Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

60S ribosomal protein L42-A (L41) (Large ribosomal subunit protein eL42-A) (YL27) (YP44)

 RL44A_YEAST             Reviewed;         106 AA.
P0CX27; D3DL90; P02405;
28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
28-JUN-2011, sequence version 1.
25-OCT-2017, entry version 56.
RecName: Full=60S ribosomal protein L42-A {ECO:0000303|PubMed:9559554};
AltName: Full=L41;
AltName: Full=Large ribosomal subunit protein eL42-A {ECO:0000303|PubMed:24524803};
AltName: Full=YL27;
AltName: Full=YP44;
Name=RPL42A {ECO:0000303|PubMed:9559554}; Synonyms=RPL41A, SCL41A;
OrderedLocusNames=YNL162W; ORFNames=N1722;
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], AND VARIANT GLN-56.
PubMed=1729213; DOI=10.1128/jb.174.1.254-262.1992;
Kawai S., Murao S., Mochizuki M., Shibuya I., Yano K., Takagi M.;
"Drastic alteration of cycloheximide sensitivity by substitution of
one amino acid in the L41 ribosomal protein of yeasts.";
J. Bacteriol. 174:254-262(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=8686380;
DOI=10.1002/(SICI)1097-0061(199602)12:2<169::AID-YEA894>3.0.CO;2-B;
Nasr F., Becam A.-M., Herbert C.J.;
"The sequence of 36.8 kb from the left arm of chromosome XIV reveals
24 complete open reading frames: 18 correspond to new genes, one of
which encodes a protein similar to the human myotonic dystrophy
kinase.";
Yeast 12:169-175(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169873;
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F.,
Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M.,
Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N.,
Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D.,
Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A.,
Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A.,
Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C.,
Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M.,
Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J.,
Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L.,
Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M.,
Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P.,
Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A.,
Wambutt R., Wedler H., Zollner A., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV
and its evolutionary implications.";
Nature 387:93-98(1997).
[4]
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).
[5]
PROTEIN SEQUENCE OF 2-106.
PubMed=365584; DOI=10.1016/0014-5793(78)80447-5;
Itoh T., Wittmann-Liebold B.;
"The primary structure of protein 44 from the large subunit of yeast
ribosomes.";
FEBS Lett. 96:399-402(1978).
[6]
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).
[7]
MASS SPECTROMETRY.
PubMed=11983894; DOI=10.1073/pnas.082119899;
Lee S.-W., Berger S.J., Martinovic S., Pasa-Tolic L., Anderson G.A.,
Shen Y., Zhao R., Smith R.D.;
"Direct mass spectrometric analysis of intact proteins of the yeast
large ribosomal subunit using capillary LC/FTICR.";
Proc. Natl. Acad. Sci. U.S.A. 99:5942-5947(2002).
[8]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[9]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[10]
METHYLATION AT LYS-40 AND LYS-55, AND MASS SPECTROMETRY.
PubMed=18957409; DOI=10.1074/jbc.M806006200;
Webb K.J., Laganowsky A., Whitelegge J.P., Clarke S.G.;
"Identification of two SET domain proteins required for methylation of
lysine residues in yeast ribosomal protein Rpl42ab.";
J. Biol. Chem. 283:35561-35568(2008).
[11]
METHYLATION AT LYS-40.
PubMed=22522802; DOI=10.1002/pmic.201100570;
Couttas T.A., Raftery M.J., Padula M.P., Herbert B.R., Wilkins M.R.;
"Methylation of translation-associated proteins in Saccharomyces
cerevisiae: Identification of methylated lysines and their
methyltransferases.";
Proteomics 12:960-972(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]
METHYLATION AT LYS-40 BY RKM3, AND METHYLATION AT LYS-55 BY RKM4.
PubMed=24517342; DOI=10.1021/pr401251k;
Hart-Smith G., Chia S.Z., Low J.K., McKay M.J., Molloy M.P.,
Wilkins M.R.;
"Stoichiometry of Saccharomyces cerevisiae lysine methylation:
insights into non-histone protein lysine methyltransferase activity.";
J. Proteome Res. 13:1744-1756(2014).
[14]
3D-STRUCTURE MODELING OF 2-92, 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).
[15]
3D-STRUCTURE MODELING, 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).
[16]
X-RAY CRYSTALLOGRAPHY (4.0 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).
[17]
X-RAY CRYSTALLOGRAPHY (3.0 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.
{ECO:0000305|PubMed:22096102}.
