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{{Infobox_gene}}
{{PBB_Controls
'''Probable histone acetyltransferase MYST1''' is an [[enzyme]] that in humans is encoded by the ''MYST1'' [[gene]].<ref name="pmid10786633">{{cite journal | vauthors = Neal KC, Pannuti A, Smith ER, Lucchesi JC | title = A new human member of the MYST family of histone acetyl transferases with high sequence similarity to Drosophila MOF | journal = Biochimica et Biophysica Acta | volume = 1490 | issue = 1-2 | pages = 170–4 | date = Jan 2000 | pmid = 10786633 | pmc =  | doi = 10.1016/s0167-4781(99)00211-0 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: MYST1 MYST histone acetyltransferase 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=84148| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_MYST1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1wgs.
| PDB = {{PDB2|1wgs}}, {{PDB2|2giv}}, {{PDB2|2pq8}}
| Name = MYST histone acetyltransferase 1
| HGNCid = 17933
| Symbol = MYST1
| AltSymbols =; FLJ14040; MOF; hMOF
| OMIM = 609912
| ECnumber = 
| Homologene = 41676
| MGIid = 1915023
| GeneAtlas_image1 = PBB_GE_MYST1_221820_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_MYST1_214885_at_tn.png
| Function = {{GNF_GO|id=GO:0003682 |text = chromatin binding}} {{GNF_GO|id=GO:0004402 |text = histone acetyltransferase activity}} {{GNF_GO|id=GO:0008134 |text = transcription factor binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016407 |text = acetyltransferase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0000785 |text = chromatin}} {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006333 |text = chromatin assembly or disassembly}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0016481 |text = negative regulation of transcription}} {{GNF_GO|id=GO:0016568 |text = chromatin modification}} {{GNF_GO|id=GO:0016573 |text = histone acetylation}} {{GNF_GO|id=GO:0030099 |text = myeloid cell differentiation}} {{GNF_GO|id=GO:0045941 |text = positive regulation of transcription}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 84148
    | Hs_Ensembl = ENSG00000103510
    | Hs_RefseqProtein = NP_115564
    | Hs_RefseqmRNA = NM_032188
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 16
    | Hs_GenLoc_start = 31036488
    | Hs_GenLoc_end = 31050206
    | Hs_Uniprot = Q9H7Z6
    | Mm_EntrezGene = 67773
    | Mm_Ensembl = ENSMUSG00000030801
    | Mm_RefseqmRNA = NM_026370
    | Mm_RefseqProtein = NP_080646
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 7
    | Mm_GenLoc_start = 127703670
    | Mm_GenLoc_end = 127716980
    | Mm_Uniprot = Q3V268
  }}
}}
'''MYST histone acetyltransferase 1''', also known as '''MYST1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MYST1 MYST histone acetyltransferase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=84148| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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.<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = 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 (Neal et al., 2000).[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: MYST1 MYST histone acetyltransferase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=84148| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
MYST1 has been shown to [[Protein-protein interaction|interact]] with [[MORF4L1]].<ref name=pmid12397079>{{cite journal | vauthors = Pardo PS, Leung JK, Lucchesi JC, Pereira-Smith OM | title = MRG15, a novel chromodomain protein, is present in two distinct multiprotein complexes involved in transcriptional activation | journal = The Journal of Biological Chemistry | volume = 277 | issue = 52 | pages = 50860–6 | date = Dec 2002 | pmid = 12397079 | doi = 10.1074/jbc.M203839200 }}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Rea S, Xouri G, Akhtar A | title = Males absent on the first (MOF): from flies to humans | journal = Oncogene | volume = 26 | issue = 37 | pages = 5385–94 | date = Aug 2007 | pmid = 17694080 | doi = 10.1038/sj.onc.1210607 }}
| citations =
* {{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides | journal = Gene | volume = 138 | issue = 1-2 | pages = 171–4 | date = Jan 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
*{{cite journal | author=Rea S, Xouri G, Akhtar A |title=Males absent on the first (MOF): from flies to humans. |journal=Oncogene |volume=26 |issue= 37 |pages= 5385-94 |year= 2007 |pmid= 17694080 |doi= 10.1038/sj.onc.1210607 }}
* {{cite journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1-2 | pages = 149–56 | date = Oct 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
* {{cite journal | vauthors = Kitabayashi I, Aikawa Y, Nguyen LA, Yokoyama A, Ohki M | title = Activation of AML1-mediated transcription by MOZ and inhibition by the MOZ-CBP fusion protein | journal = The EMBO Journal | volume = 20 | issue = 24 | pages = 7184–96 | date = Dec 2001 | pmid = 11742995 | pmc = 125775 | doi = 10.1093/emboj/20.24.7184 }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
* {{cite journal | vauthors = Pelletier N, Champagne N, Stifani S, Yang XJ | title = MOZ and MORF histone acetyltransferases interact with the Runt-domain transcription factor Runx2 | journal = Oncogene | volume = 21 | issue = 17 | pages = 2729–40 | date = Apr 2002 | pmid = 11965546 | doi = 10.1038/sj.onc.1205367 }}
*{{cite journal  | author=Neal KC, Pannuti A, Smith ER, Lucchesi JC |title=A new human member of the MYST family of histone acetyl transferases with high sequence similarity to Drosophila MOF. |journal=Biochim. Biophys. Acta |volume=1490 |issue= 1-2 |pages= 170-4 |year= 2000 |pmid= 10786633 |doi=  }}
* {{cite journal | vauthors = Pardo PS, Leung JK, Lucchesi JC, Pereira-Smith OM | title = MRG15, a novel chromodomain protein, is present in two distinct multiprotein complexes involved in transcriptional activation | journal = The Journal of Biological Chemistry | volume = 277 | issue = 52 | pages = 50860–6 | date = Dec 2002 | pmid = 12397079 | doi = 10.1074/jbc.M203839200 }}
*{{cite journal | author=Kitabayashi I, Aikawa Y, Nguyen LA, ''et al.'' |title=Activation of AML1-mediated transcription by MOZ and inhibition by the MOZ-CBP fusion protein. |journal=EMBO J. |volume=20 |issue= 24 |pages= 7184-96 |year= 2002 |pmid= 11742995 |doi= 10.1093/emboj/20.24.7184 }}
* {{cite journal | vauthors = 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 | title = Large-scale cDNA transfection screening for genes related to cancer development and progression | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 101 | issue = 44 | pages = 15724–9 | date = Nov 2004 | pmid = 15498874 | pmc = 524842 | doi = 10.1073/pnas.0404089101 }}
*{{cite journal | author=Pelletier N, Champagne N, Stifani S, Yang XJ |title=MOZ and MORF histone acetyltransferases interact with the Runt-domain transcription factor Runx2. |journal=Oncogene |volume=21 |issue= 17 |pages= 2729-40 |year= 2002 |pmid= 11965546 |doi= 10.1038/sj.onc.1205367 }}
* {{cite journal | vauthors = Gupta A, Sharma GG, Young CS, Agarwal M, Smith ER, Paull TT, Lucchesi JC, Khanna KK, Ludwig T, Pandita TK | title = Involvement of human MOF in ATM function | journal = Molecular and Cellular Biology | volume = 25 | issue = 12 | pages = 5292–305 | date = Jun 2005 | pmid = 15923642 | pmc = 1140595 | doi = 10.1128/MCB.25.12.5292-5305.2005 }}
*{{cite journal | author=Pardo PS, Leung JK, Lucchesi JC, Pereira-Smith OM |title=MRG15, a novel chromodomain protein, is present in two distinct multiprotein complexes involved in transcriptional activation. |journal=J. Biol. Chem. |volume=277 |issue= 52 |pages= 50860-6 |year= 2003 |pmid= 12397079 |doi= 10.1074/jbc.M203839200 }}
* {{cite journal | vauthors = Dou Y, Milne TA, Tackett AJ, Smith ER, Fukuda A, Wysocka J, Allis CD, Chait BT, Hess JL, Roeder RG | title = Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF | journal = Cell | volume = 121 | issue = 6 | pages = 873–85 | date = Jun 2005 | pmid = 15960975 | doi = 10.1016/j.cell.2005.04.031 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |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= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
* {{cite journal | vauthors = Taipale M, Rea S, Richter K, Vilar A, Lichter P, Imhof A, Akhtar A | title = hMOF histone acetyltransferase is required for histone H4 lysine 16 acetylation in mammalian cells | journal = Molecular and Cellular Biology | volume = 25 | issue = 15 | pages = 6798–810 | date = Aug 2005 | pmid = 16024812 | pmc = 1190338 | doi = 10.1128/MCB.25.15.6798-6810.2005 }}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
* {{cite journal | vauthors = Cereseto A, Manganaro L, Gutierrez MI, Terreni M, Fittipaldi A, Lusic M, Marcello A, Giacca M | title = Acetylation of HIV-1 integrase by p300 regulates viral integration | journal = The EMBO Journal | volume = 24 | issue = 17 | pages = 3070–81 | date = Sep 2005 | pmid = 16096645 | pmc = 1201351 | doi = 10.1038/sj.emboj.7600770 }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |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 |doi= 10.1101/gr.2596504 }}
* {{cite journal | vauthors = Smith ER, Cayrou C, Huang R, Lane WS, Côté J, Lucchesi JC | title = A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16 | journal = Molecular and Cellular Biology | volume = 25 | issue = 21 | pages = 9175–88 | date = Nov 2005 | pmid = 16227571 | pmc = 1265810 | doi = 10.1128/MCB.25.21.9175-9188.2005 }}
*{{cite journal  | author=Wan D, Gong Y, Qin W, ''et al.'' |title=Large-scale cDNA transfection screening for genes related to cancer development and progression. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 44 |pages= 15724-9 |year= 2004 |pmid= 15498874 |doi= 10.1073/pnas.0404089101 }}
* {{cite journal | vauthors = Topper M, Luo Y, Zhadina M, Mohammed K, Smith L, Muesing MA | title = Posttranslational acetylation of the human immunodeficiency virus type 1 integrase carboxyl-terminal domain is dispensable for viral replication | journal = Journal of Virology | volume = 81 | issue = 6 | pages = 3012–7 | date = Mar 2007 | pmid = 17182677 | pmc = 1865993 | doi = 10.1128/JVI.02257-06 }}
*{{cite journal | author=Gupta A, Sharma GG, Young CS, ''et al.'' |title=Involvement of human MOF in ATM function. |journal=Mol. Cell. Biol. |volume=25 |issue= 12 |pages= 5292-305 |year= 2005 |pmid= 15923642 |doi= 10.1128/MCB.25.12.5292-5305.2005 }}
*{{cite journal | author=Dou Y, Milne TA, Tackett AJ, ''et al.'' |title=Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF. |journal=Cell |volume=121 |issue= 6 |pages= 873-85 |year= 2005 |pmid= 15960975 |doi= 10.1016/j.cell.2005.04.031 }}
*{{cite journal | author=Taipale M, Rea S, Richter K, ''et al.'' |title=hMOF histone acetyltransferase is required for histone H4 lysine 16 acetylation in mammalian cells. |journal=Mol. Cell. Biol. |volume=25 |issue= 15 |pages= 6798-810 |year= 2005 |pmid= 16024812 |doi= 10.1128/MCB.25.15.6798-6810.2005 }}
*{{cite journal | author=Cereseto A, Manganaro L, Gutierrez MI, ''et al.'' |title=Acetylation of HIV-1 integrase by p300 regulates viral integration. |journal=EMBO J. |volume=24 |issue= 17 |pages= 3070-81 |year= 2005 |pmid= 16096645 |doi= 10.1038/sj.emboj.7600770 }}
*{{cite journal | author=Smith ER, Cayrou C, Huang R, ''et al.'' |title=A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16. |journal=Mol. Cell. Biol. |volume=25 |issue= 21 |pages= 9175-88 |year= 2005 |pmid= 16227571 |doi= 10.1128/MCB.25.21.9175-9188.2005 }}
*{{cite journal | author=Topper M, Luo Y, Zhadina M, ''et al.'' |title=Posttranslational acetylation of the human immunodeficiency virus type 1 integrase carboxyl-terminal domain is dispensable for viral replication. |journal=J. Virol. |volume=81 |issue= 6 |pages= 3012-7 |year= 2007 |pmid= 17182677 |doi= 10.1128/JVI.02257-06 }}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=84148}}


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{{WikiDoc Sources}}

Latest revision as of 07:16, 4 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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. ↑ 2.0 2.1 "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


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