RS8_HUMAN
ID RS8_HUMAN Reviewed; 208 AA.
AC P62241; P09058; Q6IRL7;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=40S ribosomal protein S8;
DE AltName: Full=Small ribosomal subunit protein eS8 {ECO:0000303|PubMed:24524803};
GN Name=RPS8; ORFNames=OK/SW-cl.83;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8432552; DOI=10.1006/geno.1993.1011;
RA Davies B., Fried M.;
RT "The structure of the human intron-containing S8 ribosomal protein gene and
RT determination of its chromosomal location at 1p32-p34.1.";
RL Genomics 15:68-75(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon adenocarcinoma;
RA Shichijo S., Itoh K.;
RT "Identification of immuno-peptidmics that are recognized by tumor-reactive
RT CTL generated from TIL of colon cancer patients.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 2-17, AND CLEAVAGE OF INITIATOR METHIONINE.
RC TISSUE=Placenta;
RX PubMed=8706699; DOI=10.1111/j.1432-1033.1996.0144u.x;
RA Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., Egorov T.A.,
RA Thiede B., Wittmann-Liebold B., Otto A.;
RT "Characterization of the human small-ribosomal-subunit proteins by N-
RT terminal and internal sequencing, and mass spectrometry.";
RL Eur. J. Biochem. 239:144-149(1996).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [6]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=17289661; DOI=10.1074/mcp.m600346-mcp200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-130 AND SER-160, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25255805; DOI=10.1038/ncomms5919;
RA Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H.,
RA Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
RT "Global profiling of co- and post-translationally N-myristoylated proteomes
RT in human cells.";
RL Nat. Commun. 5:4919-4919(2014).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-170 AND LYS-193, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [17]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
RX PubMed=23636399; DOI=10.1038/nature12104;
RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA Wilson D.N., Beckmann R.;
RT "Structures of the human and Drosophila 80S ribosome.";
RL Nature 497:80-85(2013).
CC -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs. {ECO:0000269|PubMed:17289661}.
CC -!- INTERACTION:
CC P62241; Q15700: DLG2; NbExp=3; IntAct=EBI-351811, EBI-80426;
CC P62241; Q92796: DLG3; NbExp=3; IntAct=EBI-351811, EBI-80440;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17289661}. Membrane
CC {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Localized in
CC cytoplasmic mRNP granules containing untranslated mRNAs.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS8 family.
CC {ECO:0000305}.
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DR EMBL; X67247; CAA47670.1; -; Genomic_DNA.
DR EMBL; AB062401; BAB93488.1; -; mRNA.
DR EMBL; BC070875; AAH70875.1; -; mRNA.
DR CCDS; CCDS513.1; -.
DR PIR; S25022; S25022.
DR RefSeq; NP_001003.1; NM_001012.1.
DR PDB; 4UG0; EM; -; SI=1-208.
DR PDB; 4V6X; EM; 5.00 A; AI=1-208.
DR PDB; 5A2Q; EM; 3.90 A; I=1-208.
DR PDB; 5AJ0; EM; 3.50 A; BI=1-208.
DR PDB; 5FLX; EM; 3.90 A; I=1-208.
DR PDB; 5LKS; EM; 3.60 A; SI=1-208.
DR PDB; 5OA3; EM; 4.30 A; I=1-208.
DR PDB; 5T2C; EM; 3.60 A; Au=1-208.
DR PDB; 5VYC; X-ray; 6.00 A; I1/I2/I3/I4/I5/I6=1-208.
DR PDB; 6FEC; EM; 6.30 A; o=2-207.
DR PDB; 6G18; EM; 3.60 A; I=1-208.
DR PDB; 6G4S; EM; 4.00 A; I=1-208.
DR PDB; 6G4W; EM; 4.50 A; I=1-208.
DR PDB; 6G51; EM; 4.10 A; I=1-208.
DR PDB; 6G53; EM; 4.50 A; I=1-208.
DR PDB; 6G5H; EM; 3.60 A; I=1-208.
DR PDB; 6G5I; EM; 3.50 A; I=1-208.
DR PDB; 6IP5; EM; 3.90 A; 2t=1-208.
DR PDB; 6IP6; EM; 4.50 A; 2t=1-208.
DR PDB; 6IP8; EM; 3.90 A; 2t=1-208.
DR PDB; 6OLE; EM; 3.10 A; SI=2-205.
DR PDB; 6OLF; EM; 3.90 A; SI=2-205.
DR PDB; 6OLG; EM; 3.40 A; BI=2-208.
DR PDB; 6OLI; EM; 3.50 A; SI=2-205.
DR PDB; 6OLZ; EM; 3.90 A; BI=2-208.
DR PDB; 6OM0; EM; 3.10 A; SI=2-205.
DR PDB; 6OM7; EM; 3.70 A; SI=2-205.
DR PDB; 6QZP; EM; 2.90 A; SI=2-207.
DR PDB; 6XA1; EM; 2.80 A; SI=2-206.
DR PDB; 6Y0G; EM; 3.20 A; SI=1-208.
DR PDB; 6Y2L; EM; 3.00 A; SI=1-208.
DR PDB; 6Y57; EM; 3.50 A; SI=1-208.
DR PDB; 6YBW; EM; 3.10 A; R=1-208.
DR PDB; 6Z6L; EM; 3.00 A; SI=1-208.
DR PDB; 6Z6M; EM; 3.10 A; SI=1-208.
DR PDB; 6Z6N; EM; 2.90 A; SI=1-208.
DR PDB; 6ZLW; EM; 2.60 A; I=1-208.
DR PDB; 6ZM7; EM; 2.70 A; SI=1-208.
DR PDB; 6ZME; EM; 3.00 A; SI=1-208.
DR PDB; 6ZMI; EM; 2.60 A; SI=1-208.
DR PDB; 6ZMO; EM; 3.10 A; SI=1-208.
DR PDB; 6ZMT; EM; 3.00 A; I=1-208.
DR PDB; 6ZMW; EM; 3.70 A; R=1-208.
DR PDB; 6ZN5; EM; 3.20 A; I=2-206.
DR PDB; 6ZOJ; EM; 2.80 A; I=1-208.
DR PDB; 6ZOK; EM; 2.80 A; I=1-208.
DR PDB; 6ZON; EM; 3.00 A; t=1-208.
DR PDB; 6ZP4; EM; 2.90 A; t=1-208.
DR PDB; 6ZUO; EM; 3.10 A; I=1-208.
DR PDB; 6ZV6; EM; 2.90 A; I=1-208.
DR PDB; 6ZVH; EM; 2.90 A; I=2-207.
DR PDB; 6ZVJ; EM; 3.80 A; t=2-206.
DR PDB; 6ZXD; EM; 3.20 A; I=1-208.
DR PDB; 6ZXE; EM; 3.00 A; I=1-208.
DR PDB; 6ZXF; EM; 3.70 A; I=1-208.
DR PDB; 6ZXG; EM; 2.60 A; I=1-208.
DR PDB; 6ZXH; EM; 2.70 A; I=1-208.
DR PDB; 7A09; EM; 3.50 A; t=1-208.
DR PDB; 7K5I; EM; 2.90 A; I=1-208.
DR PDB; 7MQ8; EM; 3.60 A; L8=1-208.
DR PDB; 7MQ9; EM; 3.87 A; L8=1-208.
DR PDB; 7MQA; EM; 2.70 A; L8=1-208.
DR PDBsum; 4UG0; -.
DR PDBsum; 4V6X; -.
DR PDBsum; 5A2Q; -.
DR PDBsum; 5AJ0; -.
DR PDBsum; 5FLX; -.
DR PDBsum; 5LKS; -.
DR PDBsum; 5OA3; -.
DR PDBsum; 5T2C; -.
DR PDBsum; 5VYC; -.
DR PDBsum; 6FEC; -.
DR PDBsum; 6G18; -.
DR PDBsum; 6G4S; -.
DR PDBsum; 6G4W; -.
DR PDBsum; 6G51; -.
DR PDBsum; 6G53; -.
DR PDBsum; 6G5H; -.
DR PDBsum; 6G5I; -.
DR PDBsum; 6IP5; -.
DR PDBsum; 6IP6; -.
DR PDBsum; 6IP8; -.
DR PDBsum; 6OLE; -.
DR PDBsum; 6OLF; -.
DR PDBsum; 6OLG; -.
DR PDBsum; 6OLI; -.
DR PDBsum; 6OLZ; -.
DR PDBsum; 6OM0; -.
DR PDBsum; 6OM7; -.
DR PDBsum; 6QZP; -.
DR PDBsum; 6XA1; -.
DR PDBsum; 6Y0G; -.
DR PDBsum; 6Y2L; -.
DR PDBsum; 6Y57; -.
DR PDBsum; 6YBW; -.
DR PDBsum; 6Z6L; -.
DR PDBsum; 6Z6M; -.
DR PDBsum; 6Z6N; -.
DR PDBsum; 6ZLW; -.
DR PDBsum; 6ZM7; -.
DR PDBsum; 6ZME; -.
DR PDBsum; 6ZMI; -.
DR PDBsum; 6ZMO; -.
DR PDBsum; 6ZMT; -.
DR PDBsum; 6ZMW; -.
DR PDBsum; 6ZN5; -.
DR PDBsum; 6ZOJ; -.
DR PDBsum; 6ZOK; -.
DR PDBsum; 6ZON; -.
DR PDBsum; 6ZP4; -.
DR PDBsum; 6ZUO; -.
DR PDBsum; 6ZV6; -.
DR PDBsum; 6ZVH; -.
DR PDBsum; 6ZVJ; -.
DR PDBsum; 6ZXD; -.
DR PDBsum; 6ZXE; -.
DR PDBsum; 6ZXF; -.
DR PDBsum; 6ZXG; -.
DR PDBsum; 6ZXH; -.
DR PDBsum; 7A09; -.
DR PDBsum; 7K5I; -.
DR PDBsum; 7MQ8; -.
DR PDBsum; 7MQ9; -.
DR PDBsum; 7MQA; -.
DR AlphaFoldDB; P62241; -.
DR SMR; P62241; -.
DR BioGRID; 112116; 547.
DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit.
DR CORUM; P62241; -.
DR IntAct; P62241; 167.
DR MINT; P62241; -.
DR STRING; 9606.ENSP00000379888; -.
DR DrugBank; DB11638; Artenimol.
DR GlyGen; P62241; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P62241; -.
DR PhosphoSitePlus; P62241; -.
DR SwissPalm; P62241; -.
DR BioMuta; RPS8; -.
DR DMDM; 50403622; -.
DR CPTAC; CPTAC-581; -.
DR EPD; P62241; -.
DR jPOST; P62241; -.
DR MassIVE; P62241; -.
DR PaxDb; P62241; -.
DR PeptideAtlas; P62241; -.
DR PRIDE; P62241; -.
DR ProteomicsDB; 57372; -.
DR TopDownProteomics; P62241; -.
DR Antibodypedia; 32545; 177 antibodies from 26 providers.
DR DNASU; 6202; -.
DR Ensembl; ENST00000396651.8; ENSP00000379888.3; ENSG00000142937.12.
DR GeneID; 6202; -.
DR KEGG; hsa:6202; -.
DR MANE-Select; ENST00000396651.8; ENSP00000379888.3; NM_001012.2; NP_001003.1.
DR CTD; 6202; -.
DR DisGeNET; 6202; -.
DR GeneCards; RPS8; -.
DR HGNC; HGNC:10441; RPS8.
DR HPA; ENSG00000142937; Low tissue specificity.
DR MIM; 600357; gene.
DR neXtProt; NX_P62241; -.
DR OpenTargets; ENSG00000142937; -.
DR PharmGKB; PA34856; -.
DR VEuPathDB; HostDB:ENSG00000142937; -.
DR eggNOG; KOG3283; Eukaryota.
DR GeneTree; ENSGT00390000012433; -.
DR HOGENOM; CLU_080597_1_1_1; -.
DR InParanoid; P62241; -.
DR OMA; VGRCDGY; -.
DR OrthoDB; 1278610at2759; -.
DR PhylomeDB; P62241; -.
DR TreeFam; TF300041; -.
DR PathwayCommons; P62241; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-156902; Peptide chain elongation.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-HSA-192823; Viral mRNA Translation.
DR Reactome; R-HSA-2408557; Selenocysteine synthesis.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-HSA-72649; Translation initiation complex formation.
DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-HSA-72764; Eukaryotic Translation Termination.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9633012; Response of EIF2AK4 (GCN2) to amino acid deficiency.
DR Reactome; R-HSA-9754678; SARS-CoV-2 modulates host translation machinery.
DR Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; P62241; -.
DR SIGNOR; P62241; -.
DR BioGRID-ORCS; 6202; 799 hits in 1053 CRISPR screens.
DR ChiTaRS; RPS8; human.
DR GeneWiki; RPS8; -.
DR GenomeRNAi; 6202; -.
DR Pharos; P62241; Tbio.
DR PRO; PR:P62241; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P62241; protein.
DR Bgee; ENSG00000142937; Expressed in left ovary and 99 other tissues.
DR ExpressionAtlas; P62241; baseline and differential.
DR Genevisible; P62241; HS.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0002181; P:cytoplasmic translation; IC:FlyBase.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
DR Gene3D; 1.10.168.20; -; 1.
DR InterPro; IPR042563; Ribosomal_protein_S8e_euk.
DR InterPro; IPR001047; Ribosomal_S8e.
DR InterPro; IPR022309; Ribosomal_S8e/biogenesis_NSA2.
DR InterPro; IPR018283; Ribosomal_S8e_CS.
DR PANTHER; PTHR10394; PTHR10394; 1.
DR Pfam; PF01201; Ribosomal_S8e; 1.
DR TIGRFAMs; TIGR00307; eS8; 1.
DR PROSITE; PS01193; RIBOSOMAL_S8E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Lipoprotein; Membrane; Myristate; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25255805,
FT ECO:0000269|PubMed:8706699"
FT CHAIN 2..208
FT /note="40S ribosomal protein S8"
FT /id="PRO_0000122240"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..26
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 37
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62242"
FT MOD_RES 128
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62242"
FT MOD_RES 130
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:25255805"
FT CROSSLNK 170
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 193
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 110
FT /note="R -> G (in dbSNP:rs11537870)"
FT /id="VAR_051861"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:6ZMT"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 68..71
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 72..83
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 107..116
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:6ZVH"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 143..151
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:6ZXG"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 179..182
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 192..205
FT /evidence="ECO:0007829|PDB:6ZLW"
SQ SEQUENCE 208 AA; 24205 MW; 407FDF59171F7422 CRC64;
MGISRDNWHK RRKTGGKRKP YHKKRKYELG RPAANTKIGP RRIHTVRVRG GNKKYRALRL
DVGNFSWGSE CCTRKTRIID VVYNASNNEL VRTKTLVKNC IVLIDSTPYR QWYESHYALP
LGRKKGAKLT PEEEEILNKK RSKKIQKKYD ERKKNAKISS LLEEQFQQGK LLACIASRPG
QCGRADGYVL EGKELEFYLR KIKARKGK
