G1TNM3 · RS3_RABIT
- ProteinSmall ribosomal subunit protein uS3
- GeneRPS3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids243 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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).
Catalytic activity
- 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H+
Activity regulation
Endonuclease activity is inhibited by MgCl2 on apurinic/apyrimidinic DNA but not on UV-irradiated DNA.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosolic ribosome | |
Cellular Component | cytosolic small ribosomal subunit | |
Cellular Component | mitochondrial inner membrane | |
Cellular Component | nucleolus | |
Cellular Component | spindle | |
Cellular Component | synapse | |
Molecular Function | class I DNA-(apurinic or apyrimidinic site) endonuclease activity | |
Molecular Function | DNA binding | |
Molecular Function | RNA binding | |
Molecular Function | structural constituent of ribosome | |
Biological Process | apoptotic process | |
Biological Process | cell division | |
Biological Process | DNA repair | |
Biological Process | positive regulation of apoptotic signaling pathway | |
Biological Process | positive regulation of protein-containing complex assembly | |
Biological Process | regulation of translation | |
Biological Process | translation |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameSmall ribosomal subunit protein uS3
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Lagomorpha > Leporidae > Oryctolagus
Accessions
- Primary accessionG1TNM3
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
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).
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
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000460052 | 2-243 | Small ribosomal subunit protein uS3 | |||
Sequence: AVQISKKRKFVADGIFKAELNEFLTRELAEDGYSGVEVRVTPTRTEIIILATRTQNVLGEKGRRIRELTAVVQKRFGFPEGSVELYAEKVATRGLCAIAQAESLRYKLLGGLAVRRACYGVLRFIMESGAKGCEVVVSGKLRGQRAKSMKFVDGLMIHSGDPVNYYVDTAVRHVLLRQGVLGIKVKIMLPWDPSGKIGPKKPLPDHVSIVEPKDEILPTTPISEQKGGKPEPPAMPQPVPTA | ||||||
Modified residue | 6 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 35 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 42 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 62 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 64 | Asymmetric dimethylarginine | ||||
Sequence: R | ||||||
Modified residue | 65 | Asymmetric dimethylarginine | ||||
Sequence: R | ||||||
Modified residue | 67 | Asymmetric dimethylarginine | ||||
Sequence: R | ||||||
Modified residue | 70 | Phosphothreonine | ||||
Sequence: T | ||||||
Cross-link | 90 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Modified residue | 104 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 132 | N6-succinyllysine | ||||
Sequence: K | ||||||
Cross-link | 202 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Modified residue | 209 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 214 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | ||||||
Cross-link | 214 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate | ||||
Sequence: K | ||||||
Modified residue | 220 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 221 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 224 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 230 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 242 | Phosphothreonine | ||||
Sequence: T |
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
- PTM
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).
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
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 21-92 | KH type-2 | ||||
Sequence: LNEFLTRELAEDGYSGVEVRVTPTRTEIIILATRTQNVLGEKGRRIRELTAVVQKRFGFPEGSVELYAEKVA | ||||||
Region | 200-243 | Disordered | ||||
Sequence: PKKPLPDHVSIVEPKDEILPTTPISEQKGGKPEPPAMPQPVPTA |
Sequence similarities
Belongs to the universal ribosomal protein uS3 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length243
- Mass (Da)26,674
- Last updated2024-03-27 v3
- Checksum6B9BB34FDEE04AAF
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AAGW02008228 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AAGW02008229 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |