GBLP_YEAST
ID GBLP_YEAST Reviewed; 319 AA.
AC P38011; D6VZT9; Q6LAA5;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Guanine nucleotide-binding protein subunit beta-like protein;
DE AltName: Full=Receptor for activated C kinase;
DE AltName: Full=Receptor of activated protein kinase C 1;
DE Short=RACK1;
DE AltName: Full=Small ribosomal subunit protein RACK1 {ECO:0000303|PubMed:24524803};
GN Name=ASC1 {ECO:0000303|PubMed:15012629}; Synonyms=CPC2;
GN OrderedLocusNames=YMR116C {ECO:0000312|SGD:S000004722};
GN ORFNames=YM9718.15C {ECO:0000312|SGD:S000004722};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
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 [3]
RP PROTEIN SEQUENCE OF 2-10; 47-59; 91-102; 138-155; 217-228 AND 262-311,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RA Bienvenut W.V., Peters C.;
RL Submitted (MAY-2005) to UniProtKB.
RN [4]
RP PROTEIN SEQUENCE OF 54-62.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7895733; DOI=10.1002/elps.11501501210;
RA Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B.,
RA Volpe T., Warner J.R., McLaughlin C.S.;
RT "Protein identifications for a Saccharomyces cerevisiae protein database.";
RL Electrophoresis 15:1466-1486(1994).
RN [5]
RP PROTEIN SEQUENCE OF 63-70 AND 138-149.
RC STRAIN=ATCC 44827 / SKQ2N;
RX PubMed=9038161; DOI=10.1074/jbc.272.9.5544;
RA Norbeck J., Blomberg A.;
RT "Metabolic and regulatory changes associated with growth of Saccharomyces
RT cerevisiae in 1.4 M NaCl. Evidence for osmotic induction of glycerol
RT dissimilation via the dihydroxyacetone pathway.";
RL J. Biol. Chem. 272:5544-5554(1997).
RN [6]
RP PROTEIN SEQUENCE OF 91-102; 162-176; 217-228 AND 250-261, INTERACTION WITH
RP SCP160, AND SUBUNIT.
RX PubMed=15012629; DOI=10.1042/bj20031962;
RA Baum S., Bittins M., Frey S., Seedorf M.;
RT "Asc1p, a WD40-domain containing adaptor protein, is required for the
RT interaction of the RNA-binding protein Scp160p with polysomes.";
RL Biochem. J. 380:823-830(2004).
RN [7]
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 [8]
RP FUNCTION, AND SUBUNIT.
RX PubMed=15340087; DOI=10.1128/mcb.24.18.8276-8287.2004;
RA Gerbasi V.R., Weaver C.M., Hill S., Friedman D.B., Link A.J.;
RT "Yeast Asc1p and mammalian RACK1 are functionally orthologous core 40S
RT ribosomal proteins that repress gene expression.";
RL Mol. Cell. Biol. 24:8276-8287(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-96, AND IDENTIFICATION BY
RP 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 [10]
RP IDENTIFICATION BY 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-168, AND IDENTIFICATION BY
RP 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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [13]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-46; LYS-53; LYS-107; LYS-137
RP AND LYS-161, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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).
RN [14]
RP NOMENCLATURE.
RX PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
RA Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
RA Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
RA Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
RA Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
RA Williamson J.R., Wilson D., Yonath A., Yusupov M.;
RT "A new system for naming ribosomal proteins.";
RL Curr. Opin. Struct. Biol. 24:165-169(2014).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28223409; DOI=10.1261/rna.060897.117;
RA Sitron C.S., Park J.H., Brandman O.;
RT "Asc1, Hel2, and Slh1 couple translation arrest to nascent chain
RT degradation.";
RL RNA 23:798-810(2017).
RN [16]
RP 3D-STRUCTURE MODELING OF 1-114, ELECTRON MICROSCOPY, AND SUBUNIT.
RX PubMed=15334071; DOI=10.1038/nsmb822;
RA Sengupta J., Nilsson J., Gursky R., Spahn C.M., Nissen P., Frank J.;
RT "Identification of the versatile scaffold protein RACK1 on the eukaryotic
RT ribosome by cryo-EM.";
RL Nat. Struct. Mol. Biol. 11:957-962(2004).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS) OF 80S RIBOSOME.
