HAT1

Histone acetyltransferase 1, also known as HAT1, is an enzyme that, in humans, is encoded by the HAT1 gene.[5][6]

HAT1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2P0W
Identifiers
Aliases	HAT1, KAT1, histone acetyltransferase 1
External IDs	OMIM: 603053 MGI: 96013 HomoloGene: 2701 GeneCards: HAT1
Gene location (Human) Chr. Chromosome 2 (human)[1] Band 2q31.1 Start 171,922,448 bp[1] End 171,983,686 bp[1]
Gene location (Mouse) Chr. Chromosome 2 (mouse)[2] Band 2|2 C2 Start 71,388,958 bp[2] End 71,441,622 bp[2]
Gene ontology Molecular function • transferase activity • histone binding • H4 histone acetyltransferase activity • histone acetyltransferase activity • GO:0001948 protein binding • transferase activity, transferring acyl groups Cellular component • cytoplasm • intracellular membrane-bounded organelle • nuclear matrix • nucleoplasm • nuclear chromatin • nuclear chromosome, telomeric region • cell nucleus • macromolecular complex Biological process • response to nutrient • internal protein amino acid acetylation • DNA packaging • DNA replication-dependent nucleosome assembly • chromatin silencing at telomere • histone acetylation • histone H4 acetylation • DNA replication-independent nucleosome assembly • chromatin organization Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	8520	107435
Ensembl	ENSG00000128708	ENSMUSG00000027018
UniProt	O14929	Q8BY71
RefSeq (mRNA)	NM_001033085 NM_003642	NM_026115
RefSeq (protein)	NP_003633	NP_080391
Location (UCSC)	Chr 2: 171.92 – 171.98 Mb	Chr 2: 71.39 – 71.44 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

The protein encoded by this gene is a type B histone acetyltransferase (HAT) that is involved in the rapid acetylation of newly synthesized cytoplasmic histones, which are, in turn, imported into the nucleus for de novo deposition onto nascent DNA chains. Histone acetylation, in particular, of histone H4, plays an important role in replication-dependent chromatin assembly. To be specific, this HAT can acetylate soluble but not nucleosomal histone H4 at lysines 5 and 12, and, to a lesser degree, histone H2A at lysine 5.[6]

References

1. GRCh38: Ensembl release 89: ENSG00000128708 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000027018 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Verreault A, Kaufman PD, Kobayashi R, Stillman B (1998). "Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase". Curr. Biol. 8 (2): 96–108. doi:10.1016/S0960-9822(98)70040-5. PMID 9427644. S2CID 201273.
6. "Entrez Gene: histone acetyltransferase 1".

Further reading

• Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.
• Hillier LW, Graves TA, Fulton RS, et al. (2005). "Generation and annotation of the DNA sequences of human chromosomes 2 and 4". Nature. 434 (7034): 724–31. doi:10.1038/nature03466. PMID 15815621.
• Benson LJ, Phillips JA, Gu Y, et al. (2007). "Properties of the type B histone acetyltransferase Hat1: H4 tail interaction, site preference, and involvement in DNA repair". J. Biol. Chem. 282 (2): 836–42. doi:10.1074/jbc.M607464200. PMID 17052979.
• 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.
• Makowski AM, Dutnall RN, Annunziato AT (2001). "Effects of acetylation of histone H4 at lysines 8 and 16 on activity of the Hat1 histone acetyltransferase". J. Biol. Chem. 276 (47): 43499–502. doi:10.1074/jbc.C100549200. PMID 11585814.
• Marmorstein R (2001). "Structure of histone acetyltransferases". J. Mol. Biol. 311 (3): 433–44. doi:10.1006/jmbi.2001.4859. PMID 11492997.
• Miyamoto N, Izumi H, Noguchi T, et al. (2008). "Tip60 is regulated by circadian transcription factor clock and is involved in cisplatin resistance". J. Biol. Chem. 283 (26): 18218–26. doi:10.1074/jbc.M802332200. PMID 18458078.
• Cheung P, Tanner KG, Cheung WL, et al. (2000). "Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation". Mol. Cell. 5 (6): 905–15. doi:10.1016/S1097-2765(00)80256-7. PMID 10911985.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "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.
• Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
• Grönroos E, Hellman U, Heldin CH, Ericsson J (2002). "Control of Smad7 stability by competition between acetylation and ubiquitination". Mol. Cell. 10 (3): 483–93. doi:10.1016/S1097-2765(02)00639-1. PMID 12408818.
• Galey D, Becker K, Haughey N, et al. (2003). "Differential transcriptional regulation by human immunodeficiency virus type 1 and gp120 in human astrocytes". J. Neurovirol. 9 (3): 358–71. doi:10.1080/13550280390201119. PMID 12775419. S2CID 22016092.
• Harrington JJ, Sherf B, Rundlett S, et al. (2001). "Creation of genome-wide protein expression libraries using random activation of gene expression". Nat. Biotechnol. 19 (5): 440–5. doi:10.1038/88107. PMID 11329013. S2CID 25064683.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.