-!- SUBUNIT: Component of the large ribosomal subunit (LSU). 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:14562095,
ECO:0000269|PubMed:22096102}.
-!- PTM: In wild-type cells, 78% of L42 is monomethylated at both Lys-
40 and Lys-55, and 22% are a mixture of species with either
residue monomethylated. {ECO:0000269|PubMed:24517342}.
-!- MASS SPECTROMETRY: Mass=12100.729; Method=Electrospray; Range=2-
106; Note=Monoisotopic mass with 2 methylation modifications.;
Evidence={ECO:0000269|PubMed:11983894};
-!- MASS SPECTROMETRY: Mass=12100.71; Method=Electrospray; Range=2-
106; Note=Monoisotopic mass with N6-methyl-Lys-40 and N6-methyl-
Lys-55.; Evidence={ECO:0000269|PubMed:18957409};
-!- MASS SPECTROMETRY: Mass=12108.0; Method=Electrospray; Range=2-106;
Note=With N6-methyl-Lys-40 and N6-methyl-Lys-55.;
Evidence={ECO:0000269|PubMed:18957409};
-!- MISCELLANEOUS: Present with 13600 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- MISCELLANEOUS: There are 2 genes for eL42 in yeast. {ECO:0000305}.
-!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL42
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA96049.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; D10578; BAA01435.1; -; Genomic_DNA.
EMBL; X92517; CAA63277.1; -; Genomic_DNA.
EMBL; Z71438; CAA96049.1; ALT_SEQ; Genomic_DNA.
EMBL; BK006947; DAA10387.1; -; Genomic_DNA.
PIR; S63114; S63114.
RefSeq; NP_012010.1; NM_001179271.1.
RefSeq; NP_014237.2; NM_001183000.1.
PDB; 1K5Y; Model; -; 1=2-92.
PDB; 3J6X; EM; 6.10 A; 82=1-106.
PDB; 3J6Y; EM; 6.10 A; 82=1-106.
PDB; 3J77; EM; 6.20 A; 92=1-106.
PDB; 3J78; EM; 6.30 A; 92=1-106.
PDB; 4U3M; X-ray; 3.00 A; Q2/q2=2-106.
PDB; 4U3N; X-ray; 3.20 A; Q2/q2=2-106.
PDB; 4U3U; X-ray; 2.90 A; Q2/q2=2-106.
PDB; 4U4N; X-ray; 3.10 A; Q2/q2=2-106.
PDB; 4U4O; X-ray; 3.60 A; Q2/q2=2-106.
PDB; 4U4Q; X-ray; 3.00 A; Q2/q2=2-106.
PDB; 4U4R; X-ray; 2.80 A; Q2/q2=2-106.
PDB; 4U4U; X-ray; 3.00 A; Q2/q2=2-106.
PDB; 4U4Y; X-ray; 3.20 A; Q2/q2=2-106.
PDB; 4U4Z; X-ray; 3.10 A; Q2/q2=2-106.
PDB; 4U50; X-ray; 3.20 A; Q2/q2=2-106.
PDB; 4U51; X-ray; 3.20 A; Q2/q2=2-106.
PDB; 4U52; X-ray; 3.00 A; Q2/q2=2-106.
PDB; 4U53; X-ray; 3.30 A; Q2/q2=2-106.
PDB; 4U55; X-ray; 3.20 A; Q2/q2=2-106.
PDB; 4U56; X-ray; 3.45 A; Q2/q2=2-106.
PDB; 4U6F; X-ray; 3.10 A; Q2/q2=2-106.
PDB; 4V4B; EM; 11.70 A; BZ=2-106.
PDB; 4V6I; EM; 8.80 A; Br=1-106.
PDB; 4V7R; X-ray; 4.00 A; Bf/Df=1-106.
PDB; 4V88; X-ray; 3.00 A; Bo/Do=1-106.
PDB; 4V8T; EM; 8.10 A; o=1-106.
PDB; 4V8Y; EM; 4.30 A; Bo=2-106.
PDB; 4V8Z; EM; 6.60 A; Bo=2-106.
PDB; 4V91; EM; 3.70 A; o=1-106.
PDB; 5APN; EM; 3.91 A; o=1-106.
PDB; 5APO; EM; 3.41 A; o=1-106.
PDB; 5DAT; X-ray; 3.15 A; Q2/q2=2-106.
PDB; 5DC3; X-ray; 3.25 A; Q2/q2=2-106.
