G1TNM3 · RS3_RABIT

Function

function

Component of the small ribosomal subunit (PubMed:23873042, PubMed:25601755, PubMed:26245381, PubMed:27863242).
The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23873042, PubMed:25601755, PubMed:26245381, PubMed:27863242).
Has endonuclease activity and plays a role in repair of damaged DNA (By similarity).
Cleaves phosphodiester bonds of DNAs containing altered bases with broad specificity and cleaves supercoiled DNA more efficiently than relaxed DNA (By similarity).
Displays high binding affinity for 7,8-dihydro-8-oxoguanine (8-oxoG), a common DNA lesion caused by reactive oxygen species (ROS) (By similarity).
Has also been shown to bind with similar affinity to intact and damaged DNA (By similarity).
Stimulates the N-glycosylase activity of the base excision protein OGG1 (By similarity).
Enhances the uracil excision activity of UNG1 (By similarity).
Also stimulates the cleavage of the phosphodiester backbone by APEX1 (By similarity).
When located in the mitochondrion, reduces cellular ROS levels and mitochondrial DNA damage (By similarity).
Has also been shown to negatively regulate DNA repair in cells exposed to hydrogen peroxide (By similarity).
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 (By similarity).
Represses its own translation by binding to its cognate mRNA (By similarity).
Binds to and protects TP53/p53 from MDM2-mediated ubiquitination (By similarity).
Involved in spindle formation and chromosome movement during mitosis by regulating microtubule polymerization (By similarity).
Involved in induction of apoptosis through its role in activation of CASP8 (By similarity).
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 (By similarity).
Interacts with TRADD following exposure to UV radiation and induces apoptosis by caspase-dependent JNK activation (By similarity).

Activity regulation

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

GO annotations

AspectTerm
Cellular Componentcytosolic ribosome
Cellular Componentcytosolic small ribosomal subunit
Cellular Componentmitochondrial inner membrane
Cellular Componentnucleolus
Cellular Componentspindle
Cellular Componentsynapse
Molecular Functionclass I DNA-(apurinic or apyrimidinic site) endonuclease activity
Molecular FunctionDNA binding
Molecular FunctionRNA binding
Molecular Functionstructural constituent of ribosome
Biological Processapoptotic process
Biological Processcell division
Biological ProcessDNA repair
Biological Processpositive regulation of apoptotic signaling pathway
Biological Processpositive regulation of protein-containing complex assembly
Biological Processregulation of translation
Biological Processtranslation

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Small ribosomal subunit protein uS3
  • Alternative names
    • 40S ribosomal protein S3 (EC:4.2.99.18
      ) . EC:4.2.99.18 (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      RPS3

Organism names

  • Taxonomic identifier
  • Strain
    • Thorbecke
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Lagomorpha > Leporidae > Oryctolagus

Accessions

  • Primary accession
    G1TNM3

Proteomes

Subcellular Location

Cytoplasm
Nucleus
Nucleus, nucleolus
Mitochondrion inner membrane
; Peripheral membrane protein
Note: In normal cells, located mainly in the cytoplasm with small amounts in the nucleus but translocates to the nucleus in cells undergoing apoptosis (By similarity).
Nuclear translocation is induced by DNA damaging agents such as hydrogen peroxide. Accumulates in the mitochondrion in response to increased ROS levels. Localizes to the spindle during mitosis. Localized in cytoplasmic mRNP granules containing untranslated mRNAs (By similarity).

Keywords

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain, cross-link.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylalanine
ChainPRO_00004600522-243Small ribosomal subunit protein uS3
Modified residue6Phosphoserine
Modified residue35Phosphoserine
Modified residue42Phosphothreonine
Modified residue62N6-acetyllysine
Modified residue64Asymmetric dimethylarginine
Modified residue65Asymmetric dimethylarginine
Modified residue67Asymmetric dimethylarginine
Modified residue70Phosphothreonine
Cross-link90Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residue104Phosphoserine
Modified residue132N6-succinyllysine
Cross-link202Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residue209Phosphoserine
Cross-link214Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Cross-link214Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
Modified residue220Phosphothreonine
Modified residue221Phosphothreonine
Modified residue224Phosphoserine
Cross-link230Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue242Phosphothreonine

