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40S ribosomal protein S6 (Phosphoprotein NP33) (Small ribosomal subunit protein eS6)

 RS6_HUMAN               Reviewed;         249 AA.
P62753; P08227; P10660; Q4VBY7; Q8N6Z7;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1988, sequence version 1.
22-NOV-2017, entry version 150.
RecName: Full=40S ribosomal protein S6;
AltName: Full=Phosphoprotein NP33;
AltName: Full=Small ribosomal subunit protein eS6 {ECO:0000303|PubMed:24524803};
Name=RPS6; ORFNames=OK/SW-cl.2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2840355; DOI=10.1016/0378-1119(88)90414-3;
Lott J.B., Mackie G.A.;
"Isolation and characterization of cloned cDNAs that code for human
ribosomal protein S6.";
Gene 65:31-39(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3279029;
Heinze H., Arnold H.H., Fischer D., Kruppa J.;
"The primary structure of the human ribosomal protein S6 derived from
a cloned cDNA.";
J. Biol. Chem. 263:4139-4144(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1301164; DOI=10.1093/hmg/1.8.565;
Antoine M., Fried M.;
"The organization of the intron-containing human S6 ribosomal protein
(rpS6) gene and determination of its location at chromosome 9p21.";
Hum. Mol. Genet. 1:565-570(1992).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1446836; DOI=10.1016/0378-1119(92)90149-J;
Pata I., Hoth S., Kruppa J., Metspalu A.;
"The human ribosomal protein S6 gene: isolation, primary structure and
location in chromosome 9.";
Gene 121:387-392(1992).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon adenocarcinoma;
Shichijo S., Itoh K.;
"Identification of immuno-peptidmics that are recognized by tumor-
reactive CTL generated from TIL of colon cancer patients.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-221.
TISSUE=Colon, Muscle, Pancreas, Skin, and Testis;
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 1-15.
TISSUE=Placenta;
PubMed=8706699; DOI=10.1111/j.1432-1033.1996.0144u.x;
Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K.,
Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A.;
"Characterization of the human small-ribosomal-subunit proteins by N-
terminal and internal sequencing, and mass spectrometry.";
Eur. J. Biochem. 239:144-149(1996).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[9]
PHOSPHORYLATION AT SER-235 AND SER-236.
PubMed=17360704; DOI=10.1074/jbc.M700906200;
Roux P.P., Shahbazian D., Vu H., Holz M.K., Cohen M.S., Taunton J.,
Sonenberg N., Blenis J.;
"RAS/ERK signaling promotes site-specific ribosomal protein S6
phosphorylation via RSK and stimulates cap-dependent translation.";
J. Biol. Chem. 282:14056-14064(2007).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235; SER-236; SER-240;
SER-244 AND SER-247, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
PHOSPHORYLATION AT SER-235 AND SER-236 BY DAPK1.
PubMed=18974095; DOI=10.1074/jbc.M805165200;
Stevens C., Lin Y., Harrison B., Burch L., Ridgway R.A., Sansom O.,
Hupp T.;
"Peptide combinatorial libraries identify TSC2 as a death-associated
protein kinase (DAPK) death domain-binding protein and reveal a
stimulatory role for DAPK in mTORC1 signaling.";
J. Biol. Chem. 284:334-344(2009).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-211, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240, 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).
[15]
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).
[16]
PHOSPHORYLATION AT SER-235 AND SER-236, AND MUTAGENESIS OF
235-SER-SER-236.
PubMed=21418524; DOI=10.1111/j.1742-4658.2011.08100.x;
Schlafli P., Troger J., Eckhardt K., Borter E., Spielmann P.,
Wenger R.H.;
"Substrate preference and phosphatidylinositol monophosphate
inhibition of the catalytic domain of the Per-Arnt-Sim domain kinase
PASKIN.";
FEBS J. 278:1757-1768(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236; SER-240 AND
SER-242, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[18]
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).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148; SER-235; SER-236
AND SER-240, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
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).
