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P01120 (RAS2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-like protein 2
Gene names
Name:RAS2
Synonyms:ASC1, CTN5, GLC5
Ordered Locus Names:YNL098C
ORF Names:N2198
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length322 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Cell membrane; Lipid-anchor.

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.

Sequence similarities

Belongs to the small GTPase superfamily. Ras family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LTE1P078665EBI-14838,EBI-10243

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 319318Ras-like protein 2
PRO_0000030195
Propeptide320 – 3223Removed in mature form
PRO_0000030196

Regions

Nucleotide binding17 – 248GTP By similarity
Nucleotide binding64 – 685GTP By similarity
Nucleotide binding123 – 1264GTP By similarity
Motif39 – 479Effector region By similarity

Amino acid modifications

Modified residue1981Phosphoserine Ref.20
Modified residue2021Phosphoserine Ref.20 Ref.21 Ref.22
Modified residue2071Phosphoserine Ref.20 Ref.21 Ref.22
Modified residue2141Phosphoserine Ref.16 Ref.20 Ref.21
Modified residue2241Phosphoserine Ref.18 Ref.22
Modified residue2251Phosphoserine Ref.22
Modified residue2261Phosphothreonine Ref.22
Modified residue2351Phosphoserine Ref.16 Ref.18 Ref.19 Ref.22
Modified residue2381Phosphoserine Ref.16 Ref.18 Ref.22
Modified residue2401Phosphothreonine Ref.22
Modified residue3191Cysteine methyl ester
Lipidation3181S-palmitoyl cysteine
Lipidation3191S-farnesyl cysteine Ref.13

Experimental info

Mutagenesis191G → V: Low sporulation efficiency. Ref.8
Mutagenesis701E → K in GLC5-1; low glycogen accumulation and sporulation deficiency. Ref.14
Sequence conflict1081L → P in CAA25207. Ref.2
Sequence conflict2101H → L in CAA25207. Ref.2
Sequence conflict2551D → V in AAA34959. Ref.1
Sequence conflict298 – 2992KQ → SK in CAA25207. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P01120 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 6CAAAC531EEAE92F

FASTA32234,705
        10         20         30         40         50         60 
MPLNKSNIRE YKLVVVGGGG VGKSALTIQL TQSHFVDEYD PTIEDSYRKQ VVIDDEVSIL 

        70         80         90        100        110        120 
DILDTAGQEE YSAMREQYMR NGEGFLLVYS ITSKSSLDEL MTYYQQILRV KDTDYVPIVV 

       130        140        150        160        170        180 
VGNKSDLENE KQVSYQDGLN MAKQMNAPFL ETSAKQAINV EEAFYTLARL VRDEGGKYNK 

       190        200        210        220        230        240 
TLTENDNSKQ TSQDTKGSGA NSVPRNSGGH RKMSNAANGK NVNSSTTVVN ARNASIESKT 

       250        260        270        280        290        300 
GLAGNQATNG KTQTDRTNID NSTGQAGQAN AQSANTVNNR VNNNSKAGQV SNAKQARKQQ 

       310        320 
AAPGGNTSEA SKSGSGGCCI IS 

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[7]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[8]"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] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLY-19.
[9]"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] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, POST-TRANSLATIONAL MODIFICATIONS.
[10]"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] [Europe PMC] [Abstract]
Cited for: METHYLATION AT CYS-318.
[11]"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] [Europe PMC] [Abstract]
Cited for: METHYLATION BY STE14.
[12]"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] [Europe PMC] [Abstract]
Cited for: POST-TRANSLATIONAL MODIFICATIONS.
[13]"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] [Europe PMC] [Abstract]
Cited for: ISOPRENYLATION AT CYS-319 BY RAM1-RAM2.
[14]"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] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLU-70.
[15]"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] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING BY RCE1.
[16]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214; SER-235 AND SER-238, MASS SPECTROMETRY.
Strain: 2124.
[17]"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] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[18]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224; SER-235 AND SER-238, MASS SPECTROMETRY.
Strain: YAL6B.
[19]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235, MASS SPECTROMETRY.
Strain: ADR376.
[20]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198; SER-202; SER-207 AND SER-214, MASS SPECTROMETRY.
[21]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202; SER-207 AND SER-214, MASS SPECTROMETRY.
[22]"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] [Europe PMC] [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

EMBL
GenBank
DDBJ
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.
BK006947 Genomic DNA. Translation: DAA10447.1.
PIRTVBYR2. S58254.
RefSeqNP_014301.1. NM_001182936.1.

3D structure databases

ProteinModelPortalP01120.
SMRP01120. Positions 10-172.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-2263N.
IntActP01120. 10 interactions.
MINTMINT-688754.
STRING4932.YNL098C.

Proteomic databases

PaxDbP01120.
PeptideAtlasP01120.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNL098C; YNL098C; YNL098C.
GeneID855625.
KEGGsce:YNL098C.

Organism-specific databases

SGDS000005042. RAS2.

Phylogenomic databases

eggNOGCOG1100.
GeneTreeENSGT00700000104315.
HOGENOMHOG000233973.
KOK07974.
OMARNASIES.
OrthoDBEOG4578H0.

Enzyme and pathway databases

BioCycYEAST:G3O-33126-MONOMER.

Gene expression databases

GenevestigatorP01120.
GermOnlineYNL098C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERPTHR24070. PTHR24070. 1 hit.
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00173. RAS. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51421. RAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio979825.
PMAP-CutDBP01120.

Entry information

Entry nameRAS2_YEAST
AccessionPrimary (citable) accession number: P01120
Secondary accession number(s): D6W181, Q45U01
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: May 29, 2013
This is version 152 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XIV

Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

SIMILARITY comments

Index of protein domains and families