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==Solution structure of the DUSP domain of hUSP15==
==Solution structure of the DUSP domain of hUSP15==
<StructureSection load='1w6v' size='340' side='right'caption='[[1w6v]], [[NMR_Ensembles_of_Models | 13 NMR models]]' scene=''>
<StructureSection load='1w6v' size='340' side='right'caption='[[1w6v]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1w6v]] 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=1W6V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W6V FirstGlance]. <br>
<table><tr><td colspan='2'>[[1w6v]] 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=1W6V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W6V FirstGlance]. <br>
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ubiquitin_thiolesterase Ubiquitin thiolesterase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.15 3.1.2.15] </span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1w6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w6v OCA], [https://pdbe.org/1w6v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w6v RCSB], [https://www.ebi.ac.uk/pdbsum/1w6v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w6v ProSAT]</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=1w6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w6v OCA], [https://pdbe.org/1w6v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w6v RCSB], [https://www.ebi.ac.uk/pdbsum/1w6v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w6v ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[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>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Ubiquitin thiolesterase]]
[[Category: Ab E]]
[[Category: Ab, E]]
[[Category: Daniels M]]
[[Category: Daniels, M]]
[[Category: De Jong RD]]
[[Category: Diercks, T]]
[[Category: Diercks T]]
[[Category: Folkers, G E]]
[[Category: Folkers GE]]
[[Category: Jong, R D.De]]
[[Category: Kaptein R]]
[[Category: Kaptein, R]]
[[Category: Truffault V]]
[[Category: Truffault, V]]
[[Category: Cleavage]]
[[Category: Deubiquitinating enzyme]]
[[Category: Deubiquitylation]]
[[Category: Dub]]
[[Category: Dub15]]
[[Category: Dusp]]
[[Category: Endopeptidase]]
[[Category: Hydrolase]]
[[Category: Spine]]
[[Category: Structural genomic]]
[[Category: Structural proteomics in europe]]
[[Category: Thiolesterase]]
[[Category: Ubiquitin]]
[[Category: Ubiquitin carboxyterminal hydrolase]]
[[Category: Ubiquitin specific protease]]
[[Category: Ubp15]]
[[Category: Uch]]
[[Category: Usp]]
[[Category: Usp15]]
Retrieved from "https://proteopedia.org/1w6v"