2do6
From Proteopedia
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- | [[Image:2do6.jpg|left|200px]] | ||
- | + | ==Solution structure of RSGI RUH-065, a UBA domain from human cDNA== | |
- | + | <StructureSection load='2do6' size='340' side='right'caption='[[2do6]]' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[2do6]] is a 2 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=2DO6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DO6 FirstGlance]. <br> | |
- | | | + | </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=2do6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2do6 OCA], [https://pdbe.org/2do6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2do6 RCSB], [https://www.ebi.ac.uk/pdbsum/2do6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2do6 ProSAT], [https://www.topsan.org/Proteins/RSGI/2do6 TOPSAN]</span></td></tr> | |
- | + | </table> | |
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/CBLB_HUMAN CBLB_HUMAN] E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome. Negatively regulates TCR (T-cell receptor), BCR (B-cell receptor) and FCER1 (high affinity immunoglobulin epsilon receptor) signal transduction pathways. In naive T-cells, inhibits VAV1 activation upon TCR engagement and imposes a requirement for CD28 costimulation for proliferation and IL-2 production. Also acts by promoting PIK3R1/p85 ubiquitination, which impairs its recruitment to the TCR and subsequent activation. In activated T-cells, inhibits PLCG1 activation and calcium mobilization upon restimulation and promotes anergy. In B-cells, acts by ubiquitinating SYK and promoting its proteasomal degradation. May also be involved in EGFR ubiquitination and internalization.<ref>PMID:10022120</ref> <ref>PMID:10086340</ref> <ref>PMID:11087752</ref> <ref>PMID:11526404</ref> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/do/2do6_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2do6 ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
- | + | ==See Also== | |
- | + | *[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]] | |
- | + | == References == | |
- | == | + | <references/> |
- | + | __TOC__ | |
+ | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: Guntert | + | [[Category: Guntert P]] |
- | [[Category: Hamada | + | [[Category: Hamada T]] |
- | [[Category: Hirota | + | [[Category: Hirota H]] |
- | [[Category: Kigawa | + | [[Category: Kigawa T]] |
- | [[Category: Koshiba | + | [[Category: Koshiba S]] |
- | [[Category: Lin | + | [[Category: Lin Y-J]] |
- | + | [[Category: Sato M]] | |
- | [[Category: Sato | + | [[Category: Yokoyama S]] |
- | [[Category: Yokoyama | + | |
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Current revision
Solution structure of RSGI RUH-065, a UBA domain from human cDNA
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Categories: Homo sapiens | Large Structures | Guntert P | Hamada T | Hirota H | Kigawa T | Koshiba S | Lin Y-J | Sato M | Yokoyama S