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Protein

40S ribosomal protein S3

Gene

RPS3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in translation as a component of the 40S small ribosomal subunit (PubMed:8706699). Has endonuclease activity and plays a role in repair of damaged DNA (PubMed:7775413). Cleaves phosphodiester bonds of DNAs containing altered bases with broad specificity and cleaves supercoiled DNA more efficiently than relaxed DNA (PubMed:15707971). Displays high binding affinity for 7,8-dihydro-8-oxoguanine (8-oxoG), a common DNA lesion caused by reactive oxygen species (ROS) (PubMed:14706345). Has also been shown to bind with similar affinity to intact and damaged DNA (PubMed:18610840). Stimulates the N-glycosylase activity of the base excision protein OGG1 (PubMed:15518571). Enhances the uracil excision activity of UNG1 (PubMed:18973764). Also stimulates the cleavage of the phosphodiester backbone by APEX1 (PubMed:18973764). When located in the mitochondrion, reduces cellular ROS levels and mitochondrial DNA damage (PubMed:23911537). Has also been shown to negatively regulate DNA repair in cells exposed to hydrogen peroxide (PubMed:17049931). Plays a role in regulating transcription as part of the NF-kappa-B p65-p50 complex where it binds to the RELA/p65 subunit, enhances binding of the complex to DNA and promotes transcription of target genes (PubMed:18045535). Represses its own translation by binding to its cognate mRNA (PubMed:20217897). Binds to and protects TP53/p53 from MDM2-mediated ubiquitination (PubMed:19656744). Involved in spindle formation and chromosome movement during mitosis by regulating microtubule polymerization (PubMed:23131551). Involved in induction of apoptosis through its role in activation of CASP8 (PubMed:14988002). Induces neuronal apoptosis by interacting with the E2F1 transcription factor and acting synergistically with it to up-regulate pro-apoptotic proteins BCL2L11/BIM and HRK/Dp5 (PubMed:20605787). Interacts with TRADD following exposure to UV radiation and induces apoptosis by caspase-dependent JNK activation (PubMed:22510408).16 Publications

Catalytic activityi

The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.1 Publication

Enzyme regulationi

Endonuclease activity is inhibited by MgCl2 on apurinic/apyrimidinic DNA but not on UV-irradiated DNA.1 Publication

pH dependencei

Optimum pH is between 8.0 and 9.0 with activity decreasing sharply below 8.0.1 Publication

GO - Molecular functioni

  • damaged DNA binding Source: UniProtKB
  • DNA-(apurinic or apyrimidinic site) lyase activity Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • iron-sulfur cluster binding Source: UniProtKB
  • mRNA binding Source: UniProtKB
  • NF-kappaB binding Source: UniProtKB
  • oxidized purine nucleobase lesion DNA N-glycosylase activity Source: GO_Central
  • poly(A) RNA binding Source: UniProtKB
  • protein kinase A binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • structural constituent of ribosome Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • cellular protein metabolic process Source: Reactome
  • cellular response to DNA damage stimulus Source: UniProtKB
  • DNA repair Source: GO_Central
  • gene expression Source: Reactome
  • mitotic nuclear division Source: UniProtKB-KW
  • negative regulation of DNA repair Source: UniProtKB
  • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  • positive regulation of apoptotic signaling pathway Source: UniProtKB
  • positive regulation of DNA N-glycosylase activity Source: UniProtKB
  • positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • regulation of translation Source: UniProtKB-KW
  • SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  • transcription, DNA-templated Source: UniProtKB-KW
  • translation Source: UniProtKB
  • translational elongation Source: Reactome
  • translational initiation Source: UniProtKB
  • translational termination Source: Reactome
  • viral life cycle Source: Reactome
  • viral process Source: Reactome
  • viral transcription Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Ribonucleoprotein, Ribosomal protein

Keywords - Biological processi

Apoptosis, Cell cycle, Cell division, DNA damage, DNA repair, Mitosis, Transcription, Transcription regulation, Translation regulation

Keywords - Ligandi

DNA-binding, RNA-binding

Enzyme and pathway databases

ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1979. Translation initiation complex formation.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.
REACT_9491. Viral mRNA Translation.

