Ras-like protein 2 precursor - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P01120 (RAS2_YEAST) Reviewed, UniProtKB/Swiss-Prot

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

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Ras-like protein 2

Gene names

Name:	RAS2
Synonyms:	ASC1, CTN5, GLC5
Ordered Locus Names:	YNL098C
ORF Names:	N2198

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [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	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.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Ligand	GTP-binding Nucleotide-binding
PTM	Lipoprotein Methylation Palmitate Phosphoprotein Prenylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	Ras protein signal transduction Traceable author statement PubMed 3891097. Source: SGD activation of adenylate cyclase activity Inferred from direct assay PubMed 8106517. Source: SGD ascospore formation Inferred from mutant phenotype PubMed 2558958. Source: SGD positive regulation of transcription by galactose Inferred from mutant phenotype PubMed 16292676. Source: SGD pseudohyphal growth Inferred from mutant phenotype PubMed 1547504. Source: SGD regulation of protein localization Inferred from mutant phenotype PubMed 15917658. Source: SGD replicative cell aging Inferred from mutant phenotype PubMed 12839995 PubMed 8034612. Source: SGD
Cellular_component	endoplasmic reticulum membrane Inferred from direct assay PubMed 22575457. Source: SGD mitochondrion Inferred from direct assay PubMed 22575457. Source: SGD plasma membrane Inferred from direct assay PubMed 11914276 PubMed 16622836 PubMed 20162532. Source: SGD
Molecular_function	GTP binding Inferred from direct assay PubMed 6438624. Source: SGD GTPase activity Inferred from direct assay PubMed 8106517. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
LTE1	P07866	5	EBI-14838,EBI-10243

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 319

318

Ras-like protein 2

PRO_0000030195

Propeptide

320 – 322

Removed in mature form

PRO_0000030196

Regions

Nucleotide binding

17 – 24

GTP By similarity

Nucleotide binding

64 – 68

GTP By similarity

Nucleotide binding

123 – 126

GTP By similarity

Motif

39 – 47

Effector region By similarity

Amino acid modifications

Modified residue

198

Phosphoserine Ref.20

Modified residue

202

Phosphoserine Ref.20 Ref.21 Ref.22

Modified residue

207

Phosphoserine Ref.20 Ref.21 Ref.22

Modified residue

214

Phosphoserine Ref.16 Ref.20 Ref.21

Modified residue

224

Phosphoserine Ref.18 Ref.22

Modified residue

225

Phosphoserine Ref.22

Modified residue

226

Phosphothreonine Ref.22

Modified residue

235

Phosphoserine Ref.16 Ref.18 Ref.19 Ref.22

Modified residue

238

Phosphoserine Ref.16 Ref.18 Ref.22

Modified residue

240

Phosphothreonine Ref.22

Modified residue

319

Cysteine methyl ester

Lipidation

318

S-palmitoyl cysteine

Lipidation

319

S-farnesyl cysteine Ref.13

Experimental info

Mutagenesis

G → V: Low sporulation efficiency. Ref.8

Mutagenesis

E → K in GLC5-1; low glycogen accumulation and sporulation deficiency. Ref.14

Sequence conflict

108

L → P in CAA25207. Ref.2

Sequence conflict

210

H → L in CAA25207. Ref.2

Sequence conflict

255

D → V in AAA34959. Ref.1

Sequence conflict

298 – 299

KQ → SK in CAA25207. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P01120 [UniParc].

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

322

34,705

        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

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References

	« Hide 'large scale' referencesShow '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. 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.
PIR	TVBYR2. S58254.
RefSeq	NP_014301.1. NM_001182936.1.
3D structure databases
ProteinModelPortal	P01120.
SMR	P01120. Positions 10-172.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2263N.
IntAct	P01120. 10 interactions.
MINT	MINT-688754.
STRING	4932.YNL098C.
Proteomic databases
PaxDb	P01120.
PeptideAtlas	P01120.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YNL098C; YNL098C; YNL098C.
GeneID	855625.
KEGG	sce:YNL098C.
Organism-specific databases
SGD	S000005042. RAS2.
Phylogenomic databases
eggNOG	COG1100.
GeneTree	ENSGT00700000104315.
HOGENOM	HOG000233973.
KO	K07974.
OMA	RNASIES.
OrthoDB	EOG4578H0.
Enzyme and pathway databases
BioCyc	YEAST:G3O-33126-MONOMER.
Gene expression databases
Genevestigator	P01120.
GermOnline	YNL098C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR027417. P-loop_NTPase. IPR005225. Small_GTP-bd_dom. IPR001806. Small_GTPase. IPR020849. Small_GTPase_Ras. [Graphical view]
PANTHER	PTHR24070. PTHR24070. 1 hit.
Pfam	PF00071. Ras. 1 hit. [Graphical view]
PRINTS	PR00449. RASTRNSFRMNG.
SMART	SM00173. RAS. 1 hit. [Graphical view]
SUPFAM	SSF52540. SSF52540. 1 hit.
TIGRFAMs	TIGR00231. small_GTP. 1 hit.
PROSITE	PS51421. RAS. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	979825.
PMAP-CutDB	P01120.

Entry information

Entry name

RAS2_YEAST

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal 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

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents