UniProtKB - P23396 (RS3_HUMAN)
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- BLAST>sp|P23396|RS3_HUMAN 40S ribosomal protein S3 OS=Homo sapiens OX=9606 GN=RPS3 PE=1 SV=2 MAVQISKKRKFVADGIFKAELNEFLTRELAEDGYSGVEVRVTPTRTEIIILATRTQNVLG EKGRRIRELTAVVQKRFGFPEGSVELYAEKVATRGLCAIAQAESLRYKLLGGLAVRRACY GVLRFIMESGAKGCEVVVSGKLRGQRAKSMKFVDGLMIHSGDPVNYYVDTAVRHVLLRQG VLGIKVKIMLPWDPTGKIGPKKPLPDHVSIVEPKDEILPTTPISEQKGGKPEPPAMPQPV PTA
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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
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.13"Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry."
Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A.
Eur. J. Biochem. 239:144-149(1996) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 188-197. - Ref.14"Implication of mammalian ribosomal protein S3 in the processing of DNA damage."
Kim J., Chubatsu L.S., Admon A., Stahl J., Fellous R., Linn S.
J. Biol. Chem. 270:13620-13629(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY. - Ref.15"Human ribosomal protein S3 interacts with DNA base excision repair proteins hAPE/Ref-1 and hOGG1."
Hegde V., Wang M., Deutsch W.A.
Biochemistry 43:14211-14217(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH APEX1 AND OGG1. - Ref.16"Characterization of human ribosomal protein S3 binding to 7,8-dihydro-8-oxoguanine and abasic sites by surface plasmon resonance."
Hegde V., Wang M., Deutsch W.A.
DNA Repair 3:121-126(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.17"RpS3, a DNA repair endonuclease and ribosomal protein, is involved in apoptosis."
Jang C.Y., Lee J.Y., Kim J.
FEBS Lett. 560:81-85(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.18"Characterization of a wide range base-damage-endonuclease activity of mammalian rpS3."
Kim S.H., Lee J.Y., Kim J.
Biochem. Biophys. Res. Commun. 328:962-967(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.25"Ribosomal protein S3: a KH domain subunit in NF-kappaB complexes that mediates selective gene regulation."
Wan F., Anderson D.E., Barnitz R.A., Snow A., Bidere N., Zheng L., Hegde V., Lam L.T., Staudt L.M., Levens D., Deutsch W.A., Lenardo M.J.
Cell 131:927-939(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH RELA, IDENTIFICATION IN THE NF-KAPPA-B P65-P50 COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.26"Knockdown of ribosomal protein S3 protects human cells from genotoxic stress."
Hegde V., Yadavilli S., Deutsch W.A.
DNA Repair 6:94-99(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.29"Interactions of human ribosomal protein S3 with undamaged and damaged DNA."
Balyeva K.E., Malygin A.A., Karpova G.G., Nevinskii G.A., Zharkov D.O.
Mol. Biol. (Mosk.) 42:314-322(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.31"Human ribosomal protein S3 (hRpS3) interacts with uracil-DNA glycosylase (hUNG) and stimulates its glycosylase activity."
Ko S.I., Park J.H., Park M.J., Kim J., Kang L.W., Han Y.S.
Mutat. Res. 648:54-64(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH UNG. - Ref.36"Ribosomal protein S3: A multi-functional protein that interacts with both p53 and MDM2 through its KH domain."
Yadavilli S., Mayo L.D., Higgins M., Lain S., Hegde V., Deutsch W.A.
DNA Repair 8:1215-1224(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH MDM2 AND TP53, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.42"Ribosomal protein S3, a new substrate of Akt, serves as a signal mediator between neuronal apoptosis and DNA repair."
Lee S.B., Kwon I.S., Park J., Lee K.H., Ahn Y., Lee C., Kim J., Choi S.Y., Cho S.W., Ahn J.Y.
