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Protein

Ras-like protein 2

Gene

RAS2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The S.cerevisiae Ras proteins modulate the activity of the adenylate cyclase catalytic subunit and therefore affect the biosynthesis of cyclic-AMP.

Enzyme regulationi

Alternates 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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi17 – 248GTPBy similarity
Nucleotide bindingi64 – 685GTPBy similarity
Nucleotide bindingi123 – 1264GTPBy similarity

GO - Molecular functioni

  • GTPase activity Source: SGD
  • GTP binding Source: SGD

GO - Biological processi

  • activation of adenylate cyclase activity Source: SGD
  • ascospore formation Source: SGD
  • CVT pathway Source: SGD
  • macroautophagy Source: SGD
  • nucleocytoplasmic transport Source: InterPro
  • positive regulation of adenylate cyclase activity Source: SGD
  • positive regulation of pseudohyphal growth Source: SGD
  • positive regulation of transcription by galactose Source: SGD
  • protein localization to bud neck Source: SGD
  • regulation of protein localization Source: SGD
  • replicative cell aging Source: SGD
  • small GTPase mediated signal transduction Source: InterPro
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33126-MONOMER.
ReactomeiR-SCE-1445148. Translocation of GLUT4 to the plasma membrane.
R-SCE-171007. p38MAPK events.
R-SCE-5218921. VEGFR2 mediated cell proliferation.
R-SCE-5658442. Regulation of RAS by GAPs.
R-SCE-5673001. RAF/MAP kinase cascade.
R-SCE-5675221. Negative regulation of MAPK pathway.
R-SCE-8849471. PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-like protein 2
Gene namesi
Name:RAS2
Synonyms:ASC1, CTN5, GLC5
Ordered Locus Names:YNL098C
ORF Names:N2198
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL098C.
SGDiS000005042. RAS2.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: SGD
  • mitochondrion Source: SGD
  • nucleus Source: SGD
  • plasma membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi19 – 191G → V: Low sporulation efficiency. 1 Publication
Mutagenesisi70 – 701E → K in GLC5-1; low glycogen accumulation and sporulation deficiency. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 319318Ras-like protein 2PRO_0000030195Add
BLAST
Propeptidei320 – 3223Removed in mature formPRO_0000030196

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei198 – 1981PhosphoserineCombined sources
Modified residuei202 – 2021PhosphoserineCombined sources
Modified residuei207 – 2071PhosphoserineCombined sources
Modified residuei214 – 2141PhosphoserineCombined sources
Modified residuei235 – 2351PhosphoserineCombined sources
Modified residuei238 – 2381PhosphoserineCombined sources
Lipidationi318 – 3181S-palmitoyl cysteine1 Publication
Modified residuei319 – 3191Cysteine methyl ester2 Publications
Lipidationi319 – 3191S-farnesyl cysteine1 Publication

Post-translational modificationi

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.4 Publications
Palmitoylated by the ERF2-SHR5 complex, which is required for proper plasma membrane localization of RAS2.1 Publication

Keywords - PTMi

Lipoprotein, Methylation, Palmitate, Phosphoprotein, Prenylation

Proteomic databases

MaxQBiP01120.
PeptideAtlasiP01120.

PTM databases

iPTMnetiP01120.
SwissPalmiP01120.

Miscellaneous databases

PMAP-CutDBP01120.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC25P048212EBI-14838,EBI-4237
LTE1P078665EBI-14838,EBI-10243
RAF1P040492EBI-14838,EBI-365996From a different organism.

Protein-protein interaction databases

BioGridi35725. 282 interactions.
DIPiDIP-2263N.
IntActiP01120. 9 interactions.
MINTiMINT-688754.

