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Ras-like protein 2

 RAS2_YEAST              Reviewed;         322 AA.
P01120; D6W181; Q45U01;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
12-SEP-2018, entry version 204.
RecName: Full=Ras-like protein 2;
Flags: Precursor;
Name=RAS2; Synonyms=ASC1, CTN5, GLC5; OrderedLocusNames=YNL098C;
ORFNames=N2198;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6365329; DOI=10.1016/0092-8674(84)90340-4;
Powers S., Kataoka T., Fasano O., Goldfarb M., Strathern J.,
Broach J., Wigler M.;
"Genes in S. cerevisiae encoding proteins with domains homologous to
the mammalian ras proteins.";
Cell 36:607-612(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6328429; DOI=10.1093/nar/12.8.3611;
Dhar R., Nieto A., Koller R., DeFeo-Jones D., Scolnick E.M.;
"Nucleotide sequence of two rasH related-genes isolated from the yeast
Saccharomyces cerevisiae.";
Nucleic Acids Res. 12:3611-3618(1984).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 64665 / S288c / DC5;
PubMed=10744740; DOI=10.1074/jbc.275.14.10492;
Mabuchi T., Ichimura Y., Takeda M., Douglas M.G.;
"ASC1/RAS2 suppresses the growth-defect on glycerol caused by the
atp1-2 mutation in the yeast Saccharomyces cerevisiae.";
J. Biol. Chem. 275:10492-10497(2000).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=SK1;
Deutschbauer A.M., Davis R.W.;
"Molecular genetic dissection of a quantitative trait in yeast.";
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=8701612;
DOI=10.1002/(SICI)1097-0061(19960330)12:4<403::AID-YEA923>3.3.CO;2-8;
Saiz J.E., Buitrago M.J., Soler A., del Rey F., Revuelta J.L.;
"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.";
Yeast 12:403-409(1996).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169873;
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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV
and its evolutionary implications.";
Nature 387:93-98(1997).
[7]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[8]
MUTAGENESIS OF GLY-19.
PubMed=6327067; DOI=10.1016/0092-8674(84)90374-X;
Kataoka T., Powers S., McGill C., Fasano O., Strathern J., Broach J.,
Wigler M.;
"Genetic analysis of yeast RAS1 and RAS2 genes.";
Cell 37:437-445(1984).
[9]
PROTEIN SEQUENCE OF 2-22 AND 313-319, CLEAVAGE OF INITIATOR
METHIONINE, CLEAVAGE OF C-TERMINAL PROPEPTIDE, AND PALMITOYLATION AT
CYS-318.
PubMed=2406252;
Fujiyama A., Tamanoi F.;
"RAS2 protein of Saccharomyces cerevisiae undergoes removal of
methionine at N-terminus and removal of three amino acids at C
terminus.";
J. Biol. Chem. 265:3362-3368(1990).
[10]
METHYLATION AT CYS-319.
PubMed=2663844;
Deschenes R.J., Stimmel J.B., Clarke S., Stock J., Broach J.R.;
"RAS2 protein of Saccharomyces cerevisiae is methyl-esterified at its
carboxyl terminus.";
J. Biol. Chem. 264:11865-11873(1989).
[11]
METHYLATION AT CYS-319 BY STE14.
PubMed=2050108;
Hrycyna C.A., Sapperstein S.K., Clarke S., Michaelis S.;
"The Saccharomyces cerevisiae STE14 gene encodes a methyltransferase
that mediates C-terminal methylation of a-factor and RAS proteins.";
EMBO J. 10:1699-1709(1991).
[12]
POST-TRANSLATIONAL MODIFICATIONS.
PubMed=1917931;
Fujiyama A., Tsunasawa S., Tamanoi F., Sakiyama F.;
"S-farnesylation and methyl esterification of C-terminal domain of
yeast RAS2 protein prior to fatty acid acylation.";
J. Biol. Chem. 266:17926-17931(1991).
[13]
ISOPRENYLATION AT CYS-319 BY RAM1-RAM2.
PubMed=1763050; DOI=10.1073/pnas.88.24.11373;
He B., Chen P., Chen S.-Y., Vancura K.L., Michaelis S., Powers S.;
"RAM2, an essential gene of yeast, and RAM1 encode the two polypeptide
components of the farnesyltransferase that prenylates a-factor and Ras
proteins.";
Proc. Natl. Acad. Sci. U.S.A. 88:11373-11377(1991).
[14]
MUTAGENESIS OF GLU-70.
PubMed=8150278;
Cannon J.F., Pringle J.R., Fiechter A., Khalil M.;
"Characterization of glycogen-deficient glc mutants of Saccharomyces
cerevisiae.";
Genetics 136:485-503(1994).
[15]
PROTEOLYTIC PROCESSING BY RCE1.
