MYST1

K(lysine) acetyltransferase 8
PDB rendering based on 1wgs.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2GIV​, 2PQ8​, 2Y0M​, 3QAH​, 3TOA​, 3TOB​, 4DNC​
Identifiers
Symbols	KAT8 ; MOF; MYST1; ZC2HC8; hMOF
External IDs	OMIM: 609912 MGI: 1915023 HomoloGene: 41676 GeneCards: KAT8 Gene
EC number	2.3.1.48
Gene ontology Molecular function • histone acetyltransferase activity • protein binding • transcription factor binding • acetyltransferase activity • enzyme binding • methylated histone binding • histone acetyltransferase activity (H4-K5 specific) • histone acetyltransferase activity (H4-K8 specific) • metal ion binding • histone acetyltransferase activity (H4-K16 specific) Cellular component • histone acetyltransferase complex • kinetochore • nucleus • nucleoplasm • nuclear membrane • MLL1 complex • MSL complex Biological process • chromatin organization • transcription, DNA-templated • regulation of autophagy • histone acetylation • myeloid cell differentiation • histone H4-K5 acetylation • histone H4-K8 acetylation • histone H4-K16 acetylation • negative regulation of transcription, DNA-templated • positive regulation of transcription, DNA-templated Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	84148	67773
Ensembl	ENSG00000103510	ENSMUSG00000030801
UniProt	Q9H7Z6	Q9D1P2
RefSeq (mRNA)	NM_032188	NM_026370
RefSeq (protein)	NP_115564	NP_080646
Location (UCSC)	Chr 16: 31.12 – 31.13 Mb	Chr 7: 127.91 – 127.93 Mb
PubMed search

Probable histone acetyltransferase MYST1 is an enzyme that in humans is encoded by the MYST1 gene.^[1][2]

Function

The MYST family of histone acetyltransferases, which includes MYST1, is named for the founding members MOZ (MYST3; MIM 601408), yeast YBF2 and SAS2, and TIP60 (HTATIP; MIM 601409). All members of this family contain a MYST region of about 240 amino acids with a canonical acetyl-CoA-binding site and a C2HC-type zinc finger motif. Most MYST proteins also have a chromodomain involved in protein-protein interactions and targeting transcriptional regulators to chromatin.^[2]

Interactions

MYST1 has been shown to interact with MORF4L1.^[3]

References

1. Neal KC, Pannuti A, Smith ER, Lucchesi JC (Jan 2000). "A new human member of the MYST family of histone acetyl transferases with high sequence similarity to Drosophila MOF". Biochimica et Biophysica Acta 1490 (1-2): 170–4. doi:10.1016/s0167-4781(99)00211-0. PMID 10786633.
2. "Entrez Gene: MYST1 MYST histone acetyltransferase 1".
3. Pardo PS, Leung JK, Lucchesi JC, Pereira-Smith OM (Dec 2002). "MRG15, a novel chromodomain protein, is present in two distinct multiprotein complexes involved in transcriptional activation". The Journal of Biological Chemistry 277 (52): 50860–6. doi:10.1074/jbc.M203839200. PMID 12397079.

Further reading

• Rea S, Xouri G, Akhtar A (Aug 2007). "Males absent on the first (MOF): from flies to humans". Oncogene 26 (37): 5385–94. doi:10.1038/sj.onc.1210607. PMID 17694080.
• Maruyama K, Sugano S (Jan 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Kitabayashi I, Aikawa Y, Nguyen LA, Yokoyama A, Ohki M (Dec 2001). "Activation of AML1-mediated transcription by MOZ and inhibition by the MOZ-CBP fusion protein". The EMBO Journal 20 (24): 7184–96. doi:10.1093/emboj/20.24.7184. PMC 125775. PMID 11742995.
• Pelletier N, Champagne N, Stifani S, Yang XJ (Apr 2002). "MOZ and MORF histone acetyltransferases interact with the Runt-domain transcription factor Runx2". Oncogene 21 (17): 2729–40. doi:10.1038/sj.onc.1205367. PMID 11965546.
• Pardo PS, Leung JK, Lucchesi JC, Pereira-Smith OM (Dec 2002). "MRG15, a novel chromodomain protein, is present in two distinct multiprotein complexes involved in transcriptional activation". The Journal of Biological Chemistry 277 (52): 50860–6. doi:10.1074/jbc.M203839200. PMID 12397079.
• Wan D, Gong Y, Qin W, Zhang P, Li J, Wei L, Zhou X, Li H, Qiu X, Zhong F, He L, Yu J, Yao G, Jiang H, Qian L, Yu Y, Shu H, Chen X, Xu H, Guo M, Pan Z, Chen Y, Ge C, Yang S, Gu J (Nov 2004). "Large-scale cDNA transfection screening for genes related to cancer development and progression". Proceedings of the National Academy of Sciences of the United States of America 101 (44): 15724–9. doi:10.1073/pnas.0404089101. PMC 524842. PMID 15498874.
• Gupta A, Sharma GG, Young CS, Agarwal M, Smith ER, Paull TT, Lucchesi JC, Khanna KK, Ludwig T, Pandita TK (Jun 2005). "Involvement of human MOF in ATM function". Molecular and Cellular Biology 25 (12): 5292–305. doi:10.1128/MCB.25.12.5292-5305.2005. PMC 1140595. PMID 15923642.
• Dou Y, Milne TA, Tackett AJ, Smith ER, Fukuda A, Wysocka J, Allis CD, Chait BT, Hess JL, Roeder RG (Jun 2005). "Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF". Cell 121 (6): 873–85. doi:10.1016/j.cell.2005.04.031. PMID 15960975.
• Taipale M, Rea S, Richter K, Vilar A, Lichter P, Imhof A, Akhtar A (Aug 2005). "hMOF histone acetyltransferase is required for histone H4 lysine 16 acetylation in mammalian cells". Molecular and Cellular Biology 25 (15): 6798–810. doi:10.1128/MCB.25.15.6798-6810.2005. PMC 1190338. PMID 16024812.
• Cereseto A, Manganaro L, Gutierrez MI, Terreni M, Fittipaldi A, Lusic M, Marcello A, Giacca M (Sep 2005). "Acetylation of HIV-1 integrase by p300 regulates viral integration". The EMBO Journal 24 (17): 3070–81. doi:10.1038/sj.emboj.7600770. PMC 1201351. PMID 16096645.
• Smith ER, Cayrou C, Huang R, Lane WS, Côté J, Lucchesi JC (Nov 2005). "A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16". Molecular and Cellular Biology 25 (21): 9175–88. doi:10.1128/MCB.25.21.9175-9188.2005. PMC 1265810. PMID 16227571.
• Topper M, Luo Y, Zhadina M, Mohammed K, Smith L, Muesing MA (Mar 2007). "Posttranslational acetylation of the human immunodeficiency virus type 1 integrase carboxyl-terminal domain is dispensable for viral replication". Journal of Virology 81 (6): 3012–7. doi:10.1128/JVI.02257-06. PMC 1865993. PMID 17182677.