RX PubMed=21109664; DOI=10.1126/science.1194294;
RA Ben-Shem A., Jenner L., Yusupova G., Yusupov M.;
RT "Crystal structure of the eukaryotic ribosome.";
RL Science 330:1203-1209(2010).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS), AND SUBUNIT.
RX PubMed=21704636; DOI=10.1016/j.jmb.2011.06.017;
RA Yatime L., Hein K.L., Nilsson J., Nissen P.;
RT "Structure of the RACK1 dimer from Saccharomyces cerevisiae.";
RL J. Mol. Biol. 411:486-498(2011).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 80S RIBOSOME, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=22096102; DOI=10.1126/science.1212642;
RA Ben-Shem A., Garreau de Loubresse N., Melnikov S., Jenner L., Yusupova G.,
RA Yusupov M.;
RT "The structure of the eukaryotic ribosome at 3.0 A resolution.";
RL Science 334:1524-1529(2011).
CC -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex
CC responsible for the synthesis of proteins in the cell. The small
CC ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the
CC encoded message by selecting cognate aminoacyl-transfer RNA (tRNA)
CC molecules. The large subunit (LSU) contains the ribosomal catalytic
CC site termed the peptidyl transferase center (PTC), which catalyzes the
CC formation of peptide bonds, thereby polymerizing the amino acids
CC delivered by tRNAs into a polypeptide chain. The nascent polypeptides
CC leave the ribosome through a tunnel in the LSU and interact with
CC protein factors that function in enzymatic processing, targeting, and
CC the membrane insertion of nascent chains at the exit of the ribosomal
CC tunnel (PubMed:22096102). Located at the head of the 40S ribosomal
CC subunit in the vicinity of the mRNA exit channel, RACK1 serves as a
CC scaffold protein that can recruit other proteins to the ribosome.
CC Involved in induction of the ribosome quality control (RQC) pathway; a
CC pathway that degrades nascent peptide chains during problematic
CC translation (PubMed:28223409). Involved in the negative regulation of
CC translation of a specific subset of proteins (PubMed:15340087).
CC {ECO:0000269|PubMed:15340087, ECO:0000305|PubMed:22096102}.
CC -!- SUBUNIT: Component of the small ribosomal subunit (SSU). Mature yeast
CC ribosomes consist of a small (40S) and a large (60S) subunit. The 40S
CC small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33
CC different proteins (encoded by 57 genes). The large 60S subunit
CC contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different
CC proteins (encoded by 81 genes). RACK1 is located at the head of the SSU
CC in the vicinity of the mRNA exit channel (PubMed:15340087,
CC PubMed:15334071, PubMed:22096102). RACK1 interacts with the mRNA-
CC binding protein SCP16 (PubMed:15012629). RACK1 also exists
CC simultaneously as a homodimer in a cytosolic non-ribosome-bound form
CC (PubMed:21704636). {ECO:0000269|PubMed:15012629,
CC ECO:0000269|PubMed:15334071, ECO:0000269|PubMed:15340087,
CC ECO:0000269|PubMed:21704636, ECO:0000269|PubMed:22096102}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}.
CC -!- DISRUPTION PHENOTYPE: Defective activation of the ribosome quality
CC control (RQC) pathway. {ECO:0000269|PubMed:28223409}.
CC -!- MISCELLANEOUS: Present with 333112 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the WD repeat G protein beta family. Ribosomal
CC protein RACK1 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA89753.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z49702; CAA89753.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z49702; CAA89754.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10013.1; -; Genomic_DNA.
DR PIR; S54578; S54578.
DR RefSeq; NP_013834.1; NM_001182616.1.
DR PDB; 1TRJ; EM; 11.70 A; A=1-314.
DR PDB; 3FRX; X-ray; 2.13 A; A/B/C/D=1-319.
DR PDB; 3J6X; EM; 6.10 A; RA=1-319.
