3pv1

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3pv1]] is a 2 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=3PV1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PV1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3pv1]] is a 2 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=3PV1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PV1 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene><br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">USP15, KIAA0529 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">USP15, KIAA0529 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
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<tr><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'>[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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3pv1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pv1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pv1 RCSB], [http://www.ebi.ac.uk/pdbsum/3pv1 PDBsum]</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=3pv1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pv1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pv1 RCSB], [http://www.ebi.ac.uk/pdbsum/3pv1 PDBsum]</span></td></tr>
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<table>
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</table>
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== 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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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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Structural variability of the ubiquitin specific protease DUSP-UBL double domains.,Elliott PR, Liu H, Pastok MW, Grossmann GJ, Rigden DJ, Clague MJ, Urbe S, Barsukov IL FEBS Lett. 2011 Nov 4;585(21):3385-90. Epub 2011 Oct 10. PMID:22001210<ref>PMID:22001210</ref>
Structural variability of the ubiquitin specific protease DUSP-UBL double domains.,Elliott PR, Liu H, Pastok MW, Grossmann GJ, Rigden DJ, Clague MJ, Urbe S, Barsukov IL FEBS Lett. 2011 Nov 4;585(21):3385-90. Epub 2011 Oct 10. PMID:22001210<ref>PMID:22001210</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Ubiquitinyl hydrolase 1]]
[[Category: Ubiquitinyl hydrolase 1]]
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[[Category: Barsukov, I L.]]
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[[Category: Barsukov, I L]]
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[[Category: Clague, M J.]]
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[[Category: Clague, M J]]
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[[Category: Elliott, P R.]]
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[[Category: Elliott, P R]]
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[[Category: Urbe, S.]]
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[[Category: Urbe, S]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]

Revision as of 15:00, 24 December 2014

Crystal structure of the USP15 DUSP-UBL domains

3pv1, resolution 2.60Å

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