RL14A_YEAST
ID RL14A_YEAST Reviewed; 138 AA.
AC P36105; D6VXT1;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=60S ribosomal protein L14-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=Large ribosomal subunit protein eL14-A {ECO:0000303|PubMed:24524803};
GN Name=RPL14A {ECO:0000303|PubMed:9559554}; OrderedLocusNames=YKL006W;
GN ORFNames=YKL153;
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].
RX PubMed=8488728; DOI=10.1002/yea.320090307;
RA Boyer J., Pascolo S., Richard G.-F., Dujon B.;
RT "Sequence of a 7.8 kb segment on the left arm of yeast chromosome XI
RT reveals four open reading frames, including the CAP1 gene, an intron-
RT containing gene and a gene encoding a homolog to the mammalian UOG-1
RT gene.";
RL Yeast 9:279-287(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(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 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, 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 [6]
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 [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 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 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 [10]
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 -!- PTM: N-terminally acetylated by acetyltransferase NatA.
CC {ECO:0000269|PubMed:10601260}.
CC -!- MISCELLANEOUS: Present with 45300 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for eL14 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL14 family.
CC {ECO:0000305}.
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DR EMBL; X61398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z28006; CAA81839.1; -; Genomic_DNA.
DR EMBL; Z28005; CAA81838.1; -; Genomic_DNA.
DR EMBL; S59773; AAC60550.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09151.1; -; Genomic_DNA.
DR PIR; S30133; S30133.
DR RefSeq; NP_012920.1; NM_001179572.1.
DR PDB; 3J6X; EM; 6.10 A; 54=1-138.
DR PDB; 3J6Y; EM; 6.10 A; 54=1-138.
DR PDB; 3J77; EM; 6.20 A; 64=1-138.
DR PDB; 3J78; EM; 6.30 A; 64=1-138.
DR PDB; 3JCT; EM; 3.08 A; M=1-138.
DR PDB; 4U3M; X-ray; 3.00 A; M4/m4=2-138.
DR PDB; 4U3N; X-ray; 3.20 A; M4/m4=2-138.
DR PDB; 4U3U; X-ray; 2.90 A; M4/m4=2-138.
DR PDB; 4U4N; X-ray; 3.10 A; M4/m4=2-138.
DR PDB; 4U4O; X-ray; 3.60 A; M4/m4=2-138.
DR PDB; 4U4Q; X-ray; 3.00 A; M4/m4=2-138.
DR PDB; 4U4R; X-ray; 2.80 A; M4/m4=2-138.
DR PDB; 4U4U; X-ray; 3.00 A; M4/m4=2-138.
DR PDB; 4U4Y; X-ray; 3.20 A; M4/m4=2-138.
DR PDB; 4U4Z; X-ray; 3.10 A; M4/m4=2-138.
DR PDB; 4U50; X-ray; 3.20 A; M4/m4=2-138.
DR PDB; 4U51; X-ray; 3.20 A; M4/m4=2-138.
DR PDB; 4U52; X-ray; 3.00 A; M4/m4=2-138.
DR PDB; 4U53; X-ray; 3.30 A; M4/m4=2-138.
DR PDB; 4U55; X-ray; 3.20 A; M4/m4=2-138.
DR PDB; 4U56; X-ray; 3.45 A; M4/m4=2-138.
DR PDB; 4U6F; X-ray; 3.10 A; M4/m4=2-138.
DR PDB; 4V6I; EM; 8.80 A; BN=1-138.
DR PDB; 4V7F; EM; 8.70 A; M=1-138.
DR PDB; 4V7R; X-ray; 4.00 A; BN/DN=1-138.
DR PDB; 4V88; X-ray; 3.00 A; BM/DM=1-138.
DR PDB; 4V8T; EM; 8.10 A; M=1-138.
DR PDB; 5APN; EM; 3.91 A; M=1-138.
DR PDB; 5APO; EM; 3.41 A; M=1-138.
DR PDB; 5DAT; X-ray; 3.15 A; M4/m4=2-138.
DR PDB; 5DC3; X-ray; 3.25 A; M4/m4=2-138.
DR PDB; 5DGE; X-ray; 3.45 A; M4/m4=2-138.
DR PDB; 5DGF; X-ray; 3.30 A; M4/m4=2-138.
DR PDB; 5DGV; X-ray; 3.10 A; M4/m4=2-138.
DR PDB; 5FCI; X-ray; 3.40 A; M4/m4=2-138.
DR PDB; 5FCJ; X-ray; 3.10 A; M4/m4=2-138.
DR PDB; 5FL8; EM; 9.50 A; M=1-138.
DR PDB; 5GAK; EM; 3.88 A; O=1-138.
DR PDB; 5H4P; EM; 3.07 A; M=1-138.
DR PDB; 5I4L; X-ray; 3.10 A; M4/m4=2-138.
DR PDB; 5JCS; EM; 9.50 A; M=1-138.
DR PDB; 5JUO; EM; 4.00 A; R=1-138.
DR PDB; 5JUP; EM; 3.50 A; R=1-138.
