KAT7 (gene)

Last updated
KAT7
Identifiers
Aliases KAT7 , HBO1, HBOA, MYST2, ZC2HC7, lysine acetyltransferase 7
External IDs OMIM: 609880 MGI: 2182799 HomoloGene: 5134 GeneCards: KAT7
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001195003
NM_001195004
NM_177619

RefSeq (protein)
Location (UCSC) Chr 17: 49.79 – 49.84 Mb Chr 11: 95.17 – 95.2 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Histone acetyltransferase KAT7 is an enzyme that in humans is encoded by the KAT7 gene. [5] [6] [7] It specifically acetylates H4 histones at the lysine12 residue (H4K12) [8] and is necessary for origin licensing and DNA replication. [9] [10] KAT7 associates with origins of replication during G1 phase of the cell cycle through complexing with CDT1. [11] Geminin is thought to inhibit the acetyltransferase activity of KAT7 when KAT7 and CDT1 are complexed together. [12]

Interactions

KAT7 has been shown to interact with:

Related Research Articles

<span class="mw-page-title-main">Histone acetyltransferase</span> Enzymes that catalyze acyl group transfer from acetyl-CoA to histones

Histone acetyltransferases (HATs) are enzymes that acetylate conserved lysine amino acids on histone proteins by transferring an acetyl group from acetyl-CoA to form ε-N-acetyllysine. DNA is wrapped around histones, and, by transferring an acetyl group to the histones, genes can be turned on and off. In general, histone acetylation increases gene expression.

<span class="mw-page-title-main">MCM6</span>

DNA replication licensing factor MCM6 is a protein that in humans is encoded by the MCM6 gene. MCM6 is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication.

<span class="mw-page-title-main">PCAF</span>

P300/CBP-associated factor (PCAF), also known as K(lysine) acetyltransferase 2B (KAT2B), is a human gene and transcriptional coactivator associated with p53.

<span class="mw-page-title-main">CREB-binding protein</span> Nuclear protein that binds to CREB

Cyclic adenosine monophosphate Response Element Binding protein Binding Protein, also known as CREBBP or CBP or KAT3A, is a coactivator encoded by the CREBBP gene in humans, located on chromosome 16p13.3. CBP has intrinsic acetyltransferase functions; it is able to add acetyl groups to both transcription factors as well as histone lysines, the latter of which has been shown to alter chromatin structure making genes more accessible for transcription. This relatively unique acetyltransferase activity is also seen in another transcription enzyme, EP300 (p300). Together, they are known as the p300-CBP coactivator family and are known to associate with more than 16,000 genes in humans; however, while these proteins share many structural features, emerging evidence suggests that these two co-activators may promote transcription of genes with different biological functions.

<span class="mw-page-title-main">Histone acetylation and deacetylation</span>

Histone acetylation and deacetylation are the processes by which the lysine residues within the N-terminal tail protruding from the histone core of the nucleosome are acetylated and deacetylated as part of gene regulation.

<span class="mw-page-title-main">HIST3H3</span> Protein-coding gene in the species Homo sapiens

Histone H3.1t is a protein that in humans is encoded by the HIST3H3 gene.

<span class="mw-page-title-main">MCM2</span>

DNA replication licensing factor MCM2 is a protein that in humans is encoded by the MCM2 gene.

<span class="mw-page-title-main">KAT2A</span> Protein-coding gene in the species Homo sapiens

Histone acetyltransferase KAT2A is an enzyme that in humans is encoded by the KAT2A gene.

<span class="mw-page-title-main">KAT5</span> Protein-coding gene in the species Homo sapiens

Histone acetyltransferase KAT5 is an enzyme that in humans is encoded by the KAT5 gene. It is also commonly identified as TIP60.

<span class="mw-page-title-main">MORF4L1</span>

Mortality factor 4-like protein 1 is a protein that in humans is encoded by the MORF4L1 gene.

<span class="mw-page-title-main">DMAP1</span> Protein-coding gene in the species Homo sapiens

DNA methyltransferase 1-associated protein 1 is an enzyme that in humans is encoded by the DMAP1 gene.

<span class="mw-page-title-main">KAT6A</span> Protein-coding gene in the species Homo sapiens

K(lysine) acetyltransferase 6A (KAT6A), is an enzyme that, in humans, is encoded by the KAT6A gene. This gene is located on human chromosome 8, band 8p11.21.

<span class="mw-page-title-main">ING2</span> Protein-coding gene in the species Homo sapiens

Inhibitor of growth protein 2 is a protein that in humans is encoded by the ING2 gene.

