1wgs
From Proteopedia
(Difference between revisions)
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==Solution Structure of the Tudor Domain from Mouse Hypothetical Protein Homologous to Histone Acetyltransferase== | ==Solution Structure of the Tudor Domain from Mouse Hypothetical Protein Homologous to Histone Acetyltransferase== | ||
- | <StructureSection load='1wgs' size='340' side='right'caption='[[1wgs | + | <StructureSection load='1wgs' size='340' side='right'caption='[[1wgs]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1wgs]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1wgs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WGS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WGS FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1wgs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wgs OCA], [https://pdbe.org/1wgs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wgs RCSB], [https://www.ebi.ac.uk/pdbsum/1wgs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wgs ProSAT], [https://www.topsan.org/Proteins/RSGI/1wgs TOPSAN]</span></td></tr> | |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
- | [ | + | [https://www.uniprot.org/uniprot/KAT8_MOUSE KAT8_MOUSE] Histone acetyltransferase which may be involved in transcriptional activation. May influence the function of ATM. As part of the MSL complex it is involved in acetylation of nucleosomal histone H4 producing specifically H4K16ac. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. That activity is less specific than the one of the MSL complex. Can also acetylate TP53/p53 at 'Lys-120'.[UniProtKB:Q9H7Z6] |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: Histone acetyltransferase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: | + | [[Category: Mus musculus]] |
- | [[Category: Inoue | + | [[Category: Inoue M]] |
- | [[Category: Kigawa | + | [[Category: Kigawa T]] |
- | [[Category: Koshiba | + | [[Category: Koshiba S]] |
- | [[Category: Li | + | [[Category: Li H]] |
- | + | [[Category: Saito K]] | |
- | [[Category: Saito | + | [[Category: Yokoyama S]] |
- | [[Category: Yokoyama | + | |
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Current revision
Solution Structure of the Tudor Domain from Mouse Hypothetical Protein Homologous to Histone Acetyltransferase
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Categories: Large Structures | Mus musculus | Inoue M | Kigawa T | Koshiba S | Li H | Saito K | Yokoyama S