PubMed=9065405; DOI=10.1126/science.275.5307.1796;
Boyartchuk V.L., Ashby M.N., Rine J.;
"Modulation of Ras and a-factor function by carboxyl-terminal
proteolysis.";
Science 275:1796-1800(1997).
[16]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235 AND SER-238, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=YAL6B;
PubMed=15665377; DOI=10.1074/mcp.M400219-MCP200;
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,
Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone
signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198; SER-202; SER-207
AND SER-214, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=17287358; DOI=10.1073/pnas.0607084104;
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.;
"Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass
spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214; SER-235 AND
SER-238, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[23]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-131, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
-!- FUNCTION: The S.cerevisiae Ras proteins modulate the activity of
the adenylate cyclase catalytic subunit and therefore affect the
biosynthesis of cyclic-AMP.
-!- ACTIVITY REGULATION: 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.
-!- INTERACTION:
P04821:CDC25; NbExp=2; IntAct=EBI-14838, EBI-4237;
P07866:LTE1; NbExp=5; IntAct=EBI-14838, EBI-10243;
P04049:RAF1 (xeno); NbExp=2; IntAct=EBI-14838, EBI-365996;
-!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor.
-!- PTM: 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.
{ECO:0000269|PubMed:2050108, ECO:0000269|PubMed:2406252,
ECO:0000269|PubMed:2663844, ECO:0000269|PubMed:9065405}.
-!- PTM: Palmitoylated by the ERF2-SHR5 complex, which is required for
proper plasma membrane localization of RAS2.
{ECO:0000269|PubMed:2406252}.
-!- 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.
-!- MISCELLANEOUS: Present with 19800 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
{ECO:0000305}.
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EMBL; K01971; AAA34959.1; -; Genomic_DNA.
EMBL; X00528; CAA25207.1; -; Genomic_DNA.
EMBL; D37950; BAA22510.1; -; Genomic_DNA.
EMBL; DQ115393; AAZ22509.1; -; Genomic_DNA.
EMBL; Z50161; CAA90528.1; -; Genomic_DNA.
EMBL; Z71374; CAA95974.1; -; Genomic_DNA.
EMBL; BK006947; DAA10447.1; -; Genomic_DNA.
PIR; S58254; TVBYR2.
RefSeq; NP_014301.1; NM_001182936.1.
ProteinModelPortal; P01120; -.
SMR; P01120; -.
BioGrid; 35725; 449.
DIP; DIP-2263N; -.
IntAct; P01120; 13.
MINT; P01120; -.
STRING; 4932.YNL098C; -.
BindingDB; P01120; -.
iPTMnet; P01120; -.
SwissPalm; P01120; -.
MaxQB; P01120; -.
PaxDb; P01120; -.
PRIDE; P01120; -.
EnsemblFungi; YNL098C; YNL098C; YNL098C.
GeneID; 855625; -.
KEGG; sce:YNL098C; -.
EuPathDB; FungiDB:YNL098C; -.
SGD; S000005042; RAS2.
GeneTree; ENSGT00860000133672; -.
HOGENOM; HOG000233973; -.
InParanoid; P01120; -.
KO; K07827; -.
OMA; SGCCIIC; -.
OrthoDB; EOG092C4VY0; -.
BioCyc; YEAST:G3O-33126-MONOMER; -.
Reactome; R-SCE-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
Reactome; R-SCE-171007; p38MAPK events.
Reactome; R-SCE-5218921; VEGFR2 mediated cell proliferation.
Reactome; R-SCE-5658442; Regulation of RAS by GAPs.
Reactome; R-SCE-5673001; RAF/MAP kinase cascade.
Reactome; R-SCE-5675221; Negative regulation of MAPK pathway.
Reactome; R-SCE-6798695; Neutrophil degranulation.
Reactome; R-SCE-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
PMAP-CutDB; P01120; -.
PRO; PR:P01120; -.
Proteomes; UP000002311; Chromosome XIV.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
GO; GO:0005739; C:mitochondrion; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0005886; C:plasma membrane; IDA:SGD.
GO; GO:0005525; F:GTP binding; IDA:SGD.
GO; GO:0003924; F:GTPase activity; IDA:SGD.
GO; GO:0007190; P:activation of adenylate cyclase activity; IDA:SGD.
GO; GO:0030437; P:ascospore formation; IMP:SGD.
GO; GO:0016236; P:macroautophagy; IGI:SGD.
GO; GO:0045762; P:positive regulation of adenylate cyclase activity; IGI:SGD.
GO; GO:2000222; P:positive regulation of pseudohyphal growth; IMP:SGD.
GO; GO:0000411; P:positive regulation of transcription by galactose; IMP:SGD.
GO; GO:0032258; P:protein localization by the Cvt pathway; IMP:SGD.
GO; GO:0097271; P:protein localization to bud neck; IGI:SGD.
