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==Covalent Ubiquitin-USP2 Complex== | ==Covalent Ubiquitin-USP2 Complex== | ||
<StructureSection load='2ibi' size='340' side='right' caption='[[2ibi]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='2ibi' size='340' side='right'caption='[[2ibi]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2ibi]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2ibi]] is a 2 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=2IBI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IBI 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">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NEH:ETHANAMINE'>NEH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id=' | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ibi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ibi OCA], [https://pdbe.org/2ibi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ibi RCSB], [https://www.ebi.ac.uk/pdbsum/2ibi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ibi ProSAT]</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/UBP2_HUMAN UBP2_HUMAN] Hydrolase that deubiquitinates polyubiquitinated target proteins such as MDM2, MDM4 and CCND1. Isoform 1 and isoform 4 possess both ubiquitin-specific peptidase and isopeptidase activities. Deubiquitinates MDM2 without reversing MDM2-mediated p53/TP53 ubiquitination and thus indirectly promotes p53/TP53 degradation and limits p53 activity. Has no deubiquitinase activity against p53/TP53. Prevents MDM2-mediated degradation of MDM4. Plays a role in the G1/S cell-cycle progression in normal and cancer cells. Plays a role in the regulation of myogenic differentiation of embryonic muscle cells.<ref>PMID:17290220</ref> <ref>PMID:19917254</ref> <ref>PMID:19838211</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ib/2ibi_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ib/2ibi_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
| Line 23: | Line 22: | ||
==See Also== | ==See Also== | ||
*[[Thioesterase|Thioesterase]] | *[[Thioesterase 3D structures|Thioesterase 3D structures]] | ||
*[[ | *[[3D structures of ubiquitin|3D structures of ubiquitin]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Arrowsmith | [[Category: Arrowsmith CH]] | ||
[[Category: Avvakumov | [[Category: Avvakumov GV]] | ||
[[Category: Bernstein | [[Category: Bernstein G]] | ||
[[Category: Bochkarev | [[Category: Bochkarev A]] | ||
[[Category: Dhe-Paganon | [[Category: Dhe-Paganon S]] | ||
[[Category: Edwards | [[Category: Edwards AM]] | ||
[[Category: Finerty | [[Category: Finerty Jr PJ]] | ||
[[Category: MacKenzie | [[Category: MacKenzie F]] | ||
[[Category: Sundstrom M]] | |||
[[Category: Sundstrom | [[Category: Walker JR]] | ||
[[Category: Walker | [[Category: Weigelt J]] | ||
[[Category: Weigelt | [[Category: Xue S]] | ||
[[Category: Xue | |||
Latest revision as of 13:08, 30 August 2023
Covalent Ubiquitin-USP2 ComplexCovalent Ubiquitin-USP2 Complex
Structural highlights
FunctionUBP2_HUMAN Hydrolase that deubiquitinates polyubiquitinated target proteins such as MDM2, MDM4 and CCND1. Isoform 1 and isoform 4 possess both ubiquitin-specific peptidase and isopeptidase activities. Deubiquitinates MDM2 without reversing MDM2-mediated p53/TP53 ubiquitination and thus indirectly promotes p53/TP53 degradation and limits p53 activity. Has no deubiquitinase activity against p53/TP53. Prevents MDM2-mediated degradation of MDM4. Plays a role in the G1/S cell-cycle progression in normal and cancer cells. Plays a role in the regulation of myogenic differentiation of embryonic muscle cells.[1] [2] [3] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See AlsoReferences
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