RS25A_YEAST
ID RS25A_YEAST Reviewed; 108 AA.
AC Q3E792; A2TBN4; D6VUG0; P05758; P07282; Q45U56;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=40S ribosomal protein S25-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=RP45;
DE AltName: Full=S31;
DE AltName: Full=Small ribosomal subunit protein eS25-A {ECO:0000303|PubMed:24524803};
DE AltName: Full=YS23;
GN Name=RPS25A {ECO:0000303|PubMed:9559554}; Synonyms=RPS31A;
GN OrderedLocusNames=YGR027C;
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].
RC STRAIN=Carlsbergensis;
RX PubMed=2856436; DOI=10.1007/bf00418486;
RA Nieuwint R.T.M., Molenaar C.M.T., van Bommel J.H.,
RA van Raamsdonk-Duin M.M.C., Mager W.H., Planta R.J.;
RT "The gene for yeast ribosomal protein S31 contains an intron in the leader
RT sequence.";
RL Curr. Genet. 10:1-5(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [3]
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 [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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-96.
RC STRAIN=ATCC 201390 / BY4743;
RX PubMed=17244705; DOI=10.1073/pnas.0610354104;
RA Juneau K., Palm C., Miranda M., Davis R.W.;
RT "High-density yeast-tiling array reveals previously undiscovered introns
RT and extensive regulation of meiotic splicing.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1522-1527(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-108, AND VARIANTS PHE-8 AND THR-13.
RC STRAIN=SK1;
RX PubMed=16273108; DOI=10.1038/ng1674;
RA Deutschbauer A.M., Davis R.W.;
RT "Quantitative trait loci mapped to single-nucleotide resolution in yeast.";
RL Nat. Genet. 37:1333-1340(2005).
RN [7]
RP PARTIAL PROTEIN SEQUENCE OF 15-22.
RX PubMed=18782943; DOI=10.1007/bf00341461;
RA Otaka E., Higo K., Itoh T.;
RT "Yeast ribosomal proteins. VIII. Isolation of two proteins and sequence
RT characterization of twenty-four proteins from cytoplasmic ribosomes.";
RL Mol. Gen. Genet. 195:544-546(1984).
RN [8]
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 [9]
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 [10]
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 [11]
RP METHYLATION AT PRO-2 BY NTM1/TAE1.
RX PubMed=20481588; DOI=10.1021/bi100428x;
RA Webb K.J., Lipson R.S., Al-Hadid Q., Whitelegge J.P., Clarke S.G.;
RT "Identification of protein N-terminal methyltransferases in yeast and
RT humans.";
RL Biochemistry 49:5225-5235(2010).
RN [12]
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 [13]
RP STRUCTURE BY ELECTRON MICROSCOPY (8.80 ANGSTROMS).
RX PubMed=20980660; DOI=10.1073/pnas.1009999107;
RA Armache J.P., Jarasch A., Anger A.M., Villa E., Becker T., Bhushan S.,
RA Jossinet F., Habeck M., Dindar G., Franckenberg S., Marquez V., Mielke T.,
RA Thomm M., Berninghausen O., Beatrix B., Soding J., Westhof E., Wilson D.N.,
RA Beckmann R.;
RT "Cryo-EM structure and rRNA model of a translating eukaryotic 80S ribosome
RT at 5.5-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:19748-19753(2010).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (4.00 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 [15]
RP X-RAY CRYSTALLOGRAPHY (3.00 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 small ribosomal subunit (SSU). 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: It is presumed that the precursor part of S25 is engaged
CC in assembling of the small subunit, thus being essential in ribosome
CC maturation. {ECO:0000305|PubMed:2856436}.
CC -!- MISCELLANEOUS: Present with 322000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for eS25 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS25 family.
CC {ECO:0000305}.
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DR EMBL; X03013; CAA26797.1; -; Genomic_DNA.
DR EMBL; Z72812; CAA97010.1; -; Genomic_DNA.
