RL30_YEAST
ID RL30_YEAST Reviewed; 105 AA.
AC P14120; D6VUA8;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=60S ribosomal protein L30 {ECO:0000303|PubMed:9559554};
DE AltName: Full=L32;
DE AltName: Full=Large ribosomal subunit protein eL30 {ECO:0000303|PubMed:24524803};
DE AltName: Full=RP73;
DE AltName: Full=YL38;
GN Name=RPL30 {ECO:0000303|PubMed:9559554}; Synonyms=RPL32;
GN OrderedLocusNames=YGL030W;
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], AND PROTEIN SEQUENCE OF 2-8.
RX PubMed=3316213; DOI=10.1016/s0021-9258(18)47695-8;
RA Dabeva M.D., Warner J.R.;
RT "The yeast ribosomal protein L32 and its gene.";
RL J. Biol. Chem. 262:16055-16059(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
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 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 [5]
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 [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 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-22; LYS-53 AND LYS-83, AND
RP 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 [8]
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 [9]
RP STRUCTURE BY NMR.
RX PubMed=10581556; DOI=10.1038/70081;
RA Mao H., White S.A., Williamson J.R.;
RT "A novel loop-loop recognition motif in the yeast ribosomal protein L30
RT autoregulatory RNA complex.";
RL Nat. Struct. Biol. 6:1139-1147(1999).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS).
RX PubMed=12589748; DOI=10.1016/s0022-2836(02)01476-6;
RA Chao J.A., Prasad G.S., White S.A., Stout C.D., Williamson J.R.;
RT "Inherent protein structural flexibility at the RNA-binding interface of
RT L30e.";
RL J. Mol. Biol. 326:999-1004(2003).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.24 ANGSTROMS) IN COMPLEX WITH MRNA.
RX PubMed=15242593; DOI=10.1016/j.str.2004.04.023;
RA Chao J.A., Williamson J.R.;
RT "Joint X-ray and NMR refinement of the yeast L30e-mRNA complex.";
RL Structure 12:1165-1176(2004).
RN [12]
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 [13]
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:22096102}.
CC -!- MISCELLANEOUS: Present with 59300 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL30 family.
CC {ECO:0000305}.
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DR EMBL; J03457; AAA35005.1; -; Genomic_DNA.
DR EMBL; Z72552; CAA96731.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08069.1; -; Genomic_DNA.
DR PIR; A29779; R6BY30.
DR RefSeq; NP_011485.1; NM_001180895.1.
DR PDB; 1CK2; NMR; -; A=2-105.
DR PDB; 1CN7; NMR; -; A=2-105.
DR PDB; 1NMU; X-ray; 2.31 A; B/D=2-105.
DR PDB; 1T0K; X-ray; 3.24 A; B=1-105.
DR PDB; 3J6X; EM; 6.10 A; 70=1-105.
DR PDB; 3J6Y; EM; 6.10 A; 70=1-105.
DR PDB; 3J77; EM; 6.20 A; 80=1-105.
DR PDB; 3J78; EM; 6.30 A; 80=1-105.
DR PDB; 3JCT; EM; 3.08 A; c=1-105.
DR PDB; 4U3M; X-ray; 3.00 A; O0/o0=2-105.
DR PDB; 4U3N; X-ray; 3.20 A; O0/o0=2-105.
DR PDB; 4U3U; X-ray; 2.90 A; O0/o0=2-105.
DR PDB; 4U4N; X-ray; 3.10 A; O0/o0=2-105.
DR PDB; 4U4O; X-ray; 3.60 A; O0/o0=2-105.
DR PDB; 4U4Q; X-ray; 3.00 A; O0/o0=2-105.
DR PDB; 4U4R; X-ray; 2.80 A; O0/o0=2-105.
DR PDB; 4U4U; X-ray; 3.00 A; O0/o0=2-105.
DR PDB; 4U4Y; X-ray; 3.20 A; O0/o0=2-105.
DR PDB; 4U4Z; X-ray; 3.10 A; O0/o0=2-105.