[21]
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).
[22]
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).
[23]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-14, 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).
[24]
STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.
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: May play an important role in controlling cell growth
and proliferation through the selective translation of particular
classes of mRNA.
-!- INTERACTION:
Q09161:NCBP1; NbExp=3; IntAct=EBI-356625, EBI-464743;
Q96RG2:PASK; NbExp=3; IntAct=EBI-356625, EBI-1042651;
-!- PTM: Ribosomal protein S6 is the major substrate of protein
kinases in eukaryote ribosomes. The phosphorylation is stimulated
by growth factors, tumor promoting agents, and mitogens. It is
dephosphorylated at growth arrest. Phosphorylated at Ser-235 and
Ser-236 by RPS6KA1 and RPS6KA3; phosphorylation at these sites
facilitates the assembly of the preinitiation complex.
{ECO:0000269|PubMed:17360704, ECO:0000269|PubMed:18974095,
ECO:0000269|PubMed:21418524}.
-!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS6
family. {ECO:0000305}.
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EMBL; M20020; AAA60288.1; -; mRNA.
EMBL; J03537; AAA60287.1; -; mRNA.
EMBL; X67309; CAA47719.1; -; Genomic_DNA.
EMBL; M77232; AAA60289.1; -; Genomic_DNA.
EMBL; AB062123; BAB93455.1; -; mRNA.
EMBL; BC000524; AAH00524.1; -; mRNA.
EMBL; BC009427; AAH09427.2; -; mRNA.
EMBL; BC027620; AAH27620.1; -; mRNA.
EMBL; BC071907; AAH71907.1; -; mRNA.
EMBL; BC071908; AAH71908.1; -; mRNA.
EMBL; BC094826; AAH94826.1; -; mRNA.
CCDS; CCDS6492.1; -.
PIR; JC1394; R3HU6.
RefSeq; NP_001001.2; NM_001010.2.
UniGene; Hs.408073; -.
PDB; 4UG0; EM; -; SG=1-249.
PDB; 4V6X; EM; 5.00 A; AG=1-249.
PDB; 5A2Q; EM; 3.90 A; G=1-249.
PDB; 5AJ0; EM; 3.50 A; BG=1-249.
PDB; 5FLX; EM; 3.90 A; G=1-249.
PDB; 5LKS; EM; 3.60 A; SG=1-249.
PDB; 5OA3; EM; 4.30 A; G=1-249.
PDB; 5T2C; EM; 3.60 A; AK=1-249.
PDB; 5VYC; X-ray; 6.00 A; G1/G2/G3/G4/G5/G6=1-249.
PDBsum; 4UG0; -.
PDBsum; 4V6X; -.
PDBsum; 5A2Q; -.
PDBsum; 5AJ0; -.
PDBsum; 5FLX; -.
PDBsum; 5LKS; -.
PDBsum; 5OA3; -.
PDBsum; 5T2C; -.
PDBsum; 5VYC; -.
ProteinModelPortal; P62753; -.
SMR; P62753; -.
BioGrid; 112108; 211.
CORUM; P62753; -.
DIP; DIP-31507N; -.
IntAct; P62753; 63.
MINT; MINT-1162101; -.
STRING; 9606.ENSP00000369757; -.
ChEMBL; CHEMBL3351215; -.
iPTMnet; P62753; -.
PhosphoSitePlus; P62753; -.
SwissPalm; P62753; -.
BioMuta; RPS6; -.
DMDM; 51338632; -.
EPD; P62753; -.
MaxQB; P62753; -.
PaxDb; P62753; -.
PeptideAtlas; P62753; -.
PRIDE; P62753; -.
TopDownProteomics; P62753; -.
DNASU; 6194; -.
Ensembl; ENST00000380394; ENSP00000369757; ENSG00000137154.
GeneID; 6194; -.
KEGG; hsa:6194; -.
UCSC; uc003znv.2; human.
CTD; 6194; -.
DisGeNET; 6194; -.
