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NAD-dependent histone deacetylase HST3 (P53687)

Identification
NameNAD-dependent histone deacetylase HST3
Synonyms
  • Homologous to SIR2 protein 3
Gene NameHST3
Enzyme ClassNot Available
Biological Properties
General FunctionTranscription
Specific FunctionNAD-dependent histone deacetylase, which contributes together with HST4 to histone H3 'Lys-56' deacetylation, regulation of telomeric silencing, proper cell cycle progression, DNA damage control, DNA recombination, and genomic maintenance
Cellular LocationCytoplasm. Nucleus
SMPDB PathwaysNot Available
KEGG PathwaysNot Available
SMPDB ReactionsNot Available
KEGG Reactions
NAD + water ↔ hydron + Niacinamide + Adenosine diphosphate ribose
Metabolites
YMDB IDNameView
GO Classification
Function
binding
ion binding
cation binding
metal ion binding
transition metal ion binding
zinc ion binding
catalytic activity
NAD binding
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
nucleotide binding
NAD or NADH binding
hydrolase activity
Process
regulation of metabolic process
regulation of macromolecule metabolic process
regulation of gene expression
regulation of transcription
cellular process
gene silencing
chromatin silencing
macromolecule metabolic process
macromolecule modification
protein modification process
post-translational protein modification
protein amino acid deacetylation
biological regulation
metabolic process
regulation of biological process
Gene Properties
Chromosome LocationNot Available
Locus
Gene Sequence>1344 bp ATGACTTCAGTATCGCCCTCGCCACCTGCCAGTCGATCGGGCTCAATGTGCTCCGACTTA CCGTCCTCTTTGCAGACTGAGAAACTGGCACATATTATAGGTCTTGATGCCGACGATGAA GTTCTCCGGCGCGTAACCAAGCAGTTGAGCAGATCTAGGAGAATTGCTTGTCTGACTGGG GCAGGCATTTCGTGCAACGCGGGCATTCCTGACTTTCGCTCTTCTGATGGGCTCTACGAC CTAGTGAAAAAGGATTGTTCACAGTATTGGTCTATCAAGTCCGGCAGGGAAATGTTTGAT ATTTCGCTATTTAGAGATGACTTCAAAATATCCATTTTTGCTAAATTTATGGAGAGGCTC TATTCAAATGTTCAATTGGCAAAGCCGACTAAGACGCACAAGTTCATTGCGCATCTAAAA GATAGGAACAAACTGCTGCGCTGTTACACGCAAAACATCGATGGGCTCGAAGAAAGCATA GGACTTACTTTATCAAATAGGAAATTACCGCTTACCTCATTTAGTTCACATTGGAAAAAT CTGGATGTCGTTCAGTTGCACGGCGACCTGAAAACTCTTTCGTGTACAAAGTGCTTCCAG ACTTTTCCCTGGAGCAGGTACTGGTCTCGTTGTCTAAGAAGAGGTGAGTTACCATTGTGT CCGGATTGCGAAGCACTTATCAACAAGAGATTGAATGAAGGAAAGCGAACTCTTGGTTCT AATGTGGGTATTCTAAGACCTAATATCGTCCTGTATGGTGAAAACCATCCATCCTGTGAA ATTATTACGCAAGGCCTAAATCTTGACATAATTAAAGGCAATCCTGATTTTTTGATCATC ATGGGTACAAGTTTGAAAGTTGATGGTGTGAAACAACTGGTAAAAAAATTAAGTAAGAAA ATTCACGATCGTGGCGGCCTGATCATTCTCGTAAACAAGACACCCATTGGCGAATCCTCT TGGCACGGCATTATAGACTACCAAATCCACTCAGATTGTGATAATTGGGTCACATTTCTT GAATCCCAAATACCAGATTTCTTCAAGACGCAAGATCAAATTAAGAAGTTAAGACAGTTA AAAAGGGAGGCGAGCGACTTGAGAAAGCAAATGAAGGCCCAAAAAGACTCAATCGGAACC CCCCCAACAACCCCTCTACGAACTGCCCAGGGGATTGATATTCAAGGAAACAACGAATTG AATACAAAAATAAAGTCGTTAAACACAGTTAAGAGAAAAATACTGTCACCAGGAAACTCC AGTGAGGAAGACGAAGAGGAAAACTTGGATACAAGAAAACGCGCTAAGATACGACCAACT TTCGGTGACAACCAAGCCTCATAA
Protein Properties
Pfam Domain Function
Protein Residues447
Protein Molecular Weight50523.39844
Protein Theoretical pI9.59
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>NAD-dependent histone deacetylase HST3 MTSVSPSPPASRSGSMCSDLPSSLQTEKLAHIIGLDADDEVLRRVTKQLSRSRRIACLTG AGISCNAGIPDFRSSDGLYDLVKKDCSQYWSIKSGREMFDISLFRDDFKISIFAKFMERL YSNVQLAKPTKTHKFIAHLKDRNKLLRCYTQNIDGLEESIGLTLSNRKLPLTSFSSHWKN LDVVQLHGDLKTLSCTKCFQTFPWSRYWSRCLRRGELPLCPDCEALINKRLNEGKRTLGS NVGILRPNIVLYGENHPSCEIITQGLNLDIIKGNPDFLIIMGTSLKVDGVKQLVKKLSKK IHDRGGLIILVNKTPIGESSWHGIIDYQIHSDCDNWVTFLESQIPDFFKTQDQIKKLRQL KREASDLRKQMKAQKDSIGTPPTTPLRTAQGIDIQGNNELNTKIKSLNTVKRKILSPENS SEEDEEENLDTRKRAKIRPTFGDNQAS
References
External Links
ResourceLink
Saccharomyces Genome Database HST3
Uniprot IDP53687
Uniprot NameHST3_YEAST
GenBank Gene IDAY723866
Genebank Protein ID51830520
General Reference
  • Brachmann, C. B., Sherman, J. M., Devine, S. E., Cameron, E. E., Pillus, L., Boeke, J. D. (1995). "The SIR2 gene family, conserved from bacteria to humans, functions in silencing, cell cycle progression, and chromosome stability." Genes Dev 9:2888-2902.7498786
  • Dujon, B., Albermann, K., Aldea, M., Alexandraki, D., Ansorge, W., Arino, J., Benes, V., Bohn, C., Bolotin-Fukuhara, M., Bordonne, R., Boyer, J., Camasses, A., Casamayor, A., Casas, C., Cheret, G., Cziepluch, C., Daignan-Fornier, B., Dang, D. V., de Haan, M., Delius, H., Durand, P., Fairhead, C., Feldmann, H., Gaillon, L., Kleine, K., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Nature 387:98-102.9169874
  • Hu, Y., Rolfs, A., Bhullar, B., Murthy, T. V., Zhu, C., Berger, M. F., Camargo, A. A., Kelley, F., McCarron, S., Jepson, D., Richardson, A., Raphael, J., Moreira, D., Taycher, E., Zuo, D., Mohr, S., Kane, M. F., Williamson, J., Simpson, A., Bulyk, M. L., Harlow, E., Marsischky, G., Kolodner, R. D., LaBaer, J. (2007). "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Genome Res 17:536-543.17322287
  • Smith, J. S., Brachmann, C. B., Celic, I., Kenna, M. A., Muhammad, S., Starai, V. J., Avalos, J. L., Escalante-Semerena, J. C., Grubmeyer, C., Wolberger, C., Boeke, J. D. (2000). "A phylogenetically conserved NAD+-dependent protein deacetylase activity in the Sir2 protein family." Proc Natl Acad Sci U S A 97:6658-6663.10841563
  • Huh, W. K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., O'Shea, E. K. (2003). "Global analysis of protein localization in budding yeast." Nature 425:686-691.14562095
  • 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
  • Pan, X., Ye, P., Yuan, D. S., Wang, X., Bader, J. S., Boeke, J. D. (2006). "A DNA integrity network in the yeast Saccharomyces cerevisiae." Cell 124:1069-1081.16487579
  • Miller, K. M., Maas, N. L., Toczyski, D. P. (2006). "Taking it off: regulation of H3 K56 acetylation by Hst3 and Hst4." Cell Cycle 5:2561-2565.17106263
  • Celic, I., Masumoto, H., Griffith, W. P., Meluh, P., Cotter, R. J., Boeke, J. D., Verreault, A. (2006). "The sirtuins hst3 and Hst4p preserve genome integrity by controlling histone h3 lysine 56 deacetylation." Curr Biol 16:1280-1289.16815704