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40S ribosomal protein S15 (RIG protein) (RP52) (S21) (Small ribosomal subunit protein uS19) (YS21)

 RS15_YEAST              Reviewed;         142 AA.
Q01855; D6W226;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 1.
25-OCT-2017, entry version 155.
RecName: Full=40S ribosomal protein S15 {ECO:0000303|PubMed:9559554};
AltName: Full=RIG protein;
AltName: Full=RP52;
AltName: Full=S21;
AltName: Full=Small ribosomal subunit protein uS19 {ECO:0000303|PubMed:24524803};
AltName: Full=YS21;
Name=RPS15 {ECO:0000303|PubMed:9559554}; Synonyms=RPS21;
OrderedLocusNames=YOL040C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
PubMed=1644188; DOI=10.1016/0014-5793(92)80704-K;
Takasawa S., Tohgo A., Unno M., Yonekura H., Okamoto H.;
"Structural determination of Saccharomyces cerevisiae rig gene and
identification of its product as ribosomal protein S21.";
FEBS Lett. 307:318-323(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169874;
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W.,
Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R.,
Boyer J., Camasses A., Casamayor A., Casas C., Cheret G.,
Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H.,
Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F.,
Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A.,
Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J.,
Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P.,
Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M.,
Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R.,
Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S.,
Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A.,
Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M.,
Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C.,
Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S.,
Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
NOMENCLATURE, AND SUBUNIT.
PubMed=9559554;
DOI=10.1002/(SICI)1097-0061(19980330)14:5<471::AID-YEA241>3.0.CO;2-U;
Planta R.J., Mager W.H.;
"The list of cytoplasmic ribosomal proteins of Saccharomyces
cerevisiae.";
Yeast 14:471-477(1998).
[6]
CLEAVAGE OF INITIATOR METHIONINE, AND ACETYLATION AT SER-2 BY NATA.
PubMed=10601260; DOI=10.1074/jbc.274.52.37035;
Arnold R.J., Polevoda B., Reilly J.P., Sherman F.;
"The action of N-terminal acetyltransferases on yeast ribosomal
proteins.";
J. Biol. Chem. 274:37035-37040(1999).
[7]
FUNCTION.
PubMed=15167894; DOI=10.1038/sj.emboj.7600252;
Leger-Silvestre I., Milkereit P., Ferreira-Cerca S., Saveanu C.,
Rousselle J.-C., Choesmel V., Guinefoleau C., Gas N., Gleizes P.-E.;
"The ribosomal protein Rps15p is required for nuclear exit of the 40S
subunit precursors in yeast.";
EMBO J. 23:2336-2347(2004).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=17287358; DOI=10.1073/pnas.0607084104;
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass
spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[11]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-24; LYS-35 AND LYS-64,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
[12]
NOMENCLATURE.
PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
Williamson J.R., Wilson D., Yonath A., Yusupov M.;
"A new system for naming ribosomal proteins.";
Curr. Opin. Struct. Biol. 24:165-169(2014).
[13]
3D-STRUCTURE MODELING OF 47-126, AND ELECTRON MICROSCOPY.
PubMed=11701127; DOI=10.1016/S0092-8674(01)00539-6;
Spahn C.M.T., Beckmann R., Eswar N., Penczek P.A., Sali A., Blobel G.,
Frank J.;
"Structure of the 80S ribosome from Saccharomyces cerevisiae -- tRNA-
ribosome and subunit-subunit interactions.";
Cell 107:373-386(2001).
[14]
3D-STRUCTURE MODELING OF 47-126, AND ELECTRON MICROSCOPY.
PubMed=14976550; DOI=10.1038/sj.emboj.7600102;
Spahn C.M.T., Gomez-Lorenzo M.G., Grassucci R.A., Joergensen R.,
Andersen G.R., Beckmann R., Penczek P.A., Ballesta J.P.G., Frank J.;
"Domain movements of elongation factor eEF2 and the eukaryotic 80S
ribosome facilitate tRNA translocation.";
EMBO J. 23:1008-1019(2004).
[15]
X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS) OF 80S RIBOSOME.
PubMed=21109664; DOI=10.1126/science.1194294;
Ben-Shem A., Jenner L., Yusupova G., Yusupov M.;
"Crystal structure of the eukaryotic ribosome.";
Science 330:1203-1209(2010).
[16]
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 80S RIBOSOME, SUBUNIT, AND
SUBCELLULAR LOCATION.
PubMed=22096102; DOI=10.1126/science.1212642;
Ben-Shem A., Garreau de Loubresse N., Melnikov S., Jenner L.,
Yusupova G., Yusupov M.;
"The structure of the eukaryotic ribosome at 3.0 A resolution.";
Science 334:1524-1529(2011).
-!- FUNCTION: Component of the ribosome, a large ribonucleoprotein
complex responsible for the synthesis of proteins in the cell. The
small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and
translates the encoded message by selecting cognate aminoacyl-
transfer RNA (tRNA) molecules. The large subunit (LSU) contains
the ribosomal catalytic site termed the peptidyl transferase
center (PTC), which catalyzes the formation of peptide bonds,
thereby polymerizing the amino acids delivered by tRNAs into a
polypeptide chain. The nascent polypeptides leave the ribosome
through a tunnel in the LSU and interact with protein factors that
function in enzymatic processing, targeting, and the membrane
insertion of nascent chains at the exit of the ribosomal tunnel
(PubMed:22096102). uS19 is involved in the nuclear export of the
small ribosomal subunit precursor. Has a role in the late stage of
the assembly of pre-40S particles within the nucleus and controls
their export to the cytoplasm (PubMed:15167894).
{ECO:0000269|PubMed:15167894, ECO:0000305|PubMed:22096102}.
-!- SUBUNIT: Component of the small ribosomal subunit (SSU). Mature
yeast ribosomes consist of a small (40S) and a large (60S)
subunit. The 40S small subunit contains 1 molecule of ribosomal
RNA (18S rRNA) and 33 different proteins (encoded by 57 genes).
The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S
rRNA) and 46 different proteins (encoded by 81 genes)
(PubMed:9559554, PubMed:22096102). {ECO:0000269|PubMed:22096102,
ECO:0000305|PubMed:9559554}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}.
-!- SIMILARITY: Belongs to the universal ribosomal protein uS19
family. {ECO:0000305}.
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EMBL; D11386; BAA01982.1; -; mRNA.
EMBL; D11387; BAA01983.1; -; Genomic_DNA.
EMBL; Z74782; CAA99042.1; -; Genomic_DNA.
EMBL; AY558426; AAS56752.1; -; Genomic_DNA.
EMBL; BK006948; DAA10742.1; -; Genomic_DNA.
PIR; S24053; S24053.
RefSeq; NP_014602.1; NM_001183294.1.
PDB; 1K5X; Model; -; S=47-126.
PDB; 3J6X; EM; 6.10 A; 15=1-142.
PDB; 3J6Y; EM; 6.10 A; 15=1-142.
PDB; 3J77; EM; 6.20 A; 15=1-142.
PDB; 3J78; EM; 6.30 A; 15=1-142.
PDB; 4U3M; X-ray; 3.00 A; C5/c5=2-142.
PDB; 4U3N; X-ray; 3.20 A; C5/c5=2-142.
PDB; 4U3U; X-ray; 2.90 A; C5/c5=2-142.
PDB; 4U4N; X-ray; 3.10 A; C5/c5=2-142.
PDB; 4U4O; X-ray; 3.60 A; C5/c5=2-142.
PDB; 4U4Q; X-ray; 3.00 A; C5/c5=2-142.
PDB; 4U4R; X-ray; 2.80 A; C5/c5=2-142.
PDB; 4U4U; X-ray; 3.00 A; C5/c5=2-142.
PDB; 4U4Y; X-ray; 3.20 A; C5/c5=2-142.