DR PDB; 3J6Y; EM; 6.10 A; RA=1-319.
DR PDB; 3J77; EM; 6.20 A; RC=1-319.
DR PDB; 3J78; EM; 6.30 A; RC=1-319.
DR PDB; 3RFG; X-ray; 3.90 A; A/B=2-319.
DR PDB; 3RFH; X-ray; 2.90 A; A/B/C/D=2-319.
DR PDB; 4U3M; X-ray; 3.00 A; SR/sR=2-319.
DR PDB; 4U3N; X-ray; 3.20 A; SR/sR=2-319.
DR PDB; 4U3U; X-ray; 2.90 A; SR/sR=2-319.
DR PDB; 4U4N; X-ray; 3.10 A; SR/sR=2-319.
DR PDB; 4U4O; X-ray; 3.60 A; SR/sR=2-319.
DR PDB; 4U4Q; X-ray; 3.00 A; SR/sR=2-319.
DR PDB; 4U4R; X-ray; 2.80 A; SR/sR=2-319.
DR PDB; 4U4U; X-ray; 3.00 A; SR/sR=2-319.
DR PDB; 4U4Y; X-ray; 3.20 A; SR/sR=2-319.
DR PDB; 4U4Z; X-ray; 3.10 A; SR/sR=2-319.
DR PDB; 4U50; X-ray; 3.20 A; SR/sR=2-319.
DR PDB; 4U51; X-ray; 3.20 A; SR/sR=2-319.
DR PDB; 4U52; X-ray; 3.00 A; SR/sR=2-319.
DR PDB; 4U53; X-ray; 3.30 A; SR/sR=2-319.
DR PDB; 4U55; X-ray; 3.20 A; SR/sR=2-319.
DR PDB; 4U56; X-ray; 3.45 A; SR/sR=2-319.
DR PDB; 4U6F; X-ray; 3.10 A; SR/sR=2-319.
DR PDB; 4V6I; EM; 8.80 A; Aa=1-319.
DR PDB; 4V7R; X-ray; 4.00 A; AT/CT=1-319.
DR PDB; 4V88; X-ray; 3.00 A; Ag/Cg=1-319.
DR PDB; 4V8Y; EM; 4.30 A; A6=1-319.
DR PDB; 4V8Z; EM; 6.60 A; A6=1-319.
DR PDB; 4V92; EM; 3.70 A; g=4-318.
DR PDB; 5DAT; X-ray; 3.15 A; SR/sR=2-319.
DR PDB; 5DC3; X-ray; 3.25 A; SR/sR=2-319.
DR PDB; 5DGE; X-ray; 3.45 A; SR/sR=2-319.
DR PDB; 5DGF; X-ray; 3.30 A; SR/sR=2-319.
DR PDB; 5DGV; X-ray; 3.10 A; SR/sR=2-319.
DR PDB; 5FCI; X-ray; 3.40 A; SR/sR=2-319.
DR PDB; 5FCJ; X-ray; 3.10 A; SR/sR=2-319.
DR PDB; 5I4L; X-ray; 3.10 A; SR/sR=2-319.
DR PDB; 5JUO; EM; 4.00 A; WA=1-319.
DR PDB; 5JUP; EM; 3.50 A; WA=1-319.
DR PDB; 5JUS; EM; 4.20 A; WA=1-319.
DR PDB; 5JUT; EM; 4.00 A; WA=1-319.
DR PDB; 5JUU; EM; 4.00 A; WA=1-319.
DR PDB; 5LYB; X-ray; 3.25 A; SR/sR=2-319.
DR PDB; 5M1J; EM; 3.30 A; g2=2-319.
DR PDB; 5MC6; EM; 3.80 A; O=1-319.
DR PDB; 5MEI; X-ray; 3.50 A; h/sR=2-319.
DR PDB; 5NDG; X-ray; 3.70 A; SR/sR=2-319.
DR PDB; 5NDV; X-ray; 3.30 A; SR/sR=2-319.
DR PDB; 5NDW; X-ray; 3.70 A; SR/sR=2-319.
DR PDB; 5OBM; X-ray; 3.40 A; SR/sR=2-319.
DR PDB; 5ON6; X-ray; 3.10 A; h/sR=2-319.
DR PDB; 5TBW; X-ray; 3.00 A; Rb/h=2-319.
DR PDB; 5TGA; X-ray; 3.30 A; SR/sR=2-319.
DR PDB; 5TGM; X-ray; 3.50 A; SR/sR=2-319.
DR PDB; 6FAI; EM; 3.40 A; g=1-319.
DR PDB; 6GQ1; EM; 4.40 A; AV=2-319.
DR PDB; 6GQB; EM; 3.90 A; AV=2-319.
DR PDB; 6GQV; EM; 4.00 A; AV=2-319.
DR PDB; 6HHQ; X-ray; 3.10 A; Rb/h=1-319.
DR PDB; 6I7O; EM; 5.30 A; O/Ob=7-319.
DR PDB; 6Q8Y; EM; 3.10 A; O=2-319.
DR PDB; 6RBE; EM; 3.80 A; g=1-319.
DR PDB; 6S47; EM; 3.28 A; Bh=2-319.
DR PDB; 6SNT; EM; 2.80 A; g=1-319.
DR PDB; 6SV4; EM; 3.30 A; O/Ob/Oc=1-319.
DR PDB; 6T4Q; EM; 2.60 A; Sg=5-316.
DR PDB; 6T7I; EM; 3.20 A; Sg=1-319.
DR PDB; 6T7T; EM; 3.10 A; Sg=1-319.
DR PDB; 6T83; EM; 4.00 A; 7/gb=1-319.
DR PDB; 6TB3; EM; 2.80 A; O=5-316.
DR PDB; 6TNU; EM; 3.10 A; O=5-316.
DR PDB; 6WDR; EM; 3.70 A; g=3-319.
DR PDB; 6WOO; EM; 2.90 A; gg=2-319.
DR PDB; 6XIQ; EM; 4.20 A; AV=1-319.
DR PDB; 6XIR; EM; 3.20 A; AV=1-319.
DR PDB; 6Z6J; EM; 3.40 A; Sg=1-319.
DR PDB; 6Z6K; EM; 3.40 A; Sg=1-319.
DR PDB; 6ZCE; EM; 5.30 A; h=1-319.
DR PDB; 6ZU9; EM; 6.20 A; h=1-319.
DR PDB; 6ZVI; EM; 3.00 A; R=7-319.
DR PDB; 7A1G; EM; 3.00 A; O=5-316.
DR PDB; 7B7D; EM; 3.30 A; O=5-316.
DR PDB; 7NRC; EM; 3.90 A; SO=5-316.
DR PDB; 7NRD; EM; 4.36 A; SO=7-319.
DR PDBsum; 1TRJ; -.
DR PDBsum; 3FRX; -.
DR PDBsum; 3J6X; -.
DR PDBsum; 3J6Y; -.
DR PDBsum; 3J77; -.
DR PDBsum; 3J78; -.
DR PDBsum; 3RFG; -.
DR PDBsum; 3RFH; -.
DR PDBsum; 4U3M; -.
DR PDBsum; 4U3N; -.
DR PDBsum; 4U3U; -.
DR PDBsum; 4U4N; -.
DR PDBsum; 4U4O; -.
DR PDBsum; 4U4Q; -.
DR PDBsum; 4U4R; -.
DR PDBsum; 4U4U; -.
DR PDBsum; 4U4Y; -.
DR PDBsum; 4U4Z; -.
DR PDBsum; 4U50; -.
DR PDBsum; 4U51; -.
DR PDBsum; 4U52; -.
DR PDBsum; 4U53; -.
DR PDBsum; 4U55; -.
DR PDBsum; 4U56; -.
DR PDBsum; 4U6F; -.
DR PDBsum; 4V6I; -.
DR PDBsum; 4V7R; -.
DR PDBsum; 4V88; -.
DR PDBsum; 4V8Y; -.
DR PDBsum; 4V8Z; -.
DR PDBsum; 4V92; -.
DR PDBsum; 5DAT; -.
