RAS2_YEAST
ID RAS2_YEAST Reviewed; 322 AA.
AC P01120; D6W181; Q45U01;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 228.
DE RecName: Full=Ras-like protein 2;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P01112};
DE Flags: Precursor;
GN Name=RAS2; Synonyms=ASC1, CTN5, GLC5; OrderedLocusNames=YNL098C;
GN ORFNames=N2198;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6365329; DOI=10.1016/0092-8674(84)90340-4;
RA Powers S., Kataoka T., Fasano O., Goldfarb M., Strathern J., Broach J.,
RA Wigler M.;
RT "Genes in S. cerevisiae encoding proteins with domains homologous to the
RT mammalian ras proteins.";
RL Cell 36:607-612(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6328429; DOI=10.1093/nar/12.8.3611;
RA Dhar R., Nieto A., Koller R., DeFeo-Jones D., Scolnick E.M.;
RT "Nucleotide sequence of two rasH related-genes isolated from the yeast
RT Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 12:3611-3618(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 64665 / S288c / DC5;
RX PubMed=10744740; DOI=10.1074/jbc.275.14.10492;
RA Mabuchi T., Ichimura Y., Takeda M., Douglas M.G.;
RT "ASC1/RAS2 suppresses the growth-defect on glycerol caused by the atp1-2
RT mutation in the yeast Saccharomyces cerevisiae.";
RL J. Biol. Chem. 275:10492-10497(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SK1;
RA Deutschbauer A.M., Davis R.W.;
RT "Molecular genetic dissection of a quantitative trait in yeast.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8701612;
RX DOI=10.1002/(sici)1097-0061(19960330)12:4<403::aid-yea923>3.0.co;2-h;
RA Saiz J.E., Buitrago M.J., Soler A., del Rey F., Revuelta J.L.;
RT "The sequence of a 21.3 kb DNA fragment from the left arm of yeast
RT chromosome XIV reveals LEU4, MET4, POL1, RAS2, and six new open reading
RT frames.";
RL Yeast 12:403-409(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [7]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [8]
RP MUTAGENESIS OF GLY-19.
RX PubMed=6327067; DOI=10.1016/0092-8674(84)90374-x;
RA Kataoka T., Powers S., McGill C., Fasano O., Strathern J., Broach J.,
RA Wigler M.;
RT "Genetic analysis of yeast RAS1 and RAS2 genes.";
RL Cell 37:437-445(1984).
RN [9]
RP PROTEIN SEQUENCE OF 2-22 AND 313-319, CLEAVAGE OF INITIATOR METHIONINE,
RP CLEAVAGE OF C-TERMINAL PROPEPTIDE, AND PALMITOYLATION AT CYS-318.
RX PubMed=2406252; DOI=10.1016/s0021-9258(19)39776-5;
RA Fujiyama A., Tamanoi F.;
RT "RAS2 protein of Saccharomyces cerevisiae undergoes removal of methionine
RT at N-terminus and removal of three amino acids at C terminus.";
RL J. Biol. Chem. 265:3362-3368(1990).
RN [10]
RP METHYLATION AT CYS-319.
RX PubMed=2663844; DOI=10.1016/s0021-9258(18)80146-6;
RA Deschenes R.J., Stimmel J.B., Clarke S., Stock J., Broach J.R.;
RT "RAS2 protein of Saccharomyces cerevisiae is methyl-esterified at its
RT carboxyl terminus.";
RL J. Biol. Chem. 264:11865-11873(1989).
RN [11]
RP METHYLATION AT CYS-319 BY STE14.
RX PubMed=2050108; DOI=10.1002/j.1460-2075.1991.tb07694.x;
RA Hrycyna C.A., Sapperstein S.K., Clarke S., Michaelis S.;
RT "The Saccharomyces cerevisiae STE14 gene encodes a methyltransferase that
RT mediates C-terminal methylation of a-factor and RAS proteins.";
RL EMBO J. 10:1699-1709(1991).
RN [12]
RP POST-TRANSLATIONAL MODIFICATIONS.
