Rps3
entrez
27050
canonical
uniprot
P62908
canonical
ensembl
ENSMUSG00000030744
resolver
ensp
ENSMUSP00000032998
resolver
enst
ENSMUST00000032998
resolver
genesymbol
Rps3
resolver
uniprot
P17073
resolver
uniprot
P47933
resolver
uniprot
Q5YLW3
resolver
uniprot_entry
Q5YLW3_MOUSE
resolver
uniprot_entry
RS3_MOUSE
resolver
uniprot_sec
P17073
resolver
uniprot_sec
P47933
resolver
amino_acid_sequence
MAVQISKKRKFVADGIFKAELNEFLTRELAEDGYSGVEVRVTPTRTEIIILATRTQNVLGEKGRRIRELTAVVQKRFGFPEGSVELYAEKVATRGLCAIAQAESLRYKLLGGLAVRRACYGVLRFIMESGAKGCEVVVSGKLRGQRAKSMKFVDGLMIHSGDPVNYYVDTAVRHVLLRQGVLGIKVKIMLPWDPSGKIGPKKPLPDHVSIVEPKDEILPTTPISEQKGGKPEPPAMPQPVPTA
uniprot
proteins
ec_number
4.2.99.18
uniprot
proteins
function
FUNCTION: Component of the small ribosomal subunit (PubMed:36517592). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:36517592). 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 (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 (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 (By similarity). Interacts with TRADD following exposure to UV radiation and induces apoptosis by caspase-dependent JNK activation (By similarity). {ECO:0000250|UniProtKB:P23396, ECO:0000269|PubMed:14988002, ECO:0000269|PubMed:36517592, ECO:0000269|PubMed:7775413}.
uniprot
proteins
mass_dalton
26674
uniprot
proteins
post_translational_modification
PTM: Methylation by PRMT1 is required for import into the nucleolus and for ribosome assembly. {ECO:0000250|UniProtKB:P23396}.; PTM: 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. {ECO:0000250|UniProtKB:P23396}.; PTM: 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. {ECO:0000250|UniProtKB:P23396}.; PTM: 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. Monoubiquitination at Lys-214 promotes interaction with RIOK3. Deubiquitinated at Lys-214 by USP10, preventing degradation by the proteasome and promoting 40S ribosome subunit recycling following ribosome dissociation. {ECO:0000250|UniProtKB:P23396}.; PTM: Ufmylated by UFL1. {ECO:0000269|PubMed:28575669}.
uniprot
proteins
protein_family
Universal ribosomal protein uS3 family
uniprot
proteins
pubmed
14988002
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
19129230
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
28575669
uniprot
proteins
pubmed
36517592
uniprot
proteins
pubmed
7775413
uniprot
proteins
sequence_length
243
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14988002, ECO:0000269|PubMed:36517592}. Nucleus {ECO:0000269|PubMed:14988002}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P23396}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P23396}; Peripheral membrane protein {ECO:0000250|UniProtKB:P23396}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P23396}. Note=In normal cells, located mainly in the cytoplasm with small amounts in the nucleus but translocates to the nucleus in cells undergoing apoptosis. Nuclear translocation is also induced by DNA damaging agents such as hydrogen peroxide (By similarity). Accumulates in the mitochondrion in response to increased ROS levels (By similarity). Localizes to the spindle during mitosis (By similarity). Localized in cytoplasmic mRNP granules containing untranslated mRNAs (By similarity). {ECO:0000250|UniProtKB:P23396, ECO:0000269|PubMed:14988002}.
uniprot
proteins