DR PDBsum; 5DC3; -.
DR PDBsum; 5DGE; -.
DR PDBsum; 5DGF; -.
DR PDBsum; 5DGV; -.
DR PDBsum; 5FCI; -.
DR PDBsum; 5FCJ; -.
DR PDBsum; 5I4L; -.
DR PDBsum; 5JUO; -.
DR PDBsum; 5JUP; -.
DR PDBsum; 5JUS; -.
DR PDBsum; 5JUT; -.
DR PDBsum; 5JUU; -.
DR PDBsum; 5LYB; -.
DR PDBsum; 5M1J; -.
DR PDBsum; 5MC6; -.
DR PDBsum; 5MEI; -.
DR PDBsum; 5NDG; -.
DR PDBsum; 5NDV; -.
DR PDBsum; 5NDW; -.
DR PDBsum; 5OBM; -.
DR PDBsum; 5ON6; -.
DR PDBsum; 5TBW; -.
DR PDBsum; 5TGA; -.
DR PDBsum; 5TGM; -.
DR PDBsum; 6FAI; -.
DR PDBsum; 6GQ1; -.
DR PDBsum; 6GQB; -.
DR PDBsum; 6GQV; -.
DR PDBsum; 6HHQ; -.
DR PDBsum; 6I7O; -.
DR PDBsum; 6Q8Y; -.
DR PDBsum; 6RBE; -.
DR PDBsum; 6S47; -.
DR PDBsum; 6SNT; -.
DR PDBsum; 6SV4; -.
DR PDBsum; 6T4Q; -.
DR PDBsum; 6T7I; -.
DR PDBsum; 6T7T; -.
DR PDBsum; 6T83; -.
DR PDBsum; 6TB3; -.
DR PDBsum; 6TNU; -.
DR PDBsum; 6WDR; -.
DR PDBsum; 6WOO; -.
DR PDBsum; 6XIQ; -.
DR PDBsum; 6XIR; -.
DR PDBsum; 6Z6J; -.
DR PDBsum; 6Z6K; -.
DR PDBsum; 6ZCE; -.
DR PDBsum; 6ZU9; -.
DR PDBsum; 6ZVI; -.
DR PDBsum; 7A1G; -.
DR PDBsum; 7B7D; -.
DR PDBsum; 7NRC; -.
DR PDBsum; 7NRD; -.
DR AlphaFoldDB; P38011; -.
DR SMR; P38011; -.
DR BioGRID; 35292; 1009.
DR ComplexPortal; CPX-1599; 40S cytosolic small ribosomal subunit.
DR DIP; DIP-6465N; -.
DR IntAct; P38011; 176.
DR MINT; P38011; -.
DR STRING; 4932.YMR116C; -.
DR MoonProt; P38011; -.
DR TCDB; 8.A.92.1.3; the g-protein AlphaBetaGama complex (gpc) family.
DR iPTMnet; P38011; -.
DR UCD-2DPAGE; P38011; -.
DR MaxQB; P38011; -.
DR PaxDb; P38011; -.
DR PRIDE; P38011; -.
DR TopDownProteomics; P38011; -.
DR EnsemblFungi; YMR116C_mRNA; YMR116C; YMR116C.
DR GeneID; 855143; -.
DR KEGG; sce:YMR116C; -.
DR SGD; S000004722; ASC1.
DR VEuPathDB; FungiDB:YMR116C; -.
DR eggNOG; KOG0279; Eukaryota.
DR GeneTree; ENSGT00940000154461; -.
DR HOGENOM; CLU_000288_57_7_1; -.
DR InParanoid; P38011; -.
DR OMA; CKAMLWD; -.
DR BioCyc; YEAST:G3O-32811-MON; -.
DR EvolutionaryTrace; P38011; -.
DR PRO; PR:P38011; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P38011; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IPI:SGD.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; IDA:SGD.
DR GO; GO:0005080; F:protein kinase C binding; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IDA:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:SGD.
DR GO; GO:0001403; P:invasive growth in response to glucose limitation; IMP:SGD.
