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 27-MAR-2024, entry version 214. DE RecName: Full=Small ribosomal subunit protein RACK1 {ECO:0000303|PubMed:24524803}; DE AltName: 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; 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 FUNCTION. RX PubMed=30465652; DOI=10.7554/elife.39637; RA Wang J., Zhou J., Yang Q., Grayhack E.J.; RT "Multi-protein bridging factor 1(Mbf1), Rps3 and Asc1 prevent stalled RT ribosomes from frameshifting."; RL Elife 7:0-0(2018). RN [17] 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 [18] 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 [19] 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 [20] 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, PubMed:30465652). Involved in the CC negative regulation of translation of a specific subset of proteins CC (PubMed:15340087). {ECO:0000269|PubMed:15340087, CC ECO:0000269|PubMed:28223409, ECO:0000269|PubMed:30465652, CC 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 7MPI; EM; 3.05 A; Bg=5-316. DR PDB; 7MPJ; EM; 2.70 A; Bg=5-316. DR PDB; 7N8B; EM; 3.05 A; Bg=5-316. DR PDB; 7NRC; EM; 3.90 A; SO=5-316. DR PDB; 7NRD; EM; 4.36 A; SO=7-319. DR PDB; 7ZPQ; EM; 3.47 A; Ag=5-316. DR PDB; 7ZRS; EM; 4.80 A; Ag=5-316. DR PDB; 7ZUW; EM; 4.30 A; Ag=5-316. DR PDB; 7ZUX; EM; 2.50 A; Dg=5-316. DR PDB; 7ZW0; EM; 2.40 A; sO=1-319. DR PDB; 8BQD; EM; 3.90 A; O=5-316. DR PDB; 8BQX; EM; 3.80 A; O=5-316. DR PDB; 8CAH; EM; 3.00 A; O=1-319. DR PDB; 8CAS; EM; 3.30 A; h=1-319. DR PDB; 8CBJ; EM; 3.80 A; g=1-319. DR PDB; 8CCS; EM; 1.97 A; 7=1-319. DR PDB; 8CDL; EM; 2.72 A; 7=1-319. DR PDB; 8CDR; EM; 2.04 A; 7=1-319. DR PDB; 8CEH; EM; 2.05 A; 7=1-319. DR PDB; 8CF5; EM; 2.71 A; 7=1-319. DR PDB; 8CG8; EM; 2.57 A; 7=1-319. DR PDB; 8CGN; EM; 2.28 A; 7=1-319. DR PDB; 8CIV; EM; 2.47 A; 7=1-319. DR PDB; 8CKU; EM; 3.11 A; 7=1-319. DR PDB; 8CMJ; EM; 3.79 A; 7=1-319. DR PDB; 8EUB; EM; 2.52 A; Bg=1-319. DR PDB; 8EVP; EM; 2.38 A; Bg=1-319. DR PDB; 8EVQ; EM; 2.72 A; Bg=1-319. DR PDB; 8EVR; EM; 2.87 A; Bg=1-319. DR PDB; 8EVS; EM; 2.62 A; Bg=1-319. DR PDB; 8EVT; EM; 2.20 A; Bg=1-319. DR PDB; 8EWB; EM; 2.87 A; Bg=1-319. DR PDB; 8EWC; EM; 2.45 A; Bg=1-319. 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; 7MPI; -. DR PDBsum; 7MPJ; -. DR PDBsum; 7N8B; -. DR PDBsum; 7NRC; -. DR PDBsum; 7NRD; -. DR PDBsum; 7ZPQ; -. DR PDBsum; 7ZRS; -. DR PDBsum; 7ZUW; -. DR PDBsum; 7ZUX; -. DR PDBsum; 7ZW0; -. DR PDBsum; 8BQD; -. DR PDBsum; 8BQX; -. DR PDBsum; 8CAH; -. DR PDBsum; 8CAS; -. DR PDBsum; 8CBJ; -. DR PDBsum; 8CCS; -. DR PDBsum; 8CDL; -. DR PDBsum; 8CDR; -. DR PDBsum; 8CEH; -. DR PDBsum; 8CF5; -. DR PDBsum; 8CG8; -. DR PDBsum; 8CGN; -. DR PDBsum; 8CIV; -. DR PDBsum; 8CKU; -. DR PDBsum; 8CMJ; -. DR PDBsum; 8EUB; -. DR PDBsum; 8EVP; -. DR PDBsum; 8EVQ; -. DR PDBsum; 8EVR; -. DR PDBsum; 8EVS; -. DR PDBsum; 8EVT; -. DR PDBsum; 8EWB; -. DR PDBsum; 8EWC; -. DR AlphaFoldDB; P38011; -. DR EMDB; EMD-0047; -. DR