View source for HAT1

{{Short description|Protein-coding gene in the species Homo sapiens}}
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{{Infobox_gene}}
'''Histone acetyltransferase 1''', also known as '''HAT1''', is an [[enzyme]] that, in humans, is encoded by the ''HAT1'' [[gene]].<ref name="Verreault_1998">{{cite journal  |vauthors=Verreault A, Kaufman PD, Kobayashi R, Stillman B |title=Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase. |journal=Curr. Biol. |volume=8 |issue= 2 |pages= 96–108 |year= 1998 |pmid= 9427644 |doi=10.1016/S0960-9822(98)70040-5  |s2cid=201273 |doi-access=free |bibcode=1998CBio....8...96V }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: histone acetyltransferase 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8520| accessdate = }}</ref>
== 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 [[histone]]s, 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.<ref name="entrez"/>
==References==
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==Further reading==
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*{{cite journal   |vauthors=Olsen JV, Blagoev B, Gnad F, etal |title=Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. |journal=Cell |volume=127 |issue= 3 |pages= 635–48 |year= 2006 |pmid= 17081983 |doi= 10.1016/j.cell.2006.09.026 |s2cid=7827573 |doi-access=free }}
*{{cite journal   |vauthors=Hillier LW, Graves TA, Fulton RS, etal |title=Generation and annotation of the DNA sequences of human chromosomes 2 and 4. |journal=Nature |volume=434 |issue= 7034 |pages= 724–31 |year= 2005 |pmid= 15815621 |doi= 10.1038/nature03466 |bibcode=2005Natur.434..724H |doi-access= free }}
*{{cite journal   |vauthors=Benson LJ, Phillips JA, Gu Y, etal |title=Properties of the type B histone acetyltransferase Hat1: H4 tail interaction, site preference, and involvement in DNA repair. |journal=J. Biol. Chem. |volume=282 |issue= 2 |pages= 836–42 |year= 2007 |pmid= 17052979 |doi= 10.1074/jbc.M607464200 |doi-access= free }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334  |pmc=528928 |doi= 10.1101/gr.2596504 }}
*{{cite journal  |vauthors=Makowski AM, Dutnall RN, Annunziato AT |title=Effects of acetylation of histone H4 at lysines 8 and 16 on activity of the Hat1 histone acetyltransferase |journal=J. Biol. Chem. |volume=276 |issue= 47 |pages= 43499–502 |year= 2001 |pmid= 11585814 |doi= 10.1074/jbc.C100549200 |doi-access= free }}
*{{cite journal  |author=Marmorstein R |title=Structure of histone acetyltransferases |journal=J. Mol. Biol. |volume=311 |issue= 3 |pages= 433–44 |year= 2001 |pmid= 11492997 |doi= 10.1006/jmbi.2001.4859 }}
*{{cite journal   |vauthors=Miyamoto N, Izumi H, Noguchi T, etal |title=Tip60 is regulated by circadian transcription factor clock and is involved in cisplatin resistance |journal=J. Biol. Chem. |volume=283 |issue= 26 |pages= 18218–26 |year= 2008 |pmid= 18458078 |doi= 10.1074/jbc.M802332200 |doi-access= free }}
*{{cite journal   |vauthors=Cheung P, Tanner KG, Cheung WL, etal |title=Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation |journal=Mol. Cell |volume=5 |issue= 6 |pages= 905–15 |year= 2000 |pmid= 10911985 |doi=10.1016/S1097-2765(00)80256-7  |doi-access=free }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2002 |pmid= 12477932  |pmc=139241 |doi= 10.1073/pnas.242603899 |bibcode=2002PNAS...9916899M |doi-access=free }}
*{{cite journal   |vauthors=Kimura K, Wakamatsu A, Suzuki Y, etal |title=Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes |journal=Genome Res. |volume=16 |issue= 1 |pages= 55–65 |year= 2006 |pmid= 16344560  |pmc=1356129 |doi= 10.1101/gr.4039406 }}
*{{cite journal  |vauthors=Grönroos E, Hellman U, Heldin CH, Ericsson J |title=Control of Smad7 stability by competition between acetylation and ubiquitination |journal=Mol. Cell |volume=10 |issue= 3 |pages= 483–93 |year= 2002 |pmid= 12408818 |doi=10.1016/S1097-2765(02)00639-1  |doi-access=free }}
*{{cite journal   |vauthors=Galey D, Becker K, Haughey N, etal |title=Differential transcriptional regulation by human immunodeficiency virus type 1 and gp120 in human astrocytes |journal=J. Neurovirol. |volume=9 |issue= 3 |pages= 358–71 |year= 2003 |pmid= 12775419 |doi=  10.1080/13550280390201119|s2cid=22016092 }}
*{{cite journal   |vauthors=Harrington JJ, Sherf B, Rundlett S, etal |title=Creation of genome-wide protein expression libraries using random activation of gene expression |journal=Nat. Biotechnol. |volume=19 |issue= 5 |pages= 440–5 |year= 2001 |pmid= 11329013 |doi= 10.1038/88107 |s2cid=25064683 }}
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