Structurei

3D structure databases

ProteinModelPortaliP01120.
SMRiP01120. Positions 10-172.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi39 – 479Effector region

Sequence similaritiesi

Belongs to the small GTPase superfamily. Ras family.Curated

Phylogenomic databases

GeneTreeiENSGT00780000121849.
HOGENOMiHOG000233973.
InParanoidiP01120.
KOiK07827.
OMAiNKSNIRE.
OrthoDBiEOG7H1JXN.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERiPTHR24070. PTHR24070. 1 hit.
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51421. RAS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P01120-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLNKSNIRE YKLVVVGGGG VGKSALTIQL TQSHFVDEYD PTIEDSYRKQ
60 70 80 90 100
VVIDDEVSIL DILDTAGQEE YSAMREQYMR NGEGFLLVYS ITSKSSLDEL
110 120 130 140 150
MTYYQQILRV KDTDYVPIVV VGNKSDLENE KQVSYQDGLN MAKQMNAPFL
160 170 180 190 200
ETSAKQAINV EEAFYTLARL VRDEGGKYNK TLTENDNSKQ TSQDTKGSGA
210 220 230 240 250
NSVPRNSGGH RKMSNAANGK NVNSSTTVVN ARNASIESKT GLAGNQATNG
260 270 280 290 300
KTQTDRTNID NSTGQAGQAN AQSANTVNNR VNNNSKAGQV SNAKQARKQQ
310 320
AAPGGNTSEA SKSGSGGCCI IS
Length:322
Mass (Da):34,705
Last modified:January 23, 2007 - v4
Checksum:i6CAAAC531EEAE92F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti108 – 1081L → P in CAA25207 (PubMed:6328429).Curated
Sequence conflicti210 – 2101H → L in CAA25207 (PubMed:6328429).Curated
Sequence conflicti255 – 2551D → V in AAA34959 (PubMed:6365329).Curated
Sequence conflicti298 – 2992KQ → SK in CAA25207 (PubMed:6328429).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS58254. TVBYR2.
RefSeqiNP_014301.1. NM_001182936.1.

Genome annotation databases

EnsemblFungiiYNL098C; YNL098C; YNL098C.
GeneIDi855625.
KEGGisce:YNL098C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS58254. TVBYR2.
RefSeqiNP_014301.1. NM_001182936.1.

3D structure databases

ProteinModelPortaliP01120.
SMRiP01120. Positions 10-172.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35725. 282 interactions.
DIPiDIP-2263N.
IntActiP01120. 9 interactions.
MINTiMINT-688754.

PTM databases

iPTMnetiP01120.
SwissPalmiP01120.

Proteomic databases

MaxQBiP01120.
PeptideAtlasiP01120.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL098C; YNL098C; YNL098C.
GeneIDi855625.
KEGGisce:YNL098C.

Organism-specific databases

EuPathDBiFungiDB:YNL098C.
SGDiS000005042. RAS2.

Phylogenomic databases

GeneTreeiENSGT00780000121849.
HOGENOMiHOG000233973.
InParanoidiP01120.
KOiK07827.
OMAiNKSNIRE.
OrthoDBiEOG7H1JXN.

Enzyme and pathway databases

BioCyciYEAST:G3O-33126-MONOMER.
ReactomeiR-SCE-1445148. Translocation of GLUT4 to the plasma membrane.
R-SCE-171007. p38MAPK events.
R-SCE-5218921. VEGFR2 mediated cell proliferation.
R-SCE-5658442. Regulation of RAS by GAPs.
R-SCE-5673001. RAF/MAP kinase cascade.
R-SCE-5675221. Negative regulation of MAPK pathway.
R-SCE-8849471. PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.

Miscellaneous databases

PMAP-CutDBP01120.
PROiP01120.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERiPTHR24070. PTHR24070. 1 hit.
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51421. RAS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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 204508 / S288c.
  7. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  8. 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: PROTEIN SEQUENCE OF 2-22 AND 313-319, CLEAVAGE OF INITIATOR METHIONINE, CLEAVAGE OF C-TERMINAL PROPEPTIDE, PALMITOYLATION AT CYS-318.
  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-319.
  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 AT CYS-319 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. 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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235 AND SER-238, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198; SER-202; SER-207 AND SER-214, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214; SER-235 AND SER-238, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRAS2_YEAST
AccessioniPrimary (citable) accession number: P01120
Secondary accession number(s): D6W181, Q45U01
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 183 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.