2d89
From Proteopedia
(Difference between revisions)
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==Solution structure of the CH domain from human EH domain binding protein 1== | ==Solution structure of the CH domain from human EH domain binding protein 1== | ||
- | <StructureSection load='2d89' size='340' side='right'caption='[[2d89 | + | <StructureSection load='2d89' size='340' side='right'caption='[[2d89]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2d89]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2d89]] 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=2D89 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D89 FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </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=2d89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d89 OCA], [https://pdbe.org/2d89 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d89 RCSB], [https://www.ebi.ac.uk/pdbsum/2d89 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d89 ProSAT], [https://www.topsan.org/Proteins/RSGI/2d89 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=2d89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d89 OCA], [https://pdbe.org/2d89 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d89 RCSB], [https://www.ebi.ac.uk/pdbsum/2d89 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d89 ProSAT], [https://www.topsan.org/Proteins/RSGI/2d89 TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
+ | == Disease == | ||
+ | [https://www.uniprot.org/uniprot/EHBP1_HUMAN EHBP1_HUMAN] Disease susceptibility is associated with variants affecting the gene represented in this entry. | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/EHBP1_HUMAN EHBP1_HUMAN] May play a role in actin reorganization. Links clathrin-mediated endocytosis to the actin cytoskeleton. May act as Rab effector protein and play a role in vesicle trafficking (PubMed:14676205, PubMed:27552051). Required for perinuclear sorting and insulin-regulated recycling of SLC2A4/GLUT4 in adipocytes (By similarity).[UniProtKB:Q69ZW3]<ref>PMID:14676205</ref> <ref>PMID:27552051</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=2d89 ConSurf]. | </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=2d89 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Inoue | + | [[Category: Inoue M]] |
- | [[Category: Kigawa | + | [[Category: Kigawa T]] |
- | [[Category: Koshiba | + | [[Category: Koshiba S]] |
- | + | [[Category: Tomizawa T]] | |
- | [[Category: Tomizawa | + | [[Category: Yokoyama S]] |
- | [[Category: Yokoyama | + | |
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Current revision
Solution structure of the CH domain from human EH domain binding protein 1
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