Reviewed,
UniProtKB/Swiss-Prot P01120 (RAS2_YEAST)
Last modified
December 15, 2009.
Version 119.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Ras-like protein 2 | ||||||||
| Gene names |
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| Organism | Saccharomyces cerevisiae (Baker's yeast) [Complete proteome] | ||||||||
| Taxonomic identifier | 4932 [NCBI] | ||||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces |
Protein attributes
| Sequence length | 322 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | The S.cerevisiae Ras proteins modulate the activity of the adenylate cyclase catalytic subunit and therefore affect the biosynthesis of cyclic-AMP. |
| Enzyme regulation | Alternate between an inactive form bound to GDP and an active form bound to GTP. Activated by guanine nucleotide-exchange factor (GEF) CDC25 and inactivated by GTPase-activating proteins (GAPs) IRA1 and IRA2. |
| Subcellular location | |
| Post-translational modification | Farnesylated by RAM1-RAM2, which is required for targeting RAS2 to the cytoplasmic site of the endoplasmic reticulum, where proteolytic processing of the C-terminus by RCE1 and methylation of the resulting carboxyl group by STE14 occurs. Palmitoylated by the ERF2-SHR5 complex, which is required for proper plasma membrane localization of RAS2. |
| Miscellaneous | RAS2 is necessary for a normal response to nutrient limitations, in general, disruption of the RAS2 locus results in an overall premature starvation response. Present with 19800 molecules/cell in log phase SD medium. Ref.16 |
| Sequence similarities | Belongs to the small GTPase superfamily. Ras family. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| ARO8 | P53090 | 1 | EBI-14838,EBI-2042933 | |
| GLN1 | P32288 | 1 | EBI-14838,EBI-7665 | |
| GPI2 | P46961 | 1 | EBI-14838,EBI-7809 | |
| IPP1 | P00817 | 1 | EBI-14838,EBI-9338 | |
| LTE1 | P07866 | 2 | EBI-14838,EBI-10243 | |
| RAS1 | P01119 | 1 | EBI-14838,EBI-14830 | |
| RNR1 | P21524 | 1 | EBI-14838,EBI-15234 | |
| RNR2 | P09938 | 1 | EBI-14838,EBI-15240 | |
| VMA4 | P22203 | 1 | EBI-14838,EBI-20268 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed | ||||||
| Chain | 2 – 319 | 318 | Ras-like protein 2 | PRO_0000030195 | |||||
| Propeptide | 320 – 322 | 3 | Removed in mature form | PRO_0000030196 | |||||
Regions | |||||||||
| Nucleotide binding | 17 – 24 | 8 | GTP By similarity | ||||||
| Nucleotide binding | 64 – 68 | 5 | GTP By similarity | ||||||
| Nucleotide binding | 123 – 126 | 4 | GTP By similarity | ||||||
| Motif | 39 – 47 | 9 | Effector region By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 198 | 1 | Phosphoserine Ref.19 | ||||||
| Modified residue | 202 | 1 | Phosphoserine Ref.19 Ref.20 Ref.21 | ||||||
| Modified residue | 207 | 1 | Phosphoserine Ref.19 Ref.20 Ref.21 | ||||||
| Modified residue | 214 | 1 | Phosphoserine Ref.19 Ref.20 Ref.15 | ||||||
| Modified residue | 224 | 1 | Phosphoserine Ref.21 Ref.17 | ||||||
| Modified residue | 225 | 1 | Phosphoserine Ref.21 | ||||||
| Modified residue | 226 | 1 | Phosphothreonine Ref.21 | ||||||
| Modified residue | 235 | 1 | Phosphoserine Ref.21 Ref.15 Ref.17 Ref.18 | ||||||
| Modified residue | 238 | 1 | Phosphoserine Ref.21 Ref.15 Ref.17 | ||||||
| Modified residue | 240 | 1 | Phosphothreonine Ref.21 | ||||||
| Modified residue | 319 | 1 | Cysteine methyl ester | ||||||
| Lipidation | 318 | 1 | S-palmitoyl cysteine | ||||||
| Lipidation | 319 | 1 | S-farnesyl cysteine | ||||||
Experimental info | |||||||||
| Mutagenesis | 19 | 1 | G → V: Low sporulation efficiency. Ref.7 | ||||||
| Mutagenesis | 70 | 1 | E → K in GLC5-1; low glycogen accumulation and sporulation deficiency. Ref.13 | ||||||
| Sequence conflict | 108 | 1 | L → P in CAA25207. Ref.2 | ||||||
| Sequence conflict | 210 | 1 | H → L in CAA25207. Ref.2 | ||||||
| Sequence conflict | 255 | 1 | D → V in AAA34959. Ref.1 | ||||||
| Sequence conflict | 298 – 299 | 2 | KQ → SK in CAA25207. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Genes in S. cerevisiae encoding proteins with domains homologous to the mammalian ras proteins." Powers S., Kataoka T., Fasano O., Goldfarb M., Strathern J., Broach J., Wigler M. Cell 36:607-612(1984) [PubMed: 6365329] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Nucleotide sequence of two rasH related-genes isolated from the yeast Saccharomyces cerevisiae." Dhar R., Nieto A., Koller R., DeFeo-Jones D., Scolnick E.M. Nucleic Acids Res. 12:3611-3618(1984) [PubMed: 6328429] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [3] | "ASC1/RAS2 suppresses the growth-defect on glycerol caused by the atp1-2 mutation in the yeast Saccharomyces cerevisiae." Mabuchi T., Ichimura Y., Takeda M., Douglas M.G. J. Biol. Chem. 275:10492-10497(2000) [PubMed: 10744740] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 64665 / S288c / DC5. |
| [4] | "Molecular genetic dissection of a quantitative trait in yeast." Deutschbauer A.M., Davis R.W. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: SK1. |
| [5] | "The sequence of a 21.3 kb DNA fragment from the left arm of yeast chromosome XIV reveals LEU4, MET4, POL1, RAS2, and six new open reading frames." Saiz J.E., Buitrago M.J., Soler A., del Rey F., Revuelta J.L. Yeast 12:403-409(1996) [PubMed: 8701612] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679. |
| [6] | "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. Hani J.Nature 387:93-98(1997) [PubMed: 9169873] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679. |
| [7] | "Genetic analysis of yeast RAS1 and RAS2 genes." Kataoka T., Powers S., McGill C., Fasano O., Strathern J., Broach J., Wigler M. Cell 37:437-445(1984) [PubMed: 6327067] [Abstract] Cited for: MUTAGENESIS OF GLY-19. |
| [8] | "RAS2 protein of Saccharomyces cerevisiae undergoes removal of methionine at N-terminus and removal of three amino acids at C terminus." Fujiyama A., Tamanoi F. J. Biol. Chem. 265:3362-3368(1990) [PubMed: 2406252] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, POST-TRANSLATIONAL MODIFICATIONS. |
| [9] | "RAS2 protein of Saccharomyces cerevisiae is methyl-esterified at its carboxyl terminus." Deschenes R.J., Stimmel J.B., Clarke S., Stock J., Broach J.R. J. Biol. Chem. 264:11865-11873(1989) [PubMed: 2663844] [Abstract] Cited for: METHYLATION AT CYS-318. |
| [10] | "The Saccharomyces cerevisiae STE14 gene encodes a methyltransferase that mediates C-terminal methylation of a-factor and RAS proteins." Hrycyna C.A., Sapperstein S.K., Clarke S., Michaelis S. EMBO J. 10:1699-1709(1991) [PubMed: 2050108] [Abstract] Cited for: METHYLATION BY STE14. |
| [11] | "S-farnesylation and methyl esterification of C-terminal domain of yeast RAS2 protein prior to fatty acid acylation." Fujiyama A., Tsunasawa S., Tamanoi F., Sakiyama F. J. Biol. Chem. 266:17926-17931(1991) [PubMed: 1917931] [Abstract] Cited for: POST-TRANSLATIONAL MODIFICATIONS. |
| [12] | "RAM2, an essential gene of yeast, and RAM1 encode the two polypeptide components of the farnesyltransferase that prenylates a-factor and Ras proteins." 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) [PubMed: 1763050] [Abstract] Cited for: ISOPRENYLATION AT CYS-319 BY RAM1-RAM2. |
