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RL4A_YEAST
ID   RL4A_YEAST              Reviewed;         362 AA.
AC   P10664; D6VQ32;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   03-AUG-2022, entry version 197.
DE   RecName: Full=60S ribosomal protein L4-A {ECO:0000303|PubMed:9559554};
DE   AltName: Full=L2;
DE   AltName: Full=Large ribosomal subunit protein uL4-A {ECO:0000303|PubMed:24524803};
DE   AltName: Full=RP2;
DE   AltName: Full=YL2;
GN   Name=RPL4A {ECO:0000303|PubMed:9559554}; Synonyms=RPL2, RPL2A;
GN   OrderedLocusNames=YBR031W; ORFNames=YBR0315;
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=2834365; DOI=10.1016/s0021-9258(18)68770-8;
RA   Presutti C., Lucioli A., Bozzoni I.;
RT   "Ribosomal protein L2 in Saccharomyces cerevisiae is homologous to
RT   ribosomal protein L1 in Xenopus laevis. Isolation and characterization of
RT   the genes.";
RL   J. Biol. Chem. 263:6188-6192(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091864; DOI=10.1002/yea.320100010;
RA   Smits P.H.M., de Haan M., Maat C., Grivell L.A.;
RT   "The complete sequence of a 33 kb fragment on the right arm of chromosome
RT   II from Saccharomyces cerevisiae reveals 16 open reading frames, including
RT   ten new open reading frames, five previously identified genes and a
RT   homologue of the SCO1 gene.";
RL   Yeast 10:S75-S80(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [4]
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   [5]
RP   FUNCTION IN L2 MRNA REGULATION.
RX   PubMed=2065661; DOI=10.1002/j.1460-2075.1991.tb07757.x;
RA   Presutti C., Ciafre S.-A., Bozzoni I.;
RT   "The ribosomal protein L2 in S. cerevisiae controls the level of
RT   accumulation of its own mRNA.";
RL   EMBO J. 10:2215-2221(1991).
RN   [6]
RP   PROTEIN SEQUENCE OF 2-21, AND ACETYLATION AT SER-2 BY NATA.
RX   PubMed=1544921; DOI=10.1016/s0021-9258(18)42785-8;
RA   Takakura H., Tsunasawa S., Miyagi M., Warner J.R.;
RT   "NH2-terminal acetylation of ribosomal proteins of Saccharomyces
RT   cerevisiae.";
RL   J. Biol. Chem. 267:5442-5445(1992).
RN   [7]
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   [8]
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   [9]
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   [10]
RP   SUBUNIT, INTERACTION WITH ACL4 AND KAP104, DOMAIN, SUBCELLULAR LOCATION,
RP   AND MUTAGENESIS OF ARG-95; ARG-98; ILE-289; ILE-290; ILE-295; LYS-314;
RP   LYS-315; LYS-319; LYS-332 AND PHE-334.
RX   PubMed=25936803; DOI=10.1016/j.molcel.2015.03.029;
RA   Stelter P., Huber F.M., Kunze R., Flemming D., Hoelz A., Hurt E.;
RT   "Coordinated ribosomal L4 protein assembly into the pre-ribosome is
RT   regulated by its eukaryote-specific extension.";
RL   Mol. Cell 58:854-862(2015).
RN   [11]
RP   METHYLATION AT ARG-95.
RX   PubMed=26046779; DOI=10.1002/pmic.201500032;
RA   Plank M., Fischer R., Geoghegan V., Charles P.D., Konietzny R., Acuto O.,
RA   Pears C., Schofield C.J., Kessler B.M.;
RT   "Expanding the yeast protein arginine methylome.";
RL   Proteomics 15:3232-3243(2015).
RN   [12]
RP   3D-STRUCTURE MODELING OF 5-260, AND ELECTRON MICROSCOPY.
RX   PubMed=11701127; DOI=10.1016/s0092-8674(01)00539-6;
RA   Spahn C.M.T., Beckmann R., Eswar N., Penczek P.A., Sali A., Blobel G.,
RA   Frank J.;
RT   "Structure of the 80S ribosome from Saccharomyces cerevisiae -- tRNA-
RT   ribosome and subunit-subunit interactions.";
RL   Cell 107:373-386(2001).
RN   [13]
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   [14]
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 (PubMed:22096102). uL4 participates in the regulation of the
CC       accumulation of its own mRNA (PubMed:2065661).
CC       {ECO:0000269|PubMed:2065661, 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). uL4 is associated with the polypeptide
CC       exit tunnel (PubMed:9559554, PubMed:22096102). uL4 interacts with its
CC       chaperone ACL4 and the nuclear import receptor KAP104
CC       (PubMed:25936803). {ECO:0000269|PubMed:22096102,
CC       ECO:0000269|PubMed:25936803, ECO:0000305|PubMed:9559554}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:22096102, ECO:0000269|PubMed:25936803}. Nucleus
CC       {ECO:0000269|PubMed:25936803}.
CC   -!- DOMAIN: The eukaryote-specific C-terminal extension harbors a nuclear
CC       import signal and delivers the ACL4-uL4/RPL4 complex to the pre-
CC       ribosome, triggering uL4 release from ACL4 and incorporation into the
CC       60S ribosomal subunit. {ECO:0000269|PubMed:25936803}.
CC   -!- PTM: N-terminally acetylated by acetyltransferase NatA.
CC       {ECO:0000269|PubMed:1544921}.
CC   -!- MISCELLANEOUS: There are 2 genes for uL4 in yeast. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL4 family.
CC       {ECO:0000305}.
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DR   EMBL; X76078; CAA53687.1; -; Genomic_DNA.
DR   EMBL; J03195; AAA34974.1; -; Genomic_DNA.
DR   EMBL; Z35900; CAA84973.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07152.1; -; Genomic_DNA.
DR   PIR; S45887; S45887.
DR   RefSeq; NP_009587.1; NM_001178379.1.
DR   PDB; 3J6X; EM; 6.10 A; L4=1-362.
DR   PDB; 3J6Y; EM; 6.10 A; L4=1-362.
DR   PDB; 3J77; EM; 6.20 A; L4=1-362.
DR   PDB; 3J78; EM; 6.30 A; L4=1-362.
DR   PDB; 3JCT; EM; 3.08 A; C=1-362.
DR   PDB; 4U3M; X-ray; 3.00 A; L4/l4=2-362.
DR   PDB; 4U3N; X-ray; 3.20 A; L4/l4=2-362.
DR   PDB; 4U3U; X-ray; 2.90 A; L4/l4=2-362.
DR   PDB; 4U4N; X-ray; 3.10 A; L4/l4=2-362.
DR   PDB; 4U4O; X-ray; 3.60 A; L4/l4=2-362.
DR   PDB; 4U4Q; X-ray; 3.00 A; L4/l4=2-362.
DR   PDB; 4U4R; X-ray; 2.80 A; L4/l4=2-362.
DR   PDB; 4U4U; X-ray; 3.00 A; L4/l4=2-362.
DR   PDB; 4U4Y; X-ray; 3.20 A; L4/l4=2-362.
DR   PDB; 4U4Z; X-ray; 3.10 A; L4/l4=2-362.
DR   PDB; 4U50; X-ray; 3.20 A; L4/l4=2-362.
DR   PDB; 4U51; X-ray; 3.20 A; L4/l4=2-362.
DR   PDB; 4U52; X-ray; 3.00 A; L4/l4=2-362.
DR   PDB; 4U53; X-ray; 3.30 A; L4/l4=2-362.
DR   PDB; 4U55; X-ray; 3.20 A; L4/l4=2-362.
DR   PDB; 4U56; X-ray; 3.45 A; L4/l4=2-362.
DR   PDB; 4U6F; X-ray; 3.10 A; L4/l4=2-362.
DR   PDB; 4V6I; EM; 8.80 A; BD=1-362.
DR   PDB; 4V7F; EM; 8.70 A; D=1-362.
DR   PDB; 4V7R; X-ray; 4.00 A; BD/DD=1-362.
DR   PDB; 4V88; X-ray; 3.00 A; BC/DC=1-362.
DR   PDB; 4V8T; EM; 8.10 A; C=1-362.
DR   PDB; 4V8Y; EM; 4.30 A; BC=2-362.
DR   PDB; 4V8Z; EM; 6.60 A; BC=2-362.
DR   PDB; 4V91; EM; 3.70 A; C=1-362.
DR   PDB; 5APN; EM; 3.91 A; C=1-362.
DR   PDB; 5APO; EM; 3.41 A; C=1-362.
DR   PDB; 5DAT; X-ray; 3.15 A; L4/l4=2-362.
DR   PDB; 5DC3; X-ray; 3.25 A; L4/l4=2-362.
DR   PDB; 5DGE; X-ray; 3.45 A; L4/l4=2-362.
DR   PDB; 5DGF; X-ray; 3.30 A; L4/l4=2-362.
DR   PDB; 5DGV; X-ray; 3.10 A; L4/l4=2-362.
DR   PDB; 5FCI; X-ray; 3.40 A; L4/l4=2-362.
DR   PDB; 5FCJ; X-ray; 3.10 A; L4/l4=2-362.
DR   PDB; 5FL8; EM; 9.50 A; C=1-362.
DR   PDB; 5GAK; EM; 3.88 A; G=1-362.
DR   PDB; 5H4P; EM; 3.07 A; C=2-362.
DR   PDB; 5I4L; X-ray; 3.10 A; L4/l4=2-362.
DR   PDB; 5JCS; EM; 9.50 A; C=1-362.
DR   PDB; 5JUO; EM; 4.00 A; H=1-362.
DR   PDB; 5JUP; EM; 3.50 A; H=1-362.
DR   PDB; 5JUS; EM; 4.20 A; H=1-362.
DR   PDB; 5JUT; EM; 4.00 A; H=1-362.
DR   PDB; 5JUU; EM; 4.00 A; H=1-362.
DR   PDB; 5LYB; X-ray; 3.25 A; L4/l4=2-362.
DR   PDB; 5M1J; EM; 3.30 A; C5=2-362.
DR   PDB; 5MC6; EM; 3.80 A; BE=1-362.
DR   PDB; 5MEI; X-ray; 3.50 A; CF/l=2-362.
DR   PDB; 5NDG; X-ray; 3.70 A; L4/l4=2-362.
DR   PDB; 5NDV; X-ray; 3.30 A; L4/l4=2-362.
DR   PDB; 5NDW; X-ray; 3.70 A; L4/l4=2-362.
DR   PDB; 5OBM; X-ray; 3.40 A; L4/l4=2-362.
DR   PDB; 5ON6; X-ray; 3.10 A; CF/l=2-362.
DR   PDB; 5T62; EM; 3.30 A; F=1-362.
DR   PDB; 5T6R; EM; 4.50 A; F=1-362.
DR   PDB; 5TBW; X-ray; 3.00 A; CF/l=2-362.
DR   PDB; 5TGA; X-ray; 3.30 A; L4/l4=2-362.
DR   PDB; 5TGM; X-ray; 3.50 A; L4/l4=2-362.
DR   PDB; 5Z3G; EM; 3.65 A; G=1-362.
DR   PDB; 6C0F; EM; 3.70 A; C=1-362.
DR   PDB; 6CB1; EM; 4.60 A; C=1-362.
DR   PDB; 6ELZ; EM; 3.30 A; C=1-362.
DR   PDB; 6EM1; EM; 3.60 A; C=1-362.
DR   PDB; 6EM3; EM; 3.20 A; C=1-362.
DR   PDB; 6EM4; EM; 4.10 A; C=1-362.
DR   PDB; 6EM5; EM; 4.30 A; C=1-362.
DR   PDB; 6FT6; EM; 3.90 A; C=1-362.
DR   PDB; 6GQ1; EM; 4.40 A; C=2-362.
DR   PDB; 6GQB; EM; 3.90 A; C=2-362.
DR   PDB; 6GQV; EM; 4.00 A; C=2-362.
DR   PDB; 6HD7; EM; 3.40 A; G=1-362.
DR   PDB; 6HHQ; X-ray; 3.10 A; CF/l=1-362.
DR   PDB; 6I7O; EM; 5.30 A; BE/YE=2-362.
DR   PDB; 6M62; EM; 3.20 A; C=1-362.
DR   PDB; 6N8J; EM; 3.50 A; C=1-362.
DR   PDB; 6N8K; EM; 3.60 A; C=1-362.
DR   PDB; 6N8L; EM; 3.60 A; C=1-362.
DR   PDB; 6N8M; EM; 3.50 A; F=1-362.
DR   PDB; 6N8N; EM; 3.80 A; F=1-362.
DR   PDB; 6N8O; EM; 3.50 A; F=1-362.
DR   PDB; 6OIG; EM; 3.80 A; C=2-362.
DR   PDB; 6Q8Y; EM; 3.10 A; BE=2-362.
DR   PDB; 6QIK; EM; 3.10 A; D=1-362.
DR   PDB; 6QT0; EM; 3.40 A; D=1-362.
DR   PDB; 6QTZ; EM; 3.50 A; D=1-362.
DR   PDB; 6R84; EM; 3.60 A; G=2-362.
DR   PDB; 6R86; EM; 3.40 A; G=2-362.
DR   PDB; 6R87; EM; 3.40 A; G=2-362.
DR   PDB; 6RI5; EM; 3.30 A; D=1-362.
DR   PDB; 6RZZ; EM; 3.20 A; D=1-362.
DR   PDB; 6S05; EM; 3.90 A; D=1-362.
DR   PDB; 6S47; EM; 3.28 A; AF=2-362.
DR   PDB; 6SNT; EM; 2.80 A; j=1-362.
DR   PDB; 6SV4; EM; 3.30 A; BE/YE/ZE=1-362.
DR   PDB; 6T4Q; EM; 2.60 A; LC=2-362.
DR   PDB; 6T7I; EM; 3.20 A; LC=1-362.
DR   PDB; 6T7T; EM; 3.10 A; LC=1-362.
DR   PDB; 6T83; EM; 4.00 A; Cy/Fa=1-362.
DR   PDB; 6TB3; EM; 2.80 A; BE=2-362.
DR   PDB; 6TNU; EM; 3.10 A; BE=2-362.
DR   PDB; 6WOO; EM; 2.90 A; C=3-361.
DR   PDB; 6YLG; EM; 3.00 A; C=1-362.
DR   PDB; 6YLH; EM; 3.10 A; C=1-362.
DR   PDB; 6YLX; EM; 3.90 A; C=1-362.
DR   PDB; 6YLY; EM; 3.80 A; C=1-362.
DR   PDB; 6Z6J; EM; 3.40 A; LC=1-362.
DR   PDB; 6Z6K; EM; 3.40 A; LC=1-362.
DR   PDB; 7AZY; EM; 2.88 A; p=1-362.
DR   PDB; 7B7D; EM; 3.30 A; LF=2-362.
DR   PDB; 7BT6; EM; 3.12 A; C=1-362.
DR   PDB; 7BTB; EM; 3.22 A; C=1-362.
DR   PDB; 7NRC; EM; 3.90 A; LF=2-362.
DR   PDB; 7NRD; EM; 4.36 A; LF=2-362.
DR   PDB; 7OF1; EM; 3.10 A; C=1-362.
DR   PDB; 7OH3; EM; 3.40 A; C=1-362.
DR   PDB; 7OHP; EM; 3.90 A; C=1-362.
DR   PDB; 7OHQ; EM; 3.10 A; C=1-362.
DR   PDB; 7OHR; EM; 4.72 A; C=1-362.
DR   PDB; 7OHS; EM; 4.38 A; C=1-362.
