Search by BoMiProt ID - Bomi8777


Primary Information

BoMiProt ID Bomi8777
Protein Name Rho-related GTP-binding protein RhoU
Organism Bos taurus
Uniprot IdA5D7J5
Milk FractionWhey
Ref Sequence Id NP_001091616.1
Aminoacid Length 255
Molecular Weight 27824
Fasta Sequence https://www.uniprot.org/uniprot/A5D7J5.fasta
Gene Name RHOU
Gene Id 781044
Protein Existence Status reviewed

Secondary Information

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
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).
PTMs Lipidation,Palmitoylation,Phosphorylation
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
NA
Predicted Disorder Regions 1-42, 223-241
DisProt Annotation
TM Helix Prediction No TM helices
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.
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