PDB; 5DGE; X-ray; 3.45 A; Q2/q2=2-106.
PDB; 5DGF; X-ray; 3.30 A; Q2/q2=2-106.
PDB; 5DGV; X-ray; 3.10 A; Q2/q2=2-106.
PDB; 5FCI; X-ray; 3.40 A; Q2/q2=2-106.
PDB; 5FCJ; X-ray; 3.10 A; Q2/q2=2-106.
PDB; 5GAK; EM; 3.88 A; C=1-106.
PDB; 5H4P; EM; 3.07 A; o=1-106.
PDB; 5I4L; X-ray; 3.10 A; Q2/q2=2-106.
PDB; 5JUO; EM; 4.00 A; TA=1-106.
PDB; 5JUP; EM; 3.50 A; TA=1-106.
PDB; 5JUS; EM; 4.20 A; TA=1-106.
PDB; 5JUT; EM; 4.00 A; TA=1-106.
PDB; 5JUU; EM; 4.00 A; TA=1-106.
PDB; 5LYB; X-ray; 3.25 A; Q2/q2=2-106.
PDB; 5MC6; EM; 3.80 A; AP=1-106.
PDB; 5MEI; X-ray; 3.50 A; AP/DQ=2-106.
PDB; 5T62; EM; 3.30 A; Q=1-106.
PDB; 5T6R; EM; 4.50 A; Q=1-106.
PDB; 5TBW; X-ray; 3.00 A; AP/DQ=2-106.
PDB; 5TGA; X-ray; 3.30 A; Q2/q2=2-106.
PDB; 5TGM; X-ray; 3.50 A; Q2/q2=2-106.
PDBsum; 1K5Y; -.
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; 4V8T; -.
PDBsum; 4V8Y; -.
PDBsum; 4V8Z; -.
PDBsum; 4V91; -.
PDBsum; 5APN; -.
PDBsum; 5APO; -.
PDBsum; 5DAT; -.
PDBsum; 5DC3; -.
PDBsum; 5DGE; -.
PDBsum; 5DGF; -.
PDBsum; 5DGV; -.
PDBsum; 5FCI; -.
PDBsum; 5FCJ; -.
PDBsum; 5GAK; -.
PDBsum; 5H4P; -.
PDBsum; 5I4L; -.
PDBsum; 5JUO; -.
PDBsum; 5JUP; -.
PDBsum; 5JUS; -.
PDBsum; 5JUT; -.
PDBsum; 5JUU; -.
PDBsum; 5LYB; -.
PDBsum; 5MC6; -.
PDBsum; 5MEI; -.
PDBsum; 5T62; -.
PDBsum; 5T6R; -.
PDBsum; 5TBW; -.
PDBsum; 5TGA; -.
PDBsum; 5TGM; -.
ProteinModelPortal; P0CX27; -.
SMR; P0CX27; -.
BioGrid; 35667; 35.
BioGrid; 36574; 28.
MINT; MINT-2782780; -.
STRING; 4932.YNL162W; -.
iPTMnet; P0CX27; -.
MaxQB; P0CX27; -.
PRIDE; P0CX27; -.
EnsemblFungi; YHR141C; YHR141C; YHR141C.
EnsemblFungi; YNL162W; YNL162W; YNL162W.
GeneID; 855560; -.
GeneID; 856544; -.
KEGG; sce:YHR141C; -.
KEGG; sce:YNL162W; -.
SGD; S000005106; RPL42A.
HOGENOM; HOG000224989; -.
InParanoid; P0CX27; -.
KO; K02929; -.
OMA; YGGFPRP; -.
OrthoDB; EOG092C5T6H; -.
BioCyc; YEAST:G3O-33178-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-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; P0CX27; -.
PRO; PR:P0CX27; -.
Proteomes; UP000002311; Chromosome XIV.
ExpressionAtlas; P0CX27; differential.
GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD.
GO; GO:0003735; F:structural constituent of ribosome; IC:SGD.
GO; GO:0002181; P:cytoplasmic translation; IC:SGD.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
GO; GO:0046898; P:response to cycloheximide; IEA:UniProtKB-KW.
InterPro; IPR000552; Ribosomal_L44e.
InterPro; IPR011332; Ribosomal_zn-bd.
PANTHER; PTHR10369; PTHR10369; 1.
Pfam; PF00935; Ribosomal_L44; 1.
ProDom; PD002841; Ribosomal_L44e; 1.
