RRAS2_MOUSE - dbPTM
RRAS2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
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).
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAAAGWRDG
------CCCCCCCCC
13.15-
10PhosphorylationAAGWRDGSGQEKYRL
CCCCCCCCCCCEEEE
41.4125266776
105PhosphorylationRGSFEEIYKFQRQIL
CCCHHHHHHHHHHHH
14.72-
106UbiquitinationGSFEEIYKFQRQILR
CCHHHHHHHHHHHHC
40.4522790023
128UbiquitinationPMILIGNKADLDHQR
CEEEEECHHHCCHHH
37.7622790023
177UbiquitinationELVRVIRKFQEQECP
HHHHHHHHHHHCCCC
40.03-
186PhosphorylationQEQECPPSPEPTRKE
HHCCCCCCCCCCCCC
27.3427087446
190PhosphorylationCPPSPEPTRKEKDKK
CCCCCCCCCCCCCCC
53.3527742792
194AcetylationPEPTRKEKDKKGCHC
CCCCCCCCCCCCCEE
77.287721145
196AcetylationPTRKEKDKKGCHCVI
CCCCCCCCCCCEEEE
63.237721157
199S-palmitoylationKEKDKKGCHCVIF--
CCCCCCCCEEEEC--
2.86-
201MethylationKDKKGCHCVIF----
CCCCCCEEEEC----
2.67-
201FarnesylationKDKKGCHCVIF----
CCCCCCEEEEC----
2.67-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 RRAS2_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RRAS2_MOUSE !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of RRAS2_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RRAS2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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