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{{Infobox_gene}}
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'''MYST histone acetyltransferase (monocytic leukemia) 3''', also known as '''MYST3''', is an enzyme that, in humans, is encoded by the ''MYST3'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MYST3 MYST histone acetyltransferase (monocytic leukemia) 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7994| accessdate = }}</ref><ref name="pmid8782817">{{cite journal |vauthors=Borrow J, Stanton VP, Andresen JM, Becher R, Behm FG, Chaganti RS, Civin CI, Disteche C, Dubé I, Frischauf AM, Horsman D, Mitelman F, Volinia S, Watmore AE, Housman DE | title = The translocation t(8;16)(p11;p13) of acute myeloid leukaemia fuses a putative acetyltransferase to the CREB-binding protein | journal = Nat. Genet. | volume = 14 | issue = 1 | pages = 33–41 |date=September 1996 | pmid = 8782817 | doi = 10.1038/ng0996-33 | url = | issn = }}</ref>
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<!-- 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_MYST3_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1m36.
| PDB = {{PDB2|1m36}}, {{PDB2|2ozu}}
| Name = MYST histone acetyltransferase (monocytic leukemia) 3
| HGNCid = 13013
| Symbol = MYST3
| AltSymbols =; MOZ; RUNXBP2; ZNF220
| OMIM = 601408
| ECnumber = 
| Homologene = 4924
| MGIid = 2442415
| GeneAtlas_image1 = PBB_GE_MYST3_202423_at_tn.png
| GeneAtlas_image2 = PBB_GE_MYST3_216361_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA 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:0000786 |text = nucleosome}} {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006323 |text = DNA packaging}} {{GNF_GO|id=GO:0006334 |text = nucleosome assembly}} {{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:0035019 |text = somatic stem cell maintenance}} {{GNF_GO|id=GO:0035162 |text = embryonic hemopoiesis}} {{GNF_GO|id=GO:0045941 |text = positive regulation of transcription}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 7994
    | Hs_Ensembl = ENSG00000083168
    | Hs_RefseqProtein = NP_006757
    | Hs_RefseqmRNA = NM_006766
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 8
    | Hs_GenLoc_start = 41907430
    | Hs_GenLoc_end = 42028635
    | Hs_Uniprot = Q92794
    | Mm_EntrezGene = 244349
    | Mm_Ensembl = ENSMUSG00000031540
    | Mm_RefseqmRNA = XM_146248
    | Mm_RefseqProtein = XP_146248
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 8
    | Mm_GenLoc_start = 24325084
    | Mm_GenLoc_end = 24406187
    | Mm_Uniprot = A0PJC5
  }}
}}
'''MYST histone acetyltransferase (monocytic leukemia) 3''', also known as '''MYST3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MYST3 MYST histone acetyltransferase (monocytic leukemia) 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7994| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
MYST3 contains two nuclear localization domains, a C<sub>2</sub>HC<sub>3</sub> [[zinc finger]] and an [[acetyltransferase]] domain.  This structure suggests that MYST3 functions as a [[chromatin]]-bound acetyltransferase.<ref name="pmid8782817"/> MYST3 is important for proper development of [[haematopoiesis|hematopoietic]] [[stem cell]]s.<ref name="pmid17694082">{{cite journal |vauthors=Yang XJ, Ullah M | title = MOZ and MORF, two large MYSTic HATs in normal and cancer stem cells | journal = Oncogene | volume = 26 | issue = 37 | pages = 5408–19 |date=August 2007 | pmid = 17694082 | doi = 10.1038/sj.onc.1210609 | url = | issn = }}</ref>
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| summary_text =  
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==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal | author=Schuler GD, Boguski MS, Stewart EA, ''et al.'' |title=A gene map of the human genome. |journal=Science |volume=274 |issue= 5287 |pages= 540-6 |year= 1996 |pmid= 8849440 |doi=  }}
*{{cite journal   |vauthors=Schuler GD, Boguski MS, Stewart EA, etal |title=A gene map of the human genome. |journal=Science |volume=274 |issue= 5287 |pages= 540–6 |year= 1996 |pmid= 8849440 |doi=10.1126/science.274.5287.540 }}
*{{cite journal | author=Borrow J, Stanton VP, Andresen JM, ''et al.'' |title=The translocation t(8;16)(p11;p13) of acute myeloid leukaemia fuses a putative acetyltransferase to the CREB-binding protein. |journal=Nat. Genet. |volume=14 |issue= 1 |pages= 33-41 |year= 1996 |pmid= 8782817 |doi= 10.1038/ng0996-33 }}
*{{cite journal   |vauthors=Borrow J, Stanton VP, Andresen JM, etal |title=The translocation t(8;16)(p11;p13) of acute myeloid leukaemia fuses a putative acetyltransferase to the CREB-binding protein. |journal=Nat. Genet. |volume=14 |issue= 1 |pages= 33–41 |year= 1996 |pmid= 8782817 |doi= 10.1038/ng0996-33 }}
*{{cite journal  | author=Carapeti M, Aguiar RC, Goldman JM, Cross NC |title=A novel fusion between MOZ and the nuclear receptor coactivator TIF2 in acute myeloid leukemia. |journal=Blood |volume=91 |issue= 9 |pages= 3127-33 |year= 1998 |pmid= 9558366 |doi=  }}
*{{cite journal  |vauthors=Carapeti M, Aguiar RC, Goldman JM, Cross NC |title=A novel fusion between MOZ and the nuclear receptor coactivator TIF2 in acute myeloid leukemia. |journal=Blood |volume=91 |issue= 9 |pages= 3127–33 |year= 1998 |pmid= 9558366 |doi=  }}
*{{cite journal | author=Chaffanet M, Gressin L, Preudhomme C, ''et al.'' |title=MOZ is fused to p300 in an acute monocytic leukemia with t(8;22). |journal=Genes Chromosomes Cancer |volume=28 |issue= 2 |pages= 138-44 |year= 2000 |pmid= 10824998 |doi= }}
*{{cite journal   |vauthors=Chaffanet M, Gressin L, Preudhomme C, etal |title=MOZ is fused to p300 in an acute monocytic leukemia with t(8;22). |journal=Genes Chromosomes Cancer |volume=28 |issue= 2 |pages= 138–44 |year= 2000 |pmid= 10824998 |doi=10.1002/(SICI)1098-2264(200006)28:2<138::AID-GCC2>3.0.CO;2-2  }}
