RS20_YEAST
ID RS20_YEAST Reviewed; 121 AA.
AC P38701; D3DKP7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=40S ribosomal protein S20 {ECO:0000303|PubMed:9559554};
DE AltName: Full=Small ribosomal subunit protein uS10 {ECO:0000303|PubMed:24524803};
GN Name=RPS20 {ECO:0000303|PubMed:9559554};
GN Synonyms=URP2 {ECO:0000303|PubMed:8021936};
GN OrderedLocusNames=YHL015W {ECO:0000312|SGD:S000001007};
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].
RC STRAIN=ATCC 28383 / FL100 / VTT C-80102;
RX PubMed=8021936; DOI=10.1006/jmbi.1994.1412;
RA Hermann-Le Denmat S., Sipickzki M., Thuriaux P.;
RT "Suppression of yeast RNA polymerase III mutations by the URP2 gene
RT encoding a protein homologous to the mammalian ribosomal protein S20.";
RL J. Mol. Biol. 240:1-7(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [3]
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 [4]
RP PROTEIN SEQUENCE OF 2-21; 33-43; 78-85 AND 90-102, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V., Peters C.;
RL Submitted (MAY-2005) to UniProtKB.
RN [5]
RP NOMENCLATURE, AND SUBUNIT.
RX PubMed=9559554;
RX DOI=10.1002/(sici)1097-0061(19980330)14:5<471::aid-yea241>3.0.co;2-u;
RA Planta R.J., Mager W.H.;
RT "The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae.";
RL Yeast 14:471-477(1998).
RN [6]
RP CLEAVAGE OF INITIATOR METHIONINE, AND ACETYLATION AT SER-2 BY NATA.
RX PubMed=10601260; DOI=10.1074/jbc.274.52.37035;
RA Arnold R.J., Polevoda B., Reilly J.P., Sherman F.;
RT "The action of N-terminal acetyltransferases on yeast ribosomal proteins.";
RL J. Biol. Chem. 274:37035-37040(1999).
RN [7]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-8, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=SUB592;
RX PubMed=12872131; DOI=10.1038/nbt849;
RA Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA Roelofs J., Finley D., Gygi S.P.;
RT "A proteomics approach to understanding protein ubiquitination.";
RL Nat. Biotechnol. 21:921-926(2003).
RN [8]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-8, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=14557538; DOI=10.1073/pnas.2135500100;
RA Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
RT "A subset of membrane-associated proteins is ubiquitinated in response to
RT mutations in the endoplasmic reticulum degradation machinery.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-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 [10]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-8; LYS-21; LYS-32 AND
RP LYS-101, AND IDENTIFICATION BY 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).
RN [11]
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 [12]
RP UBIQUITINATION AT LYS-6 AND LYS-8, AND MUTAGENESIS OF 6-LYS--LYS-8.
RX PubMed=28757607; DOI=10.1038/s41467-017-00188-1;
RA Matsuo Y., Ikeuchi K., Saeki Y., Iwasaki S., Schmidt C., Udagawa T.,
RA Sato F., Tsuchiya H., Becker T., Tanaka K., Ingolia N.T., Beckmann R.,
RA Inada T.;
RT "Ubiquitination of stalled ribosome triggers ribosome-associated quality
RT control.";
RL Nat. Commun. 8:159-159(2017).
RN [13]
RP 3D-STRUCTURE MODELING OF 21-117, AND ELECTRON MICROSCOPY.
RX PubMed=11701127; DOI=10.1016/s0092-8674(01)00539-6;
RA Spahn C.M.T., Beckmann R., Eswar N., Penczek P.A., Sali A., Blobel G.,
RA Frank J.;
RT "Structure of the 80S ribosome from Saccharomyces cerevisiae -- tRNA-
RT ribosome and subunit-subunit interactions.";
RL Cell 107:373-386(2001).
RN [14]
RP 3D-STRUCTURE MODELING OF 21-121, AND ELECTRON MICROSCOPY.
