Rab GTPase family 9 (Rab9). Rab9 is found in late endosomes, together with mannose 6-phosphate receptors (MPRs) and the tail-interacting protein of 47 kD (TIP47). Rab9 is a key mediator of vesicular transport from late endosomes to the trans-Golgi network (TGN) by redirecting the MPRs. Rab9 has been identified as a key component for the replication of several viruses, including HIV1, Ebola, Marburg, and measles, making it a potential target for inhibiting a variety of viruses. 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. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.
No pairwise interactions are available for this conserved domain.
Total Mutations Found: 122 Total Disease Mutations Found: 71 This domain occurred 109 times on human genes (195 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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