Rab GTPase family 26 (Rab26). Rab26 subfamily. First identified in rat pancreatic acinar cells, Rab26 is believed to play a role in recruiting mature granules to the plasma membrane upon beta-adrenergic stimulation. Rab26 belongs to the Rab functional group III, which are considered key regulators of intracellular vesicle transport during exocytosis. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins.
No pairwise interactions are available for this conserved domain.
Total Mutations Found: 127 Total Disease Mutations Found: 76 This domain occurred 99 times on human genes (176 proteins).
If you've navigated here from a protein, hovering over a position on the weblogo will display the corresponding protein position for that domain position.
The histograms below the weblogo indicate mutations found on the domain. Red is for disease (OMIM) and blue is for SNPs.
Functional Features are displayed as orange boxes under the histograms. You can choose which features are displayed in the box below.
Range on the Protein:
Protein ID Protein Position
Domain Position:
Feature Name:
Total Found:
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