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3lmn
From Proteopedia
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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=3lmn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lmn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lmn RCSB], [http://www.ebi.ac.uk/pdbsum/3lmn PDBsum]</span></td></tr> | <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=3lmn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lmn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lmn RCSB], [http://www.ebi.ac.uk/pdbsum/3lmn PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[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> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Thioesterase|Thioesterase]] | *[[Thioesterase|Thioesterase]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 19:58, 25 December 2014
Oligomeric structure of the DUSP domain of human USP15
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Categories: Homo sapiens | Ubiquitin thiolesterase | Alenkin, D | Arrowsmith, C H | Asinas, A | Avvakumov, G V | Bochkarev, A | Bountra, C | Dhe-Paganon, S | Edwards, A M | Walker, J R | Weigelt, J | Cleavage | Deubiquitinating enzyme | Deubiquitylation | Domain-swapping | Dub | Dub15 | Dusp | Endopeptidase | Hydrolase | Phosphoprotein | Protease | Thiol protease | Thiolesterase | Ubiquitin | Ubiquitin carboxyterminal hydrolase | Ubiquitin specific protease | Ubl conjugation pathway | Ubp15 | Uch | Usp | Usp15