DR   PDB; 7OHT; EM; 4.70 A; C=1-362.
DR   PDB; 7OHU; EM; 3.70 A; C=1-362.
DR   PDB; 7OHV; EM; 3.90 A; C=1-362.
DR   PDB; 7OHW; EM; 3.50 A; C=1-362.
DR   PDB; 7OHX; EM; 3.30 A; C=1-362.
DR   PDB; 7OHY; EM; 3.90 A; C=1-362.
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; 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; 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   AlphaFoldDB; P10664; -.
DR   SMR; P10664; -.
DR   BioGRID; 32733; 296.
DR   DIP; DIP-8314N; -.
DR   IntAct; P10664; 221.
DR   MINT; P10664; -.
DR   STRING; 4932.YBR031W; -.
DR   CarbonylDB; P10664; -.
DR   iPTMnet; P10664; -.
DR   MaxQB; P10664; -.
DR   PaxDb; P10664; -.
DR   PRIDE; P10664; -.
DR   TopDownProteomics; P10664; -.
DR   EnsemblFungi; YBR031W_mRNA; YBR031W; YBR031W.
DR   GeneID; 852319; -.
DR   KEGG; sce:YBR031W; -.
DR   SGD; S000000235; RPL4A.
DR   VEuPathDB; FungiDB:YBR031W; -.
DR   eggNOG; KOG1475; Eukaryota.
DR   GeneTree; ENSGT00390000018145; -.
DR   HOGENOM; CLU_026535_4_0_1; -.
DR   InParanoid; P10664; -.
DR   OMA; WHQKVNV; -.
DR   BioCyc; YEAST:G3O-29009-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:P10664; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P10664; protein.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR   GO; GO:0002181; P:cytoplasmic translation; IC:SGD.
DR   Gene3D; 3.40.1370.10; -; 1.
DR   InterPro; IPR025755; Ribos_L4_C_dom.
DR   InterPro; IPR002136; Ribosomal_L4/L1e.
DR   InterPro; IPR013000; Ribosomal_L4/L1e_euk/arc_CS.
DR   InterPro; IPR023574; Ribosomal_L4_dom_sf.
DR   InterPro; IPR045240; Ribosomal_L4_euk/arch.
DR   PANTHER; PTHR19431; PTHR19431; 1.
DR   Pfam; PF14374; Ribos_L4_asso_C; 1.
DR   Pfam; PF00573; Ribosomal_L4; 1.
DR   SUPFAM; SSF52166; SSF52166; 1.
DR   PROSITE; PS00939; RIBOSOMAL_L1E; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW   Methylation; Nucleus; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein; RNA-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1544921"
FT   CHAIN           2..362
FT                   /note="60S ribosomal protein L4-A"
FT                   /id="PRO_0000129367"
FT   REGION          277..362
FT                   /note="C-terminal-extended nuclear localization signal"
FT                   /evidence="ECO:0000269|PubMed:25936803"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:1544921"
FT   MOD_RES         95
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000269|PubMed:26046779"
FT   MUTAGEN         95
FT                   /note="R->E: Leads to a slower growth at higher
FT                   temperatures but allows RPL4 assembly into the 60S subunit;
FT                   when associated with E-98."
FT                   /evidence="ECO:0000269|PubMed:25936803"
FT   MUTAGEN         98
FT                   /note="R->E: Leads to a slower growth at higher
FT                   temperatures but allows RPL4 assembly into the 60S subunit;
FT                   when associated with E-95."
FT                   /evidence="ECO:0000269|PubMed:25936803"
FT   MUTAGEN         289
FT                   /note="I->A: Leads to an inefficient release from ACL4 with
FT                   a delayed assembly into the 60S subunit; when associated
FT                   with A-290 and A-295."
FT                   /evidence="ECO:0000269|PubMed:25936803"
FT   MUTAGEN         290
FT                   /note="I->A: Leads to an inefficient release from ACL4 with
FT                   a delayed assembly into the 60S subunit; when associated
FT                   with A-289 and A-295."