DR PDB; 5JUS; EM; 4.20 A; R=1-138.
DR PDB; 5JUT; EM; 4.00 A; R=1-138.
DR PDB; 5JUU; EM; 4.00 A; R=1-138.
DR PDB; 5LYB; X-ray; 3.25 A; M4/m4=2-138.
DR PDB; 5M1J; EM; 3.30 A; M5=3-138.
DR PDB; 5MC6; EM; 3.80 A; AM=1-138.
DR PDB; 5MEI; X-ray; 3.50 A; CO/u=3-138.
DR PDB; 5NDG; X-ray; 3.70 A; M4/m4=2-138.
DR PDB; 5NDV; X-ray; 3.30 A; M4/m4=2-138.
DR PDB; 5NDW; X-ray; 3.70 A; M4/m4=2-138.
DR PDB; 5OBM; X-ray; 3.40 A; M4/m4=2-138.
DR PDB; 5ON6; X-ray; 3.10 A; CO/u=3-138.
DR PDB; 5T62; EM; 3.30 A; O=1-138.
DR PDB; 5T6R; EM; 4.50 A; O=1-138.
DR PDB; 5TBW; X-ray; 3.00 A; CO/u=3-138.
DR PDB; 5TGA; X-ray; 3.30 A; M4/m4=2-138.
DR PDB; 5TGM; X-ray; 3.50 A; M4/m4=2-138.
DR PDB; 5Z3G; EM; 3.65 A; Q=1-138.
DR PDB; 6C0F; EM; 3.70 A; M=1-138.
DR PDB; 6CB1; EM; 4.60 A; M=1-138.
DR PDB; 6ELZ; EM; 3.30 A; M=1-138.
DR PDB; 6EM1; EM; 3.60 A; M=1-138.
DR PDB; 6EM3; EM; 3.20 A; M=1-138.
DR PDB; 6EM4; EM; 4.10 A; M=1-138.
DR PDB; 6EM5; EM; 4.30 A; M=1-138.
DR PDB; 6FT6; EM; 3.90 A; M=1-138.
DR PDB; 6GQ1; EM; 4.40 A; M=3-138.
DR PDB; 6GQB; EM; 3.90 A; M=3-138.
DR PDB; 6GQV; EM; 4.00 A; M=3-138.
DR PDB; 6HD7; EM; 3.40 A; O=1-138.
DR PDB; 6HHQ; X-ray; 3.10 A; CO/u=1-138.
DR PDB; 6I7O; EM; 5.30 A; AM/XM=2-138.
DR PDB; 6M62; EM; 3.20 A; M=1-138.
DR PDB; 6N8J; EM; 3.50 A; M=1-138.
DR PDB; 6N8K; EM; 3.60 A; M=1-138.
DR PDB; 6N8L; EM; 3.60 A; M=1-138.
DR PDB; 6N8M; EM; 3.50 A; O=1-138.
DR PDB; 6N8N; EM; 3.80 A; O=1-138.
DR PDB; 6N8O; EM; 3.50 A; O=1-138.
DR PDB; 6OIG; EM; 3.80 A; M=3-138.
DR PDB; 6Q8Y; EM; 3.10 A; AM=3-138.
DR PDB; 6QIK; EM; 3.10 A; M=1-138.
DR PDB; 6QT0; EM; 3.40 A; M=1-138.
DR PDB; 6QTZ; EM; 3.50 A; M=1-138.
DR PDB; 6R84; EM; 3.60 A; O=3-138.
DR PDB; 6R86; EM; 3.40 A; O=3-138.
DR PDB; 6R87; EM; 3.40 A; O=3-138.
DR PDB; 6RI5; EM; 3.30 A; M=1-138.
DR PDB; 6RZZ; EM; 3.20 A; M=1-138.
DR PDB; 6S05; EM; 3.90 A; M=1-138.
DR PDB; 6S47; EM; 3.28 A; AO=2-138.
DR PDB; 6SNT; EM; 2.80 A; s=1-138.
DR PDB; 6SV4; EM; 3.30 A; AM/XM/zM=1-138.
DR PDB; 6T4Q; EM; 2.60 A; LM=3-138.
DR PDB; 6T7I; EM; 3.20 A; LM=1-138.
DR PDB; 6T7T; EM; 3.10 A; LM=1-138.
DR PDB; 6T83; EM; 4.00 A; My/Oa=1-138.
DR PDB; 6TB3; EM; 2.80 A; AM=3-138.
DR PDB; 6TNU; EM; 3.10 A; AM=3-138.
DR PDB; 6WOO; EM; 2.90 A; M=2-137.
DR PDB; 6XIQ; EM; 4.20 A; M=1-138.
DR PDB; 6XIR; EM; 3.20 A; M=1-138.
DR PDB; 6YLG; EM; 3.00 A; M=1-138.
DR PDB; 6YLH; EM; 3.10 A; M=1-138.
DR PDB; 6YLX; EM; 3.90 A; M=1-138.
DR PDB; 6YLY; EM; 3.80 A; M=1-138.
DR PDB; 6Z6J; EM; 3.40 A; LM=1-138.
