RL38_YEAST
ID RL38_YEAST Reviewed; 78 AA.
AC P49167; D6VYW7;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=60S ribosomal protein L38 {ECO:0000303|PubMed:9559554};
DE AltName: Full=Large ribosomal subunit protein eL38 {ECO:0000303|PubMed:24524803};
GN Name=RPL38 {ECO:0000303|PubMed:9559554}; OrderedLocusNames=YLR325C;
GN ORFNames=L8543.2;
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=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 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 [4]
RP CLEAVAGE OF INITIATOR METHIONINE.
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 [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
RP X-RAY CRYSTALLOGRAPHY (4.0 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 [12]
RP X-RAY CRYSTALLOGRAPHY (3.0 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 large ribosomal subunit (LSU). 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:14562095,
CC ECO:0000269|PubMed:22096102}.
CC -!- MISCELLANEOUS: Present with 50200 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL38 family.
CC {ECO:0000305}.
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DR EMBL; U20618; AAB64512.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09633.1; -; Genomic_DNA.
DR PIR; S53402; S53402.
DR RefSeq; NP_013429.1; NM_001182214.1.
DR PDB; 3J6X; EM; 6.10 A; 78=1-78.
DR PDB; 3J6Y; EM; 6.10 A; 78=1-78.
DR PDB; 3J77; EM; 6.20 A; 88=1-78.
DR PDB; 3J78; EM; 6.30 A; 88=1-78.
DR PDB; 3JCT; EM; 3.08 A; k=1-78.
DR PDB; 4U3M; X-ray; 3.00 A; O8/o8=2-78.
DR PDB; 4U3N; X-ray; 3.20 A; O8/o8=2-78.
DR PDB; 4U3U; X-ray; 2.90 A; O8/o8=2-78.
DR PDB; 4U4N; X-ray; 3.10 A; O8/o8=2-78.
DR PDB; 4U4O; X-ray; 3.60 A; O8/o8=2-78.
DR PDB; 4U4Q; X-ray; 3.00 A; O8/o8=2-78.
DR PDB; 4U4R; X-ray; 2.80 A; O8/o8=2-78.
DR PDB; 4U4U; X-ray; 3.00 A; O8/o8=2-78.
DR PDB; 4U4Y; X-ray; 3.20 A; O8/o8=2-78.
DR PDB; 4U4Z; X-ray; 3.10 A; O8/o8=2-78.
DR PDB; 4U50; X-ray; 3.20 A; O8/o8=2-78.
DR PDB; 4U51; X-ray; 3.20 A; O8/o8=2-78.
DR PDB; 4U52; X-ray; 3.00 A; O8/o8=2-78.
DR PDB; 4U53; X-ray; 3.30 A; O8/o8=2-78.
DR PDB; 4U55; X-ray; 3.20 A; O8/o8=2-78.
DR PDB; 4U56; X-ray; 3.45 A; O8/o8=2-78.
DR PDB; 4U6F; X-ray; 3.10 A; O8/o8=2-78.
DR PDB; 4V6I; EM; 8.80 A; Bn=1-78.
DR PDB; 4V7F; EM; 8.70 A; i=1-78.
DR PDB; 4V88; X-ray; 3.00 A; Bk/Dk=1-78.
DR PDB; 4V8T; EM; 8.10 A; k=1-78.
DR PDB; 4V8Y; EM; 4.30 A; Bk=2-78.
DR PDB; 4V8Z; EM; 6.60 A; Bk=2-78.
DR PDB; 4V91; EM; 3.70 A; k=1-78.
DR PDB; 5APN; EM; 3.91 A; k=1-78.
DR PDB; 5APO; EM; 3.41 A; k=1-78.
DR PDB; 5DAT; X-ray; 3.15 A; O8/o8=2-78.
DR PDB; 5DC3; X-ray; 3.25 A; O8/o8=2-78.
DR PDB; 5DGE; X-ray; 3.45 A; O8/o8=2-78.
DR PDB; 5DGF; X-ray; 3.30 A; O8/o8=2-78.
DR PDB; 5DGV; X-ray; 3.10 A; O8/o8=2-78.
DR PDB; 5FCI; X-ray; 3.40 A; O8/o8=2-78.
DR PDB; 5FCJ; X-ray; 3.10 A; O8/o8=2-78.
DR PDB; 5FL8; EM; 9.50 A; k=1-78.
DR PDB; 5GAK; EM; 3.88 A; m=1-78.
DR PDB; 5H4P; EM; 3.07 A; k=1-78.
DR PDB; 5I4L; X-ray; 3.10 A; O8/o8=2-78.
DR PDB; 5JCS; EM; 9.50 A; k=1-78.
DR PDB; 5JUO; EM; 4.00 A; PA=1-78.
DR PDB; 5JUP; EM; 3.50 A; PA=1-78.
DR PDB; 5JUS; EM; 4.20 A; PA=1-78.
DR PDB; 5JUT; EM; 4.00 A; PA=1-78.
DR PDB; 5JUU; EM; 4.00 A; PA=1-78.
DR PDB; 5LYB; X-ray; 3.25 A; O8/o8=2-78.
DR PDB; 5M1J; EM; 3.30 A; k5=2-78.
DR PDB; 5MC6; EM; 3.80 A; AI=1-78.
DR PDB; 5MEI; X-ray; 3.50 A; AL/DM=2-78.
DR PDB; 5NDG; X-ray; 3.70 A; O8/o8=2-78.
DR PDB; 5NDV; X-ray; 3.30 A; O8/o8=2-78.
DR PDB; 5NDW; X-ray; 3.70 A; O8/o8=2-78.
DR PDB; 5OBM; X-ray; 3.40 A; O8/o8=2-78.
DR PDB; 5ON6; X-ray; 3.10 A; AL/DM=2-78.
DR PDB; 5T62; EM; 3.30 A; x=1-78.
DR PDB; 5T6R; EM; 4.50 A; x=1-78.
DR PDB; 5TBW; X-ray; 3.00 A; AL/DM=2-78.
DR PDB; 5TGA; X-ray; 3.30 A; O8/o8=2-78.
DR PDB; 5TGM; X-ray; 3.50 A; O8/o8=2-78.
DR PDB; 6CB1; EM; 4.60 A; k=1-78.
DR PDB; 6ELZ; EM; 3.30 A; k=1-78.
DR PDB; 6EM5; EM; 4.30 A; k=1-78.
DR PDB; 6FT6; EM; 3.90 A; k=1-78.
DR PDB; 6GQ1; EM; 4.40 A; k=2-78.
DR PDB; 6GQB; EM; 3.90 A; k=2-78.
DR PDB; 6GQV; EM; 4.00 A; k=2-78.
DR PDB; 6HD7; EM; 3.40 A; m=1-78.
DR PDB; 6HHQ; X-ray; 3.10 A; AL/DM=1-78.
DR PDB; 6I7O; EM; 5.30 A; AI/XI=2-78.
DR PDB; 6M62; EM; 3.20 A; k=1-78.
DR PDB; 6N8J; EM; 3.50 A; k=1-78.
DR PDB; 6N8K; EM; 3.60 A; k=1-78.
DR PDB; 6N8L; EM; 3.60 A; k=1-78.
DR PDB; 6N8M; EM; 3.50 A; x=1-78.
DR PDB; 6N8N; EM; 3.80 A; x=1-78.
DR PDB; 6N8O; EM; 3.50 A; x=1-78.
DR PDB; 6OIG; EM; 3.80 A; k=2-78.
DR PDB; 6Q8Y; EM; 3.10 A; AI=2-78.
DR PDB; 6QIK; EM; 3.10 A; j=1-78.
DR PDB; 6QT0; EM; 3.40 A; j=1-78.
DR PDB; 6QTZ; EM; 3.50 A; j=1-78.
DR PDB; 6R84; EM; 3.60 A; m=2-78.
DR PDB; 6R86; EM; 3.40 A; m=2-78.
DR PDB; 6R87; EM; 3.40 A; m=2-78.
DR PDB; 6RI5; EM; 3.30 A; j=1-78.
DR PDB; 6RZZ; EM; 3.20 A; j=1-78.
DR PDB; 6S05; EM; 3.90 A; j=1-78.
DR PDB; 6S47; EM; 3.28 A; Am=2-78.
DR PDB; 6SNT; EM; 2.80 A; af=1-78.
DR PDB; 6SV4; EM; 3.30 A; AI/XI/zI=1-78.
DR PDB; 6T4Q; EM; 2.60 A; Lk=2-78.
DR PDB; 6T7I; EM; 3.20 A; Lk=1-78.
DR PDB; 6T7T; EM; 3.10 A; Lk=1-78.
DR PDB; 6T83; EM; 4.00 A; V/kb=1-78.
DR PDB; 6TB3; EM; 2.80 A; AI=2-78.
DR PDB; 6TNU; EM; 3.10 A; AI=2-78.
DR PDB; 6WOO; EM; 2.90 A; k=3-78.
DR PDB; 6YLG; EM; 3.00 A; k=1-78.
DR PDB; 6YLH; EM; 3.10 A; k=1-78.
DR PDB; 6YLX; EM; 3.90 A; k=1-78.
DR PDB; 6YLY; EM; 3.80 A; k=1-78.
DR PDB; 6Z6J; EM; 3.40 A; Lk=1-78.
DR PDB; 6Z6K; EM; 3.40 A; Lk=1-78.
DR PDB; 7AZY; EM; 2.88 A; j=1-78.
DR PDB; 7B7D; EM; 3.30 A; Lg=2-78.
DR PDB; 7BT6; EM; 3.12 A; k=1-78.
DR PDB; 7BTB; EM; 3.22 A; k=1-78.
DR PDB; 7NRC; EM; 3.90 A; Lm=2-78.
DR PDB; 7NRD; EM; 4.36 A; Lm=2-78.
DR PDB; 7OF1; EM; 3.10 A; k=1-78.
DR PDB; 7OH3; EM; 3.40 A; k=1-78.
DR PDB; 7OHQ; EM; 3.10 A; k=1-78.
DR PDB; 7OHR; EM; 4.72 A; k=1-78.
DR PDB; 7OHV; EM; 3.90 A; k=1-78.
DR PDBsum; 3J6X; -.
DR PDBsum; 3J6Y; -.
DR PDBsum; 3J77; -.
DR PDBsum; 3J78; -.
DR PDBsum; 3JCT; -.
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; 4V7F; -.
DR PDBsum; 4V88; -.
DR PDBsum; 4V8T; -.
DR PDBsum; 4V8Y; -.
DR PDBsum; 4V8Z; -.
DR PDBsum; 4V91; -.
DR PDBsum; 5APN; -.
DR PDBsum; 5APO; -.
DR PDBsum; 5DAT; -.
DR PDBsum; 5DC3; -.
DR PDBsum; 5DGE; -.
DR PDBsum; 5DGF; -.
DR PDBsum; 5DGV; -.
DR PDBsum; 5FCI; -.
DR PDBsum; 5FCJ; -.
DR PDBsum; 5FL8; -.
DR PDBsum; 5GAK; -.
DR PDBsum; 5H4P; -.
DR PDBsum; 5I4L; -.
DR PDBsum; 5JCS; -.
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; 5T62; -.
DR PDBsum; 5T6R; -.
DR PDBsum; 5TBW; -.
DR PDBsum; 5TGA; -.
DR PDBsum; 5TGM; -.
DR PDBsum; 6CB1; -.
DR PDBsum; 6ELZ; -.
DR PDBsum; 6EM5; -.
DR PDBsum; 6FT6; -.
DR PDBsum; 6GQ1; -.
DR PDBsum; 6GQB; -.
DR PDBsum; 6GQV; -.
DR PDBsum; 6HD7; -.
DR PDBsum; 6HHQ; -.
DR PDBsum; 6I7O; -.
DR PDBsum; 6M62; -.
DR PDBsum; 6N8J; -.
DR PDBsum; 6N8K; -.
DR PDBsum; 6N8L; -.
DR PDBsum; 6N8M; -.
DR PDBsum; 6N8N; -.
DR PDBsum; 6N8O; -.
DR PDBsum; 6OIG; -.
DR PDBsum; 6Q8Y; -.
DR PDBsum; 6QIK; -.
DR PDBsum; 6QT0; -.
DR PDBsum; 6QTZ; -.
DR PDBsum; 6R84; -.
DR PDBsum; 6R86; -.
DR PDBsum; 6R87; -.
DR PDBsum; 6RI5; -.
DR PDBsum; 6RZZ; -.
DR PDBsum; 6S05; -.
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; 6WOO; -.
DR PDBsum; 6YLG; -.
DR PDBsum; 6YLH; -.
DR PDBsum; 6YLX; -.
DR PDBsum; 6YLY; -.
DR PDBsum; 6Z6J; -.
DR PDBsum; 6Z6K; -.
DR PDBsum; 7AZY; -.
DR PDBsum; 7B7D; -.
DR PDBsum; 7BT6; -.
DR PDBsum; 7BTB; -.
DR PDBsum; 7NRC; -.
DR PDBsum; 7NRD; -.
DR PDBsum; 7OF1; -.
DR PDBsum; 7OH3; -.
DR PDBsum; 7OHQ; -.
DR PDBsum; 7OHR; -.
DR PDBsum; 7OHV; -.
DR AlphaFoldDB; P49167; -.
DR SMR; P49167; -.
DR BioGRID; 31588; 212.
DR ComplexPortal; CPX-1601; 60S cytosolic large ribosomal subunit.
DR DIP; DIP-3950N; -.
DR IntAct; P49167; 17.
DR MINT; P49167; -.
DR STRING; 4932.YLR325C; -.
DR iPTMnet; P49167; -.
DR MaxQB; P49167; -.
DR PaxDb; P49167; -.
DR PRIDE; P49167; -.
DR TopDownProteomics; P49167; -.
DR EnsemblFungi; YLR325C_mRNA; YLR325C; YLR325C.
DR GeneID; 851035; -.
DR KEGG; sce:YLR325C; -.
DR SGD; S000004317; RPL38.
DR VEuPathDB; FungiDB:YLR325C; -.
DR eggNOG; KOG3499; Eukaryota.
DR GeneTree; ENSGT00390000003718; -.
DR HOGENOM; CLU_152057_1_0_1; -.
DR InParanoid; P49167; -.
DR OMA; GFSKWKE; -.
DR BioCyc; YEAST:G3O-32408-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-72689; Formation of a pool of free 40S subunits.
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 PRO; PR:P49167; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P49167; protein.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA: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:0022618; P:ribonucleoprotein complex assembly; IBA:GO_Central.
DR Gene3D; 3.30.720.90; -; 1.
DR InterPro; IPR002675; Ribosomal_L38e.
DR InterPro; IPR038464; Ribosomal_L38e_sf.
DR PANTHER; PTHR10965; PTHR10965; 1.
DR Pfam; PF01781; Ribosomal_L38e; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10601260"
FT CHAIN 2..78
FT /note="60S ribosomal protein L38"
FT /id="PRO_0000215445"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 8..14
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 22..31
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 37..46
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 59..68
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:4U4R"
SQ SEQUENCE 78 AA; 8827 MW; 0ECB20AD9A4A0D42 CRC64;
MAREITDIKQ FLELTRRADV KTATVKINKK LNKAGKPFRQ TKFKVRGSSS LYTLVINDAG
KAKKLIQSLP PTLKVNRL
