|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Solution structure of the CS domain of human USP19== | | ==Solution structure of the CS domain of human USP19== |
| - | <StructureSection load='1wh0' size='340' side='right'caption='[[1wh0]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1wh0' size='340' side='right'caption='[[1wh0]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1wh0]] 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=1WH0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WH0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1wh0]] 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=1WH0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WH0 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KAZUSA cDNA hk08201 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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='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>
| + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wh0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wh0 OCA], [https://pdbe.org/1wh0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wh0 RCSB], [https://www.ebi.ac.uk/pdbsum/1wh0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wh0 ProSAT], [https://www.topsan.org/Proteins/RSGI/1wh0 TOPSAN]</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=1wh0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wh0 OCA], [https://pdbe.org/1wh0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wh0 RCSB], [https://www.ebi.ac.uk/pdbsum/1wh0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wh0 ProSAT], [https://www.topsan.org/Proteins/RSGI/1wh0 TOPSAN]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/UBP19_HUMAN UBP19_HUMAN]] Deubiquitinating enzyme that regulates the degradation of various proteins. Deubiquitinates and prevents proteasomal degradation of RNF123 which in turn stimulates CDKN1B ubiquitin-dependent degradation thereby playing a role in cell proliferation. Involved in decreased protein synthesis in atrophying skeletal muscle. Modulates transcription of major myofibrillar proteins. Also involved in turnover of endoplasmic-reticulum-associated degradation (ERAD) substrates. Regulates the stability of BIRC2/c-IAP1 and BIRC3/c-IAP2 by preventing their ubiquitination. Required for cells to mount an appropriate response to hypoxia and rescues HIF1A from degradation in a non-catalytic manner. Plays an important role in 17 beta-estradiol (E2)-inhibited myogenesis. Decreases the levels of ubiquitinated proteins during skeletal muscle formation and acts to repress myogenesis. Exhibits a preference towards 'Lys-63'-linked Ubiquitin chains.<ref>PMID:19465887</ref> <ref>PMID:21849505</ref> <ref>PMID:22128162</ref> <ref>PMID:22689415</ref>
| + | [https://www.uniprot.org/uniprot/UBP19_HUMAN UBP19_HUMAN] Deubiquitinating enzyme that regulates the degradation of various proteins. Deubiquitinates and prevents proteasomal degradation of RNF123 which in turn stimulates CDKN1B ubiquitin-dependent degradation thereby playing a role in cell proliferation. Involved in decreased protein synthesis in atrophying skeletal muscle. Modulates transcription of major myofibrillar proteins. Also involved in turnover of endoplasmic-reticulum-associated degradation (ERAD) substrates. Regulates the stability of BIRC2/c-IAP1 and BIRC3/c-IAP2 by preventing their ubiquitination. Required for cells to mount an appropriate response to hypoxia and rescues HIF1A from degradation in a non-catalytic manner. Plays an important role in 17 beta-estradiol (E2)-inhibited myogenesis. Decreases the levels of ubiquitinated proteins during skeletal muscle formation and acts to repress myogenesis. Exhibits a preference towards 'Lys-63'-linked Ubiquitin chains.<ref>PMID:19465887</ref> <ref>PMID:21849505</ref> <ref>PMID:22128162</ref> <ref>PMID:22689415</ref> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ubiquitin thiolesterase]]
| + | [[Category: Inoue M]] |
| - | [[Category: Inoue, M]] | + | [[Category: Kigawa T]] |
| - | [[Category: Kigawa, T]] | + | [[Category: Koshiba S]] |
| - | [[Category: Koshiba, S]] | + | [[Category: Nakanishi T]] |
| - | [[Category: Nakanishi, T]] | + | [[Category: Tochio N]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Yokoyama S]] |
| - | [[Category: Tochio, N]] | + | |
| - | [[Category: Yokoyama, S]] | + | |
| - | [[Category: Cs domain]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Rsgi]]
| + | |
| - | [[Category: Usp]]
| + | |
| Structural highlights
Function
UBP19_HUMAN Deubiquitinating enzyme that regulates the degradation of various proteins. Deubiquitinates and prevents proteasomal degradation of RNF123 which in turn stimulates CDKN1B ubiquitin-dependent degradation thereby playing a role in cell proliferation. Involved in decreased protein synthesis in atrophying skeletal muscle. Modulates transcription of major myofibrillar proteins. Also involved in turnover of endoplasmic-reticulum-associated degradation (ERAD) substrates. Regulates the stability of BIRC2/c-IAP1 and BIRC3/c-IAP2 by preventing their ubiquitination. Required for cells to mount an appropriate response to hypoxia and rescues HIF1A from degradation in a non-catalytic manner. Plays an important role in 17 beta-estradiol (E2)-inhibited myogenesis. Decreases the levels of ubiquitinated proteins during skeletal muscle formation and acts to repress myogenesis. Exhibits a preference towards 'Lys-63'-linked Ubiquitin chains.[1] [2] [3] [4]
References
- ↑ Hassink GC, Zhao B, Sompallae R, Altun M, Gastaldello S, Zinin NV, Masucci MG, Lindsten K. The ER-resident ubiquitin-specific protease 19 participates in the UPR and rescues ERAD substrates. EMBO Rep. 2009 Jul;10(7):755-61. Epub 2009 May 22. PMID:19465887 doi:http://dx.doi.org/embor200969
- ↑ Mei Y, Hahn AA, Hu S, Yang X. The USP19 deubiquitinase regulates the stability of c-IAP1 and c-IAP2. J Biol Chem. 2011 Oct 14;286(41):35380-7. doi: 10.1074/jbc.M111.282020. Epub 2011, Aug 17. PMID:21849505 doi:http://dx.doi.org/10.1074/jbc.M111.282020
- ↑ Altun M, Zhao B, Velasco K, Liu H, Hassink G, Paschke J, Pereira T, Lindsten K. Ubiquitin-specific protease 19 (USP19) regulates hypoxia-inducible factor 1alpha (HIF-1alpha) during hypoxia. J Biol Chem. 2012 Jan 13;287(3):1962-9. doi: 10.1074/jbc.M111.305615. Epub 2011, Nov 29. PMID:22128162 doi:http://dx.doi.org/10.1074/jbc.M111.305615
- ↑ Iphofer A, Kummer A, Nimtz M, Ritter A, Arnold T, Frank R, van den Heuvel J, Kessler BM, Jansch L, Franke R. Profiling ubiquitin linkage specificities of deubiquitinating enzymes with branched ubiquitin isopeptide probes. Chembiochem. 2012 Jul 9;13(10):1416-20. doi: 10.1002/cbic.201200261. Epub 2012, Jun 11. PMID:22689415 doi:10.1002/cbic.201200261
|