RX PubMed=1917931; DOI=10.1016/s0021-9258(18)55216-9;
RA Fujiyama A., Tsunasawa S., Tamanoi F., Sakiyama F.;
RT "S-farnesylation and methyl esterification of C-terminal domain of yeast
RT RAS2 protein prior to fatty acid acylation.";
RL J. Biol. Chem. 266:17926-17931(1991).
RN [13]
RP ISOPRENYLATION AT CYS-319 BY RAM1-RAM2.
RX PubMed=1763050; DOI=10.1073/pnas.88.24.11373;
RA He B., Chen P., Chen S.-Y., Vancura K.L., Michaelis S., Powers S.;
RT "RAM2, an essential gene of yeast, and RAM1 encode the two polypeptide
RT components of the farnesyltransferase that prenylates a-factor and Ras
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:11373-11377(1991).
RN [14]
RP MUTAGENESIS OF GLU-70.
RX PubMed=8150278; DOI=10.1093/genetics/136.2.485;
RA Cannon J.F., Pringle J.R., Fiechter A., Khalil M.;
RT "Characterization of glycogen-deficient glc mutants of Saccharomyces
RT cerevisiae.";
RL Genetics 136:485-503(1994).
RN [15]
RP PROTEOLYTIC PROCESSING BY RCE1.
RX PubMed=9065405; DOI=10.1126/science.275.5307.1796;
RA Boyartchuk V.L., Ashby M.N., Rine J.;
RT "Modulation of Ras and a-factor function by carboxyl-terminal
RT proteolysis.";
RL Science 275:1796-1800(1997).
RN [16]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235 AND SER-238, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198; SER-202; SER-207 AND
RP SER-214, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214; SER-235 AND SER-238, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [23]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-131, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: The S.cerevisiae Ras proteins modulate the activity of the
CC adenylate cyclase catalytic subunit and therefore affect the
CC biosynthesis of cyclic-AMP.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000250|UniProtKB:P01112};
CC -!- ACTIVITY REGULATION: Alternates between an inactive form bound to GDP
CC and an active form bound to GTP. Activated by guanine nucleotide-
CC exchange factor (GEF) CDC25 and inactivated by GTPase-activating
CC proteins (GAPs) IRA1 and IRA2.
CC -!- INTERACTION:
CC P01120; P04821: CDC25; NbExp=2; IntAct=EBI-14838, EBI-4237;
CC P01120; P07866: LTE1; NbExp=5; IntAct=EBI-14838, EBI-10243;
CC P01120; P39109: YCF1; NbExp=2; IntAct=EBI-14838, EBI-21779;
CC P01120; P04049: RAF1; Xeno; NbExp=2; IntAct=EBI-14838, EBI-365996;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor.
CC -!- PTM: Farnesylated by RAM1-RAM2, which is required for targeting RAS2 to
CC the cytoplasmic site of the endoplasmic reticulum, where proteolytic
CC processing of the C-terminus by RCE1 and methylation of the resulting
CC carboxyl group by STE14 occurs. {ECO:0000269|PubMed:2050108,
CC ECO:0000269|PubMed:2406252, ECO:0000269|PubMed:2663844,
CC ECO:0000269|PubMed:9065405}.
CC -!- PTM: Palmitoylated by the ERF2-SHR5 complex, which is required for
CC proper plasma membrane localization of RAS2.
CC {ECO:0000269|PubMed:2406252}.
CC -!- MISCELLANEOUS: RAS2 is necessary for a normal response to nutrient
CC limitations, in general, disruption of the RAS2 locus results in an
CC overall premature starvation response.
CC -!- MISCELLANEOUS: Present with 19800 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; K01971; AAA34959.1; -; Genomic_DNA.
DR EMBL; X00528; CAA25207.1; -; Genomic_DNA.
DR EMBL; D37950; BAA22510.1; -; Genomic_DNA.
DR EMBL; DQ115393; AAZ22509.1; -; Genomic_DNA.
DR EMBL; Z50161; CAA90528.1; -; Genomic_DNA.
