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3ppa

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==Structure of the Dusp-Ubl domains of Usp15==
==Structure of the Dusp-Ubl domains of Usp15==
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<StructureSection load='3ppa' size='340' side='right' caption='[[3ppa]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
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<StructureSection load='3ppa' size='340' side='right'caption='[[3ppa]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ppa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PPA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PPA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3ppa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PPA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PPA FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1w6v|1w6v]], [[3lmn|3lmn]]</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1w6v|1w6v]], [[3lmn|3lmn]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KIAA0529, USP15 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KIAA0529, USP15 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<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>
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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/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>
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<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=3ppa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ppa OCA], [http://pdbe.org/3ppa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ppa RCSB], [http://www.ebi.ac.uk/pdbsum/3ppa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ppa ProSAT]</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=3ppa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ppa OCA], [https://pdbe.org/3ppa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ppa RCSB], [https://www.ebi.ac.uk/pdbsum/3ppa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ppa ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/UBP15_HUMAN UBP15_HUMAN]] Hydrolase that removes conjugated ubiquitin from target proteins and regulates various pathways such as the TGF-beta receptor signaling and NF-kappa-B pathways. Acts as a key regulator of TGF-beta receptor signaling pathway, but the precise mechanism is still unclear: according to a report, acts by promoting deubiquitination of monoubiquitinated R-SMADs (SMAD1, SMAD2 and/or SMAD3), thereby alleviating inhibition of R-SMADs and promoting activation of TGF-beta target genes (PubMed:21947082). According to another reports, regulates the TGF-beta receptor signaling pathway by mediating deubiquitination and stabilization of TGFBR1, leading to an enhanced TGF-beta signal (PubMed:22344298). Able to mediate deubiquitination of monoubiquitinated substrates as well as 'Lys-48'-linked polyubiquitin chains, protecting them against proteasomal degradation. Acts as an associated component of COP9 signalosome complex (CSN) and regulates different pathways via this association: regulates NF-kappa-B by mediating deubiquitination of NFKBIA and deubiquitinates substrates bound to VCP. Protects APC and human papillomavirus type 16 protein E6 against degradation via the ubiquitin proteasome pathway.<ref>PMID:16005295</ref> <ref>PMID:17318178</ref> <ref>PMID:19826004</ref> <ref>PMID:19576224</ref> <ref>PMID:19553310</ref> <ref>PMID:21947082</ref> <ref>PMID:22344298</ref>
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[[https://www.uniprot.org/uniprot/UBP15_HUMAN UBP15_HUMAN]] Hydrolase that removes conjugated ubiquitin from target proteins and regulates various pathways such as the TGF-beta receptor signaling and NF-kappa-B pathways. Acts as a key regulator of TGF-beta receptor signaling pathway, but the precise mechanism is still unclear: according to a report, acts by promoting deubiquitination of monoubiquitinated R-SMADs (SMAD1, SMAD2 and/or SMAD3), thereby alleviating inhibition of R-SMADs and promoting activation of TGF-beta target genes (PubMed:21947082). According to another reports, regulates the TGF-beta receptor signaling pathway by mediating deubiquitination and stabilization of TGFBR1, leading to an enhanced TGF-beta signal (PubMed:22344298). Able to mediate deubiquitination of monoubiquitinated substrates as well as 'Lys-48'-linked polyubiquitin chains, protecting them against proteasomal degradation. Acts as an associated component of COP9 signalosome complex (CSN) and regulates different pathways via this association: regulates NF-kappa-B by mediating deubiquitination of NFKBIA and deubiquitinates substrates bound to VCP. Protects APC and human papillomavirus type 16 protein E6 against degradation via the ubiquitin proteasome pathway.<ref>PMID:16005295</ref> <ref>PMID:17318178</ref> <ref>PMID:19826004</ref> <ref>PMID:19576224</ref> <ref>PMID:19553310</ref> <ref>PMID:21947082</ref> <ref>PMID:22344298</ref>
==See Also==
==See Also==
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*[[Thioesterase|Thioesterase]]
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*[[Thioesterase 3D structures|Thioesterase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Ubiquitinyl hydrolase 1]]
[[Category: Ubiquitinyl hydrolase 1]]
[[Category: Arrowsmith, C H]]
[[Category: Arrowsmith, C H]]
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[[Category: Dong, A]]
[[Category: Dong, A]]
[[Category: Edwards, A M]]
[[Category: Edwards, A M]]
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[[Category: Structural genomic]]
[[Category: Walker, J R]]
[[Category: Walker, J R]]
[[Category: Weigelt, J]]
[[Category: Weigelt, J]]

Revision as of 08:49, 25 May 2022

Structure of the Dusp-Ubl domains of Usp15

PDB ID 3ppa

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