page_title: EVI5L
section_title: Post-Translational Modifications
hierarchical_section_title: EVI5L / Protein / Post-Translational Modifications
caption_attribution_description: English: Highly conserved regions of RAB-GAP1L correspond to the RAB-GAP TBC domain in EVI5L. The conserved regions are next to each other, and form a pocket for possible interactions with RAB2A and RAB10. There are no beta-sheets present, just alpha helices.
context_page_description: EVI5L is a protein that in humans is encoded by the EVI5L gene. EVI5L is a member of the Ras superfamily of monomeric guanine nucleotide-binding proteins, and functions as a GTPase-activating protein with a broad specificity. Measurement of in vitro Rab-GAP activity has shown that EVI5L has significant Rab2A- and Rab10-GAP activity.
context_section_description: Post translational modifications of EVI5L that are evolutionarily conserved in majority of the orthologs include glycosylation (C-mannosylation), glycation, phosphorylation (non-kinase and kinase specific), and sumoylation. There is also one leucine-rich nuclear export signal.
caption: Highly conserved regions of RAB-GAP1L correspond to the RAB-GAP TBC domain in EVI5L. The conserved regions are next to each other, and form a pocket for possible interactions with RAB2A and RAB10. There are no beta-sheets present, just alpha helices.
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