DR EMBL; Z71374; CAA95974.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10447.1; -; Genomic_DNA.
DR PIR; S58254; TVBYR2.
DR RefSeq; NP_014301.1; NM_001182936.1.
DR AlphaFoldDB; P01120; -.
DR SMR; P01120; -.
DR BioGRID; 35725; 466.
DR DIP; DIP-2263N; -.
DR IntAct; P01120; 16.
DR MINT; P01120; -.
DR STRING; 4932.YNL098C; -.
DR BindingDB; P01120; -.
DR TCDB; 8.A.92.1.15; the g-protein AlphaBetaGama complex (gpc) family.
DR iPTMnet; P01120; -.
DR SwissPalm; P01120; -.
DR MaxQB; P01120; -.
DR PaxDb; P01120; -.
DR PRIDE; P01120; -.
DR EnsemblFungi; YNL098C_mRNA; YNL098C; YNL098C.
DR GeneID; 855625; -.
DR KEGG; sce:YNL098C; -.
DR SGD; S000005042; RAS2.
DR VEuPathDB; FungiDB:YNL098C; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000176617; -.
DR HOGENOM; CLU_041217_9_0_1; -.
DR InParanoid; P01120; -.
DR OMA; MXNAANG; -.
DR BioCyc; YEAST:G3O-33126-MON; -.
DR Reactome; R-SCE-9696273; RND1 GTPase cycle.
DR PRO; PR:P01120; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P01120; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0019003; F:GDP binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IDA:SGD.
DR GO; GO:0003924; F:GTPase activity; IDA:SGD.
DR GO; GO:0007190; P:activation of adenylate cyclase activity; IDA:SGD.
DR GO; GO:0030437; P:ascospore formation; IMP:SGD.
DR GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IMP:SGD.
DR GO; GO:0016236; P:macroautophagy; IGI:SGD.
DR GO; GO:0045762; P:positive regulation of adenylate cyclase activity; IGI:SGD.
DR GO; GO:2000222; P:positive regulation of pseudohyphal growth; IMP:SGD.
DR GO; GO:0000411; P:positive regulation of transcription by galactose; IMP:SGD.
DR GO; GO:0097271; P:protein localization to bud neck; IGI:SGD.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:0010603; P:regulation of cytoplasmic mRNA processing body assembly; IMP:SGD.
DR GO; GO:0032880; P:regulation of protein localization; IMP:SGD.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR020849; Small_GTPase_Ras-type.
DR PANTHER; PTHR24070; PTHR24070; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51421; RAS; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; GTP-binding; Hydrolase;
KW Isopeptide bond; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW Palmitate; Phosphoprotein; Prenylation; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2406252"
FT CHAIN 2..319
FT /note="Ras-like protein 2"
FT /id="PRO_0000030195"
FT PROPEP 320..322
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:2406252"
FT /id="PRO_0000030196"
FT REGION 178..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 39..47
FT /note="Effector region"
FT COMPBIAS 181..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 20..25
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT BINDING 36..42
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT BINDING 66..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT BINDING 123..126
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT BINDING 153..155
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 319
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000269|PubMed:2050108,
FT ECO:0000269|PubMed:2663844"
FT LIPID 318
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:2406252"
FT LIPID 319
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:1763050"
FT CROSSLNK 131
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 19
FT /note="G->V: Low sporulation efficiency."
FT /evidence="ECO:0000269|PubMed:6327067"
FT MUTAGEN 70
FT /note="E->K: In GLC5-1; low glycogen accumulation and
FT sporulation deficiency."
FT /evidence="ECO:0000269|PubMed:8150278"
FT CONFLICT 108
FT /note="L -> P (in Ref. 2; CAA25207)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="H -> L (in Ref. 2; CAA25207)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="D -> V (in Ref. 1; AAA34959)"
FT /evidence="ECO:0000305"
FT CONFLICT 298..299
FT /note="KQ -> SK (in Ref. 2; CAA25207)"
FT /evidence="ECO:0000305"
SQ 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
