Reviewed, UniProtKB/Swiss-Prot P01120 (RAS2_YEAST)

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 (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	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. Ref.16
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
Gene Ontology (GO)
Biological process	Ras protein signal transduction Traceable author statement. Source: SGD activation of adenylate cyclase activity Traceable author statement. Source: SGD ascospore formation Inferred from mutant phenotype. Source: SGD positive regulation of transcription by galactose Inferred from mutant phenotype. Source: SGD pseudohyphal growth Inferred from mutant phenotype. Source: SGD replicative cell aging Inferred from mutant phenotype. Source: SGD
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell intracellular Inferred from electronic annotation. Source: InterPro plasma membrane Inferred from direct assay. Source: SGD plasma membrane enriched fraction Inferred from direct assay. Source: SGD
Molecular function	GTP binding Inferred from direct assay. Source: SGD GTPase activity Traceable author statement. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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

	Sequence		Length	Mass (Da)
	P01120-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 6CAAAC531EEAE92F	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

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: 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. , 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: 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
EMBLGenBankDDBJ	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

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	December 15, 2009
This is version 119 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)