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60S ribosomal protein L28 (Large ribosomal subunit protein eL28)

 RL28_HUMAN              Reviewed;         137 AA.
P46779; B2R4A6; B4DEP9; C9JB50; E9PB24; G5E9L2; Q6IAY0; Q96FX1;
Q9BWQ0;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
18-JUL-2018, entry version 177.
RecName: Full=60S ribosomal protein L28;
AltName: Full=Large ribosomal subunit protein eL28 {ECO:0000303|PubMed:24524803};
Name=RPL28;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Colon;
PubMed=7772601; DOI=10.1016/0167-4781(95)00045-I;
Frigerio J.-M., Dagorn J.-C., Iovanna J.L.;
"Cloning, sequencing and expression of the L5, L21, L27a, L28, S5, S9,
S10 and S29 human ribosomal protein mRNAs.";
Biochim. Biophys. Acta 1262:64-68(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Cerebellum, and Hippocampus;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=B-cell, Kidney, Prostatic adenocarcinoma, and Uterus;
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).
[7]
PROTEIN SEQUENCE OF 2-11; 23-33; 40-58; 72-79 AND 120-127, CLEAVAGE OF
INITIATOR METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Hepatoma, and Ovarian carcinoma;
Bienvenut W.V., Boldt K., von Kriegsheim A., Lilla S., Lempens A.,
Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[8]
ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY, 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).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[11]
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).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[13]
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).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND 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).
[15]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-58 AND LYS-65, 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).
[16]
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.
{ECO:0000305|PubMed:12962325}.
-!- INTERACTION:
O95273:CCNDBP1; NbExp=6; IntAct=EBI-366357, EBI-748961;
P43146:DCC; NbExp=3; IntAct=EBI-366357, EBI-1222919;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=P46779-1; Sequence=Displayed;
Name=2;
IsoId=P46779-2; Sequence=VSP_043026;
Note=No experimental confirmation available.;
Name=3;
IsoId=P46779-3; Sequence=VSP_046173;
Note=No experimental confirmation available.;
Name=4;
IsoId=P46779-4; Sequence=VSP_047026;
Note=No experimental confirmation available. Gene prediction
based on EST data.;
Name=5;
IsoId=P46779-5; Sequence=VSP_047027;
Note=No experimental confirmation available. Gene prediction
based on EST data.;
-!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL28
family. {ECO:0000305}.
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EMBL; U14969; AAA85657.1; -; mRNA.
EMBL; CR457024; CAG33305.1; -; mRNA.
EMBL; AK311760; BAG34703.1; -; mRNA.
EMBL; AK293736; BAG57160.1; -; mRNA.
EMBL; AC020922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471135; EAW72374.1; -; Genomic_DNA.
EMBL; CH471135; EAW72375.1; -; Genomic_DNA.
EMBL; CH471135; EAW72376.1; -; Genomic_DNA.
EMBL; BC010173; AAH10173.1; -; mRNA.
EMBL; BC010182; AAH10182.1; -; mRNA.
EMBL; BC011582; AAH11582.1; -; mRNA.
EMBL; BG777550; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS12924.1; -. [P46779-1]
CCDS; CCDS46189.1; -. [P46779-3]
CCDS; CCDS46190.1; -. [P46779-2]
CCDS; CCDS46191.1; -. [P46779-4]
CCDS; CCDS46192.1; -. [P46779-5]
PIR; S55915; S55915.
RefSeq; NP_000982.2; NM_000991.4. [P46779-1]
RefSeq; NP_001129606.1; NM_001136134.1. [P46779-2]
RefSeq; NP_001129607.1; NM_001136135.1. [P46779-3]
RefSeq; NP_001129608.1; NM_001136136.1. [P46779-5]
RefSeq; NP_001129609.1; NM_001136137.1. [P46779-4]
UniGene; Hs.652114; -.
PDB; 4UG0; EM; -; Lr=1-137.
PDB; 4V6X; EM; 5.00 A; Cr=1-137.
PDB; 5AJ0; EM; 3.50 A; At=1-137.
PDB; 5LKS; EM; 3.60 A; Lr=1-137.
PDB; 5T2C; EM; 3.60 A; k=1-137.
PDB; 6EK0; EM; 2.90 A; Lr=1-137.
PDBsum; 4UG0; -.
PDBsum; 4V6X; -.
PDBsum; 5AJ0; -.
PDBsum; 5LKS; -.
PDBsum; 5T2C; -.
PDBsum; 6EK0; -.
ProteinModelPortal; P46779; -.
BioGrid; 112077; 154.
CORUM; P46779; -.
