MYST1

KAT8
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesKAT8, MOF, MYST1, ZC2HC8, hMOF, lysine acetyltransferase 8
External IDsMGI: 1915023 HomoloGene: 41676 GeneCards: KAT8
Gene location (Human)
Chr.Chromosome 16 (human)[1]
Band16p11.2Start31,115,754 bp[1]
End31,131,393 bp[1]
RNA expression pattern


More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

84148

67773

Ensembl

ENSG00000103510

ENSMUSG00000030801

UniProt

Q9H7Z6

Q9D1P2

RefSeq (mRNA)

NM_032188
NM_182958

NM_026370
NM_001360699

RefSeq (protein)

NP_115564
NP_892003

NP_080646
NP_001347628

Location (UCSC)Chr 16: 31.12 – 31.13 MbChr 7: 127.91 – 127.93 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Probable histone acetyltransferase MYST1 is an enzyme that in humans is encoded by the MYST1 gene.[5][6]

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.[6]

Interactions

MYST1 has been shown to interact with MORF4L1.[7]

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000103510 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000030801 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. ↑ 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.
  6. 1 2 "Entrez Gene: MYST1 MYST histone acetyltransferase 1".
  7. ↑ 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.


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