FT                   /evidence="ECO:0000269|PubMed:25936803"
FT   MUTAGEN         295
FT                   /note="I->A: Leads to an inefficient release from ACL4 with
FT                   a delayed assembly into the 60S subunit; when associated
FT                   with A-289 and A-290."
FT                   /evidence="ECO:0000269|PubMed:25936803"
FT   MUTAGEN         314
FT                   /note="K->A: Significantly diminished nuclear localization;
FT                   when associated with A-315 and A-319."
FT                   /evidence="ECO:0000269|PubMed:25936803"
FT   MUTAGEN         315
FT                   /note="K->A: Significantly diminished nuclear localization;
FT                   when associated with A-314 and A-319."
FT                   /evidence="ECO:0000269|PubMed:25936803"
FT   MUTAGEN         319
FT                   /note="K->A: Significantly diminished nuclear localization;
FT                   when associated with A-314 and A-315."
FT                   /evidence="ECO:0000269|PubMed:25936803"
FT   MUTAGEN         332
FT                   /note="K->E: Leads to an inefficient release from ACL4 with
FT                   a delayed assembly into the 60S subunit; when associated
FT                   with A-334."
FT                   /evidence="ECO:0000269|PubMed:25936803"
FT   MUTAGEN         334
FT                   /note="F->A: Leads to an inefficient release from ACL4 with
FT                   a delayed assembly into the 60S subunit; when associated
FT                   with e-332."
FT                   /evidence="ECO:0000269|PubMed:25936803"
FT   CONFLICT        38
FT                   /note="V -> L (in Ref. 1; AAA34974)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        144
FT                   /note="K -> T (in Ref. 1; AAA34974)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        157
FT                   /note="E -> D (in Ref. 1; AAA34974)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        224
FT                   /note="G -> S (in Ref. 1; AAA34974)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        241
FT                   /note="G -> S (in Ref. 1; AAA34974)"
FT                   /evidence="ECO:0000305"
FT   STRAND          6..9
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   STRAND          15..20
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   HELIX           32..42
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   TURN            43..45
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   TURN            56..58
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   STRAND          67..71
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   STRAND          80..84
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   STRAND          90..94
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   HELIX           115..127
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   HELIX           128..130
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   HELIX           133..138
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   STRAND          148..152
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   HELIX           154..156
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   HELIX           162..172
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   TURN            173..176
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   HELIX           177..183
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   HELIX           191..195
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   STRAND          206..211
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   HELIX           215..218
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   STRAND          219..222
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   STRAND          226..229
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   TURN            230..232
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   HELIX           235..238
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   HELIX           240..242
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   STRAND          248..251
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   HELIX           252..262
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   STRAND          265..267
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   STRAND          280..282
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   HELIX           287..290
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   HELIX           295..297
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   STRAND          317..320
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   HELIX           323..326
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   HELIX           331..336
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   STRAND          339..341
FT                   /evidence="ECO:0007829|PDB:6EM3"
SQ   SEQUENCE   362 AA;  39092 MW;  37D0942A10AAE89F CRC64;
     MSRPQVTVHS LTGEATANAL PLPAVFSAPI RPDIVHTVFT SVNKNKRQAY AVSEKAGHQT
     SAESWGTGRA VARIPRVGGG GTGRSGQGAF GNMCRGGRMF APTKTWRKWN VKVNHNEKRY
     ATASAIAATA VASLVLARGH RVEKIPEIPL VVSTDLESIQ KTKEAVAALK AVGAHSDLLK
     VLKSKKLRAG KGKYRNRRWT QRRGPLVVYA EDNGIVKALR NVPGVETANV ASLNLLQLAP
     GAHLGRFVIW TEAAFTKLDQ VWGSETVASS KVGYTLPSHI ISTSDVTRII NSSEIQSAIR
     PAGQATQKRT HVLKKNPLKN KQVLLRLNPY AKVFAAEKLG SKKAEKTGTK PAAVFTETLK
     HD
 
 
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