SUPFAM; SSF57829; SSF57829; 1.
PROSITE; PS01172; RIBOSOMAL_L44E; 1.
1: Evidence at protein level;
3D-structure; Antibiotic resistance; Complete proteome;
Cycloheximide resistance; Cytoplasm; Direct protein sequencing;
Methylation; Reference proteome; Ribonucleoprotein; Ribosomal protein.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:365584}.
CHAIN 2 106 60S ribosomal protein L42-A.
/FTId=PRO_0000149147.
MOD_RES 40 40 N6-methyllysine; by RKM3.
{ECO:0000269|PubMed:18957409,
ECO:0000269|PubMed:22522802,
ECO:0000269|PubMed:24517342}.
MOD_RES 55 55 N6-methyllysine; by RKM4.
{ECO:0000269|PubMed:18957409,
ECO:0000269|PubMed:24517342}.
VARIANT 56 56 P -> Q (confers resistance to
cycloheximide, an inhibitor of
polypeptide elongation).
{ECO:0000269|PubMed:1729213}.
CONFLICT 40 41 KR -> RK (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 88 89 Missing (in Ref. 5; AA sequence).
{ECO:0000305}.
STRAND 6 12 {ECO:0000244|PDB:4U4R}.
TURN 15 17 {ECO:0000244|PDB:4U4R}.
STRAND 19 27 {ECO:0000244|PDB:4U4R}.
HELIX 38 47 {ECO:0000244|PDB:4U4R}.
STRAND 48 52 {ECO:0000244|PDB:4U4R}.
STRAND 66 74 {ECO:0000244|PDB:4U4R}.
TURN 75 77 {ECO:0000244|PDB:4U4R}.
STRAND 80 90 {ECO:0000244|PDB:4U4R}.
STRAND 92 94 {ECO:0000244|PDB:4U4R}.
SEQUENCE 106 AA; 12212 MW; 730CA11F2CF7F2B4 CRC64;
MVNVPKTRKT YCKGKTCRKH TQHKVTQYKA GKASLFAQGK RRYDRKQSGF GGQTKPVFHK
KAKTTKKVVL RLECVKCKTR AQLTLKRCKH FELGGEKKQK GQALQF


Related products :

Catalog number Product name Quantity
30-186 Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. MRPS12 is the 28S subunit protein that belongs to the ribosomal protein S12P family. The protein is a ke 0.05 mg
29-215 RPL9 is a ribosomal protein that is a component of the 60S subunit. RPL9 belongs to the L6P family of ribosomal proteins. It is located in the cytoplasm. As is typical for genes encoding ribosomal pro 0.1 mg
29-214 RPL9 is a ribosomal protein that is a component of the 60S subunit. RPL9 belongs to the L6P family of ribosomal proteins. It is located in the cytoplasm. As is typical for genes encoding ribosomal pro 0.1 mg
EIAAB35293 39S ribosomal protein L27 homolog,39S ribosomal protein L41, mitochondrial,Bcl-2-interacting mitochondrial ribosomal protein L41,BMRP,Cell proliferation-inducing gene 3 protein,Homo sapiens,Human,L41m
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
EIAAB36455 Mouse,Mus musculus,Ribosomal large subunit pseudouridine synthase C-like protein,Rlucl,RNA pseudouridylate synthase domain-containing protein 1,Rpusd1
29-216 RPL6 is a ribosomal protein that is a component of the 60S subunit. RPL6 belongs to the L6E family of ribosomal proteins. It is located in the cytoplasm. The protein can bind specifically to domain C 0.1 mg
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
EIAAB36454 C16orf40,Homo sapiens,Human,Ribosomal large subunit pseudouridine synthase C-like protein,RLUCL,RNA pseudouridylate synthase domain-containing protein 1,RPUSD1
EIAAB35298 28S ribosomal protein S32, mitochondrial,39S ribosomal protein L31, mitochondrial,39S ribosomal protein L42, mitochondrial,Homo sapiens,HSPC204,Human,L31mt,L42mt,MRPL31,MRP-L31,MRPL42,MRP-L42,MRPS32,M
EIAAB35296 28S ribosomal protein S32, mitochondrial,39S ribosomal protein L31, mitochondrial,39S ribosomal protein L42, mitochondrial,D10Ertd322e,L31mt,L42mt,Mouse,MRP-L31,Mrpl42,MRP-L42,Mrps32,MRP-S32,Mus muscu
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


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur