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==Solution structure of the PH domain of PIP2-dependent ARF1 GTPase-activating protein from human== | ==Solution structure of the PH domain of PIP2-dependent ARF1 GTPase-activating protein from human== | ||
<StructureSection load='2da0' size='340' side='right' caption='[[2da0 | <StructureSection load='2da0' size='340' side='right'caption='[[2da0]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2da0]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2da0]] 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=2DA0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DA0 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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2da0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2da0 OCA], [https://pdbe.org/2da0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2da0 RCSB], [https://www.ebi.ac.uk/pdbsum/2da0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2da0 ProSAT], [https://www.topsan.org/Proteins/RSGI/2da0 TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/ASAP1_HUMAN ASAP1_HUMAN] Possesses phosphatidylinositol 4,5-bisphosphate-dependent GTPase-activating protein activity for ARF1 (ADP ribosylation factor 1) and ARF5 and a lesser activity towards ARF6. May coordinate membrane trafficking with cell growth or actin cytoskeleton remodeling by binding to both SRC and PIP2. May function as a signal transduction protein involved in the differentiation of fibroblasts into adipocytes and possibly other cell types (By similarity). Plays a role in ciliogenesis.<ref>PMID:20393563</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Inoue | [[Category: Large Structures]] | ||
[[Category: Kigawa | [[Category: Inoue M]] | ||
[[Category: Koshiba | [[Category: Kigawa T]] | ||
[[Category: Li | [[Category: Koshiba S]] | ||
[[Category: Li H]] | |||
[[Category: Tomizawa | [[Category: Tomizawa T]] | ||
[[Category: Yokoyama | [[Category: Yokoyama S]] | ||
Latest revision as of 14:36, 22 May 2024
Solution structure of the PH domain of PIP2-dependent ARF1 GTPase-activating protein from humanSolution structure of the PH domain of PIP2-dependent ARF1 GTPase-activating protein from human
Structural highlights
FunctionASAP1_HUMAN Possesses phosphatidylinositol 4,5-bisphosphate-dependent GTPase-activating protein activity for ARF1 (ADP ribosylation factor 1) and ARF5 and a lesser activity towards ARF6. May coordinate membrane trafficking with cell growth or actin cytoskeleton remodeling by binding to both SRC and PIP2. May function as a signal transduction protein involved in the differentiation of fibroblasts into adipocytes and possibly other cell types (By similarity). Plays a role in ciliogenesis.[1] Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. References
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