*{{cite journal  | author=Champagne N, Pelletier N, Yang XJ |title=The monocytic leukemia zinc finger protein MOZ is a histone acetyltransferase. |journal=Oncogene |volume=20 |issue= 3 |pages= 404-9 |year= 2001 |pmid= 11313971 |doi= 10.1038/sj.onc.1204114 }}
*{{cite journal  |vauthors=Champagne N, Pelletier N, Yang XJ |title=The monocytic leukemia zinc finger protein MOZ is a histone acetyltransferase. |journal=Oncogene |volume=20 |issue= 3 |pages= 404–9 |year= 2001 |pmid= 11313971 |doi= 10.1038/sj.onc.1204114 }}
*{{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=Kitabayashi I, Aikawa Y, Nguyen LA, etal |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 | pmc=125775 }}
*{{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=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 | 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=Strausberg RL, Feingold EA, Grouse LH, etal |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 | pmc=139241 }}
*{{cite journal | author=Deguchi K, Ayton PM, Carapeti M, ''et al.'' |title=MOZ-TIF2-induced acute myeloid leukemia requires the MOZ nucleosome binding motif and TIF2-mediated recruitment of CBP. |journal=Cancer Cell |volume=3 |issue= 3 |pages= 259-71 |year= 2003 |pmid= 12676584 |doi=  }}
*{{cite journal   |vauthors=Deguchi K, Ayton PM, Carapeti M, etal |title=MOZ-TIF2-induced acute myeloid leukemia requires the MOZ nucleosome binding motif and TIF2-mediated recruitment of CBP. |journal=Cancer Cell |volume=3 |issue= 3 |pages= 259–71 |year= 2003 |pmid= 12676584 |doi=10.1016/S1535-6108(03)00051-5 }}
*{{cite journal  | author=Bristow CA, Shore P |title=Transcriptional regulation of the human MIP-1alpha promoter by RUNX1 and MOZ. |journal=Nucleic Acids Res. |volume=31 |issue= 11 |pages= 2735-44 |year= 2003 |pmid= 12771199 |doi=  }}
*{{cite journal  |vauthors=Bristow CA, Shore P |title=Transcriptional regulation of the human MIP-1alpha promoter by RUNX1 and MOZ. |journal=Nucleic Acids Res. |volume=31 |issue= 11 |pages= 2735–44 |year= 2003 |pmid= 12771199 |doi=10.1093/nar/gkg401  | pmc=156734 }}
*{{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=Ota T, Suzuki Y, Nishikawa T, etal |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 | author=Kindle KB, Troke PJ, Collins HM, ''et al.'' |title=MOZ-TIF2 inhibits transcription by nuclear receptors and p53 by impairment of CBP function. |journal=Mol. Cell. Biol. |volume=25 |issue= 3 |pages= 988-1002 |year= 2005 |pmid= 15657427 |doi= 10.1128/MCB.25.3.988-1002.2005 }}
*{{cite journal   |vauthors=Kindle KB, Troke PJ, Collins HM, etal |title=MOZ-TIF2 inhibits transcription by nuclear receptors and p53 by impairment of CBP function. |journal=Mol. Cell. Biol. |volume=25 |issue= 3 |pages= 988–1002 |year= 2005 |pmid= 15657427 |doi= 10.1128/MCB.25.3.988-1002.2005 | pmc=544007 }}
*{{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   |vauthors=Cereseto A, Manganaro L, Gutierrez MI, etal |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 | pmc=1201351 }}
*{{cite journal | author=Kimura K, Wakamatsu A, Suzuki Y, ''et al.'' |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. |journal=Genome Res. |volume=16 |issue= 1 |pages= 55-65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406 }}
*{{cite journal   |vauthors=Kimura K, Wakamatsu A, Suzuki Y, etal |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. |journal=Genome Res. |volume=16 |issue= 1 |pages= 55–65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406 | pmc=1356129 }}
*{{cite journal | author=Collins HM, Kindle KB, Matsuda S, ''et al.'' |title=MOZ-TIF2 alters cofactor recruitment and histone modification at the RARbeta2 promoter: differential effects of MOZ fusion proteins on CBP- and MOZ-dependent activators. |journal=J. Biol. Chem. |volume=281 |issue= 25 |pages= 17124-33 |year= 2006 |pmid= 16613851 |doi= 10.1074/jbc.M602633200 }}
*{{cite journal   |vauthors=Collins HM, Kindle KB, Matsuda S, etal |title=MOZ-TIF2 alters cofactor recruitment and histone modification at the RARbeta2 promoter: differential effects of MOZ fusion proteins on CBP- and MOZ-dependent activators. |journal=J. Biol. Chem. |volume=281 |issue= 25 |pages= 17124–33 |year= 2006 |pmid= 16613851 |doi= 10.1074/jbc.M602633200 }}
*{{cite journal | author=Lim J, Hao T, Shaw C, ''et al.'' |title=A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration. |journal=Cell |volume=125 |issue= 4 |pages= 801-14 |year= 2006 |pmid= 16713569 |doi= 10.1016/j.cell.2006.03.032 }}
*{{cite journal   |vauthors=Lim J, Hao T, Shaw C, etal |title=A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration. |journal=Cell |volume=125 |issue= 4 |pages= 801–14 |year= 2006 |pmid= 16713569 |doi= 10.1016/j.cell.2006.03.032 }}
*{{cite journal | author=Kim SC, Sprung R, Chen Y, ''et al.'' |title=Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. |journal=Mol. Cell |volume=23 |issue= 4 |pages= 607-18 |year= 2006 |pmid= 16916647 |doi= 10.1016/j.molcel.2006.06.026 }}
*{{cite journal   |vauthors=Kim SC, Sprung R, Chen Y, etal |title=Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. |journal=Mol. Cell |volume=23 |issue= 4 |pages= 607–18 |year= 2006 |pmid= 16916647 |doi= 10.1016/j.molcel.2006.06.026 }}
*{{cite journal | author=Olsen JV, Blagoev B, Gnad F, ''et al.'' |title=Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. |journal=Cell |volume=127 |issue= 3 |pages= 635-48 |year= 2006 |pmid= 17081983 |doi= 10.1016/j.cell.2006.09.026 }}
*{{cite journal   |vauthors=Olsen JV, Blagoev B, Gnad F, etal |title=Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. |journal=Cell |volume=127 |issue= 3 |pages= 635–48 |year= 2006 |pmid= 17081983 |doi= 10.1016/j.cell.2006.09.026 }}
*{{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 }}
*{{cite journal   |vauthors=Topper M, Luo Y, Zhadina M, etal |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 | pmc=1865993 }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=7994}}
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Revision as of 07:16, 4 September 2017

