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RL34A_YEAST
ID   RL34A_YEAST             Reviewed;         121 AA.
AC   P87262; D3DLW0; Q03189;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 165.
DE   RecName: Full=60S ribosomal protein L34-A {ECO:0000303|PubMed:9559554};
DE   AltName: Full=Large ribosomal subunit protein eL34-A {ECO:0000303|PubMed:24524803};
GN   Name=RPL34A {ECO:0000303|PubMed:9559554}; OrderedLocusNames=YER056C-A;
GN   ORFNames=YER056BC;
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=9169868;
RA   Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA   Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA   Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA   Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA   Botstein D., Davis R.W.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL   Nature 387:78-81(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   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   [5]
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   [6]
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   [7]
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   [8]
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 23600 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- MISCELLANEOUS: There are 2 genes for eL34 in yeast. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL34 family.
CC       {ECO:0000305}.
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DR   EMBL; U18813; AAB64609.1; -; Genomic_DNA.
DR   EMBL; BK006939; DAA07714.1; -; Genomic_DNA.
DR   PIR; S53549; S53549.
DR   RefSeq; NP_010977.2; NM_001180036.1.
DR   PDB; 3J6X; EM; 6.10 A; 74=1-121.
DR   PDB; 3J6Y; EM; 6.10 A; 74=1-121.
DR   PDB; 3J77; EM; 6.20 A; 84=1-121.
DR   PDB; 3J78; EM; 6.30 A; 84=1-121.
DR   PDB; 3JCT; EM; 3.08 A; g=1-121.
DR   PDB; 4U3M; X-ray; 3.00 A; O4/o4=2-121.
DR   PDB; 4U3N; X-ray; 3.20 A; O4/o4=2-121.
DR   PDB; 4U3U; X-ray; 2.90 A; O4/o4=2-121.
DR   PDB; 4U4N; X-ray; 3.10 A; O4/o4=2-121.
DR   PDB; 4U4O; X-ray; 3.60 A; O4/o4=2-109.
DR   PDB; 4U4Q; X-ray; 3.00 A; O4/o4=2-120.
DR   PDB; 4U4R; X-ray; 2.80 A; O4/o4=2-121.
DR   PDB; 4U4U; X-ray; 3.00 A; O4/o4=2-121.
DR   PDB; 4U4Y; X-ray; 3.20 A; O4/o4=2-120.
DR   PDB; 4U4Z; X-ray; 3.10 A; O4/o4=2-109.
DR   PDB; 4U50; X-ray; 3.20 A; O4/o4=2-120.
DR   PDB; 4U51; X-ray; 3.20 A; O4/o4=2-120.
DR   PDB; 4U52; X-ray; 3.00 A; O4/o4=2-109.
DR   PDB; 4U53; X-ray; 3.30 A; O4/o4=2-121.
DR   PDB; 4U55; X-ray; 3.20 A; O4/o4=2-120.
DR   PDB; 4U56; X-ray; 3.45 A; O4/o4=2-120.
DR   PDB; 4U6F; X-ray; 3.10 A; O4/o4=2-120.
DR   PDB; 4V6I; EM; 8.80 A; Bi=1-118.
DR   PDB; 4V7F; EM; 8.70 A; f=1-121.
DR   PDB; 4V88; X-ray; 3.00 A; Bg/Dg=1-121.
DR   PDB; 4V8T; EM; 8.10 A; g=1-121.
DR   PDB; 4V8Y; EM; 4.30 A; Bg=2-121.
DR   PDB; 4V8Z; EM; 6.60 A; Bg=2-121.
DR   PDB; 4V91; EM; 3.70 A; g=1-121.
DR   PDB; 5APN; EM; 3.91 A; g=1-121.
DR   PDB; 5APO; EM; 3.41 A; g=1-121.
DR   PDB; 5DAT; X-ray; 3.15 A; O4/o4=2-121.
DR   PDB; 5DC3; X-ray; 3.25 A; O4/o4=2-121.
DR   PDB; 5DGE; X-ray; 3.45 A; O4/o4=2-109.
DR   PDB; 5DGF; X-ray; 3.30 A; O4/o4=2-121.
DR   PDB; 5DGV; X-ray; 3.10 A; O4/o4=2-121.
DR   PDB; 5FCI; X-ray; 3.40 A; O4/o4=2-121.
DR   PDB; 5FCJ; X-ray; 3.10 A; O4/o4=2-121.
DR   PDB; 5FL8; EM; 9.50 A; g=1-121.
DR   PDB; 5GAK; EM; 3.88 A; i=1-121.
DR   PDB; 5H4P; EM; 3.07 A; g=1-121.
DR   PDB; 5I4L; X-ray; 3.10 A; O4/o4=2-113.