<span class="mw-page-title-main">KAT8</span> Protein-coding gene in the species Homo sapiens

K(lysine) acetyltransferase 8 (KAT8) is an enzyme that in humans is encoded by the KAT8 gene.

<span class="mw-page-title-main">KAT6B</span> Protein-coding gene in the species Homo sapiens

K(lysine) acetyltransferase 6B (KAT6B) is an enzyme that in humans is encoded by the KAT6B gene.

<span class="mw-page-title-main">JADE1</span> Protein-coding gene in the species Homo sapiens

JADE1 is a protein that in humans is encoded by the JADE1 gene.

<span class="mw-page-title-main">HAT1</span>

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

<span class="mw-page-title-main">ORC1</span>

Origin recognition complex subunit 1 is a protein that in humans is encoded by the ORC1 gene. It is closely related to CDC6, and both are the same protein in archaea.

Protein acetylation are acetylation reactions that occur within living cells as drug metabolism, by enzymes in the liver and other organs. Pharmaceuticals frequently employ acetylation to enable such esters to cross the blood–brain barrier, where they are deacetylated by enzymes (carboxylesterases) in a manner similar to acetylcholine. Examples of acetylated pharmaceuticals are diacetylmorphine (heroin), acetylsalicylic acid (aspirin), THC-O-acetate, and diacerein. Conversely, drugs such as isoniazid are acetylated within the liver during drug metabolism. A drug that depends on such metabolic transformations in order to act is termed a prodrug.

<span class="mw-page-title-main">Brpf1</span> Protein-coding gene in the species Mus musculus

Peregrin also known as bromodomain and PHD finger-containing protein 1 is a protein that in humans is encoded by the BRPF1 gene located on 3p26-p25. Peregrin is a multivalent chromatin regulator that recognizes different epigenetic marks and activates three histone acetyltransferases. BRPF1 contains two PHD fingers, one bromodomain and one chromo/Tudor-related Pro-Trp-Trp-Pro (PWWP) domain.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000136504 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000038909 - 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. 1 2 3 Iizuka M, Stillman B (Aug 1999). "Histone acetyltransferase HBO1 interacts with the ORC1 subunit of the human initiator protein". The Journal of Biological Chemistry. 274 (33): 23027–34. doi: 10.1074/jbc.274.33.23027 . PMID   10438470.
  6. 1 2 Sharma M, Zarnegar M, Li X, Lim B, Sun Z (Nov 2000). "Androgen receptor interacts with a novel MYST protein, HBO1". The Journal of Biological Chemistry. 275 (45): 35200–8. doi: 10.1074/jbc.M004838200 . PMID   10930412.
  7. "Entrez Gene: MYST2 MYST histone acetyltransferase 2".
  8. Sterner DE, Berger SL (Jun 2000). "Acetylation of histones and transcription-related factors". Microbiology and Molecular Biology Reviews. 64 (2): 435–59. doi:10.1128/mmbr.64.2.435-459.2000. PMC   98999 . PMID   10839822.
  9. Doyon Y, Cayrou C, Ullah M, Landry AJ, Côté V, Selleck W, Lane WS, Tan S, Yang XJ, Côté J (Jan 2006). "ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation". Molecular Cell. 21 (1): 51–64. doi: 10.1016/j.molcel.2005.12.007 . PMID   16387653.
  10. Iizuka M, Matsui T, Takisawa H, Smith MM (Feb 2006). "Regulation of replication licensing by acetyltransferase Hbo1". Molecular and Cellular Biology. 26 (3): 1098–108. doi:10.1128/MCB.26.3.1098-1108.2006. PMC   1347032 . PMID   16428461.
  11. Miotto B, Struhl K (Oct 2008). "HBO1 histone acetylase is a coactivator of the replication licensing factor Cdt1". Genes & Development. 22 (19): 2633–8. doi:10.1101/gad.1674108. PMC   2559906 . PMID   18832067.
  12. 1 2 Miotto B, Struhl K (Jan 2010). "HBO1 histone acetylase activity is essential for DNA replication licensing and inhibited by Geminin". Molecular Cell. 37 (1): 57–66. doi:10.1016/j.molcel.2009.12.012. PMC   2818871 . PMID   20129055.
  13. Burke TW, Cook JG, Asano M, Nevins JR (May 2001). "Replication factors MCM2 and ORC1 interact with the histone acetyltransferase HBO1". The Journal of Biological Chemistry. 276 (18): 15397–408. doi: 10.1074/jbc.M011556200 . PMID   11278932.
  14. Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID   16189514. S2CID   4427026.
  15. Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (Sep 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl: 11858/00-001M-0000-0010-8592-0 . PMID   16169070. S2CID   8235923.

Further reading