5k1c: Difference between revisions

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 ==Crystal structure of the UAF1/WDR20/USP12 complex==
-<StructureSection load='5k1c' size='340' side='right' caption='[[5k1c]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
+<StructureSection load='5k1c' size='340' side='right'caption='[[5k1c]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5k1c]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K1C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K1C FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5k1c]] 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=5K1C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K1C 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>, <scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</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]] 3&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5k1a|5k1a]], [[5k1b|5k1b]], [[5k19|5k19]], [[5k16|5k16]]</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>, <scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.12 3.4.19.12] </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=5k1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k1c OCA], [https://pdbe.org/5k1c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k1c RCSB], [https://www.ebi.ac.uk/pdbsum/5k1c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k1c ProSAT]</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=5k1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k1c OCA], [http://pdbe.org/5k1c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k1c RCSB], [http://www.ebi.ac.uk/pdbsum/5k1c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k1c ProSAT]</span></td></tr>
 </table>
-== Disease ==
-[[http://www.uniprot.org/uniprot/WDR48_HUMAN WDR48_HUMAN]] Autosomal recessive spastic paraplegia type 60.
 == Function ==
-[[http://www.uniprot.org/uniprot/UBP12_HUMAN UBP12_HUMAN]] Deubiquitinating enzyme. Has almost no deubiquitinating activity by itself and requires the interaction with WDR48 to have a high activity. Not involved in deubiquitination of monoubiquitinated FANCD2.<ref>PMID:19075014</ref>  [[http://www.uniprot.org/uniprot/WDR48_HUMAN WDR48_HUMAN]] Regulator of deubiquitinating complexes. Acts as a strong activator of USP1 by enhancing the USP1-mediated deubiquitination of FANCD2; USP1 being almost inactive by itself. Also activates deubiquitinating activity of complexes containing USP12 and USP46, respectively. Activates deubiquitination by increasing the catalytic turnover without increasing the affinity of deubiquitinating enzymes for the substrate. In case of infection by Herpesvirus saimiri, may play a role in vesicular transport or membrane fusion events necessary for transport to lysosomes. Induces lysosomal vesicle formation via interaction with Herpesvirus saimiri tyrosine kinase-interacting protein (TIP). Subsequently, TIP recruits tyrosine-protein kinase LCK, resulting in down-regulation of T-cell antigen receptor TCR. May play a role in generation of enlarged endosomal vesicles via interaction with TIP. In case of infection by papillomavirus HPV11, promotes the maintenance of the viral genome via its interaction with HPV11 helicase E1.<ref>PMID:12196293</ref> <ref>PMID:18082604</ref> <ref>PMID:19075014</ref>
+[https://www.uniprot.org/uniprot/UBP12_HUMAN UBP12_HUMAN] Deubiquitinating enzyme. Has almost no deubiquitinating activity by itself and requires the interaction with WDR48 to have a high activity. Not involved in deubiquitination of monoubiquitinated FANCD2.<ref>PMID:19075014</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
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 </div>
 <div class="pdbe-citations 5k1c" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Thioesterase 3D structures|Thioesterase 3D structures]]
+*[[WD-repeat protein 3D structures|WD-repeat protein 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Ubiquitinyl hydrolase 1]]
+[[Category: Homo sapiens]]
-[[Category: Andrea, A D.D]]
+[[Category: Large Structures]]
-[[Category: Li, H]]
+[[Category: D'Andrea AD]]
-[[Category: Zheng, N]]
+[[Category: Li H]]
-[[Category: Deubiquitinating enzyme]]
+[[Category: Zheng N]]
-[[Category: Hydrolase]]
-[[Category: Uaf1]]
-[[Category: Ubiquitin-specific protease]]
-[[Category: Usp1-associated factor 1]]
-[[Category: Usp12]]
-[[Category: Wd40 repeat domain]]
-[[Category: Wdr20]]
-[[Category: Wdr48]]