PDB; 4U4Z; X-ray; 3.10 A; C5/c5=2-142.
PDB; 4U50; X-ray; 3.20 A; C5/c5=2-142.
PDB; 4U51; X-ray; 3.20 A; C5/c5=2-142.
PDB; 4U52; X-ray; 3.00 A; C5/c5=2-142.
PDB; 4U53; X-ray; 3.30 A; C5/c5=2-142.
PDB; 4U55; X-ray; 3.20 A; C5/c5=2-142.
PDB; 4U56; X-ray; 3.45 A; C5/c5=2-142.
PDB; 4U6F; X-ray; 3.10 A; C5/c5=2-142.
PDB; 4V4B; EM; 11.70 A; AS=47-126.
PDB; 4V6I; EM; 8.80 A; AR=1-142.
PDB; 4V7R; X-ray; 4.00 A; AI/CI=1-142.
PDB; 4V88; X-ray; 3.00 A; AP/CP=1-142.
PDB; 4V8Y; EM; 4.30 A; AP=1-142.
PDB; 4V8Z; EM; 6.60 A; AP=1-142.
PDB; 4V92; EM; 3.70 A; P=12-126.
PDB; 5DAT; X-ray; 3.15 A; C5/c5=2-138.
PDB; 5DC3; X-ray; 3.25 A; C5/c5=2-142.
PDB; 5DGE; X-ray; 3.45 A; C5/c5=2-142.
PDB; 5DGV; X-ray; 3.10 A; C5/c5=2-142.
PDB; 5FCI; X-ray; 3.40 A; C5/c5=2-142.
PDB; 5FCJ; X-ray; 3.10 A; C5/c5=2-142.
PDB; 5I4L; X-ray; 3.10 A; C5/c5=1-142.
PDB; 5JUO; EM; 4.00 A; MB=1-142.
PDB; 5JUP; EM; 3.50 A; MB=1-142.
PDB; 5JUS; EM; 4.20 A; MB=1-142.
PDB; 5JUT; EM; 4.00 A; MB=1-142.
PDB; 5JUU; EM; 4.00 A; MB=1-142.
PDB; 5LYB; X-ray; 3.25 A; C5=4-134, c5=1-142.
PDB; 5M1J; EM; 3.30 A; P2=8-131.
PDB; 5MC6; EM; 3.80 A; E=1-142.
PDB; 5MEI; X-ray; 3.50 A; Q/c5=2-142.
PDB; 5TBW; X-ray; 3.00 A; Q/c5=4-138.
PDB; 5TGA; X-ray; 3.30 A; C5/c5=4-138.
PDB; 5TGM; X-ray; 3.50 A; C5/c5=10-134.
PDBsum; 1K5X; -.
PDBsum; 3J6X; -.
PDBsum; 3J6Y; -.
PDBsum; 3J77; -.
PDBsum; 3J78; -.
PDBsum; 4U3M; -.
PDBsum; 4U3N; -.
PDBsum; 4U3U; -.
PDBsum; 4U4N; -.
PDBsum; 4U4O; -.
PDBsum; 4U4Q; -.
PDBsum; 4U4R; -.
PDBsum; 4U4U; -.
PDBsum; 4U4Y; -.
PDBsum; 4U4Z; -.
PDBsum; 4U50; -.
PDBsum; 4U51; -.
PDBsum; 4U52; -.
PDBsum; 4U53; -.
PDBsum; 4U55; -.
PDBsum; 4U56; -.
PDBsum; 4U6F; -.
PDBsum; 4V4B; -.
PDBsum; 4V6I; -.
PDBsum; 4V7R; -.
PDBsum; 4V88; -.
PDBsum; 4V8Y; -.
PDBsum; 4V8Z; -.
PDBsum; 4V92; -.
PDBsum; 5DAT; -.
PDBsum; 5DC3; -.
PDBsum; 5DGE; -.