J. Biol. Chem. 285:29457-29468(2010) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH E2F1 AND PKB, PHOSPHORYLATION AT THR-70, MUTAGENESIS OF THR-70. - Ref.50"Ribosomal protein S3 interacts with TRADD to induce apoptosis through caspase dependent JNK activation."
Jang C.Y., Kim H.D., Kim J.
Biochem. Biophys. Res. Commun. 421:474-478(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH TRADD. - Ref.51"Ribosomal protein S3 localizes on the mitotic spindle and functions as a microtubule associated protein in mitosis."
Jang C.Y., Kim H.D., Zhang X., Chang J.S., Kim J.
Biochem. Biophys. Res. Commun. 429:57-62(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.53"Cytoplasmic ribosomal protein S3 (rpS3) plays a pivotal role in mitochondrial DNA damage surveillance."
Kim Y., Kim H.D., Kim J.
Biochim. Biophys. Acta 1833:2943-2952(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH TOM70, SUBCELLULAR LOCATION.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.14"Implication of mammalian ribosomal protein S3 in the processing of DNA damage."
Kim J., Chubatsu L.S., Admon A., Stahl J., Fellous R., Linn S.
J. Biol. Chem. 270:13620-13629(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi
Endonuclease activity is inhibited by MgCl2 on apurinic/apyrimidinic DNA but not on UV-irradiated DNA.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.18"Characterization of a wide range base-damage-endonuclease activity of mammalian rpS3."
Kim S.H., Lee J.Y., Kim J.
Biochem. Biophys. Res. Commun. 328:962-967(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>pH dependencei
Optimum pH is between 8.0 and 9.0 with activity decreasing sharply below 8.0.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.18"Characterization of a wide range base-damage-endonuclease activity of mammalian rpS3."
Kim S.H., Lee J.Y., Kim J.
Biochem. Biophys. Res. Commun. 328:962-967(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- class I DNA-(apurinic or apyrimidinic site) endonuclease activity Source: UniProtKB-EC
- damaged DNA binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- DNA-(apurinic or apyrimidinic site) endonuclease activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- DNA binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- endodeoxyribonuclease activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- enzyme binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- Hsp70 protein binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- Hsp90 protein binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- iron-sulfur cluster binding Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- kinase binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- microtubule binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- mRNA binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- oxidized purine DNA binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- oxidized pyrimidine DNA binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- protein-containing complex binding Source: CAFA <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- protein kinase A binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- protein kinase binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- RNA binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- small ribosomal subunit rRNA binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- structural constituent of ribosome Source: UniProtKBInferred from high throughput direct assayi
- supercoiled DNA binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- transcription factor binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- tubulin binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- ubiquitin-like protein conjugating enzyme binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- apoptotic process Source: UniProtKB-KW
- cell division Source: UniProtKB-KW
- cellular response to DNA damage stimulus Source: UniProtKB <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patterni
- cellular response to hydrogen peroxide Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- cellular response to tumor necrosis factor Source: CAFA <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- chromosome segregation Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- cytoplasmic translation Source: GO_Central
- DNA damage response, detection of DNA damage Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- DNA repair Source: UniProtKB-KW
- negative regulation of DNA repair Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- negative regulation of protein ubiquitination Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- negative regulation of translation Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
- positive regulation of activated T cell proliferation Source: CAFA <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of apoptotic signaling pathway Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of base-excision repair Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of DNA N-glycosylase activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of DNA repair Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of endodeoxyribonuclease activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of gene expression Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of interleukin-2 production Source: CAFA <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of JUN kinase activity Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of microtubule polymerization Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of NF-kappaB transcription factor activity Source: CAFA <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of NIK/NF-kappaB signaling Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of protein complex assembly Source: CAFA <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of T cell receptor signaling pathway Source: CAFA <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- regulation of apoptotic process Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- response to oxidative stress Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- response to TNF agonist Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- spindle assembly Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- SRP-dependent cotranslational protein targeting to membrane Source: Reactome
- transcription, DNA-templated Source: UniProtKB-KW
- translation Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- translational initiation Source: Reactome
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | DNA-binding, Lyase, Ribonucleoprotein, Ribosomal protein, RNA-binding |
| Biological process | Apoptosis, Cell cycle, Cell division, DNA damage, DNA repair, Mitosis, Transcription, Transcription regulation, Translation regulation |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-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-9010553 Regulation of expression of SLITs and ROBOs 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) |
SIGNOR Signaling Network Open Resource More...SIGNORi | P23396 |
Protein family/group databases
MoonProt database of moonlighting proteins More...MoonProti | P23396 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: 40S ribosomal protein S3 (EC:4.2.99.181 Publication<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
Alternative name(s): Small ribosomal subunit protein uS31 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
|
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:RPS3 ORF Names:OK/SW-cl.26 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000149273.14 |
Human Gene Nomenclature Database More...HGNCi | HGNC:10420 RPS3 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 600454 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P23396 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Cytoskeleton
- spindle 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.51"Ribosomal protein S3 localizes on the mitotic spindle and functions as a microtubule associated protein in mitosis."
Jang C.Y., Kim H.D., Zhang X., Chang J.S., Kim J.
Biochem. Biophys. Res. Commun. 429:57-62(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION.
- spindle 1 Publication
Nucleus
- Nucleus 5 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.25"Ribosomal protein S3: a KH domain subunit in NF-kappaB complexes that mediates selective gene regulation."
Wan F., Anderson D.E., Barnitz R.A., Snow A., Bidere N., Zheng L., Hegde V., Lam L.T., Staudt L.M., Levens D., Deutsch W.A., Lenardo M.J.
Cell 131:927-939(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH RELA, IDENTIFICATION IN THE NF-KAPPA-B P65-P50 COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.27"Translocation of human ribosomal protein S3 to sites of DNA damage is dependant on ERK-mediated phosphorylation following genotoxic stress."
Yadavilli S., Hegde V., Deutsch W.A.
DNA Repair 6:1453-1462(2007) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, MUTAGENESIS OF THR-42. - Ref.34"Arginine methylation of ribosomal protein S3 affects ribosome assembly."
Shin H.S., Jang C.Y., Kim H.D., Kim T.S., Kim S., Kim J.
Biochem. Biophys. Res. Commun. 385:273-278(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PRMT1, SUBCELLULAR LOCATION, METHYLATION AT ARG-64; ARG-65 AND ARG-67. - Ref.47"Ribosomal protein S3 is phosphorylated by Cdk1/cdc2 during G2/M phase."
Yoon I.S., Chung J.H., Hahm S.H., Park M.J., Lee Y.R., Ko S.I., Kang L.W., Kim T.S., Kim J., Han Y.S.
BMB Rep. 44:529-534(2011) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CDK1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-221, MUTAGENESIS OF SER-6; THR-42 AND THR-221.
- nucleolus 2 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.22"Interaction of Hsp90 with ribosomal proteins protects from ubiquitination and proteasome-dependent degradation."
Kim T.S., Jang C.Y., Kim H.D., Lee J.Y., Ahn B.Y., Kim J.
Mol. Biol. Cell 17:824-833(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HSP90, SUBCELLULAR LOCATION, UBIQUITINATION. - Ref.34"Arginine methylation of ribosomal protein S3 affects ribosome assembly."
Shin H.S., Jang C.Y., Kim H.D., Kim T.S., Kim S., Kim J.
Biochem. Biophys. Res. Commun. 385:273-278(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PRMT1, SUBCELLULAR LOCATION, METHYLATION AT ARG-64; ARG-65 AND ARG-67.
- Nucleus 5 Publications
Mitochondrion
- Mitochondrion inner membrane 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.53"Cytoplasmic ribosomal protein S3 (rpS3) plays a pivotal role in mitochondrial DNA damage surveillance."
Kim Y., Kim H.D., Kim J.
Biochim. Biophys. Acta 1833:2943-2952(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH TOM70, SUBCELLULAR LOCATION.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.53"Cytoplasmic ribosomal protein S3 (rpS3) plays a pivotal role in mitochondrial DNA damage surveillance."
Kim Y., Kim H.D., Kim J.
Biochim. Biophys. Acta 1833:2943-2952(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH TOM70, SUBCELLULAR LOCATION.
- Mitochondrion inner membrane 1 Publication
Other locations
- Cytoplasm 6 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.22"Interaction of Hsp90 with ribosomal proteins protects from ubiquitination and proteasome-dependent degradation."
Kim T.S., Jang C.Y., Kim H.D., Lee J.Y., Ahn B.Y., Kim J.
Mol. Biol. Cell 17:824-833(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HSP90, SUBCELLULAR LOCATION, UBIQUITINATION. - Ref.25"Ribosomal protein S3: a KH domain subunit in NF-kappaB complexes that mediates selective gene regulation."
Wan F., Anderson D.E., Barnitz R.A., Snow A., Bidere N., Zheng L., Hegde V., Lam L.T., Staudt L.M., Levens D., Deutsch W.A., Lenardo M.J.
Cell 131:927-939(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH RELA, IDENTIFICATION IN THE NF-KAPPA-B P65-P50 COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.27"Translocation of human ribosomal protein S3 to sites of DNA damage is dependant on ERK-mediated phosphorylation following genotoxic stress."
Yadavilli S., Hegde V., Deutsch W.A.
DNA Repair 6:1453-1462(2007) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, MUTAGENESIS OF THR-42. - Ref.28"Molecular composition of IMP1 ribonucleoprotein granules."
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C.
Mol. Cell. Proteomics 6:798-811(2007) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION. - Ref.47"Ribosomal protein S3 is phosphorylated by Cdk1/cdc2 during G2/M phase."
Yoon I.S., Chung J.H., Hahm S.H., Park M.J., Lee Y.R., Ko S.I., Kang L.W., Kim T.S., Kim J., Han Y.S.
BMB Rep. 44:529-534(2011) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CDK1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-221, MUTAGENESIS OF SER-6; THR-42 AND THR-221.
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).By similarity- Cytoplasm 6 Publications
- Ref.27"Translocation of human ribosomal protein S3 to sites of DNA damage is dependant on ERK-mediated phosphorylation following genotoxic stress."
Yadavilli S., Hegde V., Deutsch W.A.
DNA Repair 6:1453-1462(2007) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, MUTAGENESIS OF THR-42. - Ref.28"Molecular composition of IMP1 ribonucleoprotein granules."
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C.
Mol. Cell. Proteomics 6:798-811(2007) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION. - Ref.51"Ribosomal protein S3 localizes on the mitotic spindle and functions as a microtubule associated protein in mitosis."
Jang C.Y., Kim H.D., Zhang X., Chang J.S., Kim J.
Biochem. Biophys. Res. Commun. 429:57-62(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.53"Cytoplasmic ribosomal protein S3 (rpS3) plays a pivotal role in mitochondrial DNA damage surveillance."
Kim Y., Kim H.D., Kim J.
Biochim. Biophys. Acta 1833:2943-2952(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH TOM70, SUBCELLULAR LOCATION.
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
4 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
Cytoskeleton
- mitotic spindle Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Cytosol
- cytosol Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- cytosolic small ribosomal subunit Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Endoplasmic reticulum
- endoplasmic reticulum Source: HPA
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
Mitochondrion
- mitochondrial inner membrane Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- mitochondrial matrix Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Nucleus
- nucleolus Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- nucleoplasm Source: Reactome
- nucleus Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Plasma Membrane
- plasma membrane Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- ruffle membrane Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Other locations
- cytoplasm Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- focal adhesion Source: UniProtKBInferred from high throughput direct assayi
- membrane Source: UniProtKBInferred from high throughput direct assayi
- NF-kappaB complex Source: CAFA <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- polysome Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- ribonucleoprotein complex Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- ribosome Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Cytoplasm, Cytoskeleton, Membrane, Mitochondrion, Mitochondrion inner membrane, Nucleus<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 6 | S → A: No effect on phosphorylation by CDK1. Greatly reduced phosphorylation by PRKCD. Abolishes phosphorylation by PRKCD; when associated with A-221. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 18 | K → R: No effect on sumoylation. Abolishes sumoylation; when associated with R-214 and R-230. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 35 | S → A: No effect on phosphorylation by PRKCD. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 42 | 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. 4 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 42 | T → D: Phosphomimetic mutant which is detected exclusively in the nucleus. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 70 | T → A: No effect on phosphorylation by PRKCD. Abolishes phosphorylation by PKB. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 70 | T → D, E or R: Abolishes phosphorylation by PKB. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 132 | K → A: Does not affect ability to cleave DNA but abolishes binding to 8-oxoG. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 139 | S → A: No effect on phosphorylation by PRKCD. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 149 | S → A: No effect on phosphorylation by PRKCD. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 195 | T → A: No effect on phosphorylation by PRKCD. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 209 | S → A: Reduced phosphorylation by IKKB. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 214 | K → R: No effect on sumoylation. Abolishes sumoylation; when associated with R-18 and R-230. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 221 | 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. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 230 | K → R: No effect on sumoylation. Abolishes sumoylation; when associated with R-18 and R-214. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Organism-specific databases
DisGeNET More...DisGeNETi | 6188 |
Open Targets More...OpenTargetsi | ENSG00000149273 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA34829 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | RPS3 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 417719 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | RemovedCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| |||
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000130320 | 2 – 243 | 40S ribosomal protein S3Add BLAST | 242 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 2 | N-acetylalanineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 6 | Phosphoserine; by PKC/PRKCD1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 35 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 42 | Phosphothreonine; by MAPK1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 62 | N6-acetyllysineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 64 | Asymmetric dimethylarginine; by PRMT11 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 65 | Asymmetric dimethylarginine; by PRMT11 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 67 | Asymmetric dimethylarginine; by PRMT11 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 70 | Phosphothreonine; by PKB1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 90 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 104 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 132 | N6-succinyllysineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 202 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 209 | Phosphoserine; by IKKB1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 214 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 214 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 220 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 221 | Phosphothreonine; by CDK1 and PKC/PRKCDCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 224 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 230 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 242 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
Methylation by PRMT1 is required for import into the nucleolus and for ribosome assembly.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.34"Arginine methylation of ribosomal protein S3 affects ribosome assembly."
Shin H.S., Jang C.Y., Kim H.D., Kim T.S., Kim S., Kim J.
Biochem. Biophys. Res. Commun. 385:273-278(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PRMT1, SUBCELLULAR LOCATION, METHYLATION AT ARG-64; ARG-65 AND ARG-67.
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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.46"Ribosomal protein S3 is stabilized by sumoylation."
Jang C.Y., Shin H.S., Kim H.D., Kim J.W., Choi S.Y., Kim J.
Biochem. Biophys. Res. Commun. 414:523-527(2011) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SUMO1 AND UBC9, SUMOYLATION AT LYS-18; LYS-214 AND LYS-230, MUTAGENESIS OF LYS-18; LYS-214 AND LYS-230.
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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.27"Translocation of human ribosomal protein S3 to sites of DNA damage is dependant on ERK-mediated phosphorylation following genotoxic stress."
Yadavilli S., Hegde V., Deutsch W.A.
DNA Repair 6:1453-1462(2007) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, MUTAGENESIS OF THR-42. - Ref.35"PKCdelta-dependent functional switch of rpS3 between translation and DNA repair."
Kim T.S., Kim H.D., Kim J.
Biochim. Biophys. Acta 1793:395-405(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PRKCD, PHOSPHORYLATION AT SER-6 AND THR-221, MUTAGENESIS OF SER-6; SER-35; THR-42; THR-70; SER-139; SER-149; THR-195 AND THR-221. - Ref.42"Ribosomal protein S3, a new substrate of Akt, serves as a signal mediator between neuronal apoptosis and DNA repair."
Lee S.B., Kwon I.S., Park J., Lee K.H., Ahn Y., Lee C., Kim J., Choi S.Y., Cho S.W., Ahn J.Y.
J. Biol. Chem. 285:29457-29468(2010) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH E2F1 AND PKB, PHOSPHORYLATION AT THR-70, MUTAGENESIS OF THR-70. - Ref.47"Ribosomal protein S3 is phosphorylated by Cdk1/cdc2 during G2/M phase."
Yoon I.S., Chung J.H., Hahm S.H., Park M.J., Lee Y.R., Ko S.I., Kang L.W., Kim T.S., Kim J., Han Y.S.
BMB Rep. 44:529-534(2011) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CDK1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-221, MUTAGENESIS OF SER-6; THR-42 AND THR-221. - Ref.48"IKKbeta phosphorylation regulates RPS3 nuclear translocation and NF-kappaB function during infection with Escherichia coli strain O157:H7."
Wan F., Weaver A., Gao X., Bern M., Hardwidge P.R., Lenardo M.J.
Nat. Immunol. 12:335-343(2011) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH IKKB AND E.COLI NLEH1, PHOSPHORYLATION AT SER-209, MUTAGENESIS OF SER-209.
Ubiquitinated (PubMed:16314389). This is prevented by interaction with HSP90 which stabilizes the protein (PubMed:16314389). Monoubiquitinated at Lys-214 by 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).3 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.22"Interaction of Hsp90 with ribosomal proteins protects from ubiquitination and proteasome-dependent degradation."
Kim T.S., Jang C.Y., Kim H.D., Lee J.Y., Ahn B.Y., Kim J.
Mol. Biol. Cell 17:824-833(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HSP90, SUBCELLULAR LOCATION, UBIQUITINATION. - Ref.61"Initiation of quality control during poly(A) translation requires site-specific ribosome ubiquitination."
Juszkiewicz S., Hegde R.S.
Mol. Cell 0:0-0(2016) [PubMed] [Europe PMC] [Abstract]Cited for: UBIQUITINATION AT LYS-214. - Ref.62"ZNF598 and RACK1 regulate mammalian ribosome-associated quality control function by mediating regulatory 40S ribosomal ubiquitylation."
Sundaramoorthy E., Leonard M., Mak R., Liao J., Fulzele A., Bennett E.J.
Mol. Cell 0:0-0(2017) [PubMed] [Europe PMC] [Abstract]Cited for: UBIQUITINATION AT LYS-214.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P23396 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P23396 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P23396 |
PeptideAtlas More...PeptideAtlasi | P23396 |
PRoteomics IDEntifications database More...PRIDEi | P23396 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 54087 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P23396 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P23396 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P23396 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000149273 |
CleanEx database of gene expression profiles More...CleanExi | HS_RPS3 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P23396 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P23396 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA063339 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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 Publication
<p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
- Ref.48"IKKbeta phosphorylation regulates RPS3 nuclear translocation and NF-kappaB function during infection with Escherichia coli strain O157:H7."
Wan F., Weaver A., Gao X., Bern M., Hardwidge P.R., Lenardo M.J.
Nat. Immunol. 12:335-343(2011) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH IKKB AND E.COLI NLEH1, PHOSPHORYLATION AT SER-209, MUTAGENESIS OF SER-209.
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
19 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.13"Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry."
Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A.
Eur. J. Biochem. 239:144-149(1996) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 188-197. - Ref.15"Human ribosomal protein S3 interacts with DNA base excision repair proteins hAPE/Ref-1 and hOGG1."
Hegde V., Wang M., Deutsch W.A.
Biochemistry 43:14211-14217(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH APEX1 AND OGG1. - Ref.22"Interaction of Hsp90 with ribosomal proteins protects from ubiquitination and proteasome-dependent degradation."
Kim T.S., Jang C.Y., Kim H.D., Lee J.Y., Ahn B.Y., Kim J.
Mol. Biol. Cell 17:824-833(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HSP90, SUBCELLULAR LOCATION, UBIQUITINATION. - Ref.25"Ribosomal protein S3: a KH domain subunit in NF-kappaB complexes that mediates selective gene regulation."
Wan F., Anderson D.E., Barnitz R.A., Snow A., Bidere N., Zheng L., Hegde V., Lam L.T., Staudt L.M., Levens D., Deutsch W.A., Lenardo M.J.
Cell 131:927-939(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH RELA, IDENTIFICATION IN THE NF-KAPPA-B P65-P50 COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.28"Molecular composition of IMP1 ribonucleoprotein granules."
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C.
Mol. Cell. Proteomics 6:798-811(2007) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION. - Ref.31"Human ribosomal protein S3 (hRpS3) interacts with uracil-DNA glycosylase (hUNG) and stimulates its glycosylase activity."
Ko S.I., Park J.H., Park M.J., Kim J., Kang L.W., Han Y.S.
Mutat. Res. 648:54-64(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH UNG. - Ref.34"Arginine methylation of ribosomal protein S3 affects ribosome assembly."
Shin H.S., Jang C.Y., Kim H.D., Kim T.S., Kim S., Kim J.
Biochem. Biophys. Res. Commun. 385:273-278(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PRMT1, SUBCELLULAR LOCATION, METHYLATION AT ARG-64; ARG-65 AND ARG-67. - Ref.35"PKCdelta-dependent functional switch of rpS3 between translation and DNA repair."
Kim T.S., Kim H.D., Kim J.
Biochim. Biophys. Acta 1793:395-405(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PRKCD, PHOSPHORYLATION AT SER-6 AND THR-221, MUTAGENESIS OF SER-6; SER-35; THR-42; THR-70; SER-139; SER-149; THR-195 AND THR-221. - Ref.36"Ribosomal protein S3: A multi-functional protein that interacts with both p53 and MDM2 through its KH domain."
Yadavilli S., Mayo L.D., Higgins M., Lain S., Hegde V., Deutsch W.A.
DNA Repair 8:1215-1224(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH MDM2 AND TP53, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.38"Bacterial effector binding to ribosomal protein s3 subverts NF-kappaB function."
Gao X., Wan F., Mateo K., Callegari E., Wang D., Deng W., Puente J., Li F., Chaussee M.S., Finlay B.B., Lenardo M.J., Hardwidge P.R.
PLoS Pathog. 5:E1000708-E1000708(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH E.COLI NLEH1 AND NLEH2, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.39"IGF2BP1 enhances HCV IRES-mediated translation initiation via the 3'UTR."
Weinlich S., Huettelmaier S., Schierhorn A., Behrens S.-E., Ostareck-Lederer A., Ostareck D.H.
RNA 15:1528-1542(2009) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN A HCV IRES-MEDIATED TRANSLATION COMPLEX. - Ref.42"Ribosomal protein S3, a new substrate of Akt, serves as a signal mediator between neuronal apoptosis and DNA repair."
Lee S.B., Kwon I.S., Park J., Lee K.H., Ahn Y., Lee C., Kim J., Choi S.Y., Cho S.W., Ahn J.Y.
J. Biol. Chem. 285:29457-29468(2010) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH E2F1 AND PKB, PHOSPHORYLATION AT THR-70, MUTAGENESIS OF THR-70. - Ref.46"Ribosomal protein S3 is stabilized by sumoylation."
Jang C.Y., Shin H.S., Kim H.D., Kim J.W., Choi S.Y., Kim J.
Biochem. Biophys. Res. Commun. 414:523-527(2011) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SUMO1 AND UBC9, SUMOYLATION AT LYS-18; LYS-214 AND LYS-230, MUTAGENESIS OF LYS-18; LYS-214 AND LYS-230. - Ref.47"Ribosomal protein S3 is phosphorylated by Cdk1/cdc2 during G2/M phase."
Yoon I.S., Chung J.H., Hahm S.H., Park M.J., Lee Y.R., Ko S.I., Kang L.W., Kim T.S., Kim J., Han Y.S.
