RHOJ is a Cdc42-related small GTPase that regulates endothelial cytoskeletal organization and vascular morphogenesis. The 153-residue human G3V4H1 product shares its first 103 residues with the 214-residue reference RHOJ but has a divergent C-terminal portion that does not preserve the complete reference nucleotide-binding architecture or prenylated tail. Its nucleotide binding, hydrolysis and membrane association are unresolved.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003924 GTPase activity | IEA GO_REF:0000120 | UNDECIDED | Summary: Full-length RHOJ/TCL hydrolyzes GTP, but G3V4H1 preserves only the first 103 reference residues before a highly divergent tail. The complete nucleotide-binding architecture is not retained. Lack of exact-product biochemical measurements prevents assigning either normal hydrolysis or an active GTPase-deficient state. Supporting Evidence: PMID:10967094 In vitro, TCL shows rapid GDP/GTP exchange and displays higher GTP dissociation and hydolysis rates than TC10. file:human/RHOJ/RHOJ-bioinformatics/RESULTS.md | Binding site: | 136–136 | 0 / 1 | 0 | |
| GO:0003925 G protein activity | IEA GO_REF:0000003 | UNDECIDED | Summary: G protein activity requires a functional guanine-nucleotide-regulated signaling protein. The short product retains the N-terminal switch/effector region but loses key C-terminal features of the reference G-domain. Its signaling competence cannot be inferred from the full-length gene. Supporting Evidence: file:human/RHOJ/RHOJ-bioinformatics/RESULTS.md | Binding site: | 136–136 | 0 / 1 | 0 | PMID:27660391 Chimeras of TCL and TC10 revealed amino acids 121-129 of TCL contributed to the differences in nucleotide loading. |
| GO:0005525 GTP binding | IEA GO_REF:0000120 | UNDECIDED | Summary: Several N-terminal nucleotide-contact residues are retained, but reference guanine-contact residue 136 is missing and a further contact at 177 is not conserved. The incomplete binding pocket makes GTP binding uncertain even though the full-length protein binds and hydrolyzes GTP. Supporting Evidence: file:human/RHOJ/RHOJ-bioinformatics/RESULTS.md | Binding site: | 136–136 | 0 / 1 | 0 | PMID:10967094 In vitro, TCL shows rapid GDP/GTP exchange and displays higher GTP dissociation and hydolysis rates than TC10. |
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