UniProt ID | RAS2_YEAST | |
---|---|---|
UniProt AC | P01120 | |
Protein Name | Ras-like protein 2 | |
Gene Name | RAS2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 322 | |
Subcellular Localization |
Cell membrane Lipid-anchor. |
|
Protein Description | The S.cerevisiae Ras proteins modulate the activity of the adenylate cyclase catalytic subunit and therefore affect the biosynthesis of cyclic-AMP.. | |
Protein Sequence | MPLNKSNIREYKLVVVGGGGVGKSALTIQLTQSHFVDEYDPTIEDSYRKQVVIDDEVSILDILDTAGQEEYSAMREQYMRNGEGFLLVYSITSKSSLDELMTYYQQILRVKDTDYVPIVVVGNKSDLENEKQVSYQDGLNMAKQMNAPFLETSAKQAINVEEAFYTLARLVRDEGGKYNKTLTENDNSKQTSQDTKGSGANSVPRNSGGHRKMSNAANGKNVNSSTTVVNARNASIESKTGLAGNQATNGKTQTDRTNIDNSTGQAGQANAQSANTVNNRVNNNSKAGQVSNAKQARKQQAAPGGNTSEASKSGSGGCCIIS | |
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 |
---|---|---|---|---|---|
6 | Phosphorylation | --MPLNKSNIREYKL --CCCCHHCCCEEEE | 36.09 | 30377154 | |
31 | Phosphorylation | SALTIQLTQSHFVDE HHHHHEHHHHHCCCC | 16.20 | 22369663 | |
33 | Phosphorylation | LTIQLTQSHFVDEYD HHHEHHHHHCCCCCC | 17.41 | 21551504 | |
39 | Phosphorylation | QSHFVDEYDPTIEDS HHHCCCCCCCCCCHH | 23.82 | 22369663 | |
42 | Phosphorylation | FVDEYDPTIEDSYRK CCCCCCCCCCHHHCC | 33.82 | 22369663 | |
90 | Phosphorylation | EGFLLVYSITSKSSL CCEEEEEEECCCCHH | 16.35 | 27017623 | |
92 | Phosphorylation | FLLVYSITSKSSLDE EEEEEEECCCCHHHH | 24.94 | 27017623 | |
93 | Phosphorylation | LLVYSITSKSSLDEL EEEEEECCCCHHHHH | 28.95 | 28889911 | |
95 | Phosphorylation | VYSITSKSSLDELMT EEEECCCCHHHHHHH | 35.58 | 22369663 | |
96 | Phosphorylation | YSITSKSSLDELMTY EEECCCCHHHHHHHH | 43.51 | 22369663 | |
102 | Phosphorylation | SSLDELMTYYQQILR CHHHHHHHHHHHHHC | 31.53 | 22369663 | |
103 | Phosphorylation | SLDELMTYYQQILRV HHHHHHHHHHHHHCC | 5.82 | 22369663 | |
104 | Phosphorylation | LDELMTYYQQILRVK HHHHHHHHHHHHCCC | 5.69 | 22369663 | |
111 | 2-Hydroxyisobutyrylation | YQQILRVKDTDYVPI HHHHHCCCCCCCEEE | 48.77 | - | |
124 | Ubiquitination | PIVVVGNKSDLENEK EEEEEECHHHCCCCC | 39.14 | 24961812 | |
125 | Phosphorylation | IVVVGNKSDLENEKQ EEEEECHHHCCCCCC | 51.97 | 21440633 | |
131 | Ubiquitination | KSDLENEKQVSYQDG HHHCCCCCCCCHHHH | 68.53 | 23749301 | |
131 | Acetylation | KSDLENEKQVSYQDG HHHCCCCCCCCHHHH | 68.53 | 24489116 | |
134 | Phosphorylation | LENEKQVSYQDGLNM CCCCCCCCHHHHHHH | 18.00 | 30377154 | |
143 | Ubiquitination | QDGLNMAKQMNAPFL HHHHHHHHHCCCCCC | 39.03 | 23749301 | |
165 | Phosphorylation | INVEEAFYTLARLVR CCHHHHHHHHHHHHH | 14.11 | 24603354 | |
166 | Phosphorylation | NVEEAFYTLARLVRD CHHHHHHHHHHHHHC | 13.90 | 24603354 | |
180 | Ubiquitination | DEGGKYNKTLTENDN CCCCCCCCEECCCCC | 41.65 | 23749301 | |
181 | Phosphorylation | EGGKYNKTLTENDNS CCCCCCCEECCCCCC | 34.96 | 23749301 | |
183 | Phosphorylation | GKYNKTLTENDNSKQ CCCCCEECCCCCCCC | 37.66 | 23749301 | |
188 | Phosphorylation | TLTENDNSKQTSQDT EECCCCCCCCCCCCC | 29.07 | 23749301 | |
189 | Ubiquitination | LTENDNSKQTSQDTK ECCCCCCCCCCCCCC | 64.94 | 23749301 | |
191 | Phosphorylation | ENDNSKQTSQDTKGS CCCCCCCCCCCCCCC | 31.90 | 20377248 | |
192 | Phosphorylation | NDNSKQTSQDTKGSG CCCCCCCCCCCCCCC | 24.46 | 20377248 | |
195 | Phosphorylation | SKQTSQDTKGSGANS CCCCCCCCCCCCCCC | 29.66 | 23749301 | |
196 | Ubiquitination | KQTSQDTKGSGANSV CCCCCCCCCCCCCCC | 60.41 | 23749301 | |
198 | Phosphorylation | TSQDTKGSGANSVPR CCCCCCCCCCCCCCC | 35.97 | 22369663 | |
202 | Phosphorylation | TKGSGANSVPRNSGG CCCCCCCCCCCCCCC | 32.72 | 22369663 | |
207 | Phosphorylation | ANSVPRNSGGHRKMS CCCCCCCCCCCCCCC | 47.64 | 19823750 | |
214 | Phosphorylation | SGGHRKMSNAANGKN CCCCCCCCCCCCCCC | 26.76 | 9228053 | |
