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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
  • DNA binding Source: UniProtKB
  • endodeoxyribonuclease activity Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • Hsp70 protein binding Source: UniProtKB
  • Hsp90 protein binding Source: UniProtKB
  • iron-sulfur cluster binding Source: UniProtKB
  • kinase binding Source: UniProtKB
  • microtubule binding Source: UniProtKB
  • mRNA binding Source: UniProtKB
  • oxidized purine DNA binding Source: UniProtKB
  • oxidized pyrimidine DNA binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • protein kinase A binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • small ribosomal subunit rRNA binding Source: UniProtKB
  • structural constituent of ribosome Source: UniProtKB
  • SUMO binding Source: UniProtKB
  • supercoiled DNA binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB
  • tubulin binding Source: UniProtKB
  • ubiquitin-like protein conjugating enzyme binding Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • cellular response to DNA damage stimulus Source: UniProtKB
  • cellular response to hydrogen peroxide Source: UniProtKB
  • chromosome segregation Source: UniProtKB
  • DNA damage response, detection of DNA damage Source: UniProtKB
  • DNA repair Source: UniProtKB-KW
  • mitotic nuclear division Source: UniProtKB-KW
  • negative regulation of DNA repair Source: UniProtKB
  • negative regulation of protein ubiquitination Source: UniProtKB
  • negative regulation of translation Source: UniProtKB
  • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  • positive regulation of apoptotic signaling pathway Source: UniProtKB
  • positive regulation of base-excision repair Source: UniProtKB
  • positive regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis Source: UniProtKB
  • positive regulation of DNA N-glycosylase activity Source: UniProtKB
  • positive regulation of DNA repair Source: UniProtKB
  • positive regulation of endodeoxyribonuclease activity Source: UniProtKB
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage Source: UniProtKB
  • positive regulation of JUN kinase activity Source: UniProtKB
  • positive regulation of microtubule polymerization Source: UniProtKB
  • positive regulation of NIK/NF-kappaB signaling Source: UniProtKB
  • regulation of apoptotic process Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • response to oxidative stress Source: UniProtKB
  • response to TNF agonist Source: UniProtKB
  • rRNA processing Source: Reactome
  • spindle assembly Source: UniProtKB
  • SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  • transcription, DNA-templated Source: UniProtKB-KW
  • translation Source: UniProtKB
  • translational initiation Source: UniProtKB
  • 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

BioCyciZFISH:ENSG00000149273-MONOMER.
ReactomeiR-HSA-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-HSA-156902. Peptide chain elongation.
R-HSA-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-HSA-192823. Viral mRNA Translation.
R-HSA-2408557. Selenocysteine synthesis.
R-HSA-6791226. Major pathway of rRNA processing in the nucleolus and cytosol.
R-HSA-72649. Translation initiation complex formation.
R-HSA-72689. Formation of a pool of free 40S subunits.
R-HSA-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-HSA-72702. Ribosomal scanning and start codon recognition.
R-HSA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-HSA-72764. Eukaryotic Translation Termination.
R-HSA-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-HSA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
SIGNORiP23396.

