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60S ribosomal protein L8 (Large ribosomal subunit protein uL2)

 RL8_HUMAN               Reviewed;         257 AA.
P62917; A8K094; D3DWN2; P25120; Q567Q7; Q969V7; Q9BWQ9;
31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
23-MAY-2018, entry version 149.
RecName: Full=60S ribosomal protein L8;
AltName: Full=Large ribosomal subunit protein uL2 {ECO:0000303|PubMed:24524803};
Name=RPL8;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Ovary;
PubMed=7506540; DOI=10.1006/bbrc.1993.2607;
Hanes J., Klaudiny J., von der Kammer H., Scheit K.H.;
"Characterization by cDNA cloning of the mRNA of human ribosomal
protein L8.";
Biochem. Biophys. Res. Commun. 197:1223-1228(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11875025; DOI=10.1101/gr.214202;
Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S.,
Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.;
"The human ribosomal protein genes: sequencing and comparative
analysis of 73 genes.";
Genome Res. 12:379-390(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-98.
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-98.
TISSUE=Kidney, Placenta, Skin, and Spinal cord;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-134.
PubMed=9582194;
Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N.,
Hudson T.J., Tanaka T., Page D.C.;
"A map of 75 human ribosomal protein genes.";
Genome Res. 8:509-523(1998).
[9]
PROTEIN SEQUENCE OF 2-11, IDENTIFICATION BY MASS SPECTROMETRY,
SUBCELLULAR LOCATION, FUNCTION, AND SUBUNIT.
PubMed=12962325; DOI=10.1023/A:1025068419698;
Odintsova T.I., Muller E.C., Ivanov A.V., Egorov T.A., Bienert R.,
Vladimirov S.N., Kostka S., Otto A., Wittmann-Liebold B.,
Karpova G.G.;
"Characterization and analysis of posttranslational modifications of
the human large cytoplasmic ribosomal subunit proteins by mass
spectrometry and Edman sequencing.";
J. Protein Chem. 22:249-258(2003).
[10]
PROTEIN REPLACEMENT STUDIES IN E.COLI, AND MUTAGENESIS.
PubMed=9531480; DOI=10.1042/bj3310423;
Uehlein M., Wegloehner W., Urlaub H., Wittmann-Liebold B.;
"Functional implications of ribosomal protein L2 in protein
biosynthesis as shown by in vivo replacement studies.";
Biochem. J. 331:423-430(1998).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
HYDROXYLATION AT HIS-216 BY RIOX1.
PubMed=23103944; DOI=10.1038/nchembio.1093;
Ge W., Wolf A., Feng T., Ho C.H., Sekirnik R., Zayer A., Granatino N.,
Cockman M.E., Loenarz C., Loik N.D., Hardy A.P., Claridge T.D.,
Hamed R.B., Chowdhury R., Gong L., Robinson C.V., Trudgian D.C.,
Jiang M., Mackeen M.M., McCullagh J.S., Gordiyenko Y., Thalhammer A.,
Yamamoto A., Yang M., Liu-Yi P., Zhang Z., Schmidt-Zachmann M.,
Kessler B.M., Ratcliffe P.J., Preston G.M., Coleman M.L.,
Schofield C.J.;
"Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and
humans.";
Nat. Chem. Biol. 8:960-962(2012).
[14]
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).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[17]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-42; LYS-149; LYS-234 AND
LYS-250, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[18]
STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
PubMed=23636399; DOI=10.1038/nature12104;
Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
Wilson D.N., Beckmann R.;
"Structures of the human and Drosophila 80S ribosome.";
Nature 497:80-85(2013).
-!- FUNCTION: Component of the large ribosomal subunit.
{ECO:0000305|PubMed:12962325}.
-!- SUBUNIT: Component of the large ribosomal subunit (Probable).
Interacts with CRY1 (By similarity).
{ECO:0000250|UniProtKB:P62918, ECO:0000305|PubMed:12962325}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000303|PubMed:12962325}.
-!- PTM: Hydroxylated on His-216 by RIOX1. The modification is
impaired by hypoxia. {ECO:0000269|PubMed:23103944}.
-!- MISCELLANEOUS: This protein can be partially incorporated into
E.coli polysomes in vivo, indicating it can replace the endogenous
protein.
-!- SIMILARITY: Belongs to the universal ribosomal protein uL2 family.
{ECO:0000305}.
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EMBL; Z28407; CAA82248.1; -; mRNA.
EMBL; AB061821; BAB79459.1; -; Genomic_DNA.
EMBL; BT007379; AAP36043.1; -; mRNA.
EMBL; CR457046; CAG33327.1; -; mRNA.
EMBL; AK289459; BAF82148.1; -; mRNA.
EMBL; CH471162; EAW82048.1; -; Genomic_DNA.
EMBL; CH471162; EAW82051.1; -; Genomic_DNA.
EMBL; CH471162; EAW82052.1; -; Genomic_DNA.
EMBL; BC000047; AAH00047.2; -; mRNA.
EMBL; BC000077; AAH00077.1; -; mRNA.
EMBL; BC012197; AAH12197.1; -; mRNA.
EMBL; BC013104; AAH13104.1; -; mRNA.
EMBL; BC093064; AAH93064.1; -; mRNA.
EMBL; AB007168; BAA25829.1; -; Genomic_DNA.
CCDS; CCDS6433.1; -.
PIR; JN0923; JN0923.
RefSeq; NP_000964.1; NM_000973.4.
RefSeq; NP_001304700.1; NM_001317771.1.
RefSeq; NP_001304711.1; NM_001317782.1.
RefSeq; NP_150644.1; NM_033301.2.
UniGene; Hs.178551; -.
PDB; 4CCM; X-ray; 2.51 A; C/D=205-239.
PDB; 4CCN; X-ray; 2.23 A; C/D=205-239.
PDB; 4CCO; X-ray; 2.30 A; C/D=205-224.
PDB; 4UG0; EM; -; LA=1-257.
PDB; 4V6X; EM; 5.00 A; CA=1-257.
PDB; 4Y3O; X-ray; 2.20 A; C/D=212-222.
PDB; 5AJ0; EM; 3.50 A; AA=1-257.
PDB; 5LKS; EM; 3.60 A; LA=1-257.
PDB; 5T2C; EM; 3.60 A; D=1-257.
PDB; 6EK0; EM; 2.90 A; LA=1-257.
PDBsum; 4CCM; -.
PDBsum; 4CCN; -.
PDBsum; 4CCO; -.
PDBsum; 4UG0; -.
PDBsum; 4V6X; -.
PDBsum; 4Y3O; -.
PDBsum; 5AJ0; -.
PDBsum; 5LKS; -.
PDBsum; 5T2C; -.
PDBsum; 6EK0; -.
ProteinModelPortal; P62917; -.
SMR; P62917; -.
BioGrid; 112052; 223.
CORUM; P62917; -.
DIP; DIP-37967N; -.
IntAct; P62917; 59.
MINT; P62917; -.
STRING; 9606.ENSP00000262584; -.
DrugBank; DB02494; Alpha-Hydroxy-Beta-Phenyl-Propionic Acid.
DrugBank; DB07374; Anisomycin.
DrugBank; DB08437; Puromycin.
iPTMnet; P62917; -.
PhosphoSitePlus; P62917; -.
SwissPalm; P62917; -.
BioMuta; RPL8; -.
DMDM; 51702823; -.
EPD; P62917; -.
MaxQB; P62917; -.
PaxDb; P62917; -.
PeptideAtlas; P62917; -.
PRIDE; P62917; -.
TopDownProteomics; P62917; -.
DNASU; 6132; -.
Ensembl; ENST00000262584; ENSP00000262584; ENSG00000161016.
Ensembl; ENST00000394920; ENSP00000378378; ENSG00000161016.
Ensembl; ENST00000528957; ENSP00000433464; ENSG00000161016.
GeneID; 6132; -.
KEGG; hsa:6132; -.
UCSC; uc003zeb.4; human.
CTD; 6132; -.
DisGeNET; 6132; -.
EuPathDB; HostDB:ENSG00000161016.15; -.
GeneCards; RPL8; -.
HGNC; HGNC:10368; RPL8.
HPA; HPA045095; -.
HPA; HPA050165; -.
MIM; 604177; gene.
neXtProt; NX_P62917; -.
OpenTargets; ENSG00000161016; -.
PharmGKB; PA34768; -.
eggNOG; KOG2309; Eukaryota.
eggNOG; COG0090; LUCA.
GeneTree; ENSGT00390000009907; -.
HOVERGEN; HBG079431; -.
InParanoid; P62917; -.
KO; K02938; -.
OMA; HGYIKGV; -.
OrthoDB; EOG091G0K1G; -.
