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Identification
NameHistone-lysine N-methyltransferase, H3 lysine-79 specific
Synonyms
  • Disrupter of telomere silencing protein 1
  • Histone H3-K79 methyltransferase
  • H3-K79-HMTase
  • Lysine N-methyltransferase 4
Gene NameDOT1
Enzyme Class
Biological Properties
General FunctionInvolved in histone-lysine N-methyltransferase activity
Specific FunctionHistone methyltransferase that specifically methylates histone H3 to form H3K79me. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histones. Can bind to DNA (in vitro)
Cellular LocationNucleus
SMPDB PathwaysNot Available
KEGG Pathways
Lysine degradationec00310 Map00310
SMPDB ReactionsNot Available
KEGG ReactionsNot Available
Metabolites
YMDB IDNameView
YMDB00438S-Adenosyl-L-methionineShow
GO Classification
Component
Not Available
Function
transferase activity, transferring one-carbon groups
methyltransferase activity
protein methyltransferase activity
protein-lysine N-methyltransferase activity
histone-lysine N-methyltransferase activity
catalytic activity
transferase activity
Process
Not Available
Gene Properties
Chromosome Locationchromosome 4
LocusYDR440W
Gene Sequence>1749 bp ATGGGCGGTCAAGAAAGTATATCAAATAATAACTCAGACTCATTCATTATGTCGTCCCCC AACTTAGACTCTCAGGAATCTTCAATATCACCTATTGATGAGAAGAAAGGCACCGATATG CAAACCAAGTCGCTTTCAAGCTATTCTAAAGGTACGCTTCTCTCTAAGCAAGTACAAAAT TTATTAGAAGAAGCTAATAAATACGATCCAATATATGGGTCATCTTTACCTCGAGGATTT TTAAGAGATAGAAACACCAAGGGTAAGGATAATGGGTTGGTTCCGCTGGTGGAGAAGGTT ATACCTCCCATTCACAAGAAAACCAATAATAGAAACACAAGGAAGAAGTCATCTACCACC ACGAAGAAGGATGTAAAGAAGCCAAAAGCTGCAAAAGTAAAAGGAAAAAATGGCAGGACT AACCATAAACATACCCCAATTTCAAAGCAAGAAATAGATACTGCACGAGAAAAAAAGCCA TTGAAAAAAGGTCGGGCAAACAAGAAGAATGATCGCGATAGTCCTTCATCAACATTTGTT GATTGGAATGGCCCGTGTCTACGGTTACAATATCCATTATTTGACATAGAGTACTTAAGA TCACATGAAATATATTCTGGAACTCCTATACAATCCATTAGTTTAAGAACAAATTCTCCA CAGCCAACGAGCTTGACATCAGATAACGACACTTCCTCAGTAACGACAGCAAAGTTGCAG AGTATTTTATTTTCAAATTATATGGAAGAGTACAAAGTCGACTTCAAAAGGTCAACAGCC ATTTATAATCCAATGAGTGAAATTGGTAAATTAATTGAATACAGCTGCCTGGTCTTTTTA CCTTCACCTTATGCTGAACAATTGAAGGAAACTATACTACCGGACCTAAATGCATCATTT GATAACTCTGACACGAAAGGTTTCGTGAATGCTATAAATTTATACAACAAAATGATTCGT GAAATTCCTAGGCAAAGAATAATTGACCATTTAGAAACAATTGATAAAATTCCTCGTTCA TTCATTCATGACTTCTTGCATATCGTCTATACCAGGAGTATCCATCCGCAGGCGAATAAA TTGAAACATTACAAAGCATTCAGCAATTATGTTTATGGAGAACTTTTGCCCAATTTCCTA TCTGATGTATATCAACAATGCCAGTTGAAGAAGGGTGACACTTTCATGGATCTCGGTTCG GGAGTAGGTAATTGCGTAGTACAAGCTGCGTTGGAATGTGGATGTGCATTAAGCTTCGGA TGTGAAATCATGGATGATGCTAGCGATTTAACTATACTGCAGTACGAGGAACTAAAGAAG AGGTGTAAGTTATATGGGATGCGTTTGAACAACGTGGAGTTTTCATTGAAGAAAAGCTTT GTGGACAATAACAGGGTCGCTGAACTAATTCCTCAGTGCGATGTTATCCTCGTAAATAAT TTTTTATTTGATGAAGATTTGAATAAAAAAGTCGAAAAGATACTACAAACGGCAAAAGTT GGATGTAAGATCATAAGTTTGAAAAGTTTAAGAAGCCTCACTTATCAGATCAACTTCTAC AATGTTGAGAACATCTTCAATAGATTAAAGGTGCAAAGGTATGATCTTAAGGAGGATAGT GTTTCATGGACGCATAGTGGCGGAGAGTATTATATATCAACAGTGATGGAGGATGTGGAC GAAAGTTTATTCAGCCCTGCTGCAAGAGGTAGGAGGAACAGAGGTACGCCGGTGAAGTAT ACCAGATGA
Protein Properties
Pfam Domain Function
Protein Residues582
Protein Molecular Weight66200.70313
Protein Theoretical pI9.46
PDB Fileshow
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Histone-lysine N-methyltransferase, H3 lysine-79 specific MGGQESISNNNSDSFIMSSPNLDSQESSISPIDEKKGTDMQTKSLSSYSKGTLLSKQVQN LLEEANKYDPIYGSSLPRGFLRDRNTKGKDNGLVPLVEKVIPPIHKKTNNRNTRKKSSTT TKKDVKKPKAAKVKGKNGRTNHKHTPISKQEIDTAREKKPLKKGRANKKNDRDSPSSTFV DWNGPCLRLQYPLFDIEYLRSHEIYSGTPIQSISLRTNSPQPTSLTSDNDTSSVTTAKLQ SILFSNYMEEYKVDFKRSTAIYNPMSEIGKLIEYSCLVFLPSPYAEQLKETILPDLNASF DNSDTKGFVNAINLYNKMIREIPRQRIIDHLETIDKIPRSFIHDFLHIVYTRSIHPQANK LKHYKAFSNYVYGELLPNFLSDVYQQCQLKKGDTFMDLGSGVGNCVVQAALECGCALSFG CEIMDDASDLTILQYEELKKRCKLYGMRLNNVEFSLKKSFVDNNRVAELIPQCDVILVNN FLFDEDLNKKVEKILQTAKVGCKIISLKSLRSLTYQINFYNVENIFNRLKVQRYDLKEDS VSWTHSGGEYYISTVMEDVDESLFSPAARGRRNRGTPVKYTR