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
Proteomesi
  • UP000005640 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
  • extracellular matrix Source: BHF-UCL
  • focal adhesion Source: UniProtKB
  • intracellular ribonucleoprotein complex Source: UniProtKB
  • membrane Source: UniProtKB
  • mitochondrial inner membrane Source: UniProtKB
  • mitochondrial matrix Source: UniProtKB
  • mitotic spindle Source: UniProtKB
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • polysome Source: UniProtKB
  • ribosome Source: UniProtKB
  • ruffle membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi6S → A: No effect on phosphorylation by CDK1. Greatly reduced phosphorylation by PRKCD. Abolishes phosphorylation by PRKCD; when associated with A-221. 2 Publications1
Mutagenesisi18K → R: No effect on sumoylation. Abolishes sumoylation; when associated with R-214 and R-230. 1 Publication1
Mutagenesisi35S → A: No effect on phosphorylation by PRKCD. 1 Publication1
Mutagenesisi42T → 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 Publications1
Mutagenesisi42T → D: Phosphomimetic mutant which is detected exclusively in the nucleus. 1 Publication1
Mutagenesisi70T → A: No effect on phosphorylation by PRKCD. Abolishes phosphorylation by PKB. 2 Publications1
Mutagenesisi70T → D, E or R: Abolishes phosphorylation by PKB. 1 Publication1
Mutagenesisi132K → A: Does not affect ability to cleave DNA but abolishes binding to 8-oxoG. 1 Publication1
Mutagenesisi139S → A: No effect on phosphorylation by PRKCD. 1 Publication1
Mutagenesisi149S → A: No effect on phosphorylation by PRKCD. 1 Publication1
Mutagenesisi195T → A: No effect on phosphorylation by PRKCD. 1 Publication1
Mutagenesisi209S → A: Reduced phosphorylation by IKKB. 1 Publication1
Mutagenesisi214K → R: No effect on sumoylation. Abolishes sumoylation; when associated with R-18 and R-230. 1 Publication1
Mutagenesisi221T → 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 Publications1
Mutagenesisi230K → R: No effect on sumoylation. Abolishes sumoylation; when associated with R-18 and R-214. 1 Publication1

Organism-specific databases

DisGeNETi6188.
OpenTargetsiENSG00000149273.
PharmGKBiPA34829.

Polymorphism and mutation databases

BioMutaiRPS3.
DMDMi417719.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00001303202 – 24340S ribosomal protein S3Add BLAST242

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei6Phosphoserine; by PKC/PRKCD1 Publication1
Modified residuei35PhosphoserineCombined sources1
Modified residuei42Phosphothreonine; by MAPK1 Publication1
Modified residuei62N6-acetyllysineCombined sources1
Modified residuei64Asymmetric dimethylarginine; by PRMT11 Publication1
Modified residuei65Asymmetric dimethylarginine; by PRMT11 Publication1
Modified residuei67Asymmetric dimethylarginine; by PRMT11 Publication1
Modified residuei70Phosphothreonine; by PKB1 Publication1
Cross-linki90Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residuei104PhosphoserineCombined sources1
Modified residuei132N6-succinyllysineBy similarity1
Cross-linki202Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residuei209Phosphoserine; by IKKB1 Publication1
Modified residuei220PhosphothreonineCombined sources1
Modified residuei221Phosphothreonine; by CDK1 and PKC/PRKCDCombined sources3 Publications1
Modified residuei224PhosphoserineCombined sources1
Cross-linki230Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei242PhosphothreonineCombined sources1

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

EPDiP23396.
MaxQBiP23396.
PaxDbiP23396.
PeptideAtlasiP23396.
PRIDEiP23396.

PTM databases

iPTMnetiP23396.
PhosphoSitePlusiP23396.
SwissPalmiP23396.

Expressioni

Gene expression databases

BgeeiENSG00000149273.
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
NFKB1P198384EBI-351193,EBI-300010
NFKBIAP259636EBI-351193,EBI-307386
PPIDQ087524EBI-351193,EBI-716596
RELAQ042068EBI-351193,EBI-73886
TP53P046374EBI-351193,EBI-366083
YWHAZP631042EBI-351193,EBI-347088

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • Hsp70 protein binding Source: UniProtKB
  • Hsp90 protein binding Source: UniProtKB
  • kinase binding Source: UniProtKB
  • microtubule binding Source: UniProtKB
  • protein kinase A binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • SUMO binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB
  • tubulin binding Source: UniProtKB
  • ubiquitin-like protein conjugating enzyme binding Source: UniProtKB

Protein-protein interaction databases

BioGridi112102. 257 interactors.
DIPiDIP-33177N.
IntActiP23396. 72 interactors.
MINTiMINT-4999144.
STRINGi9606.ENSP00000433821.

Structurei

Secondary structure

1243
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi17 – 28Combined sources12
Turni29 – 33Combined sources5
Beta strandi34 – 41Combined sources8
Beta strandi46 – 53Combined sources8
Helixi55 – 59Combined sources5
Helixi61 – 63Combined sources3
Helixi64 – 77Combined sources14
Beta strandi83 – 90Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WH9NMR-A17-95[»]
4UG0electron microscopy-SD1-243[»]
4V6Xelectron microscopy5.00AD1-243[»]
5A2Qelectron microscopy3.90D1-243[»]
5AJ0electron microscopy3.50BD1-243[»]
5FLXelectron microscopy3.90D1-243[»]
ProteinModelPortaliP23396.
SMRiP23396.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23396.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini21 – 92KH type-2PROSITE-ProRule annotationAdd BLAST72

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG3181. Eukaryota.
COG0092. LUCA.
GeneTreeiENSGT00390000008610.
HOGENOMiHOG000210611.
HOVERGENiHBG002195.
InParanoidiP23396.
KOiK02985.
OMAiQKFTEGY.
OrthoDBiEOG091G0I8D.
PhylomeDBiP23396.
TreeFamiTF300901.

Family and domain databases

Gene3Di3.30.1140.32. 1 hit.
3.30.300.20. 1 hit.
InterProiIPR015946. 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.
[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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti8K → R in AAB19349 (PubMed:1712897).Curated1
Sequence conflicti104S → C in CAA39248 (PubMed:2129557).Curated1
Sequence conflicti233P → L in CAA39248 (PubMed:2129557).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_04666785E → ELKIMVMVTGYPLLPLK in isoform 2. Curated1

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.5. 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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WH9NMR-A17-95[»]
4UG0electron microscopy-SD1-243[»]
4V6Xelectron microscopy5.00AD1-243[»]
5A2Qelectron microscopy3.90D1-243[»]
5AJ0electron microscopy3.50BD1-243[»]
5FLXelectron microscopy3.90D1-243[»]
ProteinModelPortaliP23396.
SMRiP23396.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112102. 257 interactors.
DIPiDIP-33177N.
IntActiP23396. 72 interactors.
MINTiMINT-4999144.
STRINGi9606.ENSP00000433821.

PTM databases

iPTMnetiP23396.
PhosphoSitePlusiP23396.
SwissPalmiP23396.

Polymorphism and mutation databases

BioMutaiRPS3.
DMDMi417719.

Proteomic databases

EPDiP23396.
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.5. human. [P23396-1]

Organism-specific databases

CTDi6188.
DisGeNETi6188.
GeneCardsiRPS3.
HGNCiHGNC:10420. RPS3.
HPAiHPA063339.
MIMi600454. gene.
neXtProtiNX_P23396.
OpenTargetsiENSG00000149273.
PharmGKBiPA34829.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3181. Eukaryota.
COG0092. LUCA.
GeneTreeiENSGT00390000008610.
HOGENOMiHOG000210611.
HOVERGENiHBG002195.
InParanoidiP23396.
KOiK02985.
OMAiQKFTEGY.
OrthoDBiEOG091G0I8D.
PhylomeDBiP23396.
TreeFamiTF300901.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000149273-MONOMER.
ReactomeiR-HSA-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-HSA-156902. Peptide chain elongation.
R-HSA-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-HSA-192823. Viral mRNA Translation.
R-HSA-2408557. Selenocysteine synthesis.
R-HSA-6791226. Major pathway of rRNA processing in the nucleolus and cytosol.
R-HSA-72649. Translation initiation complex formation.
R-HSA-72689. Formation of a pool of free 40S subunits.
R-HSA-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-HSA-72702. Ribosomal scanning and start codon recognition.
R-HSA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-HSA-72764. Eukaryotic Translation Termination.
R-HSA-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-HSA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
SIGNORiP23396.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000149273.
CleanExiHS_RPS3.
ExpressionAtlasiP23396. baseline and differential.
GenevisibleiP23396. HS.

Family and domain databases

Gene3Di3.30.1140.32. 1 hit.
3.30.300.20. 1 hit.
InterProiIPR015946. 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.
[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...

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: November 30, 2016
This is version 192 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

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 one 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.