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==Acetyltransferase domain of Human HIV-1 Tat interacting protein, 60kDa, isoform 3==
==Acetyltransferase domain of Human HIV-1 Tat interacting protein, 60kDa, isoform 3==
<StructureSection load='2ou2' size='340' side='right' caption='[[2ou2]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='2ou2' size='340' side='right'caption='[[2ou2]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2ou2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OU2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2OU2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2ou2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OU2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OU2 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HTATIP, TIP60 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ou2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ou2 OCA], [https://pdbe.org/2ou2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ou2 RCSB], [https://www.ebi.ac.uk/pdbsum/2ou2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ou2 ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ou2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ou2 OCA], [http://pdbe.org/2ou2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ou2 RCSB], [http://www.ebi.ac.uk/pdbsum/2ou2 PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/KAT5_HUMAN KAT5_HUMAN]] Catalytic subunit of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome-DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Directly acetylates and activates ATM. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome. In case of HIV-1 infection, interaction with the viral Tat protein leads to KAT5 polyubiquitination and targets it to degradation. Relieves NR1D2-mediated inhibition of APOC3 expression by acetylating NR1D2.<ref>PMID:12776177</ref> <ref>PMID:15310756</ref> <ref>PMID:14966270</ref> <ref>PMID:15121871</ref> <ref>PMID:15042092</ref> <ref>PMID:16141325</ref> <ref>PMID:16387653</ref> <ref>PMID:17996965</ref> <ref>PMID:19909775</ref> <ref>PMID:24463511</ref>
[https://www.uniprot.org/uniprot/KAT5_HUMAN KAT5_HUMAN] Catalytic subunit of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome-DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Directly acetylates and activates ATM. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome. In case of HIV-1 infection, interaction with the viral Tat protein leads to KAT5 polyubiquitination and targets it to degradation. Relieves NR1D2-mediated inhibition of APOC3 expression by acetylating NR1D2.<ref>PMID:12776177</ref> <ref>PMID:15310756</ref> <ref>PMID:14966270</ref> <ref>PMID:15121871</ref> <ref>PMID:15042092</ref> <ref>PMID:16141325</ref> <ref>PMID:16387653</ref> <ref>PMID:17996965</ref> <ref>PMID:19909775</ref> <ref>PMID:24463511</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ou/2ou2_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ou/2ou2_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ou2 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Histone acetyltransferase|Histone acetyltransferase]]
*[[Histone acetyltransferase 3D structures|Histone acetyltransferase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Histone acetyltransferase]]
[[Category: Homo sapiens]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C H]]
[[Category: Arrowsmith CH]]
[[Category: Bochkarev, A]]
[[Category: Bochkarev A]]
[[Category: Dombrovski, L]]
[[Category: Dombrovski L]]
[[Category: Edwards, A M]]
[[Category: Edwards AM]]
[[Category: Loppnau, P]]
[[Category: Loppnau P]]
[[Category: Min, J]]
[[Category: Min J]]
[[Category: Plotnikov, A N]]
[[Category: Plotnikov AN]]
[[Category: Structural genomic]]
[[Category: Sundstrom M]]
[[Category: Sundstrom, M]]
[[Category: Weigelt J]]
[[Category: Weigelt, J]]
[[Category: Wu H]]
[[Category: Wu, H]]
[[Category: Histone acetyltransferase htatip]]
[[Category: Sgc]]
[[Category: Tip]]
[[Category: Tip60]]
[[Category: Transferase]]

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