EuPathDB; HostDB:ENSG00000137154.12; -.
GeneCards; RPS6; -.
HGNC; HGNC:10429; RPS6.
HPA; CAB004027; -.
HPA; HPA031153; -.
MIM; 180460; gene.
neXtProt; NX_P62753; -.
OpenTargets; ENSG00000137154; -.
PharmGKB; PA34844; -.
eggNOG; KOG1646; Eukaryota.
eggNOG; COG2125; LUCA.
GeneTree; ENSGT00390000009819; -.
HOGENOM; HOG000190952; -.
HOVERGEN; HBG011441; -.
InParanoid; P62753; -.
KO; K02991; -.
OMA; KGYIFRI; -.
OrthoDB; EOG091G089B; -.
PhylomeDB; P62753; -.
TreeFam; TF300035; -.
Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
Reactome; R-HSA-156902; Peptide chain elongation.
Reactome; R-HSA-166208; mTORC1-mediated signalling.
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-6790901; rRNA modification in the nucleus and cytosol.
Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
Reactome; R-HSA-72649; Translation initiation complex formation.
Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
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).
SignaLink; P62753; -.
SIGNOR; P62753; -.
ChiTaRS; RPS6; human.
GenomeRNAi; 6194; -.
PRO; PR:P62753; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000137154; -.
CleanEx; HS_RPS6; -.
ExpressionAtlas; P62753; baseline and differential.
Genevisible; P62753; 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:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; IDA:ParkinsonsUK-UCL.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IDA:MGI.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005844; C:polysome; IEA:Ensembl.
GO; GO:0015935; C:small ribosomal subunit; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
GO; GO:0006924; P:activation-induced cell death of T cells; IEA:Ensembl.
GO; GO:0048821; P:erythrocyte development; IEA:Ensembl.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
GO; GO:0007369; P:gastrulation; IEA:Ensembl.
GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
GO; GO:0007093; P:mitotic cell cycle checkpoint; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
GO; GO:0022605; P:oogenesis stage; IEA:Ensembl.
GO; GO:0001890; P:placenta development; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:UniProtKB.
GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl.
GO; GO:0002309; P:T cell proliferation involved in immune response; IEA:Ensembl.
GO; GO:0031929; P:TOR signaling; IDA:UniProtKB.
GO; GO:0006412; P:translation; IC:UniProtKB.
GO; GO:0006413; P:translational initiation; TAS:Reactome.
GO; GO:0019083; P:viral transcription; TAS:Reactome.
InterPro; IPR014401; Ribosomal_S6_euk.
InterPro; IPR001377; Ribosomal_S6e.
InterPro; IPR018282; Ribosomal_S6e_CS.
PANTHER; PTHR11502; PTHR11502; 1.
Pfam; PF01092; Ribosomal_S6e; 1.
PIRSF; PIRSF002129; Ribosom_S6_euk; 1.
SMART; SM01405; Ribosomal_S6e; 1.
PROSITE; PS00578; RIBOSOMAL_S6E; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; Isopeptide bond; Phosphoprotein;
Polymorphism; Reference proteome; Ribonucleoprotein;
Ribosomal protein; Ubl conjugation.
CHAIN 1 249 40S ribosomal protein S6.
/FTId=PRO_0000137312.
MOD_RES 148 148 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 211 211 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 235 235 Phosphoserine; by RPS6KA1, RPS6KA3, DAPK1
and PASK. {ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:17360704,
ECO:0000269|PubMed:18974095,
ECO:0000269|PubMed:21418524}.
MOD_RES 236 236 Phosphoserine; by RPS6KA1, RPS6KA3, DAPK1
and PASK. {ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:17360704,
ECO:0000269|PubMed:18974095,
ECO:0000269|PubMed:21418524}.
MOD_RES 240 240 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 242 242 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 244 244 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 247 247 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
CROSSLNK 14 14 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 221 221 K -> R (in dbSNP:rs17852447).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_025314.
MUTAGEN 235 236 SS->AA: Abolishes phosphorylation by
PASK. {ECO:0000269|PubMed:21418524}.