DR   PDB; 5JCS; EM; 9.50 A; g=1-121.
DR   PDB; 5JUO; EM; 4.00 A; LA=1-121.
DR   PDB; 5JUP; EM; 3.50 A; LA=1-121.
DR   PDB; 5JUS; EM; 4.20 A; LA=1-121.
DR   PDB; 5JUT; EM; 4.00 A; LA=1-121.
DR   PDB; 5JUU; EM; 4.00 A; LA=1-121.
DR   PDB; 5LYB; X-ray; 3.25 A; O4/o4=2-113.
DR   PDB; 5M1J; EM; 3.30 A; g5=2-113.
DR   PDB; 5MC6; EM; 3.80 A; BN=1-121.
DR   PDB; 5MEI; X-ray; 3.50 A; AH/DI=2-113.
DR   PDB; 5NDG; X-ray; 3.70 A; O4/o4=2-113.
DR   PDB; 5NDV; X-ray; 3.30 A; O4/o4=2-113.
DR   PDB; 5NDW; X-ray; 3.70 A; O4/o4=2-113.
DR   PDB; 5OBM; X-ray; 3.40 A; O4/o4=2-113.
DR   PDB; 5ON6; X-ray; 3.10 A; AH/DI=2-113.
DR   PDB; 5T62; EM; 3.30 A; t=1-121.
DR   PDB; 5T6R; EM; 4.50 A; t=1-121.
DR   PDB; 5TBW; X-ray; 3.00 A; AH/DI=2-113.
DR   PDB; 5TGA; X-ray; 3.30 A; O4/o4=2-113.
DR   PDB; 5TGM; X-ray; 3.50 A; O4/o4=2-113.
DR   PDB; 6CB1; EM; 4.60 A; g=1-121.
DR   PDB; 6ELZ; EM; 3.30 A; g=1-121.
DR   PDB; 6EM5; EM; 4.30 A; g=1-121.
DR   PDB; 6FT6; EM; 3.90 A; g=1-121.
DR   PDB; 6GQ1; EM; 4.40 A; g=2-113.
DR   PDB; 6GQB; EM; 3.90 A; g=2-113.
DR   PDB; 6GQV; EM; 4.00 A; g=2-113.
DR   PDB; 6HD7; EM; 3.40 A; i=1-121.
DR   PDB; 6HHQ; X-ray; 3.10 A; AH/DI=1-121.
DR   PDB; 6I7O; EM; 5.30 A; BN/YN=2-113.
DR   PDB; 6M62; EM; 3.20 A; g=1-121.
DR   PDB; 6N8J; EM; 3.50 A; g=1-121.
DR   PDB; 6N8K; EM; 3.60 A; g=1-121.
DR   PDB; 6N8L; EM; 3.60 A; g=1-121.
DR   PDB; 6N8M; EM; 3.50 A; t=1-121.
DR   PDB; 6N8N; EM; 3.80 A; t=1-121.
DR   PDB; 6N8O; EM; 3.50 A; t=1-121.
DR   PDB; 6OIG; EM; 3.80 A; g=2-113.
DR   PDB; 6Q8Y; EM; 3.10 A; BN=2-113.
DR   PDB; 6QIK; EM; 3.10 A; g=1-121.
DR   PDB; 6QT0; EM; 3.40 A; g=1-121.
DR   PDB; 6QTZ; EM; 3.50 A; g=1-121.
DR   PDB; 6R84; EM; 3.60 A; i=2-113.
DR   PDB; 6R86; EM; 3.40 A; i=2-113.
DR   PDB; 6R87; EM; 3.40 A; i=2-113.
DR   PDB; 6RI5; EM; 3.30 A; g=1-121.
DR   PDB; 6RZZ; EM; 3.20 A; g=1-121.
DR   PDB; 6S05; EM; 3.90 A; g=1-121.
DR   PDB; 6S47; EM; 3.28 A; Ai=1-121.
DR   PDB; 6SNT; EM; 2.80 A; aj=1-121.
DR   PDB; 6SV4; EM; 3.30 A; BN/YN/ZN=1-121.
DR   PDB; 6T4Q; EM; 2.60 A; Lg=2-113.
DR   PDB; 6T7I; EM; 3.20 A; Lg=1-121.
DR   PDB; 6T7T; EM; 3.10 A; Lg=1-121.
DR   PDB; 6T83; EM; 4.00 A; R/gy=1-121.
DR   PDB; 6TB3; EM; 2.80 A; BN=2-113.
DR   PDB; 6TNU; EM; 3.10 A; BN=2-113.
DR   PDB; 6WOO; EM; 2.90 A; g=2-121.
DR   PDB; 6XIQ; EM; 4.20 A; g=1-121.
