2lbc: Difference between revisions

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==solution structure of tandem UBA of USP13==
==solution structure of tandem UBA of USP13==
<StructureSection load='2lbc' size='340' side='right'caption='[[2lbc]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''>
<StructureSection load='2lbc' size='340' side='right'caption='[[2lbc]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2lbc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LBC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LBC FirstGlance]. <br>
<table><tr><td colspan='2'>[[2lbc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LBC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LBC FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">USP13, ISOT3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
</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=2lbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lbc OCA], [https://pdbe.org/2lbc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lbc RCSB], [https://www.ebi.ac.uk/pdbsum/2lbc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lbc ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1], with EC number [https://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=2lbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lbc OCA], [https://pdbe.org/2lbc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lbc RCSB], [https://www.ebi.ac.uk/pdbsum/2lbc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lbc ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/UBP13_HUMAN UBP13_HUMAN]] Deubiquitinase that mediates deubiquitination of target proteins such as BECN1, MITF, SKP2 and USP10 and is involved in various processes such as autophagy and endoplasmic reticulum-associated degradation (ERAD). Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes. Also deubiquitinates USP10, an essential regulator of p53/TP53 stability. In turn, PIK3C3/VPS34-containing complexes regulate USP13 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13. Recruited by nuclear UFD1 and mediates deubiquitination of SKP2, thereby regulating endoplasmic reticulum-associated degradation (ERAD). Mediates stabilization of SIAH2 independently of deubiquitinase activity: binds ubiquitinated SIAH2 and acts by impairing SIAH2 autoubiquitination. Has a weak deubiquitinase activity in vitro and preferentially cleaves 'Lys-63'-linked polyubiquitin chains. In contrast to USP5, it is not able to mediate unanchored polyubiquitin disassembly. Able to cleave ISG15 in vitro; however, additional experiments are required to confirm such data.<ref>PMID:17653289</ref> <ref>PMID:21962518</ref> <ref>PMID:21659512</ref> <ref>PMID:21811243</ref> <ref>PMID:21571647</ref> <ref>PMID:22216260</ref>
[https://www.uniprot.org/uniprot/UBP13_HUMAN UBP13_HUMAN] Deubiquitinase that mediates deubiquitination of target proteins such as BECN1, MITF, SKP2 and USP10 and is involved in various processes such as autophagy and endoplasmic reticulum-associated degradation (ERAD). Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes. Also deubiquitinates USP10, an essential regulator of p53/TP53 stability. In turn, PIK3C3/VPS34-containing complexes regulate USP13 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13. Recruited by nuclear UFD1 and mediates deubiquitination of SKP2, thereby regulating endoplasmic reticulum-associated degradation (ERAD). Mediates stabilization of SIAH2 independently of deubiquitinase activity: binds ubiquitinated SIAH2 and acts by impairing SIAH2 autoubiquitination. Has a weak deubiquitinase activity in vitro and preferentially cleaves 'Lys-63'-linked polyubiquitin chains. In contrast to USP5, it is not able to mediate unanchored polyubiquitin disassembly. Able to cleave ISG15 in vitro; however, additional experiments are required to confirm such data.<ref>PMID:17653289</ref> <ref>PMID:21962518</ref> <ref>PMID:21659512</ref> <ref>PMID:21811243</ref> <ref>PMID:21571647</ref> <ref>PMID:22216260</ref>  
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Ubiquitinyl hydrolase 1]]
[[Category: Hu H]]
[[Category: Hu, H]]
[[Category: Song A]]
[[Category: Song, A]]
[[Category: Zhang Y]]
[[Category: Zhang, Y]]
[[Category: Zhou C]]
[[Category: Zhou, C]]
[[Category: Zhou Z]]
[[Category: Zhou, Z]]
[[Category: Hydrolase]]
[[Category: Tandem uba of usp13]]