DR EMBL; DQ115389; AAZ22490.1; -; Genomic_DNA.
DR EMBL; EF123137; ABM97481.1; -; mRNA.
DR EMBL; BK006941; DAA08121.1; -; Genomic_DNA.
DR PIR; S05844; R3BY31.
DR RefSeq; NP_011541.1; NM_001181156.1.
DR PDB; 3J6X; EM; 6.10 A; 25=1-108.
DR PDB; 3J6Y; EM; 6.10 A; 25=1-108.
DR PDB; 3J77; EM; 6.20 A; 25=1-108.
DR PDB; 3J78; EM; 6.30 A; 25=1-108.
DR PDB; 4U3M; X-ray; 3.00 A; D5/d5=2-108.
DR PDB; 4U3N; X-ray; 3.20 A; D5/d5=2-108.
DR PDB; 4U3U; X-ray; 2.90 A; D5/d5=2-108.
DR PDB; 4U4N; X-ray; 3.10 A; D5/d5=2-108.
DR PDB; 4U4O; X-ray; 3.60 A; D5/d5=2-108.
DR PDB; 4U4Q; X-ray; 3.00 A; D5/d5=2-108.
DR PDB; 4U4R; X-ray; 2.80 A; D5/d5=2-108.
DR PDB; 4U4U; X-ray; 3.00 A; D5/d5=2-108.
DR PDB; 4U4Y; X-ray; 3.20 A; D5/d5=2-108.
DR PDB; 4U4Z; X-ray; 3.10 A; D5/d5=2-108.
DR PDB; 4U50; X-ray; 3.20 A; D5/d5=2-108.
DR PDB; 4U51; X-ray; 3.20 A; D5/d5=2-108.
DR PDB; 4U52; X-ray; 3.00 A; D5/d5=2-108.
DR PDB; 4U53; X-ray; 3.30 A; D5/d5=2-108.
DR PDB; 4U55; X-ray; 3.20 A; D5/d5=2-108.
DR PDB; 4U56; X-ray; 3.45 A; D5/d5=2-108.
DR PDB; 4U6F; X-ray; 3.10 A; D5/d5=2-108.
DR PDB; 4V6I; EM; 8.80 A; AV=1-108.
DR PDB; 4V7R; X-ray; 4.00 A; AQ/CQ=1-108.
DR PDB; 4V88; X-ray; 3.00 A; AZ/CZ=1-108.
DR PDB; 4V8Y; EM; 4.30 A; AZ=1-108.
DR PDB; 4V8Z; EM; 6.60 A; AZ=1-108.
DR PDB; 4V92; EM; 3.70 A; Z=42-105.
DR PDB; 5DAT; X-ray; 3.15 A; D5/d5=2-108.
DR PDB; 5DC3; X-ray; 3.25 A; D5/d5=2-108.
DR PDB; 5DGE; X-ray; 3.45 A; D5/d5=2-108.
DR PDB; 5DGF; X-ray; 3.30 A; D5/d5=2-108.
DR PDB; 5DGV; X-ray; 3.10 A; D5/d5=2-108.
DR PDB; 5FCI; X-ray; 3.40 A; D5/d5=2-108.
DR PDB; 5FCJ; X-ray; 3.10 A; D5/d5=2-108.
DR PDB; 5I4L; X-ray; 3.10 A; D5/d5=36-105.
DR PDB; 5JUO; EM; 4.00 A; WB=1-108.
DR PDB; 5JUP; EM; 3.50 A; WB=1-108.
DR PDB; 5JUS; EM; 4.20 A; WB=1-108.
DR PDB; 5JUT; EM; 4.00 A; WB=1-108.
DR PDB; 5JUU; EM; 4.00 A; WB=1-108.
DR PDB; 5LYB; X-ray; 3.25 A; D5/d5=36-105.
DR PDB; 5M1J; EM; 3.30 A; Z2=36-105.
DR PDB; 5MC6; EM; 3.80 A; K=1-108.
