3shq

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[[Image:3shq.png|left|200px]]
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==Crystal Structure of UBLCP1==
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<StructureSection load='3shq' size='340' side='right' caption='[[3shq]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3shq]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SHQ FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CG6697, Dmel_CG6697, UBLCP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster])</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3shq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3shq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3shq RCSB], [http://www.ebi.ac.uk/pdbsum/3shq PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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The line below this paragraph, containing "STRUCTURE_3shq", creates the "Structure Box" on the page.
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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or leave the SCENE parameter empty for the default display.
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{{STRUCTURE_3shq| PDB=3shq | SCENE= }}
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===Crystal Structure of UBLCP1===
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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The line below this paragraph, {{ABSTRACT_PUBMED_21949367}}, adds the Publication Abstract to the page
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__TOC__
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(as it appears on PubMed at http://www.pubmed.gov), where 21949367 is the PubMed ID number.
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</StructureSection>
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{{ABSTRACT_PUBMED_21949367}}
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==About this Structure==
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[[3shq]] is a 1 chain structure with sequence from [http://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].
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==Reference==
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<ref group="xtra">PMID:021949367</ref><references group="xtra"/>
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[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
[[Category: Phosphoprotein phosphatase]]
[[Category: Phosphoprotein phosphatase]]

Revision as of 05:24, 5 June 2014

Crystal Structure of UBLCP1

3shq, resolution 1.96Å

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