PDBsum; 5DGV; -.
PDBsum; 5FCI; -.
PDBsum; 5FCJ; -.
PDBsum; 5I4L; -.
PDBsum; 5JUO; -.
PDBsum; 5JUP; -.
PDBsum; 5JUS; -.
PDBsum; 5JUT; -.
PDBsum; 5JUU; -.
PDBsum; 5LYB; -.
PDBsum; 5M1J; -.
PDBsum; 5MC6; -.
PDBsum; 5MEI; -.
PDBsum; 5TBW; -.
PDBsum; 5TGA; -.
PDBsum; 5TGM; -.
ProteinModelPortal; Q01855; -.
SMR; Q01855; -.
BioGrid; 34362; 175.
IntAct; Q01855; 6.
MINT; MINT-4986189; -.
STRING; 4932.YOL040C; -.
iPTMnet; Q01855; -.
MaxQB; Q01855; -.
PRIDE; Q01855; -.
TopDownProteomics; Q01855; -.
EnsemblFungi; YOL040C; YOL040C; YOL040C.
GeneID; 854117; -.
KEGG; sce:YOL040C; -.
EuPathDB; FungiDB:YOL040C; -.
SGD; S000005400; RPS15.
GeneTree; ENSGT00390000000475; -.
HOGENOM; HOG000111561; -.
InParanoid; Q01855; -.
KO; K02958; -.
OMA; VIRTHCR; -.
OrthoDB; EOG092C5E45; -.
BioCyc; YEAST:G3O-33454-MONOMER; -.
Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
Reactome; R-SCE-1799339; SRP-dependent cotranslational protein targeting to membrane.
Reactome; R-SCE-72689; Formation of a pool of free 40S subunits.
Reactome; R-SCE-72695; Formation of the ternary complex, and subsequently, the 43S complex.
Reactome; R-SCE-72702; Ribosomal scanning and start codon recognition.
Reactome; R-SCE-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
Reactome; R-SCE-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
Reactome; R-SCE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
EvolutionaryTrace; Q01855; -.
PRO; PR:Q01855; -.
Proteomes; UP000002311; Chromosome XV.
GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; IEA:InterPro.
GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
GO; GO:0002181; P:cytoplasmic translation; NAS:SGD.
GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
GO; GO:0006407; P:rRNA export from nucleus; IMP:SGD.
Gene3D; 3.30.860.10; -; 1.
HAMAP; MF_00531; Ribosomal_S19; 1.
InterPro; IPR002222; Ribosomal_S19.
InterPro; IPR020934; Ribosomal_S19_CS.
InterPro; IPR023575; Ribosomal_S19_SF.
InterPro; IPR005713; Ribosomal_S19A/S15e.
PANTHER; PTHR11880; PTHR11880; 1.
Pfam; PF00203; Ribosomal_S19; 1.
PIRSF; PIRSF002144; Ribosomal_S19; 1.
PRINTS; PR00975; RIBOSOMALS19.
SUPFAM; SSF54570; SSF54570; 1.
TIGRFAMs; TIGR01025; uS19_arch; 1.
PROSITE; PS00323; RIBOSOMAL_S19; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Isopeptide bond; Reference proteome; Ribonucleoprotein;
Ribosomal protein; Ribosome biogenesis; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:10601260}.
CHAIN 2 142 40S ribosomal protein S15.
/FTId=PRO_0000130051.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:10601260}.
CROSSLNK 24 24 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CROSSLNK 35 35 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CROSSLNK 64 64 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
STRAND 16 19 {ECO:0000244|PDB:4U4R}.
HELIX 22 26 {ECO:0000244|PDB:4U4R}.
HELIX 30 34 {ECO:0000244|PDB:4U4R}.
HELIX 39 46 {ECO:0000244|PDB:4U4R}.
STRAND 50 53 {ECO:0000244|PDB:4U4R}.
HELIX 54 62 {ECO:0000244|PDB:4U4R}.