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S3 (EC:4.2.99.181 Publication)
Gene namesi
Name:RPS3
ORF Names:OK/SW-cl.26
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:10420. RPS3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • cytosolic small ribosomal subunit Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • membrane Source: UniProtKB
  • mitochondrial inner membrane Source: UniProtKB-SubCell
  • nucleolus Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB
  • ribonucleoprotein complex Source: UniProtKB
  • ruffle membrane Source: UniProtKB
  • spindle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane, Mitochondrion, Mitochondrion inner membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi6 – 61S → A: No effect on phosphorylation by CDK1. Greatly reduced phosphorylation by PRKCD. Abolishes phosphorylation by PRKCD; when associated with A-221. 2 Publications
Mutagenesisi18 – 181K → R: No effect on sumoylation. Abolishes sumoylation; when associated with R-214 and R-230. 1 Publication
Mutagenesisi35 – 351S → A: No effect on phosphorylation by PRKCD. 1 Publication
Mutagenesisi42 – 421T → A: Abolishes phosphorylation by MAPK and translocation to the nucleus following exposure of cells to hydrogen peroxide. No effect on phosphorylation by CDK1 or PRKCD. 4 Publications
Mutagenesisi42 – 421T → D: Phosphomimetic mutant which is detected exclusively in the nucleus. 1 Publication
Mutagenesisi70 – 701T → A: No effect on phosphorylation by PRKCD. Abolishes phosphorylation by PKB. 2 Publications
Mutagenesisi70 – 701T → D, E or R: Abolishes phosphorylation by PKB. 1 Publication
Mutagenesisi132 – 1321K → A: Does not affect ability to cleave DNA but abolishes binding to 8-oxoG. 1 Publication
Mutagenesisi139 – 1391S → A: No effect on phosphorylation by PRKCD. 1 Publication
Mutagenesisi149 – 1491S → A: No effect on phosphorylation by PRKCD. 1 Publication
Mutagenesisi195 – 1951T → A: No effect on phosphorylation by PRKCD. 1 Publication
Mutagenesisi209 – 2091S → A: Reduced phosphorylation by IKKB. 1 Publication
Mutagenesisi214 – 2141K → R: No effect on sumoylation. Abolishes sumoylation; when associated with R-18 and R-230. 1 Publication
Mutagenesisi221 – 2211T → A: No effect on phosphorylation by MAPK. Significantly reduces phosphorylation by CDK1 and nuclear accumulation. Greatly reduced phosphorylation by PRKCD. Abolishes phosphorylation by PRKCD; when associated with A-6. 3 Publications
Mutagenesisi230 – 2301K → R: No effect on sumoylation. Abolishes sumoylation; when associated with R-18 and R-214. 1 Publication

Organism-specific databases

PharmGKBiPA34829.

Polymorphism and mutation databases

BioMutaiRPS3.
DMDMi417719.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 24324240S ribosomal protein S3PRO_0000130320Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei6 – 61Phosphoserine; by PKC/PRKCD1 Publication
Modified residuei42 – 421Phosphothreonine; by MAPK1 Publication
Modified residuei62 – 621N6-acetyllysine1 Publication
Modified residuei64 – 641Asymmetric dimethylarginine; by PRMT11 Publication
Modified residuei65 – 651Asymmetric dimethylarginine; by PRMT11 Publication
Modified residuei67 – 671Asymmetric dimethylarginine; by PRMT11 Publication
Modified residuei70 – 701Phosphothreonine; by PKB1 Publication
Cross-linki90 – 90Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residuei132 – 1321N6-succinyllysineBy similarity
Cross-linki202 – 202Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residuei209 – 2091Phosphoserine; by IKKB1 Publication
Modified residuei221 – 2211Phosphothreonine; by CDK1 and PKC/PRKCD9 Publications
Modified residuei224 – 2241Phosphoserine1 Publication
Modified residuei242 – 2421Phosphothreonine2 Publications

Post-translational modificationi

Methylation by PRMT1 is required for import into the nucleolus and for ribosome assembly.1 Publication
Sumoylation by SUMO1 enhances protein stability through increased resistance to proteolysis. Sumoylation occurs at one or more of the three consensus sites, Lys-18, Lys-214 and Lys-230.1 Publication
Phosphorylation at Thr-221 by CDK1 occurs mainly in G2/M phase (PubMed:21871177). Phosphorylation by PRKCD occurs on a non-ribosomal-associated form which results in translocation of RPS3 to the nucleus and enhances its endonuclease activity (PubMed:19059439). Phosphorylated on Ser-209 by IKKB in response to activation of the NF-kappa-B p65-p50 complex which enhances the association of RPS3 with importin-alpha and mediates the nuclear translocation of RPS3 (PubMed:21399639). Phosphorylation by MAPK is required for translocation to the nucleus following exposure of cells to DNA damaging agents such as hydrogen peroxide (PubMed:17560175). Phosphorylation by PKB/AKT mediates RPS3 nuclear translocation, enhances RPS3 endonuclease activity and suppresses RPS3-induced neuronal apoptosis (PubMed:20605787).5 Publications
Ubiquitinated. This is prevented by interaction with HSP90 which stabilizes the protein.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP23396.
PaxDbiP23396.
PeptideAtlasiP23396.
PRIDEiP23396.

PTM databases

PhosphoSiteiP23396.

Expressioni

Gene expression databases

BgeeiP23396.
CleanExiHS_RPS3.
ExpressionAtlasiP23396. baseline and differential.
GenevisibleiP23396. HS.

Organism-specific databases

HPAiHPA063339.

Interactioni

Subunit structurei

Component of the 40S small ribosomal subunit (PubMed:8706699). Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (PubMed:17289661). Interacts with HNRPD (PubMed:24423872). Interacts with PRMT1; the interaction methylates RPS3 (PubMed:19460357). Interacts with SUMO1; the interaction sumoylates RPS3 (PubMed:21968017). Interacts with UBC9 (PubMed:21968017). Interacts with CDK1; the interaction phosphorylates RPS3 (PubMed:21871177). Interacts with PRKCD; the interaction phosphorylates RPS3 (PubMed:19059439). Interacts with PKB/AKT; the interaction phosphorylates RPS3 (PubMed:20605787). Interacts with E2F1; the interaction occurs in the absence of nerve growth factor and increases transcription of pro-apoptotic proteins BCL2L11/BIM and HRK/Dp5 (PubMed:20605787). Interacts with the base excision repair proteins APEX1 and OGG1; interaction with OGG1 increases OGG1 N-glycosylase activity (PubMed:15518571). Interacts with UNG; the interaction increases the uracil excision activity of UNG1 (PubMed:18973764). Interacts with HSP90; the interaction prevents the ubiquitination and proteasome-dependent degradation of RPS3 and is suppressed by increased ROS levels (PubMed:16314389). Interacts with TOM70; the interaction promotes translocation of RPS3 to the mitochondrion (PubMed:23911537). Interacts (via N-terminus) with RELA (via N-terminus); the interaction enhances the DNA-binding activity of the NF-kappa-B p65-p50 complex (PubMed:18045535). Interacts with NFKBIA; the interaction is direct and may bridge the interaction between RPS3 and RELA (PubMed:24457201). Interacts with IKKB; the interaction phosphorylates RPS3 and enhances its translocation to the nucleus (PubMed:21399639). Interacts (via KH domain) with MDM2 and TP53 (PubMed:19656744). Interacts with TRADD (PubMed:22510408). Interacts (via N-terminus) with E.coli O157:H7 (strain EDL933) nleH1 and nleH2; the interaction with nleH1 inhibits phosphorylation by IKKB, reduces RPS3 nuclear abundance and inhibits transcriptional activation by the NF-kappa-B p65-p50 complex (PubMed:20041225, PubMed:21399639). Identified in a HCV IRES-mediated translation complex, at least composed of EIF3C, IGF2BP1, RPS3 and HCV RNA-replicon (PubMed:19541769). Interacts with CRY1 (By similarity).1 PublicationBy similarity19 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
IKBKBO149204EBI-351193,EBI-81266
LRRK2Q5S0072EBI-351193,EBI-5323863
MDM2Q009878EBI-351193,EBI-389668
NEDD8Q158432EBI-351193,EBI-716247
NFKB1P198382EBI-351193,EBI-300010
NFKBIAP259636EBI-351193,EBI-307386
PPIDQ087524EBI-351193,EBI-716596
RELAQ042067EBI-351193,EBI-73886
TP53P046374EBI-351193,EBI-366083
YWHAZP631042EBI-351193,EBI-347088

Protein-protein interaction databases

BioGridi112102. 197 interactions.
IntActiP23396. 47 interactions.
MINTiMINT-4999144.
STRINGi9606.ENSP00000433821.

Structurei

Secondary structure

1
243
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi17 – 2812Combined sources
Turni29 – 335Combined sources
Beta strandi34 – 418Combined sources
Beta strandi46 – 538Combined sources
Helixi55 – 595Combined sources
Helixi61 – 633Combined sources
Helixi64 – 7714Combined sources
Beta strandi83 – 908Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WH9NMR-A17-95[»]
4V6Xelectron microscopy5.00AD1-243[»]
ProteinModelPortaliP23396.
SMRiP23396. Positions 2-213.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23396.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 9272KH type-2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ribosomal protein S3P family.Curated
Contains 1 KH type-2 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0092.
GeneTreeiENSGT00390000008610.
HOGENOMiHOG000210611.
HOVERGENiHBG002195.
InParanoidiP23396.
KOiK02985.
OMAiQKFTEGY.
OrthoDBiEOG7F7W9M.
PhylomeDBiP23396.
TreeFamiTF300901.

Family and domain databases

Gene3Di3.30.1140.32. 1 hit.
3.30.300.20. 1 hit.
InterProiIPR004087. KH_dom.
IPR015946. KH_dom-like_a/b.
IPR004044. KH_dom_type_2.
IPR009019. KH_prok-type.
IPR001351. Ribosomal_S3_C.
IPR018280. Ribosomal_S3_CS.
IPR005703. Ribosomal_S3_euk/arc.
[Graphical view]
PfamiPF07650. KH_2. 1 hit.
PF00189. Ribosomal_S3_C. 1 hit.
[Graphical view]
SMARTiSM00322. KH. 1 hit.
[Graphical view]
SUPFAMiSSF54814. SSF54814. 1 hit.
SSF54821. SSF54821. 1 hit.
TIGRFAMsiTIGR01008. uS3_euk_arch. 1 hit.
PROSITEiPS50823. KH_TYPE_2. 1 hit.
PS00548. RIBOSOMAL_S3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P23396-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAVQISKKRK FVADGIFKAE LNEFLTRELA EDGYSGVEVR VTPTRTEIII
60 70 80 90 100
LATRTQNVLG EKGRRIRELT AVVQKRFGFP EGSVELYAEK VATRGLCAIA
110 120 130 140 150
QAESLRYKLL GGLAVRRACY GVLRFIMESG AKGCEVVVSG KLRGQRAKSM
160 170 180 190 200
KFVDGLMIHS GDPVNYYVDT AVRHVLLRQG VLGIKVKIML PWDPTGKIGP
210 220 230 240
KKPLPDHVSI VEPKDEILPT TPISEQKGGK PEPPAMPQPV PTA
Length:243
Mass (Da):26,688
Last modified:October 1, 1993 - v2
Checksum:i6ECBB34A8EE04AAF
GO
Isoform 2 (identifier: P23396-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     85-85: E → ELKIMVMVTGYPLLPLK

Note: No experimental confirmation available. Gene prediction based on EST data.
Show »
Length:259
Mass (Da):28,487
Checksum:i68FF5C2DF8769693
GO

Sequence cautioni

The sequence BAB93471.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81K → R in AAB19349 (PubMed:1712897).Curated
Sequence conflicti104 – 1041S → C in CAA39248 (PubMed:2129557).Curated
Sequence conflicti233 – 2331P → L in CAA39248 (PubMed:2129557).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei85 – 851E → ELKIMVMVTGYPLLPLK in isoform 2. CuratedVSP_046667

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14990 mRNA. Translation: AAB60336.1.
U14991 mRNA. Translation: AAB60337.1.
U14992 mRNA. Translation: AAB60338.1.
X55715 mRNA. Translation: CAA39248.1.
S42658 mRNA. Translation: AAB19349.2.
AB061838 Genomic DNA. Translation: BAB79476.1.
AY791291 Genomic DNA. Translation: AAV40835.1.
AK313051 mRNA. Translation: BAG35882.1.
AP000744 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74963.1.
BC003137 mRNA. Translation: AAH03137.1.
BC003577 mRNA. Translation: AAH03577.1.
BC013196 mRNA. Translation: AAH13196.1.
BC034149 mRNA. Translation: AAH34149.1.
BC071917 mRNA. Translation: AAH71917.1.
BC100284 mRNA. Translation: AAI00285.1.
L16016 Genomic DNA. Translation: AAA18095.1.
AB062288 mRNA. Translation: BAB93471.1. Different initiation.
CCDSiCCDS58161.1. [P23396-2]
CCDS8236.1. [P23396-1]
PIRiA41247. R3HUS3.
RefSeqiNP_000996.2. NM_001005.4. [P23396-1]
NP_001243731.1. NM_001256802.1. [P23396-1]
NP_001247435.1. NM_001260506.1. [P23396-2]
NP_001247436.1. NM_001260507.1.
UniGeneiHs.546286.
Hs.740358.

Genome annotation databases

EnsembliENST00000278572; ENSP00000278572; ENSG00000149273. [P23396-2]
ENST00000524851; ENSP00000433821; ENSG00000149273. [P23396-1]
ENST00000527446; ENSP00000436971; ENSG00000149273. [P23396-1]
ENST00000531188; ENSP00000434643; ENSG00000149273. [P23396-1]
GeneIDi6188.
KEGGihsa:6188.
UCSCiuc001owh.4. human. [P23396-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14990 mRNA. Translation: AAB60336.1.
U14991 mRNA. Translation: AAB60337.1.
U14992 mRNA. Translation: AAB60338.1.
X55715 mRNA. Translation: CAA39248.1.
S42658 mRNA. Translation: AAB19349.2.
AB061838 Genomic DNA. Translation: BAB79476.1.
AY791291 Genomic DNA. Translation: AAV40835.1.
AK313051 mRNA. Translation: BAG35882.1.
AP000744 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74963.1.
BC003137 mRNA. Translation: AAH03137.1.
BC003577 mRNA. Translation: AAH03577.1.
BC013196 mRNA. Translation: AAH13196.1.
BC034149 mRNA. Translation: AAH34149.1.
BC071917 mRNA. Translation: AAH71917.1.
BC100284 mRNA. Translation: AAI00285.1.
L16016 Genomic DNA. Translation: AAA18095.1.
AB062288 mRNA. Translation: BAB93471.1. Different initiation.
CCDSiCCDS58161.1. [P23396-2]
CCDS8236.1. [P23396-1]
PIRiA41247. R3HUS3.
RefSeqiNP_000996.2. NM_001005.4. [P23396-1]
NP_001243731.1. NM_001256802.1. [P23396-1]
NP_001247435.1. NM_001260506.1. [P23396-2]
NP_001247436.1. NM_001260507.1.
UniGeneiHs.546286.
Hs.740358.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WH9NMR-A17-95[»]
4V6Xelectron microscopy5.00AD1-243[»]
ProteinModelPortaliP23396.
SMRiP23396. Positions 2-213.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112102. 197 interactions.
IntActiP23396. 47 interactions.
MINTiMINT-4999144.
STRINGi9606.ENSP00000433821.

PTM databases

PhosphoSiteiP23396.

Polymorphism and mutation databases

BioMutaiRPS3.
DMDMi417719.

Proteomic databases

MaxQBiP23396.
PaxDbiP23396.
PeptideAtlasiP23396.
PRIDEiP23396.

Protocols and materials databases

DNASUi6188.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000278572; ENSP00000278572; ENSG00000149273. [P23396-2]
ENST00000524851; ENSP00000433821; ENSG00000149273. [P23396-1]
ENST00000527446; ENSP00000436971; ENSG00000149273. [P23396-1]
ENST00000531188; ENSP00000434643; ENSG00000149273. [P23396-1]
GeneIDi6188.
KEGGihsa:6188.
UCSCiuc001owh.4. human. [P23396-1]

Organism-specific databases

CTDi6188.
GeneCardsiGC11P075110.
HGNCiHGNC:10420. RPS3.
HPAiHPA063339.
MIMi600454. gene.
neXtProtiNX_P23396.
PharmGKBiPA34829.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0092.
GeneTreeiENSGT00390000008610.
HOGENOMiHOG000210611.
HOVERGENiHBG002195.
InParanoidiP23396.
KOiK02985.
OMAiQKFTEGY.
OrthoDBiEOG7F7W9M.
PhylomeDBiP23396.
TreeFamiTF300901.

Enzyme and pathway databases

ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1979. Translation initiation complex formation.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.
REACT_9491. Viral mRNA Translation.

Miscellaneous databases

ChiTaRSiRPS3. human.
EvolutionaryTraceiP23396.
GeneWikiiRPS3.
GenomeRNAii6188.
NextBioi24029.
PROiP23396.
SOURCEiSearch...

Gene expression databases

BgeeiP23396.
CleanExiHS_RPS3.
ExpressionAtlasiP23396. baseline and differential.
GenevisibleiP23396. HS.

Family and domain databases

Gene3Di3.30.1140.32. 1 hit.
3.30.300.20. 1 hit.
InterProiIPR004087. KH_dom.
IPR015946. KH_dom-like_a/b.
IPR004044. KH_dom_type_2.
IPR009019. KH_prok-type.
IPR001351. Ribosomal_S3_C.
IPR018280. Ribosomal_S3_CS.
IPR005703. Ribosomal_S3_euk/arc.
[Graphical view]
PfamiPF07650. KH_2. 1 hit.
PF00189. Ribosomal_S3_C. 1 hit.
[Graphical view]
SMARTiSM00322. KH. 1 hit.
[Graphical view]
SUPFAMiSSF54814. SSF54814. 1 hit.
SSF54821. SSF54821. 1 hit.
TIGRFAMsiTIGR01008. uS3_euk_arch. 1 hit.
PROSITEiPS50823. KH_TYPE_2. 1 hit.
PS00548. RIBOSOMAL_S3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

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  1. "Isolation of a cDNA encoding human 40S ribosomal protein s3."
    Zhang X.T., Tan Y.M., Tan Y.H.
    Nucleic Acids Res. 18:6689-6689(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Ribosomal protein genes are overexpressed in colorectal cancer: isolation of a cDNA clone encoding the human S3 ribosomal protein."
    Pogue-Geile K., Geiser J.R., Shu M., Miller C., Wool I.G., Meisler A.I., Pipas J.M.
    Mol. Cell. Biol. 11:3842-3849(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "The human ribosomal protein genes: sequencing and comparative analysis of 73 genes."
    Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S., Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.
    Genome Res. 12:379-390(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. NIEHS SNPs program
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Adrenal cortex, Liver, Lymph, Skin and Testis.
  9. "A small nucleolar RNA is processed from an intron of the human gene encoding ribosomal protein S3."
    Tycowski K.T., Shu M.D., Steitz J.A.
    Genes Dev. 7:1176-1190(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 1-94 (ISOFORM 1).
  10. Bienvenut W.V., Murray L., Brunton V.G., Frame M.C., Calvo F., Kolch W.
    Submitted (FEB-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-8; 10-64; 68-116; 118-141; 152-173; 186-197 AND 202-243, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma and Colon adenocarcinoma.
  11. "Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
    Shichijo S., Itoh K.
    Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-243 (ISOFORM 1).
    Tissue: Colon adenocarcinoma.
  12. Bienvenut W.V., Waridel P., Quadroni M.
    Submitted (MAR-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 10-40; 46-54; 76-90; 95-106; 109-116; 118-132; 152-173; 179-185; 188-197 AND 202-243, PHOSPHORYLATION AT THR-221, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma.
  13. "Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry."
    Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A.
    Eur. J. Biochem. 239:144-149(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 188-197.
    Tissue: Placenta.
  14. "Implication of mammalian ribosomal protein S3 in the processing of DNA damage."
    Kim J., Chubatsu L.S., Admon A., Stahl J., Fellous R., Linn S.
    J. Biol. Chem. 270:13620-13629(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  15. "Human ribosomal protein S3 interacts with DNA base excision repair proteins hAPE/Ref-1 and hOGG1."
    Hegde V., Wang M., Deutsch W.A.
    Biochemistry 43:14211-14217(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH APEX1 AND OGG1.
  16. "Characterization of human ribosomal protein S3 binding to 7,8-dihydro-8-oxoguanine and abasic sites by surface plasmon resonance."
    Hegde V., Wang M., Deutsch W.A.
    DNA Repair 3:121-126(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "RpS3, a DNA repair endonuclease and ribosomal protein, is involved in apoptosis."
    Jang C.Y., Lee J.Y., Kim J.
    FEBS Lett. 560:81-85(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. "Characterization of a wide range base-damage-endonuclease activity of mammalian rpS3."
    Kim S.H., Lee J.Y., Kim J.
    Biochem. Biophys. Res. Commun. 328:962-967(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
  19. "Erk phosphorylates threonine 42 residue of ribosomal protein S3."
    Kim H.D., Lee J.Y., Kim J.
    Biochem. Biophys. Res. Commun. 333:110-115(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-42, MUTAGENESIS OF THR-42 AND THR-221.
  20. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. "The high binding affinity of human ribosomal protein S3 to 7,8-dihydro-8-oxoguanine is abrogated by a single amino acid change."
    Hegde V., Wang M., Mian I.S., Spyres L., Deutsch W.A.
    DNA Repair 5:810-815(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LYS-132.
  22. "Interaction of Hsp90 with ribosomal proteins protects from ubiquitination and proteasome-dependent degradation."
    Kim T.S., Jang C.Y., Kim H.D., Lee J.Y., Ahn B.Y., Kim J.
    Mol. Biol. Cell 17:824-833(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HSP90, SUBCELLULAR LOCATION, UBIQUITINATION.
  23. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Pituitary.
  25. "Ribosomal protein S3: a KH domain subunit in NF-kappaB complexes that mediates selective gene regulation."
    Wan F., Anderson D.E., Barnitz R.A., Snow A., Bidere N., Zheng L., Hegde V., Lam L.T., Staudt L.M., Levens D., Deutsch W.A., Lenardo M.J.
    Cell 131:927-939(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RELA, IDENTIFICATION IN THE NF-KAPPA-B P65-P50 COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  26. "Knockdown of ribosomal protein S3 protects human cells from genotoxic stress."
    Hegde V., Yadavilli S., Deutsch W.A.
    DNA Repair 6:94-99(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  27. "Translocation of human ribosomal protein S3 to sites of DNA damage is dependant on ERK-mediated phosphorylation following genotoxic stress."
    Yadavilli S., Hegde V., Deutsch W.A.
    DNA Repair 6:1453-1462(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, MUTAGENESIS OF THR-42.
  28. Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  29. "Interactions of human ribosomal protein S3 with undamaged and damaged DNA."
    Balyeva K.E., Malygin A.A., Karpova G.G., Nevinskii G.A., Zharkov D.O.
    Mol. Biol. (Mosk.) 42:314-322(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  30. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-242, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  31. "Human ribosomal protein S3 (hRpS3) interacts with uracil-DNA glycosylase (hUNG) and stimulates its glycosylase activity."
    Ko S.I., Park J.H., Park M.J., Kim J., Kang L.W., Han Y.S.
    Mutat. Res. 648:54-64(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH UNG.
  32. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  33. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  34. "Arginine methylation of ribosomal protein S3 affects ribosome assembly."
    Shin H.S., Jang C.Y., Kim H.D., Kim T.S., Kim S., Kim J.
    Biochem. Biophys. Res. Commun. 385:273-278(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRMT1, SUBCELLULAR LOCATION, METHYLATION AT ARG-64; ARG-65 AND ARG-67.
  35. "PKCdelta-dependent functional switch of rpS3 between translation and DNA repair."
    Kim T.S., Kim H.D., Kim J.
    Biochim. Biophys. Acta 1793:395-405(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRKCD, PHOSPHORYLATION AT SER-6 AND THR-221, MUTAGENESIS OF SER-6; SER-35; THR-42; THR-70; SER-139; SER-149; THR-195 AND THR-221.
  36. "Ribosomal protein S3: A multi-functional protein that interacts with both p53 and MDM2 through its KH domain."
    Yadavilli S., Mayo L.D., Higgins M., Lain S., Hegde V., Deutsch W.A.
    DNA Repair 8:1215-1224(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MDM2 AND TP53, IDENTIFICATION BY MASS SPECTROMETRY.
  37. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  38. Cited for: INTERACTION WITH E.COLI NLEH1 AND NLEH2, IDENTIFICATION BY MASS SPECTROMETRY.
  39. "IGF2BP1 enhances HCV IRES-mediated translation initiation via the 3'UTR."
    Weinlich S., Huettelmaier S., Schierhorn A., Behrens S.-E., Ostareck-Lederer A., Ostareck D.H.
    RNA 15:1528-1542(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A HCV IRES-MEDIATED TRANSLATION COMPLEX.
  40. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  41. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  42. "Ribosomal protein S3, a new substrate of Akt, serves as a signal mediator between neuronal apoptosis and DNA repair."
    Lee S.B., Kwon I.S., Park J., Lee K.H., Ahn Y., Lee C., Kim J., Choi S.Y., Cho S.W., Ahn J.Y.
    J. Biol. Chem. 285:29457-29468(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH E2F1 AND PKB, PHOSPHORYLATION AT THR-70, MUTAGENESIS OF THR-70.
  43. "RpS3 translation is repressed by interaction with its own mRNA."
    Kim H.D., Kim T.S., Joo Y.J., Shin H.S., Kim S.H., Jang C.Y., Lee C.E., Kim J.
    J. Cell. Biochem. 110:294-303(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  44. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    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.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  45. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  46. Cited for: INTERACTION WITH SUMO1 AND UBC9, SUMOYLATION AT LYS-18; LYS-214 AND LYS-230, MUTAGENESIS OF LYS-18; LYS-214 AND LYS-230.
  47. "Ribosomal protein S3 is phosphorylated by Cdk1/cdc2 during G2/M phase."
    Yoon I.S., Chung J.H., Hahm S.H., Park M.J., Lee Y.R., Ko S.I., Kang L.W., Kim T.S., Kim J., Han Y.S.
    BMB Rep. 44:529-534(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDK1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-221, MUTAGENESIS OF SER-6; THR-42 AND THR-221.
  48. "IKKbeta phosphorylation regulates RPS3 nuclear translocation and NF-kappaB function during infection with Escherichia coli strain O157:H7."
    Wan F., Weaver A., Gao X., Bern M., Hardwidge P.R., Lenardo M.J.
    Nat. Immunol. 12:335-343(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IKKB AND E.COLI NLEH1, PHOSPHORYLATION AT SER-209, MUTAGENESIS OF SER-209.
  49. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  50. "Ribosomal protein S3 interacts with TRADD to induce apoptosis through caspase dependent JNK activation."
    Jang C.Y., Kim H.D., Kim J.
    Biochem. Biophys. Res. Commun. 421:474-478(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TRADD.
  51. "Ribosomal protein S3 localizes on the mitotic spindle and functions as a microtubule associated protein in mitosis."
    Jang C.Y., Kim H.D., Zhang X., Chang J.S., Kim J.
    Biochem. Biophys. Res. Commun. 429:57-62(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  52. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  53. "Cytoplasmic ribosomal protein S3 (rpS3) plays a pivotal role in mitochondrial DNA damage surveillance."
    Kim Y., Kim H.D., Kim J.
    Biochim. Biophys. Acta 1833:2943-2952(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TOM70, SUBCELLULAR LOCATION.
  54. "Ribosomal protein S3 interacts with the NF-kappaB inhibitor IkappaBalpha."
    Stanborough T., Niederhauser J., Koch B., Bergler H., Pertschy B.
    FEBS Lett. 588:659-664(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NFKBIA.
  55. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221 AND THR-242, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  56. "AUF1 contributes to Cryptochrome1 mRNA degradation and rhythmic translation."
    Lee K.H., Kim S.H., Kim H.J., Kim W., Lee H.R., Jung Y., Choi J.H., Hong K.Y., Jang S.K., Kim K.T.
    Nucleic Acids Res. 42:3590-3606(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HNRPD.
  57. "Solution structure of the KH domain of human ribosomal protein S3."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 17-95.
  58. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.

Entry informationi

Entry nameiRS3_HUMAN
AccessioniPrimary (citable) accession number: P23396
Secondary accession number(s): B2R7N5
, J3KN86, Q498B5, Q8NI95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: October 1, 1993
Last modified: June 24, 2015
This is version 176 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Ribosomal proteins
    Ribosomal proteins families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.