EMDB; EMD-0048; -. DR EMDB; EMD-0049; -. DR EMDB; EMD-10098; -. DR EMDB; EMD-10262; -. DR EMDB; EMD-10315; -. DR EMDB; EMD-10377; -. DR EMDB; EMD-10396; -. DR EMDB; EMD-10397; -. DR EMDB; EMD-10398; -. DR EMDB; EMD-10431; -. DR EMDB; EMD-10537; -. DR EMDB; EMD-11096; -. DR EMDB; EMD-11097; -. DR EMDB; EMD-11160; -. DR EMDB; EMD-11439; -. DR EMDB; EMD-11457; -. DR EMDB; EMD-11608; -. DR EMDB; EMD-12081; -. DR EMDB; EMD-12534; -. DR EMDB; EMD-12535; -. DR EMDB; EMD-14990; -. DR EMDB; EMD-16563; -. DR EMDB; EMD-16591; -. DR EMDB; EMD-16594; -. DR EMDB; EMD-16609; -. DR EMDB; EMD-16616; -. DR EMDB; EMD-16634; -. DR EMDB; EMD-16648; -. DR EMDB; EMD-16684; -. DR EMDB; EMD-16702; -. DR EMDB; EMD-16729; -. DR EMDB; EMD-21644; -. DR EMDB; EMD-21859; -. DR EMDB; EMD-22196; -. DR EMDB; EMD-22198; -. DR EMDB; EMD-23934; -. DR EMDB; EMD-23935; -. DR EMDB; EMD-24235; -. DR EMDB; EMD-28610; -. DR EMDB; EMD-28632; -. DR EMDB; EMD-28633; -. DR EMDB; EMD-28634; -. DR EMDB; EMD-28635; -. DR EMDB; EMD-28636; -. DR EMDB; EMD-28642; -. DR EMDB; EMD-28643; -. DR EMDB; EMD-3461; -. DR EMDB; EMD-4140; -. DR EMDB; EMD-4214; -. DR EMDB; EMD-4427; -. DR EMDB; EMD-4474; -. DR EMDB; EMD-4793; -. DR SMR; P38011; -. DR BioGRID; 35292; 1047. 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 MaxQB; P38011; -. DR PaxDb; 4932-YMR116C; -. DR PeptideAtlas; P38011; -. DR TopDownProteomics; P38011; -. DR EnsemblFungi; YMR116C_mRNA; YMR116C; YMR116C. DR GeneID; 855143; -. DR KEGG; sce:YMR116C; -. DR AGR; SGD:S000004722; -. 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 OrthoDB; 1513008at2759; -. DR BioCyc; YEAST:G3O-32811-MONOMER; -. DR BioGRID-ORCS; 855143; 5 hits in 10 CRISPR screens. 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:0045182; F:translation regulator activity; IEA:InterPro. DR GO; GO:0002181; P:cytoplasmic translation; NAS:ComplexPortal. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; 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; IBA:GO_Central. DR GO; GO:0072344; P:rescue of stalled ribosome; IDA:UniProtKB. DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; IMP:UniProtKB. DR CDD; cd00200; WD40; 1. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. DR InterPro; IPR020472; G-protein_beta_WD-40_rep. DR InterPro; IPR045223; RACK1-like. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR019775; WD40_repeat_CS. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR19868; RECEPTOR FOR ACTIVATED PROTEIN KINASE C RACK1; 1. DR PANTHER; PTHR19868:SF0; RECEPTOR OF ACTIVATED PROTEIN C KINASE 1; 1. DR Pfam; PF00400; WD40; 7. DR PRINTS; PR00320; GPROTEINBRPT. DR SMART; SM00320; WD40; 7. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS00678; WD_REPEATS_1; 3. DR PROSITE; PS50082; WD_REPEATS_2; 6. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. DR UCD-2DPAGE; P38011; -. 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="Small ribosomal subunit protein RACK1" 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 //