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4h9q

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Revision as of 08:06, 3 November 2022

Complex structure 4 of DAXX(E225A)/H3.3(sub5)/H4

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Retrieved from "http://52.214.119.220/wiki/index.php/4h9q"

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 ==Complex structure 4 of DAXX(E225A)/H3.3(sub5)/H4==
-<StructureSection load='4h9q' size='340' side='right' caption='[[4h9q]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
+<StructureSection load='4h9q' size='340' side='right'caption='[[4h9q]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4h9q]] is a 3 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=4H9Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4H9Q FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4h9q]] is a 3 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=4H9Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4H9Q FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4h9n|4h9n]], [[4h9o|4h9o]], [[4h9p|4h9p]], [[4h9r|4h9r]], [[4h9s|4h9s]]</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=4h9q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h9q OCA], [https://pdbe.org/4h9q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4h9q RCSB], [https://www.ebi.ac.uk/pdbsum/4h9q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4h9q ProSAT]</span></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">H3F3A, H3.3A, H3F3, PP781, H3F3B, H3.3B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), HIST1H4A, H4/A, H4FA, HIST1H4B, H4/I, H4FI, HIST1H4C, H4/G, H4FG, HIST1H4D, H4/B, H4FB, HIST1H4E, H4/J, H4FJ, HIST1H4F, H4/C, H4FC, HIST1H4H, H4/H, H4FH, HIST1H4I, H4/M, H4FM, HIST1H4J, H4/E, H4FE, HIST1H4K, H4/D, H4FD, HIST1H4L, H4/K, H4FK, HIST2H4A, H4/N, H4F2, H4FN, HIST2H4, HIST2H4B, H4/O, H4FO, HIST4H4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), DAXX, BING2, DAP6 ([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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4h9q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h9q OCA], [http://pdbe.org/4h9q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4h9q RCSB], [http://www.ebi.ac.uk/pdbsum/4h9q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4h9q ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/DAXX_HUMAN DAXX_HUMAN]] Transcription corepressor known to repress transcriptional potential of several sumoylated transcription factors. Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition, in association with the deubiquitinating USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage, its association with MDM2 and USP7 is disrupted, resulting in increased MDM2 autoubiquitination and consequently, MDM2 degradation, which leads to TP53 stabilization. Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Down-regulates basal and activated transcription. Seems to act as a transcriptional corepressor and inhibits PAX3 and ETS1 through direct protein-protein interaction. Modulates PAX5 activity. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively.<ref>PMID:12140263</ref> <ref>PMID:15364927</ref> <ref>PMID:17081986</ref> <ref>PMID:16845383</ref>
+[https://www.uniprot.org/uniprot/H33_HUMAN H33_HUMAN]
 ==See Also==
-*[[Death-associated protein|Death-associated protein]]
+*[[Death-associated protein 3D structures|Death-associated protein 3D structures]]
-*[[Histone|Histone]]
+*[[Histone 3D structures|Histone 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Allis, D C]]
+[[Category: Large Structures]]
-[[Category: Chin, J W]]
+[[Category: Allis DC]]
-[[Category: Elsasser, S J]]
+[[Category: Chin JW]]
-[[Category: Huang, H]]
+[[Category: Elsasser SJ]]
-[[Category: Lewis, P W]]
+[[Category: Huang H]]
-[[Category: Patel, D J]]
+[[Category: Lewis PW]]
-[[Category: Dna binding protein-apoptosis complex]]
+[[Category: Patel DJ]]
-[[Category: Histone chaperone]]

4h9q

From Proteopedia

Revision as of 08:06, 3 November 2022

Complex structure 4 of DAXX(E225A)/H3.3(sub5)/H4

Structural highlights

Function

See Also

Contents

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