3ppa

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{{STRUCTURE_3ppa| PDB=3ppa | SCENE= }}
 
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===Structure of the Dusp-Ubl domains of Usp15===
 
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==Function==
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==Structure of the Dusp-Ubl domains of Usp15==
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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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<StructureSection load='3ppa' size='340' side='right'caption='[[3ppa]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3ppa]] is a 1 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=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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35&#8491;</td></tr>
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<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='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>
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</table>
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== Function ==
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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>
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==About this Structure==
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==See Also==
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[[3ppa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PPA OCA].
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*[[Thioesterase 3D structures|Thioesterase 3D structures]]
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== References ==
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==Reference==
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<references/>
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<references group="xtra"/><references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Ubiquitinyl hydrolase 1]]
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[[Category: Large Structures]]
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[[Category: Arrowsmith, C H.]]
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[[Category: Arrowsmith CH]]
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[[Category: Asinas, A E.]]
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[[Category: Asinas AE]]
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[[Category: Bountra, C.]]
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[[Category: Bountra C]]
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[[Category: Dhe-Paganon, S.]]
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[[Category: Dhe-Paganon S]]
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[[Category: Dong, A.]]
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[[Category: Dong A]]
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[[Category: Edwards, A M.]]
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[[Category: Edwards AM]]
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[[Category: Walker, J R.]]
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[[Category: Walker JR]]
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[[Category: Weigelt, J.]]
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[[Category: Weigelt J]]
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[[Category: Cleavage]]
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[[Category: Deubiquitinating enzyme]]
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[[Category: Deubiquitylation]]
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[[Category: Domain-swapping]]
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[[Category: Dub]]
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[[Category: Dub15]]
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[[Category: Dusp]]
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[[Category: Endopeptidase]]
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[[Category: Hydrolase]]
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[[Category: Phosphoprotein]]
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[[Category: Protease]]
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[[Category: Thiol protease]]
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[[Category: Thiolesterase]]
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[[Category: Ubiquitin]]
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[[Category: Ubiquitin carboxyterminal hydrolase]]
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[[Category: Ubiquitin specific protease]]
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[[Category: Ubl conjugation pathway]]
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[[Category: Ubp15]]
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[[Category: Uch]]
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[[Category: Usp]]
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[[Category: Usp15]]
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Current revision

Structure of the Dusp-Ubl domains of Usp15

PDB ID 3ppa

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