KAT7 (gene)

KAT7
Identifiers
Aliases	KAT7, HBO1, HBOA, MYST2, ZC2HC7, lysine acetyltransferase 7
External IDs	OMIM: 609880; MGI: 2182799; HomoloGene: 5134; GeneCards: KAT7; OMA:KAT7 - orthologs
Gene location (Human)
Chr.	Chromosome 17 (human)
End	49,835,026 bp
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)
End	95,201,072 bp
RNA expression pattern
	Top expressed in
	sural nerve; ; testicle; ; left testis; ; Achilles tendon; ; right testis; ; ventricular zone; ; gonad; ; epithelium of colon; ; popliteal artery; ; tibial arteries;
	Top expressed in
	spermatocyte; ; ankle joint; ; Rostral migratory stream; ; zygote; ; spermatid; ; secondary oocyte; ; seminiferous tubule; ; tail of embryo; ; cumulus cell; ; granulocyte;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	transferase activity; DNA-binding transcription factor activity; zinc ion binding; metal ion binding; histone acetyltransferase activity; protein binding; acyltransferase activity; DNA replication origin binding; DNA-binding transcription factor activity, RNA polymerase II-specific; H4 histone acetyltransferase activity; histone binding;
Cellular component	nucleoplasm; nucleolus; histone acetyltransferase complex; nucleus; cytoplasm; cytosol;
Biological process	regulation of transcription, DNA-templated; transcription, DNA-templated; histone H4-K5 acetylation; DNA replication; histone H3 acetylation; histone H4-K16 acetylation; histone H4-K8 acetylation; histone H4-K12 acetylation; positive regulation of protein localization to nucleus; stress-activated protein kinase signaling cascade; positive regulation of transcription by RNA polymerase II; response to sorbitol; response to hydroxyurea; response to actinomycin D; response to dithiothreitol; response to anisomycin; positive regulation of histone H4 acetylation; histone acetylation; chromatin organization; negative regulation of transcription, DNA-templated; internal peptidyl-lysine acetylation;
	Sources:Amigo / QuickGO
Orthologs
	11143
	217127
	ENSG00000136504
	ENSMUSG00000038909
	O95251
	Q5SVQ0
NM_001199155; NM_001199156; NM_001199157; NM_001199158; NM_007067;
	NM_001346706
	NM_001195003; NM_001195004; NM_177619
NP_001186084; NP_001186085; NP_001186086; NP_001186087; NP_001333635;
	NP_008998
NP_001181932; NP_001181933; NP_808287; NP_001392123; NP_001392124;
	NP_001392125; NP_001392126; NP_001392127; NP_001392128; NP_001392129; NP_001392130; NP_001392131; NP_001392132; NP_001392133; NP_001392134; NP_001392135; NP_001392136; NP_001392137; NP_001392138; NP_001392139; NP_001392140; NP_001392141; NP_001392142; NP_001392143; NP_001392144; NP_001392145; NP_001392146; NP_001392147; NP_001392148; NP_001392149; NP_001392150; NP_001392151; NP_001392152; NP_001392153; NP_001392154; NP_001392155; NP_001392156
	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]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000136504 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000038909 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ 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.
^ "Entrez Gene: MYST2 MYST histone acetyltransferase 2".
^ 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.
^ 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.
^ 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.
^ 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.
^ 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.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000136504 – Ensembl, May 2017

[refGRCm38Ensembl-2] 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.

[pmid10438470-5] 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.

[pmid10930412-6] 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.

[entrez-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.

[Miotto_2010-12] 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.

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