IntAct; P46779; 39.
MINT; P46779; -.
STRING; 9606.ENSP00000401450; -.
iPTMnet; P46779; -.
PhosphoSitePlus; P46779; -.
SwissPalm; P46779; -.
BioMuta; RPL28; -.
EPD; P46779; -.
MaxQB; P46779; -.
PaxDb; P46779; -.
PeptideAtlas; P46779; -.
PRIDE; P46779; -.
ProteomicsDB; 55761; -.
ProteomicsDB; 55762; -. [P46779-2]
TopDownProteomics; P46779-1; -. [P46779-1]
DNASU; 6158; -.
Ensembl; ENST00000344063; ENSP00000342787; ENSG00000108107. [P46779-1]
Ensembl; ENST00000428193; ENSP00000391665; ENSG00000108107. [P46779-4]
Ensembl; ENST00000431533; ENSP00000400596; ENSG00000108107. [P46779-5]
Ensembl; ENST00000558815; ENSP00000452909; ENSG00000108107. [P46779-3]
Ensembl; ENST00000559463; ENSP00000453319; ENSG00000108107. [P46779-1]
Ensembl; ENST00000560583; ENSP00000453029; ENSG00000108107. [P46779-2]
GeneID; 6158; -.
KEGG; hsa:6158; -.
UCSC; uc002qkv.4; human. [P46779-1]
CTD; 6158; -.
DisGeNET; 6158; -.
EuPathDB; HostDB:ENSG00000108107.12; -.
GeneCards; RPL28; -.
HGNC; HGNC:10330; RPL28.
HPA; HPA050459; -.
MIM; 603638; gene.
neXtProt; NX_P46779; -.
OpenTargets; ENSG00000108107; -.
PharmGKB; PA34710; -.
eggNOG; KOG3412; Eukaryota.
eggNOG; ENOG4111T32; LUCA.
GeneTree; ENSGT00390000008732; -.
HOGENOM; HOG000186171; -.
HOVERGEN; HBG000701; -.
InParanoid; P46779; -.
KO; K02903; -.
OMA; WMIIRNN; -.
PhylomeDB; P46779; -.
TreeFam; TF300173; -.
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; RPL28; human.
GeneWiki; 60S_ribosomal_protein_L28; -.
GenomeRNAi; 6158; -.
PMAP-CutDB; P46779; -.
PRO; PR:P46779; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000108107; -.
CleanEx; HS_RPL28; -.
ExpressionAtlas; P46779; baseline and differential.
Genevisible; P46779; HS.
GO; GO:0044297; C:cell body; IDA:ParkinsonsUK-UCL.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:ParkinsonsUK-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0022625; C:cytosolic large ribosomal subunit; HDA:UniProtKB.
GO; GO:0030425; C:dendrite; IDA:ParkinsonsUK-UCL.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
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; IBA:GO_Central.
GO; GO:0006413; P:translational initiation; TAS:Reactome.
InterPro; IPR029004; L28e/Mak16.
InterPro; IPR002672; Ribosomal_L28e.
PANTHER; PTHR10544; PTHR10544; 1.
Pfam; PF01778; Ribosomal_L28e; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Direct protein sequencing; Isopeptide bond; Phosphoprotein;
Polymorphism; Reference proteome; Ribonucleoprotein;
Ribosomal protein; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:12962325,
ECO:0000269|Ref.7}.
CHAIN 2 137 60S ribosomal protein L28.
/FTId=PRO_0000122389.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:12962325,
ECO:0000269|Ref.7}.
MOD_RES 115 115 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
CROSSLNK 58 58 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 65 65 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 69 137 GQRKPATSYVRTTINKNARATLSSIRHMIRKNKYRPDLRMA
AIRRASAILRSQKPVMVKRKRTRPTKSS -> E (in
isoform 4). {ECO:0000305}.
/FTId=VSP_047026.
VAR_SEQ 70 137 QRKPATSYVRTTINKNARATLSSIRHMIRKNKYRPDLRMAA
IRRASAILRSQKPVMVKRKRTRPTKSS -> EFCLVWARER
PLSRVWEL (in isoform 5). {ECO:0000305}.
/FTId=VSP_047027.
VAR_SEQ 109 137 AAIRRASAILRSQKPVMVKRKRTRPTKSS -> VSWGLGIR
LGETGQCCGEGPPTTGCNMGWRGMDSCFQPTPHTQHWPRGR
LVECMG (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043026.
VAR_SEQ 109 137 AAIRRASAILRSQKPVMVKRKRTRPTKSS -> DMLASTGS
GLCCSVAVQPWASSSTSLCLRTLICNMRVDRPYYSGLMRRL
NVQNLLDCAHKS (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_046173.
VARIANT 66 66 R -> L (in dbSNP:rs13502).
/FTId=VAR_034460.
CONFLICT 84 84 K -> R (in Ref. 6; AAH10182).
{ECO:0000305}.
CONFLICT 120 120 S -> T (in Ref. 1; AAA85657).
{ECO:0000305}.
SEQUENCE 137 AA; 15748 MW; 44DCDE45473D7C7B CRC64;
MSAHLQWMVV RNCSSFLIKR NKQTYSTEPN NLKARNSFRY NGLIHRKTVG VEPAADGKGV
VVVIKRRSGQ RKPATSYVRT TINKNARATL SSIRHMIRKN KYRPDLRMAA IRRASAILRS
QKPVMVKRKR TRPTKSS


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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


 

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