RX PubMed=14976550; DOI=10.1038/sj.emboj.7600102;
RA Spahn C.M.T., Gomez-Lorenzo M.G., Grassucci R.A., Joergensen R.,
RA Andersen G.R., Beckmann R., Penczek P.A., Ballesta J.P.G., Frank J.;
RT "Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome
RT facilitate tRNA translocation.";
RL EMBO J. 23:1008-1019(2004).
RN [15]
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 [16]
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. {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) (PubMed:9559554, PubMed:22096102).
CC {ECO:0000269|PubMed:22096102, ECO:0000305|PubMed:9559554}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}.
CC -!- PTM: Ubiquitinated at 'Lys-6' and 'Lys-8' by HEL2/UBC4, to activate the
CC ribosome quality control (RQC) pathway in response to stalled
CC ribosomes. {ECO:0000269|PubMed:28757607}.
CC -!- PTM: N-terminally acetylated by acetyltransferase NatA. Also partially
CC acetylated by NatC. {ECO:0000269|PubMed:10601260, ECO:0000269|Ref.4}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS10 family.
CC {ECO:0000305}.
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DR EMBL; Z29089; CAA82331.1; -; Genomic_DNA.
DR EMBL; U11582; AAB65068.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06671.1; -; Genomic_DNA.
DR PIR; S46829; S46829.
DR RefSeq; NP_011848.1; NM_001179095.1.
DR PDB; 3J6X; EM; 6.10 A; 20=1-121.
DR PDB; 3J6Y; EM; 6.10 A; 20=1-121.
DR PDB; 3J77; EM; 6.20 A; 20=1-121.
DR PDB; 3J78; EM; 6.30 A; 20=1-121.
DR PDB; 4U3M; X-ray; 3.00 A; D0/d0=2-121.
DR PDB; 4U3N; X-ray; 3.20 A; D0/d0=2-121.
DR PDB; 4U3U; X-ray; 2.90 A; D0/d0=2-121.
DR PDB; 4U4N; X-ray; 3.10 A; D0/d0=2-121.
DR PDB; 4U4O; X-ray; 3.60 A; D0/d0=2-121.
DR PDB; 4U4Q; X-ray; 3.00 A; D0/d0=2-121.
DR PDB; 4U4R; X-ray; 2.80 A; D0/d0=2-121.
DR PDB; 4U4U; X-ray; 3.00 A; D0/d0=2-121.
DR PDB; 4U4Y; X-ray; 3.20 A; D0/d0=2-121.
DR PDB; 4U4Z; X-ray; 3.10 A; D0/d0=2-121.
DR PDB; 4U50; X-ray; 3.20 A; D0/d0=2-121.
DR PDB; 4U51; X-ray; 3.20 A; D0/d0=2-121.
DR PDB; 4U52; X-ray; 3.00 A; D0/d0=2-121.
DR PDB; 4U53; X-ray; 3.30 A; D0/d0=2-121.
DR PDB; 4U55; X-ray; 3.20 A; D0/d0=2-121.
DR PDB; 4U56; X-ray; 3.45 A; D0/d0=2-121.
DR PDB; 4U6F; X-ray; 3.10 A; D0/d0=2-121.
DR PDB; 4V4B; EM; 11.70 A; AJ=21-117.
DR PDB; 4V6I; EM; 8.80 A; AJ=1-121.
DR PDB; 4V7R; X-ray; 4.00 A; AN/CN=1-121.
DR PDB; 4V88; X-ray; 3.00 A; AU/CU=1-121.
DR PDB; 4V8Y; EM; 4.30 A; AU=1-121.
DR PDB; 4V8Z; EM; 6.60 A; AU=1-121.
DR PDB; 4V92; EM; 3.70 A; U=17-120.
DR PDB; 5DAT; X-ray; 3.15 A; D0/d0=2-121.
DR PDB; 5DC3; X-ray; 3.25 A; D0/d0=2-121.
DR PDB; 5DGE; X-ray; 3.45 A; D0/d0=2-121.
DR PDB; 5DGF; X-ray; 3.30 A; D0/d0=2-121.
DR PDB; 5DGV; X-ray; 3.10 A; D0/d0=2-121.
DR PDB; 5FCI; X-ray; 3.40 A; D0/d0=2-121.
DR PDB; 5FCJ; X-ray; 3.10 A; D0/d0=2-121.
DR PDB; 5I4L; X-ray; 3.10 A; D0/d0=12-121.
DR PDB; 5JUO; EM; 4.00 A; RB=1-121.
DR PDB; 5JUP; EM; 3.50 A; RB=1-121.
DR PDB; 5JUS; EM; 4.20 A; RB=1-121.
DR PDB; 5JUT; EM; 4.00 A; RB=1-121.
DR PDB; 5JUU; EM; 4.00 A; RB=1-121.
DR PDB; 5LYB; X-ray; 3.25 A; D0/d0=12-121.
DR PDB; 5M1J; EM; 3.30 A; U2=15-121.
DR PDB; 5MC6; EM; 3.80 A; J=1-121.
DR PDB; 5MEI; X-ray; 3.50 A; V/d0=12-121.
DR PDB; 5NDG; X-ray; 3.70 A; D0/d0=15-121.
DR PDB; 5NDV; X-ray; 3.30 A; D0/d0=13-121.
DR PDB; 5NDW; X-ray; 3.70 A; D0/d0=15-121.
DR PDB; 5OBM; X-ray; 3.40 A; D0/d0=12-121.
DR PDB; 5ON6; X-ray; 3.10 A; V/d0=12-121.
DR PDB; 5TBW; X-ray; 3.00 A; V/d0=12-121.
DR PDB; 5TGA; X-ray; 3.30 A; D0/d0=12-121.
DR PDB; 5TGM; X-ray; 3.50 A; D0/d0=12-121.
DR PDB; 6FAI; EM; 3.40 A; U=1-121.
DR PDB; 6GQ1; EM; 4.40 A; AK=15-121.
DR PDB; 6GQB; EM; 3.90 A; AK=15-121.
DR PDB; 6GQV; EM; 4.00 A; AK=15-121.
DR PDB; 6HHQ; X-ray; 3.10 A; V/d0=1-121.
DR PDB; 6I7O; EM; 5.30 A; J/Jb=19-119.
DR PDB; 6Q8Y; EM; 3.10 A; J=15-121.
DR PDB; 6RBD; EM; 3.47 A; U=1-121.
DR PDB; 6RBE; EM; 3.80 A; U=1-121.
DR PDB; 6S47; EM; 3.28 A; BV=2-121.
DR PDB; 6SNT; EM; 2.80 A; U=1-121.
DR PDB; 6SV4; EM; 3.30 A; J/Jb/Jc=1-121.
DR PDB; 6T4Q; EM; 2.60 A; SU=20-119.
DR PDB; 6T7I; EM; 3.20 A; SU=1-121.
DR PDB; 6T7T; EM; 3.10 A; SU=1-121.
DR PDB; 6T83; EM; 4.00 A; Ub/v=1-121.
DR PDB; 6TB3; EM; 2.80 A; J=20-119.
DR PDB; 6TNU; EM; 3.10 A; J=20-119.
DR PDB; 6WDR; EM; 3.70 A; U=19-121.
DR PDB; 6WOO; EM; 2.90 A; UU=15-120.
DR PDB; 6Y7C; EM; 3.80 A; U=1-121.
DR PDB; 6Z6J; EM; 3.40 A; SU=1-121.
DR PDB; 6Z6K; EM; 3.40 A; SU=1-121.
DR PDB; 6ZCE; EM; 5.30 A; V=1-121.
DR PDB; 6ZU9; EM; 6.20 A; L=1-121.
DR PDB; 6ZVI; EM; 3.00 A; C=19-119.
DR PDB; 7A1G; EM; 3.00 A; K=20-119.
DR PDB; 7B7D; EM; 3.30 A; J=20-119.
DR PDB; 7NRC; EM; 3.90 A; SJ=20-119.
DR PDB; 7NRD; EM; 4.36 A; SJ=19-119.
DR PDBsum; 3J6X; -.
DR PDBsum; 3J6Y; -.
DR PDBsum; 3J77; -.
DR PDBsum; 3J78; -.
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; 4V4B; -.
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; 6RBD; -.
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; 6Y7C; -.
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; P38701; -.
DR SMR; P38701; -.
DR BioGRID; 36408; 677.
DR ComplexPortal; CPX-1599; 40S cytosolic small ribosomal subunit.
DR DIP; DIP-4060N; -.
DR IntAct; P38701; 15.
DR MINT; P38701; -.
DR STRING; 4932.YHL015W; -.
DR iPTMnet; P38701; -.
DR MaxQB; P38701; -.
DR PaxDb; P38701; -.
DR PRIDE; P38701; -.
DR TopDownProteomics; P38701; -.
DR EnsemblFungi; YHL015W_mRNA; YHL015W; YHL015W.
DR GeneID; 856371; -.
DR KEGG; sce:YHL015W; -.
DR SGD; S000001007; RPS20.
DR VEuPathDB; FungiDB:YHL015W; -.
DR eggNOG; KOG0900; Eukaryota.
DR GeneTree; ENSGT00390000003248; -.
DR HOGENOM; CLU_122625_0_0_1; -.
DR InParanoid; P38701; -.
DR OMA; DAPKIHK; -.
DR BioCyc; YEAST:G3O-31035-MON; -.
DR Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-SCE-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-SCE-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-SCE-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-SCE-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-SCE-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-SCE-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-SCE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR EvolutionaryTrace; P38701; -.
DR PRO; PR:P38701; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38701; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:SGD.
DR GO; GO:0015935; C:small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0002181; P:cytoplasmic translation; IC:SGD.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR Gene3D; 3.30.70.600; -; 1.
DR HAMAP; MF_00508; Ribosomal_S10; 1.
DR InterPro; IPR001848; Ribosomal_S10.
DR InterPro; IPR018268; Ribosomal_S10_CS.
DR InterPro; IPR027486; Ribosomal_S10_dom.
DR InterPro; IPR036838; Ribosomal_S10_dom_sf.
DR InterPro; IPR005729; Ribosomal_S10_euk/arc.
DR PANTHER; PTHR11700; PTHR11700; 1.
DR Pfam; PF00338; Ribosomal_S10; 1.
DR PRINTS; PR00971; RIBOSOMALS10.
DR SMART; SM01403; Ribosomal_S10; 1.
DR SUPFAM; SSF54999; SSF54999; 1.
DR TIGRFAMs; TIGR01046; uS10_euk_arch; 1.
DR PROSITE; PS00361; RIBOSOMAL_S10; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10601260, ECO:0000269|Ref.4,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..121
FT /note="40S ribosomal protein S20"
FT /id="PRO_0000146692"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:10601260, ECO:0000269|Ref.4,
FT ECO:0007744|PubMed:22814378"
FT CROSSLNK 6
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:28757607,
FT ECO:0007744|PubMed:22106047"
FT CROSSLNK 8
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:28757607,
FT ECO:0007744|PubMed:22106047"
FT CROSSLNK 21
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 32
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 101
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 6..8
FT /note="KEK->RER: Abolishes ubiquitination by HEL2/UBC4.
FT Defective activation of the ribosome quality control (RQC)
FT pathway. Sensitive to anisomycin (stalls ribosomes in the
FT rotated state)."
FT /evidence="ECO:0000269|PubMed:28757607"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 31..47
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:7A1G"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 82..91
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 97..106
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:6ZVI"
SQ SEQUENCE 121 AA; 13907 MW; 8B1607EDB63017F1 CRC64;
MSDFQKEKVE EQEQQQQQII KIRITLTSTK VKQLENVSSN IVKNAEQHNL VKKGPVRLPT
KVLKISTRKT PNGEGSKTWE TYEMRIHKRY IDLEAPVQIV KRITQITIEP GVDVEVVVAS
N
