| UniProt ID | RHOU_HUMAN | |
|---|---|---|
| UniProt AC | Q7L0Q8 | |
| Protein Name | Rho-related GTP-binding protein RhoU | |
| Gene Name | RHOU {ECO:0000312|HGNC:HGNC:17794} | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 258 | |
| Subcellular Localization |
Cell membrane Lipid-anchor Cytoplasmic side . Golgi apparatus membrane Lipid-anchor . Cell junction, focal adhesion . Cell projection, podosome . Localizes to podosomes in SRC-transformed cells. |
|
| Protein Description | 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.. | |
| Protein Sequence | MPPQQGDPAFPDRCEAPPVPPRRERGGRGGRGPGEPGGRGRAGGAEGRGVKCVLVGDGAVGKTSLVVSYTTNGYPTEYIPTAFDNFSAVVSVDGRPVRLQLCDTAGQDEFDKLRPLCYTNTDIFLLCFSVVSPSSFQNVSEKWVPEIRCHCPKAPIILVGTQSDLREDVKVLIELDKCKEKPVPEEAAKLCAEEIKAASYIECSALTQKNLKEVFDAAIVAGIQYSDTQQQPKKSKSRTPDKMKNLSKSWWKKYCCFV | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 170 | Ubiquitination | SDLREDVKVLIELDK CHHHHHHHHHHCHHH | 43.58 | - | |
| 196 | Ubiquitination | KLCAEEIKAASYIEC HHHHHHHHHHHHECC | 40.97 | - | |
| 248 | Ubiquitination | DKMKNLSKSWWKKYC HHHHHHCHHHHHHHC | 53.94 | - | |
| 254 | Phosphorylation | SKSWWKKYCCFV--- CHHHHHHHCCCC--- | 7.25 | 20547754 | |
| 256 | S-palmitoylation | SWWKKYCCFV----- HHHHHHCCCC----- | 3.29 | 16046391 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 254 | Y | Phosphorylation | Kinase | SRC | P12931 | PSP |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RHOU_HUMAN !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of RHOU_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Palmitoylation | |
| Reference | PubMed |
| "Biochemical analyses of the Wrch atypical Rho family GTPases."; Shutes A., Berzat A.C., Chenette E.J., Cox A.D., Der C.J.; Methods Enzymol. 406:11-26(2006). Cited for: FUNCTION, COFACTOR, SUBCELLULAR LOCATION, GTP-BINDING, ANDPALMITOYLATION. | |
| "Transforming activity of the Rho family GTPase, Wrch-1, a Wnt-regulated Cdc42 homolog, is dependent on a novel carboxyl-terminalpalmitoylation motif."; Berzat A.C., Buss J.E., Chenette E.J., Weinbaum C.A., Shutes A.,Der C.J., Minden A., Cox A.D.; J. Biol. Chem. 280:33055-33065(2005). Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-255 AND CYS-256, ANDPALMITOYLATION AT CYS-256. | |