References
External Links
ResourceLink
Saccharomyces Genome Database DOT1
Uniprot IDQ04089
Uniprot NameDOT1_YEAST
GenBank Gene IDU33007
Genebank Protein ID927702
PDB ID
1U2Z
General Reference
  • Singer, M. S., Kahana, A., Wolf, A. J., Meisinger, L. L., Peterson, S. E., Goggin, C., Mahowald, M., Gottschling, D. E. (1998). "Identification of high-copy disruptors of telomeric silencing in Saccharomyces cerevisiae." Genetics 150:613-632.9755194
  • Jacq, C., Alt-Morbe, J., Andre, B., Arnold, W., Bahr, A., Ballesta, J. P., Bargues, M., Baron, L., Becker, A., Biteau, N., Blocker, H., Blugeon, C., Boskovic, J., Brandt, P., Bruckner, M., Buitrago, M. J., Coster, F., Delaveau, T., del Rey, F., Dujon, B., Eide, L. G., Garcia-Cantalejo, J. M., Goffeau, A., Gomez-Peris, A., Zaccaria, P., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Nature 387:75-78.9169867
  • San-Segundo, P. A., Roeder, G. S. (2000). "Role for the silencing protein Dot1 in meiotic checkpoint control." Mol Biol Cell 11:3601-3615.11029058
  • van Leeuwen, F., Gafken, P. R., Gottschling, D. E. (2002). "Dot1p modulates silencing in yeast by methylation of the nucleosome core." Cell 109:745-756.12086673
  • Ng, H. H., Feng, Q., Wang, H., Erdjument-Bromage, H., Tempst, P., Zhang, Y., Struhl, K. (2002). "Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association." Genes Dev 16:1518-1527.12080090
  • Lacoste, N., Utley, R. T., Hunter, J. M., Poirier, G. G., Cote, J. (2002). "Disruptor of telomeric silencing-1 is a chromatin-specific histone H3 methyltransferase." J Biol Chem 277:30421-30424.12097318
  • Ng, H. H., Xu, R. M., Zhang, Y., Struhl, K. (2002). "Ubiquitination of histone H2B by Rad6 is required for efficient Dot1-mediated methylation of histone H3 lysine 79." J Biol Chem 277:34655-34657.12167634
  • Briggs, S. D., Xiao, T., Sun, Z. W., Caldwell, J. A., Shabanowitz, J., Hunt, D. F., Allis, C. D., Strahl, B. D. (2002). "Gene silencing: trans-histone regulatory pathway in chromatin." Nature 418:498.12152067
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Ng, H. H., Ciccone, D. N., Morshead, K. B., Oettinger, M. A., Struhl, K. (2003). "Lysine-79 of histone H3 is hypomethylated at silenced loci in yeast and mammalian cells: a potential mechanism for position-effect variegation." Proc Natl Acad Sci U S A 100:1820-1825.12574507
  • Giannattasio, M., Lazzaro, F., Plevani, P., Muzi-Falconi, M. (2005). "The DNA damage checkpoint response requires histone H2B ubiquitination by Rad6-Bre1 and H3 methylation by Dot1." J Biol Chem 280:9879-9886.15632126
  • Wysocki, R., Javaheri, A., Allard, S., Sha, F., Cote, J., Kron, S. J. (2005). "Role of Dot1-dependent histone H3 methylation in G1 and S phase DNA damage checkpoint functions of Rad9." Mol Cell Biol 25:8430-8443.16166626
  • Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., Zhou, H. (2008). "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Mol Cell Proteomics 7:1389-1396.18407956
  • Sawada, K., Yang, Z., Horton, J. R., Collins, R. E., Zhang, X., Cheng, X. (2004). "Structure of the conserved core of the yeast Dot1p, a nucleosomal histone H3 lysine 79 methyltransferase." J Biol Chem 279:43296-43306.15292170