| [13] | "Characterization of glycogen-deficient glc mutants of Saccharomyces cerevisiae." Cannon J.F., Pringle J.R., Fiechter A., Khalil M. Genetics 136:485-503(1994) [PubMed: 8150278] [Abstract] Cited for: MUTAGENESIS OF GLU-70. |
| [14] | "Modulation of Ras and a-factor function by carboxyl-terminal proteolysis." Boyartchuk V.L., Ashby M.N., Rine J. Science 275:1796-1800(1997) [PubMed: 9065405] [Abstract] Cited for: PROTEOLYTIC PROCESSING BY RCE1. |
| [15] | "Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces 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) [PubMed: 11875433] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214; SER-235 AND SER-238, MASS SPECTROMETRY. |
| [16] | "Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. |
| [17] | "Quantitative phosphoproteomics applied to the yeast pheromone signaling 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) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224; SER-235 AND SER-238, MASS SPECTROMETRY. |
| [18] | "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces 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) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235, MASS SPECTROMETRY. |
| [19] | "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." 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) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198; SER-202; SER-207 AND SER-214, MASS SPECTROMETRY. |
| [20] | "Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202; SER-207 AND SER-214, MASS SPECTROMETRY. |
| [21] | "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202; SER-207; SER-224; SER-225; THR-226; SER-235; SER-238 AND THR-240, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| K01971 Genomic DNA. Translation: AAA34959.1. X00528 Genomic DNA. Translation: CAA25207.1. D37950 Genomic DNA. Translation: BAA22510.1. DQ115393 Genomic DNA. Translation: AAZ22509.1. Z50161 Genomic DNA. Translation: CAA90528.1. Z71374 Genomic DNA. Translation: CAA95974.1. | |
| PIR | TVBYR2. S58254. |
| RefSeq | NP_014301.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-2263N. |
| IntAct | P01120. 20 interactions. |
| STRING | P01120. |
Proteomic databases | |
| PeptideAtlas | P01120. |
| PRIDE | P01120. |
Genome annotation databases | |
| Ensembl | YNL098C; YNL098C; YNL098C; Saccharomyces cerevisiae. [Genome view] |
| GeneID | 855625. |
| KEGG | sce:YNL098C. |
| NMPDR | fig|4932.3.peg.5372. |
Organism-specific databases | |
| CYGD | YNL098c. |
| SGD | S000005042. RAS2. |
Phylogenomic databases | |
| HOGENOM | HBG745225. |
| OMA | NINVEES. |
| OrthoDB | EOG90031N. |
Gene expression databases | |
| ArrayExpress | P01120. |
| Genevestigator | P01120. |
| GermOnline | YNL098C. Saccharomyces cerevisiae. |
Family and domain databases | |
| InterPro | IPR003577. GTPase_Ras. IPR013753. Ras. IPR001806. Ras_GTPase. IPR020849. Ras_small_GTPase. IPR005225. Small_GTP_bd. [Graphical view] |
| Pfam | PF00071. Ras. 1 hit. [Graphical view] |
| PRINTS | PR00449. RASTRNSFRMNG. |
| SMART | SM00173. RAS. 1 hit. [Graphical view] |
| PROSITE | PS51421. RAS. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 979825. |
| PMAP-CutDB | P01120. |
Entry information
| Entry name | RAS2_YEAST | ||||||||
| Accession | Primary (citable) accession number: P01120 Secondary accession number(s): Q45U01 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |
| Yeast chromosome XIV Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names |

Clusters with