220 | Ubiquitination | MSNAANGKNVNSSTT CCCCCCCCCCCCCCE | 58.49 | 23749301 | |
224 | Phosphorylation | ANGKNVNSSTTVVNA CCCCCCCCCCEEEEC | 25.44 | 25521595 | |
225 | Phosphorylation | NGKNVNSSTTVVNAR CCCCCCCCCEEEECC | 23.93 | 22369663 | |
226 | Phosphorylation | GKNVNSSTTVVNARN CCCCCCCCEEEECCC | 24.35 | 22369663 | |
227 | Phosphorylation | KNVNSSTTVVNARNA CCCCCCCEEEECCCC | 25.14 | 22369663 | |
235 | Phosphorylation | VVNARNASIESKTGL EEECCCCEECCCCCC | 30.36 | 25521595 | |
238 | Phosphorylation | ARNASIESKTGLAGN CCCCEECCCCCCCCC | 33.57 | 25521595 | |
239 | Ubiquitination | RNASIESKTGLAGNQ CCCEECCCCCCCCCC | 33.55 | 23749301 | |
240 | Phosphorylation | NASIESKTGLAGNQA CCEECCCCCCCCCCC | 46.86 | 17330950 | |
248 | Phosphorylation | GLAGNQATNGKTQTD CCCCCCCCCCCCCCC | 34.44 | 23749301 | |
251 | Ubiquitination | GNQATNGKTQTDRTN CCCCCCCCCCCCCCC | 39.26 | 23749301 | |
262 | Phosphorylation | DRTNIDNSTGQAGQA CCCCCCCCCCCHHHH | 30.11 | 23749301 | |
263 | Phosphorylation | RTNIDNSTGQAGQAN CCCCCCCCCCHHHHH | 39.30 | 21440633 | |
273 | Phosphorylation | AGQANAQSANTVNNR HHHHHHHHCCCHHHH | 22.52 | 25704821 | |
276 | Phosphorylation | ANAQSANTVNNRVNN HHHHHCCCHHHHHCC | 25.07 | 21440633 | |
285 | Phosphorylation | NNRVNNNSKAGQVSN HHHHCCCCCCCCCCC | 26.46 | 23749301 | |
286 | Ubiquitination | NRVNNNSKAGQVSNA HHHCCCCCCCCCCCH | 59.67 | 23749301 | |
291 | Phosphorylation | NSKAGQVSNAKQARK CCCCCCCCCHHHHHH | 24.15 | 23749301 | |
294 | Ubiquitination | AGQVSNAKQARKQQA CCCCCCHHHHHHHHC | 49.06 | 23749301 | |
298 | Ubiquitination | SNAKQARKQQAAPGG CCHHHHHHHHCCCCC | 50.18 | 23749301 | |
307 | Phosphorylation | QAAPGGNTSEASKSG HCCCCCCCCHHHHCC | 31.08 | 22890988 | |
308 | Phosphorylation | AAPGGNTSEASKSGS CCCCCCCCHHHHCCC | 34.85 | 22890988 | |
311 | Phosphorylation | GGNTSEASKSGSGGC CCCCCHHHHCCCCCE | 24.25 | 22890988 | |
318 | S-palmitoylation | SKSGSGGCCIIS--- HHCCCCCEEEEC--- | 1.39 | - | |
318 | S-palmitoylation | SKSGSGGCCIIS--- HHCCCCCEEEEC--- | 1.39 | 8063791 | |
319 | Methylation | KSGSGGCCIIS---- HCCCCCEEEEC---- | 3.33 | 2663844 | |
319 | Farnesylation | KSGSGGCCIIS---- HCCCCCEEEEC---- | 3.33 | 1763050 | |
319 | S-palmitoylation | KSGSGGCCIIS---- HCCCCCEEEEC---- | 3.33 | 3302674 | |
319 | Farnesylation | KSGSGGCCIIS---- HCCCCCEEEEC---- | 3.33 | 1763050 |
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 RAS2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RAS2_YEAST !! |
* 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 RAS2_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202; SER-207; SER-224;SER-225; THR-226; SER-235; SER-238 AND THR-240, AND MASS SPECTROMETRY. | |
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202; SER-207 ANDSER-214, AND MASS SPECTROMETRY. | |
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198; SER-202; SER-207AND SER-214, AND MASS SPECTROMETRY. | |
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235, AND MASSSPECTROMETRY. | |
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224; SER-235 ANDSER-238, AND MASS SPECTROMETRY. | |
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae."; Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.; Nat. Biotechnol. 20:301-305(2002). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214; SER-235 ANDSER-238, AND MASS SPECTROMETRY. | |
Prenylation | |
Reference | PubMed |
"RAM2, an essential gene of yeast, and RAM1 encode the two polypeptidecomponents of the farnesyltransferase that prenylates a-factor and Rasproteins."; He B., Chen P., Chen S.-Y., Vancura K.L., Michaelis S., Powers S.; Proc. Natl. Acad. Sci. U.S.A. 88:11373-11377(1991). Cited for: ISOPRENYLATION AT CYS-319 BY RAM1-RAM2. |