| UniProt ID | RHOQ_HUMAN | |
|---|---|---|
| UniProt AC | P17081 | |
| Protein Name | Rho-related GTP-binding protein RhoQ | |
| Gene Name | RHOQ | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 205 | |
| Subcellular Localization |
Cytoplasm . Cell membrane Lipid-anchor . |
|
| Protein Description | Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses. Involved in epithelial cell polarization processes. May play a role in CFTR trafficking to the plasma membrane. Causes the formation of thin, actin-rich surface projections called filopodia.. | |
| Protein Sequence | MAHGPGALMLKCVVVGDGAVGKTCLLMSYANDAFPEEYVPTVFDHYAVSVTVGGKQYLLGLYDTAGQEDYDRLRPLSYPMTDVFLICFSVVNPASFQNVKEEWVPELKEYAPNVPFLLIGTQIDLRDDPKTLARLNDMKEKPICVEQGQKLAKEIGACCYVECSALTQKGLKTVFDEAIIAILTPKKHTVKKRIGSRCINCCLIT | |
| 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 |
|---|---|---|---|---|---|
| 12 | S-palmitoylation | PGALMLKCVVVGDGA CCEEEEEEEEECCCC | 2.18 | 29575903 | |
| 23 | Phosphorylation | GDGAVGKTCLLMSYA CCCCCCHHHHHHHHC | 11.49 | 21406692 | |
| 28 | Phosphorylation | GKTCLLMSYANDAFP CHHHHHHHHCCCCCC | 22.51 | 21406692 | |
| 29 | Phosphorylation | KTCLLMSYANDAFPE HHHHHHHHCCCCCCH | 8.75 | 21406692 | |
| 38 | Phosphorylation | NDAFPEEYVPTVFDH CCCCCHHHCCCCCCE | 15.29 | 21406692 | |
| 41 | Phosphorylation | FPEEYVPTVFDHYAV CCHHHCCCCCCEEEE | 24.62 | 21406692 | |
| 46 | Phosphorylation | VPTVFDHYAVSVTVG CCCCCCEEEEEEEEC | 15.56 | 21406692 | |
| 49 | Phosphorylation | VFDHYAVSVTVGGKQ CCCEEEEEEEECCEE | 12.14 | 21406692 | |
| 51 | Phosphorylation | DHYAVSVTVGGKQYL CEEEEEEEECCEEEE | 13.11 | 21406692 | |
| 70 | Phosphorylation | DTAGQEDYDRLRPLS CCCCCCCHHHCCCCC | 11.38 | 20736484 | |
| 160 | Phosphorylation | KEIGACCYVECSALT HHHCCCEEEECHHHC | 10.12 | 29759185 | |
| 163 | S-palmitoylation | GACCYVECSALTQKG CCCEEEECHHHCHHC | 1.74 | 29575903 | |
| 164 | Phosphorylation | ACCYVECSALTQKGL CCEEEECHHHCHHCH | 16.89 | 29759185 | |
| 169 | Ubiquitination | ECSALTQKGLKTVFD ECHHHCHHCHHHHHC | 62.06 | 2189047 | |
| 169 | Acetylation | ECSALTQKGLKTVFD ECHHHCHHCHHHHHC | 62.06 | 25953088 | |
| 172 | Ubiquitination | ALTQKGLKTVFDEAI HHCHHCHHHHHCHHH | 51.84 | - | |
| 173 | Phosphorylation | LTQKGLKTVFDEAII HCHHCHHHHHCHHHH | 31.29 | - | |
| 202 | Methylation | GSRCINCCLIT---- CCCEEEEEEEC---- | 2.38 | - | |
| 202 | Farnesylation | GSRCINCCLIT---- CCCEEEEEEEC---- | 2.38 | - |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of RHOQ_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RHOQ_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 RHOQ_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| GOPC_HUMAN | GOPC | physical | 11162552 | |
| EXOC7_HUMAN | EXOC7 | physical | 12687004 | |
| PAR6B_HUMAN | PARD6B | physical | 11162552 | |
| CIP4_HUMAN | TRIP10 | physical | 12242347 | |
| GOPC_HUMAN | GOPC | physical | 25416956 |
| 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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