STRAND 65 67 {ECO:0000244|PDB:4U4R}.
STRAND 69 71 {ECO:0000244|PDB:4U4R}.
STRAND 76 78 {ECO:0000244|PDB:4U4R}.
HELIX 87 89 {ECO:0000244|PDB:4U4R}.
STRAND 93 106 {ECO:0000244|PDB:4U4R}.
HELIX 109 111 {ECO:0000244|PDB:4U4R}.
HELIX 116 119 {ECO:0000244|PDB:4U4R}.
STRAND 131 133 {ECO:0000244|PDB:4U6F}.
SEQUENCE 142 AA; 16002 MW; 06B564FD68051CD2 CRC64;
MSQAVNAKKR VFKTHSYRGV DLEKLLEMST EDFVKLAPAR VRRRFARGMT SKPAGFMKKL
RAAKLAAPEN EKPAPVRTHM RNMIIVPEMI GSVVGIYNGK AFNQVEIRPE MLGHYLGEFS
ITYTPVRHGR AGATTSRFIP LK


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EIAAB35181 C15orf15,Homo sapiens,Human,My024,Probable ribosome biogenesis protein RLP24,Ribosomal L24 domain-containing protein 1,Ribosomal protein L24-like,RPL24L,RSL24D1
EIAAB36079 40S ribosomal protein S2,40S ribosomal protein S4,Homo sapiens,Human,Protein LLRep3,RPS2,RPS4
26-118 Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. MRPL39 is a 39S subunit protein. Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes 0.05 mg
EIAAB35073 60S ribosomal protein L36a,60S ribosomal protein L44,Cell growth-inhibiting gene 15 protein,Cell migration-inducing gene 6 protein,GIG15,Homo sapiens,Human,MIG6,RPL36A,RPL44
29-101 Mammalian mitochondrial ribosomal proteins help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. MRPS15 is 0.1 mg
EIAAB35249 39S ribosomal protein L23, mitochondrial,Homo sapiens,Human,L23 mitochondrial-related protein,L23MRP,L23mt,MRPL23,MRP-L23,Ribosomal protein L23-like,RPL23L
EIAAB35154 60S acidic ribosomal protein P0,60S ribosomal protein L10E,Arbp,Rat,Rattus norvegicus,Rplp0
EIAAB35156 60S acidic ribosomal protein P0,60S ribosomal protein L10E,Arbp,Mouse,Mus musculus,Rplp0
EIAAB33379 60S ribosomal protein L39 pseudogene 5,Homo sapiens,Human,Putative 60S ribosomal protein L39-like 5,RPL39P5
EIAAB35158 60S acidic ribosomal protein P0,60S ribosomal protein L10E,Homo sapiens,Human,RPLP0
18-783-75538 RABBIT ANTI RIBOSOMAL S6 KINASE 2 (C-TERMINAL) - RIBOSOMAL PROTEIN S6 KINASE ALPHA-2; EC 2.7.11.1; S6K-alpha 2; 90 kDa ribosomal protein S6 kinase 2; p90-RSK 2; Ribosomal S6 kinase 3; RSK-3; pp90RSK3; 0.1 ml
29-221 RPL32 is a ribosomal protein that is a component of the 60S subunit. RPL32 belongs to the L32E family of ribosomal proteins. It is located in the cytoplasm. Although some studies have mapped this gene 0.1 mg
EIAAB35108 60S ribosomal protein L1,60S ribosomal protein L4,Homo sapiens,Human,RPL1,RPL4
EIAAB35096 60S ribosomal protein L39-2,60S ribosomal protein L39-like,Homo sapiens,Human,RPL39L,RPL39L1
EIAAB35157 60S acidic ribosomal protein P0,60S ribosomal protein L10E,Bos taurus,Bovine,RPLP0
EIAAB35072 60S ribosomal protein L36a,60S ribosomal protein L44,Rat,Rattus norvegicus,Rpl36a,Rpl44


 

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