Primary Information |
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BoMiProt ID | Bomi8777 |
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Protein Name | Rho-related GTP-binding protein RhoU |
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Organism | Bos taurus |
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Uniprot ID | A5D7J5 |
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Milk Fraction | Whey |
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Ref Sequence ID | NP_001091616.1 |
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Aminoacid Length | 255 |
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Molecular Weight | 27824 |
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FASTA Sequence |
Download |
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Gene Name | RHOU |
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Gene ID | 781044 |
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Protein Existence Status | reviewed |
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Secondary Information |
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Protein Function | Acts upstream of PAK1 to regulate the actin cytoskeleton, adhesion turnover and increase cell migration. Stimulates quiescent cells to reenter the cell cycle. Has no detectable GTPase activity but its high intrinsic guanine nucleotide exchange activity suggests it is constitutively GTP-bound. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape |
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Biochemical Properties | RhoU is considered to be an atypical GTPase because it has been reported to have a 10-fold higher intrinsic guanine nucleotide exchange rate in vitro compared with Cdc42, and is therefore presumed to be predominantly GTP-bound in cells.Contain an unique N-terminal and C-terminal regions either side of the core GTP-binding domain.N-terminal region of RhoU contains 3 proline-rich motifs (PRMs). |
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PTMs | Lipidation,Palmitoylation,Phosphorylation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| NA |
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Predicted Disorder Regions | 1-42, 223-241 |
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DisProt Annotation | |
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TM Helix Prediction | No TM helices |
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Significance of PTMs | Tyrosine phosphorylated by SRC in response to PTK2B/PYK2 activation.At the C-terminus is a CFV motif (amino acids 256–258) which is modified on the cysteine by palmitoylation and is required for membrane localization.The Src tyrosine kinase phosphorylates Tyr254, which alters RhoU localization.Phosphorylation of RhoU on a C-terminal tyrosine, Y254, results in a rapid relocalization of RhoU from the plasma membrane to the endosomal compartment. |
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Bibliography | 1.Richard G. Hodge & Anne J. Ridley (2020) Regulation and functions of RhoU and RhoV, Small GTPases, 11:1, 8-15, DOI: 10.1080/21541248.2017.1362495 |