UniProt ID | RRAS2_MOUSE | |
---|---|---|
UniProt AC | P62071 | |
Protein Name | Ras-related protein R-Ras2 | |
Gene Name | Rras2 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 204 | |
Subcellular Localization |
Cell membrane Lipid-anchor Cytoplasmic side. Inner surface of plasma membrane possibly with attachment requiring acylation of the C-terminal cysteine (By similarity with RAS). |
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Protein Description | It is a plasma membrane-associated GTP-binding protein with GTPase activity. Might transduce growth inhibitory signals across the cell membrane, exerting its effect through an effector shared with the Ras proteins but in an antagonistic fashion.. | |
Protein Sequence | MAAAGWRDGSGQEKYRLVVVGGGGVGKSALTIQFIQSYFVTDYDPTIEDSYTKQCVIDDRAARLDILDTAGQEEFGAMREQYMRTGEGFLLVFSVTDRGSFEEIYKFQRQILRVKDRDEFPMILIGNKADLDHQRQVTQEEGQQLARQLKVTYMEASAKIRMNVDQAFHELVRVIRKFQEQECPPSPEPTRKEKDKKGCHCVIF | |
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 |
---|---|---|---|---|---|
2 | Acetylation | ------MAAAGWRDG ------CCCCCCCCC | 13.15 | - | |
10 | Phosphorylation | AAGWRDGSGQEKYRL CCCCCCCCCCCEEEE | 41.41 | 25266776 | |
105 | Phosphorylation | RGSFEEIYKFQRQIL CCCHHHHHHHHHHHH | 14.72 | - | |
106 | Ubiquitination | GSFEEIYKFQRQILR CCHHHHHHHHHHHHC | 40.45 | 22790023 | |
128 | Ubiquitination | PMILIGNKADLDHQR CEEEEECHHHCCHHH | 37.76 | 22790023 | |
177 | Ubiquitination | ELVRVIRKFQEQECP HHHHHHHHHHHCCCC | 40.03 | - | |
186 | Phosphorylation | QEQECPPSPEPTRKE HHCCCCCCCCCCCCC | 27.34 | 27087446 | |
190 | Phosphorylation | CPPSPEPTRKEKDKK CCCCCCCCCCCCCCC | 53.35 | 27742792 | |
194 | Acetylation | PEPTRKEKDKKGCHC CCCCCCCCCCCCCEE | 77.28 | 7721145 | |
196 | Acetylation | PTRKEKDKKGCHCVI CCCCCCCCCCCEEEE | 63.23 | 7721157 | |
199 | S-palmitoylation | KEKDKKGCHCVIF-- CCCCCCCCEEEEC-- | 2.86 | - | |
201 | Methylation | KDKKGCHCVIF---- CCCCCCEEEEC---- | 2.67 | - | |
201 | Farnesylation | KDKKGCHCVIF---- CCCCCCEEEEC---- | 2.67 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of RRAS2_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RRAS2_MOUSE !! |
* 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 RRAS2_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of RRAS2_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND MASSSPECTROMETRY. | |
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND MASSSPECTROMETRY. | |
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND MASSSPECTROMETRY. | |
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND MASSSPECTROMETRY. |