GO; GO:0010603; P:regulation of cytoplasmic mRNA processing body assembly; IMP:SGD.
GO; GO:0032880; P:regulation of protein localization; IMP:SGD.
GO; GO:0001302; P:replicative cell aging; IMP:SGD.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
InterPro; IPR020849; Small_GTPase_Ras-type.
PANTHER; PTHR24070; PTHR24070; 1.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51421; RAS; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Direct protein sequencing;
GTP-binding; Isopeptide bond; Lipoprotein; Membrane; Methylation;
Nucleotide-binding; Palmitate; Phosphoprotein; Prenylation;
Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:2406252}.
CHAIN 2 319 Ras-like protein 2.
/FTId=PRO_0000030195.
PROPEP 320 322 Removed in mature form.
/FTId=PRO_0000030196.
NP_BIND 17 24 GTP. {ECO:0000250}.
NP_BIND 64 68 GTP. {ECO:0000250}.
NP_BIND 123 126 GTP. {ECO:0000250}.
MOTIF 39 47 Effector region.
MOD_RES 198 198 Phosphoserine.
{ECO:0000244|PubMed:17287358}.
MOD_RES 202 202 Phosphoserine.
{ECO:0000244|PubMed:17287358,
ECO:0000244|PubMed:18407956}.
MOD_RES 207 207 Phosphoserine.
{ECO:0000244|PubMed:17287358}.
MOD_RES 214 214 Phosphoserine.
{ECO:0000244|PubMed:17287358,
ECO:0000244|PubMed:19779198}.
MOD_RES 235 235 Phosphoserine.
{ECO:0000244|PubMed:15665377,
ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
MOD_RES 238 238 Phosphoserine.
{ECO:0000244|PubMed:15665377,
ECO:0000244|PubMed:19779198}.
MOD_RES 319 319 Cysteine methyl ester.
{ECO:0000269|PubMed:2050108,
ECO:0000269|PubMed:2663844}.
LIPID 318 318 S-palmitoyl cysteine.
{ECO:0000269|PubMed:2406252}.
LIPID 319 319 S-farnesyl cysteine.
{ECO:0000269|PubMed:1763050}.
CROSSLNK 131 131 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
MUTAGEN 19 19 G->V: Low sporulation efficiency.
{ECO:0000269|PubMed:6327067}.
MUTAGEN 70 70 E->K: In GLC5-1; low glycogen
accumulation and sporulation deficiency.
{ECO:0000269|PubMed:8150278}.
CONFLICT 108 108 L -> P (in Ref. 2; CAA25207).
{ECO:0000305}.
CONFLICT 210 210 H -> L (in Ref. 2; CAA25207).
{ECO:0000305}.
CONFLICT 255 255 D -> V (in Ref. 1; AAA34959).
{ECO:0000305}.
CONFLICT 298 299 KQ -> SK (in Ref. 2; CAA25207).
{ECO:0000305}.
SEQUENCE 322 AA; 34705 MW; 6CAAAC531EEAE92F CRC64;
MPLNKSNIRE YKLVVVGGGG VGKSALTIQL TQSHFVDEYD PTIEDSYRKQ VVIDDEVSIL
DILDTAGQEE YSAMREQYMR NGEGFLLVYS ITSKSSLDEL MTYYQQILRV KDTDYVPIVV
VGNKSDLENE KQVSYQDGLN MAKQMNAPFL ETSAKQAINV EEAFYTLARL VRDEGGKYNK
TLTENDNSKQ TSQDTKGSGA NSVPRNSGGH RKMSNAANGK NVNSSTTVVN ARNASIESKT
GLAGNQATNG KTQTDRTNID NSTGQAGQAN AQSANTVNNR VNNNSKAGQV SNAKQARKQQ
AAPGGNTSEA SKSGSGGCCI IS


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EIAAB33912 E3 ubiquitin-protein ligase RBBP6,Mouse,Mus musculus,P2pr,p53-associated cellular protein of testis,Pact,Proliferation potential-related protein,Protein P2P-R,Rbbp6,Retinoblastoma-binding protein 6
EIAAB38162 Homo sapiens,Human,MAP,Merlin-associated protein,RabGAPLP,RABGAPLP,Rab-GTPase-activating protein-like protein,RUN and TBC1 domain-containing protein 3,RUTBC3,SGSM3,Small G protein signaling modulator
EIAAB29908 Cap1,Contraception-associated protein 1,Fertility protein SP22,Park7,Parkinson disease protein 7 homolog,Protein CAP1,Protein DJ-1,Rat,Rattus norvegicus
EIAAB31031 DDXBP1,DEAD_H box-binding protein 1,E3 SUMO-protein ligase PIAS1,GBP,Gu-binding protein,Homo sapiens,Human,PIAS1,Protein inhibitor of activated STAT protein 1,RNA helicase II-binding protein


 

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