DR GO; GO:0061157; P:mRNA destabilization; IMP:SGD.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:SGD.
DR GO; GO:1902660; P:negative regulation of glucose mediated signaling pathway; IMP:SGD.
DR GO; GO:0017148; P:negative regulation of translation; IMP:SGD.
DR GO; GO:2001125; P:negative regulation of translational frameshifting; IMP:SGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:SGD.
DR GO; GO:0008104; P:protein localization; IMP:SGD.
DR GO; GO:0080135; P:regulation of cellular response to stress; IMP:SGD.
DR GO; GO:0072344; P:rescue of stalled ribosome; IBA:GO_Central.
DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR045223; Asc1/RACK1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR19868; PTHR19868; 1.
DR Pfam; PF00400; WD40; 6.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Phosphoprotein; Reference proteome; Repeat;
KW Ribonucleoprotein; Ribosomal protein; Ubl conjugation; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:22814378"
FT CHAIN 2..319
FT /note="Guanine nucleotide-binding protein subunit beta-like
FT protein"
FT /id="PRO_0000127758"
FT REPEAT 15..55
FT /note="WD 1"
FT REPEAT 63..102
FT /note="WD 2"
FT REPEAT 105..145
FT /note="WD 3"
FT REPEAT 147..191
FT /note="WD 4"
FT REPEAT 194..233
FT /note="WD 5"
FT REPEAT 235..275
FT /note="WD 6"
FT REPEAT 284..319
FT /note="WD 7"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:22814378"
FT MOD_RES 96
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 168
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CROSSLNK 46
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 53
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 107
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 137
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 161
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT STRAND 5..13
FT /evidence="ECO:0007829|PDB:3FRX"
FT STRAND 20..25
FT /evidence="ECO:0007829|PDB:3FRX"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:3FRX"
FT STRAND 40..50
FT /evidence="ECO:0007829|PDB:3FRX"
FT STRAND 53..62
FT /evidence="ECO:0007829|PDB:3FRX"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:3FRX"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:3FRX"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:3FRX"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:3FRX"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:3FRX"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:3FRX"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:7A1G"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:3FRX"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:3FRX"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:3FRX"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:3FRX"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:3FRX"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:3FRX"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:3FRX"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:3FRX"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:3FRX"
FT STRAND 208..215
FT /evidence="ECO:0007829|PDB:3FRX"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:3RFH"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:3FRX"
FT TURN 225..228
FT /evidence="ECO:0007829|PDB:3FRX"
FT STRAND 229..235
FT /evidence="ECO:0007829|PDB:3FRX"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:3FRX"
FT STRAND 247..256
FT /evidence="ECO:0007829|PDB:3FRX"
FT STRAND 259..264
FT /evidence="ECO:0007829|PDB:3FRX"
FT TURN 265..268
FT /evidence="ECO:0007829|PDB:3FRX"
FT STRAND 269..274
FT /evidence="ECO:0007829|PDB:3FRX"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:3FRX"
FT STRAND 289..294
FT /evidence="ECO:0007829|PDB:3FRX"
FT STRAND 298..305
FT /evidence="ECO:0007829|PDB:3FRX"
FT STRAND 310..317
FT /evidence="ECO:0007829|PDB:3FRX"
SQ SEQUENCE 319 AA; 34805 MW; B9A5D4959A3C54FB CRC64;
MASNEVLVLR GTLEGHNGWV TSLATSAGQP NLLLSASRDK TLISWKLTGD DQKFGVPVRS
FKGHSHIVQD CTLTADGAYA LSASWDKTLR LWDVATGETY QRFVGHKSDV MSVDIDKKAS
MIISGSRDKT IKVWTIKGQC LATLLGHNDW VSQVRVVPNE KADDDSVTII SAGNDKMVKA
WNLNQFQIEA DFIGHNSNIN TLTASPDGTL IASAGKDGEI MLWNLAAKKA MYTLSAQDEV
FSLAFSPNRY WLAAATATGI KVFSLDPQYL VDDLRPEFAG YSKAAEPHAV SLAWSADGQT
LFAGYTDNVI RVWQVMTAN