VALUE_ERROR (nil)
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

MYST histone acetyltransferase (monocytic leukemia) 3, also known as MYST3, is an enzyme that, in humans, is encoded by the MYST3 gene.[1][2]

Function

MYST3 contains two nuclear localization domains, a C2HC3 zinc finger and an acetyltransferase domain. This structure suggests that MYST3 functions as a chromatin-bound acetyltransferase.[2] MYST3 is important for proper development of hematopoietic stem cells.[3]

References

  1. ↑ "Entrez Gene: MYST3 MYST histone acetyltransferase (monocytic leukemia) 3".
  2. ↑ 2.0 2.1 Borrow J, Stanton VP, Andresen JM, Becher R, Behm FG, Chaganti RS, Civin CI, Disteche C, Dubé I, Frischauf AM, Horsman D, Mitelman F, Volinia S, Watmore AE, Housman DE (September 1996). "The translocation t(8;16)(p11;p13) of acute myeloid leukaemia fuses a putative acetyltransferase to the CREB-binding protein". Nat. Genet. 14 (1): 33–41. doi:10.1038/ng0996-33. PMID 8782817.
  3. ↑ Yang XJ, Ullah M (August 2007). "MOZ and MORF, two large MYSTic HATs in normal and cancer stem cells". Oncogene. 26 (37): 5408–19. doi:10.1038/sj.onc.1210609. PMID 17694082.

Further reading



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