3dwd
From Proteopedia
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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=3dwd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dwd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3dwd RCSB], [http://www.ebi.ac.uk/pdbsum/3dwd PDBsum]</span></td></tr> | <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=3dwd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dwd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3dwd RCSB], [http://www.ebi.ac.uk/pdbsum/3dwd PDBsum]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/ARFG1_HUMAN ARFG1_HUMAN]] GTPase-activating protein (GAP) for the ADP ribosylation factor 1 (ARF1). Involved in membrane trafficking and /or vesicle transport. Promotes hydrolysis of the ARF1-bound GTP and thus, is required for the dissociation of coat proteins from Golgi-derived membranes and vesicles, a prerequisite for vesicle's fusion with target compartment. Probably regulates ARF1-mediated transport via its interaction with the KDELR proteins and TMED2. Overexpression induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, as when ARF1 is deactivated. Its activity is stimulated by phosphoinosides and inhibited by phosphatidylcholine (By similarity). | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] |
Revision as of 18:38, 25 December 2014
Crystal structure of the ArfGAP domain of human ARFGAP1
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Categories: Homo sapiens | Arrowsmith, C H | Bochkarev, A | Bountra, C | Edwards, A M | Landry, R | Nedyalkova, L | Park, H | Structural genomic | Tempel, W | Tong, Y | Wilkstrom, M | Er-golgi transport | Gap | Golgi apparatus | Gtpase activating protein | Gtpase activation | Metal-binding | Phosphoprotein | Protein transport | Transport | Transport protein | Zinc-finger