3shq

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Current revision (09:50, 1 March 2024) (edit) (undo)
 
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<StructureSection load='3shq' size='340' side='right'caption='[[3shq]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
<StructureSection load='3shq' size='340' side='right'caption='[[3shq]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3shq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SHQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SHQ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3shq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SHQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SHQ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.96&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CG6697, Dmel_CG6697, UBLCP1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3shq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3shq OCA], [https://pdbe.org/3shq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3shq RCSB], [https://www.ebi.ac.uk/pdbsum/3shq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3shq ProSAT]</span></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=3shq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3shq OCA], [https://pdbe.org/3shq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3shq RCSB], [https://www.ebi.ac.uk/pdbsum/3shq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3shq ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q9XZ16_DROME Q9XZ16_DROME]
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Protein degradation by the 26S proteasome is a fundamental process involved in a broad range of cellular activities, yet how proteasome activity is regulated remains poorly understood. We report here that ubiquitin-like domain-containing C-terminal domain phosphatase 1 (UBLCP1) is a 26S proteasome phosphatase that regulates nuclear proteasome activity. UBLCP1 directly interacts with the proteasome via its UBL domain and is exclusively localized in the nucleus. UBLCP1 dephosphorylates the 26S proteasome and inhibits proteasome activity in vitro. Knockdown of UBLCP1 in cells promotes 26S proteasome assembly and selectively enhances nuclear proteasome activity. Our results describe the first identified proteasome-specific phosphatase and uncover a unique mechanism for phosphoregulation of the proteasome.
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UBLCP1 is a 26S proteasome phosphatase that regulates nuclear proteasome activity.,Guo X, Engel JL, Xiao J, Tagliabracci VS, Wang X, Huang L, Dixon JE Proc Natl Acad Sci U S A. 2011 Sep 26. PMID:21949367<ref>PMID:21949367</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3shq" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Drome]]
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[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Phosphoprotein phosphatase]]
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[[Category: Engel JL]]
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[[Category: Engel, J L]]
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[[Category: Xiao J]]
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[[Category: Xiao, J]]
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[[Category: Hydrolase]]
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[[Category: Phosphatase]]
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Current revision

Crystal Structure of UBLCP1

PDB ID 3shq

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OCA

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