human breast cancer cells is associated with aberrant expression of DNA methyltransferase 1, Suv4-20h2 histone methyltransferase and methyl-binding proteins". Cancer Biol. Ther. 5 (1): 65–70. doi:10.4161/cbt.5.1.2288. PMID 16322686.
• Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.