DR PDB; 5MEI; X-ray; 3.50 A; a/d5=36-105.
DR PDB; 5NDG; X-ray; 3.70 A; D5/d5=36-105.
DR PDB; 5NDV; X-ray; 3.30 A; D5/d5=36-105.
DR PDB; 5NDW; X-ray; 3.70 A; D5/d5=36-105.
DR PDB; 5OBM; X-ray; 3.40 A; D5/d5=36-105.
DR PDB; 5ON6; X-ray; 3.10 A; a/d5=36-105.
DR PDB; 5TBW; X-ray; 3.00 A; a/d5=36-105.
DR PDB; 5TGA; X-ray; 3.30 A; D5/d5=36-105.
DR PDB; 5TGM; X-ray; 3.50 A; D5/d5=36-105.
DR PDB; 6EML; EM; 3.60 A; K=1-108.
DR PDB; 6FAI; EM; 3.40 A; Z=1-108.
DR PDB; 6GQ1; EM; 4.40 A; AP=36-105.
DR PDB; 6GQB; EM; 3.90 A; AP=36-105.
DR PDB; 6GQV; EM; 4.00 A; AP=36-105.
DR PDB; 6HHQ; X-ray; 3.10 A; a/d5=1-108.
DR PDB; 6I7O; EM; 5.30 A; K/Kb=37-105.
DR PDB; 6Q8Y; EM; 3.10 A; K=36-105.
DR PDB; 6RBD; EM; 3.47 A; Z=1-108.
DR PDB; 6RBE; EM; 3.80 A; Z=1-108.
DR PDB; 6S47; EM; 3.28 A; Ba=2-108.
DR PDB; 6SNT; EM; 2.80 A; Z=1-105.
DR PDB; 6SV4; EM; 3.30 A; K/Kb/Kc=1-108.
DR PDB; 6T4Q; EM; 2.60 A; SZ=24-105.
DR PDB; 6T7I; EM; 3.20 A; SZ=1-108.
DR PDB; 6T7T; EM; 3.10 A; SZ=1-108.
DR PDB; 6T83; EM; 4.00 A; 0/Zb=1-108.
DR PDB; 6TB3; EM; 2.80 A; K=24-105.
DR PDB; 6TNU; EM; 3.10 A; K=24-105.
DR PDB; 6WDR; EM; 3.70 A; Z=42-104.
DR PDB; 6WOO; EM; 2.90 A; ZZ=36-105.
DR PDB; 6Y7C; EM; 3.80 A; Z=1-108.
DR PDB; 6Z6J; EM; 3.40 A; SZ=1-108.
DR PDB; 6Z6K; EM; 3.40 A; SZ=1-108.
DR PDB; 6ZCE; EM; 5.30 A; a=1-108.
DR PDB; 6ZQF; EM; 4.90 A; DZ=1-108.
DR PDB; 6ZQG; EM; 3.50 A; DZ=1-108.
DR PDB; 6ZU9; EM; 6.20 A; M=1-108.
DR PDB; 6ZVI; EM; 3.00 A; J=37-105.
DR PDB; 7A1G; EM; 3.00 A; L=24-105.
DR PDB; 7B7D; EM; 3.30 A; K=24-105.
DR PDB; 7D8D; X-ray; 1.05 A; D=2-7.
DR PDB; 7NRC; EM; 3.90 A; SK=24-105.
DR PDB; 7NRD; EM; 4.36 A; SK=37-105.
DR PDBsum; 3J6X; -.
DR PDBsum; 3J6Y; -.
DR PDBsum; 3J77; -.
DR PDBsum; 3J78; -.
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; 4V7R; -.
DR PDBsum; 4V88; -.
DR PDBsum; 4V8Y; -.
DR PDBsum; 4V8Z; -.
DR PDBsum; 4V92; -.
DR PDBsum; 5DAT; -.
DR PDBsum; 5DC3; -.
DR PDBsum; 5DGE; -.