DR PDB; 4U50; X-ray; 3.20 A; O0/o0=2-105.
DR PDB; 4U51; X-ray; 3.20 A; O0/o0=2-105.
DR PDB; 4U52; X-ray; 3.00 A; O0/o0=2-105.
DR PDB; 4U53; X-ray; 3.30 A; O0/o0=2-105.
DR PDB; 4U55; X-ray; 3.20 A; O0/o0=2-105.
DR PDB; 4U56; X-ray; 3.45 A; O0/o0=2-105.
DR PDB; 4U6F; X-ray; 3.10 A; O0/o0=2-105.
DR PDB; 4V6I; EM; 8.80 A; Bf=1-105.
DR PDB; 4V7F; EM; 8.70 A; b=1-105.
DR PDB; 4V7R; X-ray; 4.00 A; BZ/DZ=1-105.
DR PDB; 4V88; X-ray; 3.00 A; Bc/Dc=1-105.
DR PDB; 4V8T; EM; 8.10 A; c=1-105.
DR PDB; 4V8Y; EM; 4.30 A; Bc=2-105.
DR PDB; 4V8Z; EM; 6.60 A; Bc=2-105.
DR PDB; 4V91; EM; 3.70 A; c=1-105.
DR PDB; 5APN; EM; 3.91 A; c=1-105.
DR PDB; 5APO; EM; 3.41 A; c=1-105.
DR PDB; 5DAT; X-ray; 3.15 A; O0/o0=2-105.
DR PDB; 5DC3; X-ray; 3.25 A; O0/o0=2-105.
DR PDB; 5DGE; X-ray; 3.45 A; O0/o0=2-105.
DR PDB; 5DGF; X-ray; 3.30 A; O0/o0=2-105.
DR PDB; 5DGV; X-ray; 3.10 A; O0/o0=2-105.
DR PDB; 5FCI; X-ray; 3.40 A; O0/o0=2-105.
DR PDB; 5FCJ; X-ray; 3.10 A; O0/o0=2-105.
DR PDB; 5FL8; EM; 9.50 A; c=1-105.
DR PDB; 5GAK; EM; 3.88 A; e=1-105.
DR PDB; 5H4P; EM; 3.07 A; c=1-105.
DR PDB; 5I4L; X-ray; 3.10 A; O0/o0=6-105.
DR PDB; 5JCS; EM; 9.50 A; c=1-105.
DR PDB; 5JUO; EM; 4.00 A; HA=1-105.
DR PDB; 5JUP; EM; 3.50 A; HA=1-105.
DR PDB; 5JUS; EM; 4.20 A; HA=1-105.
DR PDB; 5JUT; EM; 4.00 A; HA=1-105.
DR PDB; 5JUU; EM; 4.00 A; HA=1-105.
DR PDB; 5LYB; X-ray; 3.25 A; O0/o0=6-105.
DR PDB; 5M1J; EM; 3.30 A; c5=9-105.
DR PDB; 5MC6; EM; 3.80 A; AY=1-105.
DR PDB; 5MEI; X-ray; 3.50 A; AD/DE=9-105.
DR PDB; 5NDG; X-ray; 3.70 A; O0/o0=6-105.
DR PDB; 5NDV; X-ray; 3.30 A; O0/o0=6-105.
DR PDB; 5NDW; X-ray; 3.70 A; O0/o0=6-105.
DR PDB; 5OBM; X-ray; 3.40 A; O0/o0=6-105.
DR PDB; 5ON6; X-ray; 3.10 A; AD/DE=9-105.
DR PDB; 5T62; EM; 3.30 A; p=1-105.
DR PDB; 5T6R; EM; 4.50 A; p=1-105.
DR PDB; 5TBW; X-ray; 3.00 A; AD/DE=9-105.
DR PDB; 5TGA; X-ray; 3.30 A; O0/o0=6-105.
DR PDB; 5TGM; X-ray; 3.50 A; O0/o0=6-105.
DR PDB; 6CB1; EM; 4.60 A; c=1-105.