DR   PDB; 6XIR; EM; 3.20 A; g=1-121.
DR   PDB; 6YLG; EM; 3.00 A; g=1-121.
DR   PDB; 6YLH; EM; 3.10 A; g=1-121.
DR   PDB; 6YLX; EM; 3.90 A; g=1-121.
DR   PDB; 6YLY; EM; 3.80 A; g=1-121.
DR   PDB; 6Z6J; EM; 3.40 A; Lg=1-121.
DR   PDB; 6Z6K; EM; 3.40 A; Lg=1-121.
DR   PDB; 7AZY; EM; 2.88 A; B=1-121.
DR   PDB; 7B7D; EM; 3.30 A; Lc=2-113.
DR   PDB; 7BT6; EM; 3.12 A; g=1-121.
DR   PDB; 7BTB; EM; 3.22 A; g=1-121.
DR   PDB; 7NRC; EM; 3.90 A; Li=2-113.
DR   PDB; 7NRD; EM; 4.36 A; Li=2-113.
DR   PDB; 7OF1; EM; 3.10 A; g=1-121.
DR   PDB; 7OH3; EM; 3.40 A; g=1-121.
DR   PDB; 7OHQ; EM; 3.10 A; g=1-121.
DR   PDB; 7OHR; EM; 4.72 A; g=1-121.
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; 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; 7OHQ; -.
DR   PDBsum; 7OHR; -.
DR   AlphaFoldDB; P87262; -.
DR   SMR; P87262; -.
DR   BioGRID; 36797; 113.
DR   IntAct; P87262; 17.
DR   MINT; P87262; -.
DR   STRING; 4932.YER056C-A; -.
DR   iPTMnet; P87262; -.
DR   MaxQB; P87262; -.
DR   PaxDb; P87262; -.
DR   PRIDE; P87262; -.
DR   EnsemblFungi; YER056C-A_mRNA; YER056C-A; YER056C-A.
DR   GeneID; 856784; -.
DR   KEGG; sce:YER056C-A; -.
DR   SGD; S000002135; RPL34A.
DR   VEuPathDB; FungiDB:YER056C-A; -.
DR   eggNOG; KOG1790; Eukaryota.
DR   GeneTree; ENSGT00940000168239; -.
DR   HOGENOM; CLU_118652_1_1_1; -.
DR   InParanoid; P87262; -.
DR   OMA; KTHAFAK; -.
DR   BioCyc; YEAST:G3O-30350-MON; -.
DR   PRO; PR:P87262; -.
DR   Proteomes; UP000002311; Chromosome V.
DR   RNAct; P87262; protein.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0030687; C:preribosome, large subunit precursor; 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:0042254; P:ribosome biogenesis; IDA:SGD.
DR   InterPro; IPR008195; Ribosomal_L34Ae.
DR   InterPro; IPR018065; Ribosomal_L34e_CS.
DR   PANTHER; PTHR10759; PTHR10759; 1.
DR   Pfam; PF01199; Ribosomal_L34e; 1.
DR   PRINTS; PR01250; RIBOSOMALL34.
DR   PROSITE; PS01145; RIBOSOMAL_L34E; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein.
FT   CHAIN           1..121
FT                   /note="60S ribosomal protein L34-A"
FT                   /id="PRO_0000131845"
FT   STRAND          8..10
FT                   /evidence="ECO:0007829|PDB:4U4R"
FT   HELIX           16..18
FT                   /evidence="ECO:0007829|PDB:4U4R"
FT   STRAND          19..24
FT                   /evidence="ECO:0007829|PDB:4U4R"
FT   TURN            26..28
FT                   /evidence="ECO:0007829|PDB:4U53"
FT   STRAND          30..35
FT                   /evidence="ECO:0007829|PDB:4U4R"
FT   TURN            45..47
FT                   /evidence="ECO:0007829|PDB:4U4R"
FT   STRAND          52..54
FT                   /evidence="ECO:0007829|PDB:4U50"
FT   HELIX           59..64
FT                   /evidence="ECO:0007829|PDB:4U4R"
FT   HELIX           67..70
FT                   /evidence="ECO:0007829|PDB:4U4R"
FT   TURN            75..79
FT                   /evidence="ECO:0007829|PDB:4U4R"
FT   HELIX           83..111
FT                   /evidence="ECO:0007829|PDB:4U4R"
SQ   SEQUENCE   121 AA;  13639 MW;  F3315816CD85ACEA CRC64;
     MAQRVTFRRR NPYNTRSNKI KVVKTPGGIL RAQHVKKLAT RPKCGDCGSA LQGISTLRPR
     QYATVSKTHK TVSRAYGGSR CANCVKERII RAFLIEEQKI VKKVVKEQTE AAKKSEKKAK
     K
 
 
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