PhylomeDB; P62917; -.
TreeFam; TF300748; -.
Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
Reactome; R-HSA-156902; Peptide chain elongation.
Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
Reactome; R-HSA-192823; Viral mRNA Translation.
Reactome; R-HSA-2408557; Selenocysteine synthesis.
Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
Reactome; R-HSA-72764; Eukaryotic Translation Termination.
Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
ChiTaRS; RPL8; human.
GeneWiki; RPL8; -.
GenomeRNAi; 6132; -.
PRO; PR:P62917; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000161016; -.
CleanEx; HS_RPL8; -.
ExpressionAtlas; P62917; baseline and differential.
Genevisible; P62917; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0042788; C:polysomal ribosome; IDA:UniProtKB.
GO; GO:1990932; F:5.8S rRNA binding; IEA:Ensembl.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEA:Ensembl.
GO; GO:0002181; P:cytoplasmic translation; IDA:UniProtKB.
GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
GO; GO:0006412; P:translation; TAS:ProtInc.
GO; GO:0006413; P:translational initiation; TAS:Reactome.
Gene3D; 2.30.30.30; -; 1.
Gene3D; 4.10.950.10; -; 1.
HAMAP; MF_01320_A; Ribosomal_L2_A; 1.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR022666; Rbsml_prot_L2_RNA-bd_dom.
InterPro; IPR014722; Rib_L2_dom2.
InterPro; IPR002171; Ribosomal_L2.
InterPro; IPR023672; Ribosomal_L2_arc.
InterPro; IPR022669; Ribosomal_L2_C.
InterPro; IPR022671; Ribosomal_L2_CS.
InterPro; IPR014726; Ribosomal_L2_dom3.
InterPro; IPR008991; Translation_prot_SH3-like_sf.
PANTHER; PTHR13691; PTHR13691; 1.
Pfam; PF00181; Ribosomal_L2; 1.
Pfam; PF03947; Ribosomal_L2_C; 1.
PIRSF; PIRSF002158; Ribosomal_L2; 1.
SMART; SM01383; Ribosomal_L2; 1.
SMART; SM01382; Ribosomal_L2_C; 1.
SUPFAM; SSF50104; SSF50104; 1.
SUPFAM; SSF50249; SSF50249; 1.
PROSITE; PS00467; RIBOSOMAL_L2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
Hydroxylation; Isopeptide bond; Polymorphism; Reference proteome;
Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:12962325}.
CHAIN 2 257 60S ribosomal protein L8.
/FTId=PRO_0000129743.
MOD_RES 216 216 (3S)-3-hydroxyhistidine.
{ECO:0000269|PubMed:23103944}.
CROSSLNK 42 42 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 149 149 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 234 234 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 250 250 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 98 98 I -> V (in dbSNP:rs11539893).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.3}.
/FTId=VAR_019658.
MUTAGEN 209 209 H->A,G: No incorporation into translating
E.coli polysomes; ribosomes assembled
normally. Significantly reduced
translational activity.
{ECO:0000269|PubMed:9531480}.
SEQUENCE 257 AA; 28025 MW; CE1610449749318B CRC64;
MGRVIRGQRK GAGSVFRAHV KHRKGAARLR AVDFAERHGY IKGIVKDIIH DPGRGAPLAK
VVFRDPYRFK KRTELFIAAE GIHTGQFVYC GKKAQLNIGN VLPVGTMPEG TIVCCLEEKP
GDRGKLARAS GNYATVISHN PETKKTRVKL PSGSKKVISS ANRAVVGVVA GGGRIDKPIL
KAGRAYHKYK AKRNCWPRVR GVAMNPVEHP FGGGNHQHIG KPSTIRRDAP AGRKVGLIAA
RRTGRLRGTK TVQEKEN


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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
EIAAB35182 Mouse,Mus musculus,Probable ribosome biogenesis protein RLP24,Ribosomal L24 domain-containing protein 1,Ribosomal protein L24-like,Rsl24d1
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
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
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
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
E11431h Human Ribosomal Protein, Large, P1 ELISA Kit 96T
201-20-0069 RPLP0{ribosomal protein, large, P0}goat.pAb 0.2ml
E11432h Human Ribosomal Protein, Large, P2 ELISA Kit 96T
201-20-5003 RPLP0{ribosomal protein, large, P0}rabbit.pAb 0.2ml
E11430h Human Ribosomal Protein, Large, P0 ELISA Kit 96T


 

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