Post-translational modification

Methylation by PRMT1 is required for import into the nucleolus and for ribosome assembly.
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.
Phosphorylation at Thr-221 by CDK1 occurs mainly in G2/M phase. Phosphorylation by PRKCD occurs on a non-ribosomal-associated form which results in translocation of RPS3 to the nucleus and enhances its endonuclease activity. 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. Phosphorylation by MAPK is required for translocation to the nucleus following exposure of cells to DNA damaging agents such as hydrogen peroxide. Phosphorylation by PKB/AKT mediates RPS3 nuclear translocation, enhances RPS3 endonuclease activity and suppresses RPS3-induced neuronal apoptosis.
Ubiquitinated; ubiquitination is prevented by interaction with HSP90 which stabilizes the protein. Monoubiquitinated at Lys-214 by RNF10 and ZNF598 when a ribosome has stalled during translation of poly(A) sequences, leading to preclude synthesis of a long poly-lysine tail and initiate the ribosome quality control (RQC) pathway to degrade the potentially detrimental aberrant nascent polypeptide. Deubiquitinated at Lys-214 by USP10, preventing degradation by the proteasome and promoting 40S ribosome subunit recycling following ribosome dissociation.
Ufmylated by UFL1.

Keywords

Proteomic databases

Expression

Gene expression databases

Interaction

Subunit

Component of the 40S small ribosomal subunit (PubMed:23873042, PubMed:25601755, PubMed:26245381, PubMed:27863242, PubMed:29856316, PubMed:30293783, PubMed:31246176, PubMed:31609474, PubMed:31768042, PubMed:32286223, PubMed:33296660, PubMed:35679869, PubMed:35709277, PubMed:35822879, PubMed:36653451).
Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (By similarity).
Interacts with HNRPD (By similarity).
Interacts with PRMT1; the interaction methylates RPS3 (By similarity).
Interacts with SUMO1; the interaction sumoylates RPS3 (By similarity).
Interacts with UBC9 (By similarity).
Interacts with CDK1; the interaction phosphorylates RPS3 (By similarity).
Interacts with PRKCD; the interaction phosphorylates RPS3 (By similarity).
Interacts with PKB/AKT; the interaction phosphorylates RPS3 (By similarity).
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 (By similarity).
Interacts with the base excision repair proteins APEX1 and OGG1; interaction with OGG1 increases OGG1 N-glycosylase activity (By similarity).
Interacts with UNG; the interaction increases the uracil excision activity of UNG1 (By similarity).
Interacts with HSP90; the interaction prevents the ubiquitination and proteasome-dependent degradation of RPS3 and is suppressed by increased ROS levels (By similarity).
Interacts with TOM70; the interaction promotes translocation of RPS3 to the mitochondrion (By similarity).
Interacts (via N-terminus) with RELA (via N-terminus); the interaction enhances the DNA-binding activity of the NF-kappa-B p65-p50 complex (By similarity).
Interacts with NFKBIA; the interaction is direct and may bridge the interaction between RPS3 and RELA (By similarity).
Interacts with IKKB; the interaction phosphorylates RPS3 and enhances its translocation to the nucleus (By similarity).
Interacts (via KH domain) with MDM2 and TP53 (By similarity).
Interacts with TRADD (By similarity).
Interacts with ASCC3. Identified in a HCV IRES-mediated translation complex, at least composed of EIF3C, IGF2BP1, RPS3 and HCV RNA-replicon. Interacts with CRY1 (By similarity).

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain21-92KH type-2
Region200-243Disordered

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    243
  • Mass (Da)
    26,674
  • Last updated
    2024-03-27 v3
  • Checksum
    6B9BB34FDEE04AAF
MAVQISKKRKFVADGIFKAELNEFLTRELAEDGYSGVEVRVTPTRTEIIILATRTQNVLGEKGRRIRELTAVVQKRFGFPEGSVELYAEKVATRGLCAIAQAESLRYKLLGGLAVRRACYGVLRFIMESGAKGCEVVVSGKLRGQRAKSMKFVDGLMIHSGDPVNYYVDTAVRHVLLRQGVLGIKVKIMLPWDPSGKIGPKKPLPDHVSIVEPKDEILPTTPISEQKGGKPEPPAMPQPVPTA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AAGW02008228
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AAGW02008229
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

Disclaimer

Any 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. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp