UniProt ID | RAC3_ARATH | |
---|---|---|
UniProt AC | Q38912 | |
Protein Name | Rac-like GTP-binding protein ARAC3 | |
Gene Name | ARAC3 | |
Organism | Arabidopsis thaliana (Mouse-ear cress). | |
Sequence Length | 198 | |
Subcellular Localization |
Cytoplasm. Membrane Peripheral membrane protein. Associated with the membrane when activated. |
|
Protein Description | Inactive GDP-bound Rho GTPases reside in the cytosol, are found in a complex with Rho GDP-dissociation inhibitors (Rho GDIs), and are released from the GDI protein in order to translocate to membranes upon activation. May be involved in cell polarity control during the actin-dependent tip growth of root hairs. [PubMed: 11387211 SPK1-dependent activation is required for auxin-mediated inhibition of PIN2 internalization during gravitropic responses] | |
Protein Sequence | MSASRFIKCVTVGDGAVGKTCLLISYTSNTFPTDYVPTVFDNFSANVIVDGNTINLGLWDTAGQEDYNRLRPLSYRGADVFLLAFSLVSKASYENVSKKWVPELRHYAPGVPIILVGTKLDLRDDKQFFAEHPGAVPISTAQGEELKKLIGAPAYIECSAKTQQNVKAVFDAAIKVVLQPPKNKKKKKRKSQKGCSIL | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
21 | S-palmitoylation | DGAVGKTCLLISYTS CCCCCCEEEEEEEEC | 3.11 | 20451389 | |
158 | S-palmitoylation | GAPAYIECSAKTQQN CCCEEEECCHHCHHH | 3.30 | - | |
158 | S-palmitoylation | GAPAYIECSAKTQQN CCCEEEECCHHCHHH | 3.30 | 20451389 | |
195 | Geranylgeranylation | KRKSQKGCSIL---- CCCCCCCCCCC---- | 2.70 | 17242203 | |
195 | Methylation | KRKSQKGCSIL---- CCCCCCCCCCC---- | 2.70 | - | |
195 | S-palmitoylation | KRKSQKGCSIL---- CCCCCCCCCCC---- | 2.70 | 28894027 | |
195 | Geranylgeranylation | KRKSQKGCSIL---- CCCCCCCCCCC---- | 2.70 | 17242203 |
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 RAC3_ARATH !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RAC3_ARATH !! |
* 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 RAC3_ARATH !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
GDIR_ARATH | SCN1 | physical | 10798620 | |
RIC1_ARATH | RIC1 | physical | 19818614 | |
ROGF8_ARATH | ROPGEF8 | physical | 19070620 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Palmitoylation | |
Reference | PubMed |
"Activation status-coupled transient S acylation determines membranepartitioning of a plant Rho-related GTPase."; Sorek N., Poraty L., Sternberg H., Bar E., Lewinsohn E., Yalovsky S.; Mol. Cell. Biol. 27:2144-2154(2007). Cited for: SUBCELLULAR LOCATION,PALMITOYLATION AT CYS-158, ISOPRENYLATION ATCYS-195, MUTAGENESIS OF CYS-158, AND MASS SPECTROMETRY. | |
Prenylation | |
Reference | PubMed |
"Activation status-coupled transient S acylation determines membranepartitioning of a plant Rho-related GTPase."; Sorek N., Poraty L., Sternberg H., Bar E., Lewinsohn E., Yalovsky S.; Mol. Cell. Biol. 27:2144-2154(2007). Cited for: SUBCELLULAR LOCATION,PALMITOYLATION AT CYS-158, ISOPRENYLATION ATCYS-195, MUTAGENESIS OF CYS-158, AND MASS SPECTROMETRY. |