CONFLICT 23 23 K -> T (in Ref. 1; AAA60288).
{ECO:0000305}.
CONFLICT 144 144 L -> R (in Ref. 1; AAA60288).
{ECO:0000305}.
CONFLICT 155 156 QY -> EC (in Ref. 2; AAA60287).
{ECO:0000305}.
CONFLICT 168 168 K -> R (in Ref. 2; AAA60287).
{ECO:0000305}.
CONFLICT 196 196 K -> Q (in Ref. 1; AAA60288).
{ECO:0000305}.
CONFLICT 219 219 E -> Q (in Ref. 2; AAA60287).
{ECO:0000305}.
SEQUENCE 249 AA; 28681 MW; A61E435884E636AE CRC64;
MKLNISFPAT GCQKLIEVDD ERKLRTFYEK RMATEVAADA LGEEWKGYVV RISGGNDKQG
FPMKQGVLTH GRVRLLLSKG HSCYRPRRTG ERKRKSVRGC IVDANLSVLN LVIVKKGEKD
IPGLTDTTVP RRLGPKRASR IRKLFNLSKE DDVRQYVVRK PLNKEGKKPR TKAPKIQRLV
TPRVLQHKRR RIALKKQRTK KNKEEAAEYA KLLAKRMKEA KEKRQEQIAK RRRLSSLRAS
TSKSESSQK


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18-785-210401 S6 Ribosomal Protein (Phospho-Ser235) - Phosphoprotein NP33 Polyclonal 0.1 mg
EIAAB36158 40S ribosomal protein S6,Homo sapiens,Human,OK_SW-cl.2,Phosphoprotein NP33,RPS6
orb81325 Human Ribosomal Phosphoprotein P0 protein Ribosomal Phosphoprotein P0 Human Recombinant produced in SF9 is glycosylated, polypeptide chain having a molecular mass of 35,096 Dalton. RPLP0 is expressed 5
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
H-9380.0025 S6 Phosphate Acceptor Peptide Salt _ Binding _ Synonym 40S Ribosomal Protein S6 (232_239) (human, chicken, mouse, rat), RRLSSLRA, Phosphoprotein NP33 (232_239) (human, chicken, mouse, rat) SumFormu 25.0 mg
H-9380.0005 S6 Phosphate Acceptor Peptide Salt _ Binding _ Synonym 40S Ribosomal Protein S6 (232_239) (human, chicken, mouse, rat), RRLSSLRA, Phosphoprotein NP33 (232_239) (human, chicken, mouse, rat) SumFormu 5.0 mg
H-9380.0005 S6 Phosphate Acceptor Peptide Salt _ Binding _ Synonym 40S Ribosomal Protein S6 (232_239) (human, chicken, mouse, rat), RRLSSLRA, Phosphoprotein NP33 (232_239) (human, chicken, mouse, rat) SumFormu 5.0 mg
H-9380.0025 S6 Phosphate Acceptor Peptide Salt _ Binding _ Synonym 40S Ribosomal Protein S6 (232_239) (human, chicken, mouse, rat), RRLSSLRA, Phosphoprotein NP33 (232_239) (human, chicken, mouse, rat) SumFormu 25.0 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
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
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
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
29-101 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
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
H-6098.0025 Biotinyl_S6 Phosphate Acceptor Peptide Salt Trifluoroacetate Binding _ Synonym Biotinyl_RRLSSLRA, Biotinyl_Phosphoprotein NP33 (232_239) (human, chicken, mouse, rat), Biotinyl_40S Ribosomal Protein 25.0 mg
H-6098.0025 Biotinyl_S6 Phosphate Acceptor Peptide Salt Trifluoroacetate Binding _ Synonym Biotinyl_RRLSSLRA, Biotinyl_Phosphoprotein NP33 (232_239) (human, chicken, mouse, rat), Biotinyl_40S Ribosomal Protein 25.0 mg


 

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