RPS3
entrez
6188
canonical
uniprot
P23396
canonical
ensembl
ENSG00000149273
resolver
ensp
ENSP00000278572
resolver
ensp
ENSP00000416745
resolver
ensp
ENSP00000434643
resolver
ensp
ENSP00000436971
resolver
genesymbol
RPS3
resolver
hgnc
HGNC:10420
resolver
uniprot
B2R7N5
resolver
uniprot
J3KN86
resolver
uniprot
Q498B5
resolver
uniprot
Q8NI95
resolver
uniprot_entry
RS3_HUMAN
resolver
uniprot_sec
B2R7N5
resolver
uniprot_sec
J3KN86
resolver
uniprot_sec
Q498B5
resolver
uniprot_sec
Q8NI95
resolver
activity_regulation
ACTIVITY REGULATION: Endonuclease activity is inhibited by MgCl2 on apurinic/apyrimidinic DNA but not on UV-irradiated DNA. {ECO:0000269|PubMed:15707971}.
uniprot
proteins
amino_acid_sequence
MAVQISKKRKFVADGIFKAELNEFLTRELAEDGYSGVEVRVTPTRTEIIILATRTQNVLGEKGRRIRELTAVVQKRFGFPEGSVELYAEKVATRGLCAIAQAESLRYKLLGGLAVRRACYGVLRFIMESGAKGCEVVVSGKLRGQRAKSMKFVDGLMIHSGDPVNYYVDTAVRHVLLRQGVLGIKVKIMLPWDPTGKIGPKKPLPDHVSIVEPKDEILPTTPISEQKGGKPEPPAMPQPVPTA
uniprot
proteins
ec_number
4.2.99.18
uniprot
proteins
function
FUNCTION: Component of the small ribosomal subunit (PubMed:23636399, PubMed:8706699). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399, 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). {ECO:0000269|PubMed:14706345, ECO:0000269|PubMed:14988002, ECO:0000269|PubMed:15518571, ECO:0000269|PubMed:15707971, ECO:0000269|PubMed:17049931, ECO:0000269|PubMed:18045535, ECO:0000269|PubMed:18610840, ECO:0000269|PubMed:18973764, ECO:0000269|PubMed:19656744, ECO:0000269|PubMed:20217897, ECO:0000269|PubMed:20605787, ECO:0000269|PubMed:22510408, ECO:0000269|PubMed:23131551, ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:23911537, ECO:0000269|PubMed:7775413, ECO:0000269|PubMed:8706699}.
uniprot
proteins
mass_dalton
26688
uniprot
proteins
mutagenesis
MUTAGEN 6; /note="S->A: No effect on phosphorylation by CDK1. Greatly reduced phosphorylation by PRKCD. Abolishes phosphorylation by PRKCD; when associated with A-221."; /evidence="ECO:0000269|PubMed:19059439, ECO:0000269|PubMed:21871177"; MUTAGEN 18; /note="K->R: No effect on sumoylation. Abolishes sumoylation; when associated with R-214 and R-230."; /evidence="ECO:0000269|PubMed:21968017"; MUTAGEN 35; /note="S->A: No effect on phosphorylation by PRKCD."; /evidence="ECO:0000269|PubMed:19059439"; MUTAGEN 42; /note="T->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."; /evidence="ECO:0000269|PubMed:15950189, ECO:0000269|PubMed:17560175, ECO:0000269|PubMed:19059439, ECO:0000269|PubMed:21871177"; MUTAGEN 42; /note="T->D: Phosphomimetic mutant which is detected exclusively in the nucleus."; /evidence="ECO:0000269|PubMed:17560175"; MUTAGEN 70; /note="T->A: No effect on phosphorylation by PRKCD. Abolishes phosphorylation by PKB."; /evidence="ECO:0000269|PubMed:19059439, ECO:0000269|PubMed:20605787"; MUTAGEN 70; /note="T->D,E,R: Abolishes phosphorylation by PKB."; /evidence="ECO:0000269|PubMed:20605787"; MUTAGEN 132; /note="K->A: Does not affect ability to cleave DNA but abolishes binding to 8-oxoG."; /evidence="ECO:0000269|PubMed:16737853"; MUTAGEN 139; /note="S->A: No effect on phosphorylation by PRKCD."; /evidence="ECO:0000269|PubMed:19059439"; MUTAGEN 149; /note="S->A: No effect on phosphorylation by PRKCD."; /evidence="ECO:0000269|PubMed:19059439"; MUTAGEN 195; /note="T->A: No effect on phosphorylation by PRKCD."; /evidence="ECO:0000269|PubMed:19059439"; MUTAGEN 209; /note="S->A: Reduced phosphorylation by IKKB."; /evidence="ECO:0000269|PubMed:21399639"; MUTAGEN 214; /note="K->R: No effect on sumoylation. Abolishes sumoylation; when associated with R-18 and R-230. Abolished ubiquitination by RNF10 in response to ribosome stalling and deubiquitination by USP10."; /evidence="ECO:0000269|PubMed:21968017, ECO:0000269|PubMed:31981475, ECO:0000269|PubMed:34348161, ECO:0000269|PubMed:39609413, ECO:0000269|PubMed:39947182"; MUTAGEN 221; /note="T->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."; /evidence="ECO:0000269|PubMed:15950189, ECO:0000269|PubMed:19059439, ECO:0000269|PubMed:21871177"; MUTAGEN 227; /note="K->R: Does not affect ubiquitination in response to ribosome stalling."; /evidence="ECO:0000269|PubMed:31981475, ECO:0000269|PubMed:34348161"; MUTAGEN 230; /note="K->R: No effect on sumoylation. Abolishes sumoylation; when associated with R-18 and R-214. Does not affect ubiquitination in response to ribosome stalling."; /evidence="ECO:0000269|PubMed:21968017, ECO:0000269|PubMed:31981475, ECO:0000269|PubMed:34348161
uniprot
proteins
post_translational_modification
PTM: Methylation by PRMT1 is required for import into the nucleolus and for ribosome assembly. {ECO:0000269|PubMed:19460357}.; 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:0000269|PubMed:21968017}.; PTM: 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). {ECO:0000269|PubMed:17560175, ECO:0000269|PubMed:19059439, ECO:0000269|PubMed:20605787, ECO:0000269|PubMed:21399639, ECO:0000269|PubMed:21871177}.; PTM: Ubiquitinated; ubiquitination is prevented by interaction with HSP90 which stabilizes the protein (PubMed:16314389). 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 (PubMed:28065601, PubMed:28132843, PubMed:32011234, PubMed:34348161, PubMed:34469731, PubMed:39609413, PubMed:39947182, PubMed:39947183). Monoubiquitination at Lys-214 promotes interaction with RIOK3 (PubMed:39947182, PubMed:39947183). Deubiquitinated at Lys-214 by USP10, preventing degradation by the proteasome and promoting 40S ribosome subunit recycling following ribosome dissociation (PubMed:31981475, PubMed:34469731). {ECO:0000269|PubMed:16314389, ECO:0000269|PubMed:28065601, ECO:0000269|PubMed:28132843, ECO:0000269|PubMed:31981475, ECO:0000269|PubMed:32011234, ECO:0000269|PubMed:34348161, ECO:0000269|PubMed:34469731, ECO:0000269|PubMed:39609413, ECO:0000269|PubMed:39947182, ECO:0000269|PubMed:39947183}.; PTM: Ufmylated by UFL1. {ECO:0000250|UniProtKB:P62908}.
uniprot
proteins
protein_family
Universal ribosomal protein uS3 family
uniprot
proteins
pubmed
11875025
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14706345
uniprot
proteins
pubmed
14988002
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15518571
uniprot
proteins
pubmed
15707971
uniprot
proteins
pubmed
15950189
uniprot
proteins
pubmed
16314389
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
16737853
uniprot
proteins
pubmed
16807684
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17049931
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
1712897
uniprot
proteins
pubmed
17289661
uniprot
proteins
pubmed
17560175
uniprot
proteins
pubmed
18045535
uniprot
proteins
pubmed
18610840
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
18973764
uniprot
proteins
pubmed
19059439
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19460357
uniprot
proteins
pubmed
19541769
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19656744
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20041225
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20217897
uniprot
proteins
pubmed
20605787
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
2129557
uniprot
proteins
pubmed
21399639
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21871177
uniprot
proteins
pubmed
21968017
uniprot
proteins
pubmed
22510408
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23131551
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23636399
uniprot
proteins
pubmed
23911537
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24423872
uniprot
proteins
pubmed
24457201
uniprot
proteins
pubmed
24524803
uniprot
proteins
pubmed
25114211
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
28065601
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28132843
uniprot
proteins
pubmed
28757607
uniprot
proteins
pubmed
31981475
uniprot
proteins
pubmed
32011234
uniprot
proteins
pubmed
34348161
uniprot
proteins
pubmed
34469731
uniprot
proteins
pubmed
39609413
uniprot
proteins
pubmed
39947182
uniprot
proteins
pubmed
39947183
uniprot
proteins
pubmed
7775413
uniprot
proteins
pubmed
8319909
uniprot
proteins
pubmed
8706699
uniprot
proteins
sequence_length
243
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16314389, ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:17560175, ECO:0000269|PubMed:18045535, ECO:0000269|PubMed:20217897, ECO:0000269|PubMed:21871177, ECO:0000269|PubMed:23636399}. Nucleus {ECO:0000269|PubMed:17560175, ECO:0000269|PubMed:18045535, ECO:0000269|PubMed:19460357, ECO:0000269|PubMed:20217897, ECO:0000269|PubMed:21871177}. Nucleus, nucleolus {ECO:0000269|PubMed:16314389, ECO:0000269|PubMed:19460357}. Mitochondrion inner membrane {ECO:0000269|PubMed:23911537}; Peripheral membrane protein {ECO:0000269|PubMed:23911537}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:23131551}. 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 (PubMed:17560175). Accumulates in the mitochondrion in response to increased ROS levels (PubMed:23911537). Localizes to the spindle during mitosis (PubMed:23131551). Localized in cytoplasmic mRNP granules containing untranslated mRNAs (PubMed:17289661). {ECO:0000250|UniProtKB:P62908, ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:17560175, ECO:0000269|PubMed:23131551, ECO:0000269|PubMed:23911537}.
uniprot
proteins