DR PDB; 6Z6K; EM; 3.40 A; LM=1-138.
DR PDB; 7AZY; EM; 2.88 A; N=1-138.
DR PDB; 7B7D; EM; 3.30 A; LO=3-138.
DR PDB; 7BT6; EM; 3.12 A; M=1-138.
DR PDB; 7BTB; EM; 3.22 A; M=1-138.
DR PDB; 7NRC; EM; 3.90 A; LO=3-138.
DR PDB; 7NRD; EM; 4.36 A; LO=3-138.
DR PDB; 7OF1; EM; 3.10 A; M=1-138.
DR PDB; 7OH3; EM; 3.40 A; M=1-138.
DR PDB; 7OHP; EM; 3.90 A; M=1-138.
DR PDB; 7OHQ; EM; 3.10 A; M=1-138.
DR PDB; 7OHR; EM; 4.72 A; M=1-138.
DR PDB; 7OHS; EM; 4.38 A; M=1-138.
DR PDB; 7OHT; EM; 4.70 A; M=1-138.
DR PDB; 7OHU; EM; 3.70 A; M=1-138.
DR PDB; 7OHV; EM; 3.90 A; M=1-138.
DR PDB; 7OHW; EM; 3.50 A; M=1-138.
DR PDB; 7OHX; EM; 3.30 A; M=1-138.
DR PDB; 7OHY; EM; 3.90 A; M=1-138.
DR PDB; 7OSA; X-ray; 3.00 A; eL14=1-138.
DR PDB; 7OSM; X-ray; 3.00 A; eL14=1-138.
DR PDB; 7RR5; EM; 3.23 A; LM=1-138.
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; 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; 5Z3G; -.
DR PDBsum; 6C0F; -.
DR PDBsum; 6CB1; -.
DR PDBsum; 6ELZ; -.
DR PDBsum; 6EM1; -.
DR PDBsum; 6EM3; -.
DR PDBsum; 6EM4; -.
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; 7AZY; -.
DR PDBsum; 7B7D; -.
DR PDBsum; 7BT6; -.
DR PDBsum; 7BTB; -.
DR PDBsum; 7NRC; -.
DR PDBsum; 7NRD; -.
DR PDBsum; 7OF1; -.
DR PDBsum; 7OH3; -.
DR PDBsum; 7OHP; -.
DR PDBsum; 7OHQ; -.
DR PDBsum; 7OHR; -.
DR PDBsum; 7OHS; -.
DR PDBsum; 7OHT; -.
DR PDBsum; 7OHU; -.
DR PDBsum; 7OHV; -.
DR PDBsum; 7OHW; -.
DR PDBsum; 7OHX; -.
DR PDBsum; 7OHY; -.
DR PDBsum; 7OSA; -.
DR PDBsum; 7OSM; -.
DR PDBsum; 7RR5; -.
DR AlphaFoldDB; P36105; -.
DR SMR; P36105; -.
DR BioGRID; 34127; 571.
DR DIP; DIP-8081N; -.
DR IntAct; P36105; 23.
DR MINT; P36105; -.
DR STRING; 4932.YKL006W; -.
DR iPTMnet; P36105; -.
DR MaxQB; P36105; -.
DR PaxDb; P36105; -.
DR PRIDE; P36105; -.
DR EnsemblFungi; YKL006W_mRNA; YKL006W; YKL006W.
DR GeneID; 853864; -.
DR KEGG; sce:YKL006W; -.
DR SGD; S000001489; RPL14A.
DR VEuPathDB; FungiDB:YKL006W; -.
DR eggNOG; KOG3421; Eukaryota.
DR GeneTree; ENSGT00390000007888; -.
DR HOGENOM; CLU_082438_3_1_1; -.
DR InParanoid; P36105; -.
DR OMA; VKAANWR; -.
DR BioCyc; YEAST:G3O-31816-MON; -.
DR PRO; PR:P36105; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36105; protein.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; 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:0016236; P:macroautophagy; IMP:SGD.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IBA:GO_Central.
DR CDD; cd06088; KOW_RPL14; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR002784; Ribosomal_L14e_dom.
DR InterPro; IPR039660; Ribosomal_protein_L14.
DR InterPro; IPR041985; RPL14_KOW.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR11127; PTHR11127; 1.
DR Pfam; PF01929; Ribosomal_L14e; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10601260"
FT CHAIN 2..138
FT /note="60S ribosomal protein L14-A"
FT /id="PRO_0000132043"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:10601260"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 40..48
FT /evidence="ECO:0007829|PDB:6EM3"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 78..88
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 90..95
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 98..110
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 114..134
FT /evidence="ECO:0007829|PDB:6EM3"
SQ SEQUENCE 138 AA; 15167 MW; F8F2A346ABB395BC CRC64;
MSTDSIVKAS NWRLVEVGRV VLIKKGQSAG KLAAIVEIID QKKVLIDGPK AGVPRQAINL
GQVVLTPLTF ALPRGARTAT VSKKWAAAAV CEKWAASSWA KKIAQRERRA ALTDFERFQV
MVLRKQKRYT VKKALAKA