DR PDB; 6ELZ; EM; 3.30 A; c=1-105.
DR PDB; 6EM5; EM; 4.30 A; c=1-105.
DR PDB; 6FT6; EM; 3.90 A; c=1-105.
DR PDB; 6GQ1; EM; 4.40 A; c=9-105.
DR PDB; 6GQB; EM; 3.90 A; c=9-105.
DR PDB; 6GQV; EM; 4.00 A; c=9-105.
DR PDB; 6HD7; EM; 3.40 A; e=1-105.
DR PDB; 6HHQ; X-ray; 3.10 A; AD/DE=1-105.
DR PDB; 6I7O; EM; 5.30 A; AY/XY=6-105.
DR PDB; 6M62; EM; 3.20 A; c=1-105.
DR PDB; 6N8J; EM; 3.50 A; c=1-105.
DR PDB; 6N8K; EM; 3.60 A; c=1-105.
DR PDB; 6N8L; EM; 3.60 A; c=1-105.
DR PDB; 6N8M; EM; 3.50 A; p=1-105.
DR PDB; 6N8N; EM; 3.80 A; p=1-105.
DR PDB; 6N8O; EM; 3.50 A; p=1-105.
DR PDB; 6OIG; EM; 3.80 A; c=9-105.
DR PDB; 6Q8Y; EM; 3.10 A; AY=9-105.
DR PDB; 6QIK; EM; 3.10 A; c=1-105.
DR PDB; 6QT0; EM; 3.40 A; c=1-105.
DR PDB; 6QTZ; EM; 3.50 A; c=1-105.
DR PDB; 6R84; EM; 3.60 A; e=9-105.
DR PDB; 6R86; EM; 3.40 A; e=9-105.
DR PDB; 6R87; EM; 3.40 A; e=9-105.
DR PDB; 6RI5; EM; 3.30 A; c=1-105.
DR PDB; 6RZZ; EM; 3.20 A; c=1-105.
DR PDB; 6S05; EM; 3.90 A; c=1-105.
DR PDB; 6S47; EM; 3.28 A; Ae=2-105.
DR PDB; 6SNT; EM; 2.80 A; an=1-105.
DR PDB; 6SV4; EM; 3.30 A; AY/XY/zY=1-105.
DR PDB; 6T4Q; EM; 2.60 A; Lc=9-104.
DR PDB; 6T7I; EM; 3.20 A; Lc=1-105.
DR PDB; 6T7T; EM; 3.10 A; Lc=1-105.
DR PDB; 6T83; EM; 4.00 A; N/cy=1-105.
DR PDB; 6TB3; EM; 2.80 A; AY=9-104.
DR PDB; 6TNU; EM; 3.10 A; AY=9-104.
DR PDB; 6WOO; EM; 2.90 A; c=9-105.
DR PDB; 6XIQ; EM; 4.20 A; c=1-105.
DR PDB; 6XIR; EM; 3.20 A; c=1-105.
DR PDB; 6YLG; EM; 3.00 A; n=1-105.
DR PDB; 6YLH; EM; 3.10 A; n=1-105.
DR PDB; 6YLX; EM; 3.90 A; c=1-105.
DR PDB; 6YLY; EM; 3.80 A; c=1-105.
DR PDB; 6Z6J; EM; 3.40 A; Lc=1-105.
DR PDB; 6Z6K; EM; 3.40 A; Lc=1-105.
DR PDB; 7B7D; EM; 3.30 A; LY=9-104.
DR PDB; 7BT6; EM; 3.12 A; c=1-105.
DR PDB; 7BTB; EM; 3.22 A; c=1-105.
DR PDB; 7NRC; EM; 3.90 A; Le=9-104.
DR PDB; 7NRD; EM; 4.36 A; Le=9-104.
DR PDB; 7OF1; EM; 3.10 A; c=1-105.
DR PDB; 7OH3; EM; 3.40 A; c=1-105.
DR PDB; 7OHQ; EM; 3.10 A; c=1-105.
DR PDB; 7OHR; EM; 4.72 A; c=1-105.
DR PDB; 7RR5; EM; 3.23 A; Lc=1-105.
DR PDBsum; 1CK2; -.
DR PDBsum; 1CN7; -.
DR PDBsum; 1NMU; -.
DR PDBsum; 1T0K; -.
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; 4V7R; -.
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; 6XIQ; -.
DR PDBsum; 6XIR; -.
DR PDBsum; 6YLG; -.
DR PDBsum; 6YLH; -.
DR PDBsum; 6YLX; -.
DR PDBsum; 6YLY; -.
DR PDBsum; 6Z6J; -.
DR PDBsum; 6Z6K; -.
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; 7RR5; -.
DR AlphaFoldDB; P14120; -.
DR BMRB; P14120; -.
DR SMR; P14120; -.
DR BioGRID; 33216; 133.
DR ComplexPortal; CPX-1601; 60S cytosolic large ribosomal subunit.
DR DIP; DIP-1891N; -.
DR IntAct; P14120; 93.
DR MINT; P14120; -.
DR STRING; 4932.YGL030W; -.
DR MoonProt; P14120; -.
DR iPTMnet; P14120; -.
DR MaxQB; P14120; -.
DR PaxDb; P14120; -.
DR PRIDE; P14120; -.
DR TopDownProteomics; P14120; -.
DR EnsemblFungi; YGL030W_mRNA; YGL030W; YGL030W.
DR GeneID; 852853; -.
DR KEGG; sce:YGL030W; -.
DR SGD; S000002998; RPL30.
DR VEuPathDB; FungiDB:YGL030W; -.
DR eggNOG; KOG2988; Eukaryota.
DR GeneTree; ENSGT00390000012138; -.
DR HOGENOM; CLU_130502_0_1_1; -.
DR InParanoid; P14120; -.
DR OMA; RPHKIMA; -.
DR BioCyc; YEAST:G3O-30546-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 EvolutionaryTrace; P14120; -.
DR PRO; PR:P14120; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P14120; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD.
DR GO; GO:0030627; F:pre-mRNA 5'-splice site binding; IMP:SGD.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; IC:SGD.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IMP:SGD.
DR GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR Gene3D; 3.30.1330.30; -; 1.
DR InterPro; IPR039109; L30/L30e/YlxQ.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR022991; Ribosomal_L30e_CS.
DR InterPro; IPR004038; Ribosomal_L7Ae/L30e/S12e/Gad45.
DR PANTHER; PTHR11449; PTHR11449; 1.
DR Pfam; PF01248; Ribosomal_L7Ae; 1.
DR SUPFAM; SSF55315; SSF55315; 1.
DR PROSITE; PS00709; RIBOSOMAL_L30E_1; 1.
DR PROSITE; PS00993; RIBOSOMAL_L30E_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Isopeptide bond;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10601260,
FT ECO:0000269|PubMed:3316213"
FT CHAIN 2..105
FT /note="60S ribosomal protein L30"
FT /id="PRO_0000146143"
FT CROSSLNK 22
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 83
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT HELIX 7..20
FT /evidence="ECO:0007829|PDB:1NMU"
FT STRAND 21..25
FT /evidence="ECO:0007829|PDB:1NMU"
FT HELIX 26..35
FT /evidence="ECO:0007829|PDB:1NMU"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:1NMU"
FT HELIX 53..62
FT /evidence="ECO:0007829|PDB:1NMU"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:1NMU"
FT HELIX 79..87
FT /evidence="ECO:0007829|PDB:1NMU"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:1NMU"
FT HELIX 100..104
FT /evidence="ECO:0007829|PDB:1NMU"
SQ SEQUENCE 105 AA; 11415 MW; 963C973A02E9C8E5 CRC64;
MAPVKSQESI NQKLALVIKS GKYTLGYKST VKSLRQGKSK LIIIAANTPV LRKSELEYYA
MLSKTKVYYF QGGNNELGTA VGKLFRVGVV SILEAGDSDI LTTLA