DR PDBsum; 5DGF; -.
DR PDBsum; 5DGV; -.
DR PDBsum; 5FCI; -.
DR PDBsum; 5FCJ; -.
DR PDBsum; 5I4L; -.
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; 5TBW; -.
DR PDBsum; 5TGA; -.
DR PDBsum; 5TGM; -.
DR PDBsum; 6EML; -.
DR PDBsum; 6FAI; -.
DR PDBsum; 6GQ1; -.
DR PDBsum; 6GQB; -.
DR PDBsum; 6GQV; -.
DR PDBsum; 6HHQ; -.
DR PDBsum; 6I7O; -.
DR PDBsum; 6Q8Y; -.
DR PDBsum; 6RBD; -.
DR PDBsum; 6RBE; -.
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; 6WDR; -.
DR PDBsum; 6WOO; -.
DR PDBsum; 6Y7C; -.
DR PDBsum; 6Z6J; -.
DR PDBsum; 6Z6K; -.
DR PDBsum; 6ZCE; -.
DR PDBsum; 6ZQF; -.
DR PDBsum; 6ZQG; -.
DR PDBsum; 6ZU9; -.
DR PDBsum; 6ZVI; -.
DR PDBsum; 7A1G; -.
DR PDBsum; 7B7D; -.
DR PDBsum; 7D8D; -.
DR PDBsum; 7NRC; -.
DR PDBsum; 7NRD; -.
DR AlphaFoldDB; Q3E792; -.
DR SMR; Q3E792; -.
DR BioGRID; 33268; 286.
DR IntAct; Q3E792; 11.
DR MINT; Q3E792; -.
DR STRING; 4932.YGR027C; -.
DR CarbonylDB; Q3E792; -.
DR iPTMnet; Q3E792; -.
DR MaxQB; Q3E792; -.
DR PaxDb; Q3E792; -.
DR PRIDE; Q3E792; -.
DR TopDownProteomics; Q3E792; -.
DR EnsemblFungi; YGR027C_mRNA; YGR027C; YGR027C.
DR GeneID; 852911; -.
DR KEGG; sce:YGR027C; -.
DR SGD; S000003259; RPS25A.
DR VEuPathDB; FungiDB:YGR027C; -.
DR eggNOG; KOG1767; Eukaryota.
DR GeneTree; ENSGT00390000004856; -.
DR HOGENOM; CLU_129470_4_0_1; -.
DR InParanoid; Q3E792; -.
DR OMA; RIVHHSG; -.
DR BioCyc; YEAST:G3O-30751-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-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-SCE-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-SCE-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-SCE-72702; Ribosomal scanning and start codon recognition.
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:Q3E792; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; Q3E792; protein.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:SGD.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; IC:SGD.
DR InterPro; IPR004977; Ribosomal_S25.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR12850; PTHR12850; 1.
DR Pfam; PF03297; Ribosomal_S25; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Methylation;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..108
FT /note="40S ribosomal protein S25-A"
FT /id="PRO_0000043376"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N,N-dimethylproline; by NTM1"
FT /evidence="ECO:0000269|PubMed:20481588"
FT VARIANT 8
FT /note="S -> F (in strain: SK1)"
FT /evidence="ECO:0000269|PubMed:16273108"
FT VARIANT 13
FT /note="A -> T (in strain: SK1)"
FT /evidence="ECO:0000269|PubMed:16273108"
FT CONFLICT 16
FT /note="A -> R (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 47..51
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 62..68
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:6RBD"
FT HELIX 76..85
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 88..95
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:6ZVI"
SQ SEQUENCE 108 AA; 12039 MW; C52D0328DEA125B5 CRC64;
MPPKQQLSKA AKAAAALAGG KKSKKKWSKK SMKDRAQHAV ILDQEKYDRI LKEVPTYRYV
SVSVLVDRLK IGGSLARIAL RHLEKEGIIK PISKHSKQAI YTRATASE
