Q7L0Q8 · RHOU_HUMAN
- ProteinRho-related GTP-binding protein RhoU
- GeneRHOU
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids258 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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.
Cofactor
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cell projection | |
Cellular Component | cytosol | |
Cellular Component | endosome membrane | |
Cellular Component | focal adhesion | |
Cellular Component | Golgi membrane | |
Cellular Component | plasma membrane | |
Cellular Component | podosome | |
Molecular Function | GTP binding | |
Molecular Function | GTPase activity | |
Molecular Function | guanyl-nucleotide exchange factor activity | |
Molecular Function | metal ion binding | |
Molecular Function | protein kinase binding | |
Biological Process | actin filament organization | |
Biological Process | Cdc42 protein signal transduction | |
Biological Process | cytoskeleton organization | |
Biological Process | endocytosis | |
Biological Process | establishment or maintenance of cell polarity | |
Biological Process | G1/S transition of mitotic cell cycle | |
Biological Process | positive regulation of protein targeting to mitochondrion | |
Biological Process | Rac protein signal transduction | |
Biological Process | regulation of cell shape | |
Biological Process | regulation of small GTPase mediated signal transduction |
Keywords
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRho-related GTP-binding protein RhoU
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ7L0Q8
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Lipid-anchor
Golgi apparatus membrane ; Lipid-anchor
Note: Localizes to podosomes in SRC-transformed cells.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 63 | Loss of GTP-binding and localization to focal adhesions. No effect on ARHGAP30-binding. | ||||
Sequence: T → N | ||||||
Mutagenesis | 80 | No effect on ARHGAP30-binding. | ||||
Sequence: P → G | ||||||
Mutagenesis | 81 | Loss of binding to PAK3; when associated with A-83 and C-86. | ||||
Sequence: T → S | ||||||
Mutagenesis | 83 | Loss of binding to PAK3; when associated with S-81 and C-86. | ||||
Sequence: F → A | ||||||
Mutagenesis | 83 | Loss of ARHGAP30-binding. | ||||
Sequence: F → G | ||||||
Mutagenesis | 86 | Loss of PAK3-binding; when associated with S-81 and A-83. No effect on ARHGAP30-binding. | ||||
Sequence: F → C | ||||||
Mutagenesis | 107 | Constitutively active. Results in increased rates of stress fiber dissolution and cell migration. No effect on ARHGAP30-binding. | ||||
Sequence: Q → L | ||||||
Natural variant | VAR_051975 | 121 | in dbSNP:rs3820264 | |||
Sequence: T → A | ||||||
Mutagenesis | 255 | No effect on subcellular location. | ||||
Sequence: C → S | ||||||
Mutagenesis | 256 | Loss of subcellular location to plasma and intracellular membranes. | ||||
Sequence: C → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 464 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, lipidation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000326435 | 1-258 | Rho-related GTP-binding protein RhoU | |||
Sequence: MPPQQGDPAFPDRCEAPPVPPRRERGGRGGRGPGEPGGRGRAGGAEGRGVKCVLVGDGAVGKTSLVVSYTTNGYPTEYIPTAFDNFSAVVSVDGRPVRLQLCDTAGQDEFDKLRPLCYTNTDIFLLCFSVVSPSSFQNVSEKWVPEIRCHCPKAPIILVGTQSDLREDVKVLIELDKCKEKPVPEEAAKLCAEEIKAASYIECSALTQKNLKEVFDAAIVAGIQYSDTQQQPKKSKSRTPDKMKNLSKSWWKKYCCFV | ||||||
Lipidation | 256 | S-palmitoyl cysteine | ||||
Sequence: C |
Post-translational modification
Tyrosine phosphorylated by SRC in response to PTK2B/PYK2 activation.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitously expressed in all tissues examined. Expressed at high levels in the stomach, small intestine, brain, skeletal muscle and placenta.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with PAK3. Interacts with ARHGAP30 in a GTP-independent manner. In its GTP-loaded conformation, interacts with ARHGAP31. Interacts with PTK2B/PYK2.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q7L0Q8 | ARHGAP30 Q7Z6I6 | 2 | EBI-1638043, EBI-2814810 | |
BINARY | Q7L0Q8 | ARHGAP30 Q7Z6I6-2 | 3 | EBI-1638043, EBI-26970905 | |
XENO | Q7L0Q8 | Arhgap31 A6X8Z5 | 2 | EBI-1638043, EBI-4325995 | |
BINARY | Q7L0Q8 | NCK2 O43639 | 6 | EBI-1638043, EBI-713635 | |
BINARY | Q7L0Q8 | PAK1 Q13153-2 | 2 | EBI-1638043, EBI-1019502 | |
BINARY | Q7L0Q8 | PTK2B Q14289 | 4 | EBI-1638043, EBI-298640 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-45 | Disordered | ||||
Sequence: MPPQQGDPAFPDRCEAPPVPPRRERGGRGGRGPGEPGGRGRAGGA |
Sequence similarities
Belongs to the small GTPase superfamily. Rho family.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q7L0Q8-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length258
- Mass (Da)28,218
- Last updated2008-02-05 v1
- ChecksumD90059DE82288B97
Q7L0Q8-2
- Name2
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 1-13 | in Ref. 7; BAD92748 | ||||
Sequence: MPPQQGDPAFPDR → QLLPTATLRGGGAVGPGPASPRPQA | ||||||
Alternative sequence | VSP_052732 | 1-61 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_052733 | 62-66 | in isoform 2 | |||
Sequence: KTSLV → MTNIG | ||||||
Sequence conflict | 71 | in Ref. 2; AAL99390 | ||||
Sequence: T → P |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF378087 EMBL· GenBank· DDBJ | AAK83340.1 EMBL· GenBank· DDBJ | mRNA | ||
AB074878 EMBL· GenBank· DDBJ | BAB86361.1 EMBL· GenBank· DDBJ | mRNA | ||
AB051826 EMBL· GenBank· DDBJ | BAB18638.1 EMBL· GenBank· DDBJ | mRNA | ||
DQ384420 EMBL· GenBank· DDBJ | ABD48870.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DQ384421 EMBL· GenBank· DDBJ | ABD48871.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DQ384422 EMBL· GenBank· DDBJ | ABD48872.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DQ384423 EMBL· GenBank· DDBJ | ABD48873.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DQ384424 EMBL· GenBank· DDBJ | ABD48874.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DQ384425 EMBL· GenBank· DDBJ | ABD48875.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF211836 EMBL· GenBank· DDBJ | AAL54874.1 EMBL· GenBank· DDBJ | mRNA | ||
AF282258 EMBL· GenBank· DDBJ | AAG46058.1 EMBL· GenBank· DDBJ | mRNA | ||
AF251701 EMBL· GenBank· DDBJ | AAL99390.1 EMBL· GenBank· DDBJ | mRNA | ||
AK289971 EMBL· GenBank· DDBJ | BAF82660.1 EMBL· GenBank· DDBJ | mRNA | ||
AB209511 EMBL· GenBank· DDBJ | BAD92748.1 EMBL· GenBank· DDBJ | mRNA | ||
AL096776 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471098 EMBL· GenBank· DDBJ | EAW69885.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC040076 EMBL· GenBank· DDBJ | AAH40076.1 EMBL· GenBank· DDBJ | mRNA |