BMB Rep. 44:529-534(2011) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CDK1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-221, MUTAGENESIS OF SER-6; THR-42 AND THR-221. - Ref.48"IKKbeta phosphorylation regulates RPS3 nuclear translocation and NF-kappaB function during infection with Escherichia coli strain O157:H7."
Wan F., Weaver A., Gao X., Bern M., Hardwidge P.R., Lenardo M.J.
Nat. Immunol. 12:335-343(2011) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH IKKB AND E.COLI NLEH1, PHOSPHORYLATION AT SER-209, MUTAGENESIS OF SER-209. - Ref.50"Ribosomal protein S3 interacts with TRADD to induce apoptosis through caspase dependent JNK activation."
Jang C.Y., Kim H.D., Kim J.
Biochem. Biophys. Res. Commun. 421:474-478(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH TRADD. - Ref.53"Cytoplasmic ribosomal protein S3 (rpS3) plays a pivotal role in mitochondrial DNA damage surveillance."
Kim Y., Kim H.D., Kim J.
Biochim. Biophys. Acta 1833:2943-2952(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH TOM70, SUBCELLULAR LOCATION. - Ref.56"Ribosomal protein S3 interacts with the NF-kappaB inhibitor IkappaBalpha."
Stanborough T., Niederhauser J., Koch B., Bergler H., Pertschy B.
FEBS Lett. 588:659-664(2014) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH NFKBIA.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| IKBKB | O14920 | 4 | EBI-351193,EBI-81266 | |
| LRRK2 | Q5S007 | 2 | EBI-351193,EBI-5323863 | |
| MDM2 | Q00987 | 8 | EBI-351193,EBI-389668 | |
| NEDD8 | Q15843 | 2 | EBI-351193,EBI-716247 | |
| NFKB1 | P19838 | 5 | EBI-351193,EBI-300010 | |
| NFKBIA | P25963 | 6 | EBI-351193,EBI-307386 | |
| PPID | Q08752 | 4 | EBI-351193,EBI-716596 | |
| RELA | Q04206 | 8 | EBI-351193,EBI-73886 | |
| TP53 | P04637 | 4 | EBI-351193,EBI-366083 | |
| YWHAZ | P63104 | 2 | EBI-351193,EBI-347088 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- enzyme binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- Hsp70 protein binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- Hsp90 protein binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- kinase binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- microtubule binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- protein kinase A binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- protein kinase binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- transcription factor binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- tubulin binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- ubiquitin-like protein conjugating enzyme binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 112102, 282 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P23396 |
Database of interacting proteins More...DIPi | DIP-33177N |
The Eukaryotic Linear Motif resource for Functional Sites in Proteins More...ELMi | P23396 |
Protein interaction database and analysis system More...IntActi | P23396, 86 interactors |
Molecular INTeraction database More...MINTi | P23396 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000433821 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 17 – 28 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 29 – 33 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 34 – 41 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 46 – 53 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 55 – 59 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 61 – 63 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 64 – 77 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 83 – 90 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P23396 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P23396 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P23396 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 21 – 92 | KH type-2PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 72 |
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Belongs to the universal ribosomal protein uS3 family.Curated
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG3181 Eukaryota COG0092 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000008610 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000210611 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG002195 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P23396 |
KEGG Orthology (KO) More...KOi | K02985 |
Identification of Orthologs from Complete Genome Data More...OMAi | AVRHVLM |
Database of Orthologous Groups More...OrthoDBi | EOG091G0I8D |
Database for complete collections of gene phylogenies More...PhylomeDBi | P23396 |
TreeFam database of animal gene trees More...TreeFami | TF300901 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.30.1140.32, 1 hit 3.30.300.20, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR015946 KH_dom-like_a/b IPR004044 KH_dom_type_2 IPR009019 KH_sf_prok-type IPR001351 Ribosomal_S3_C IPR036419 Ribosomal_S3_C_sf IPR018280 Ribosomal_S3_CS IPR005703 Ribosomal_S3_euk/arc |
Pfam protein domain database More...Pfami | View protein in Pfam PF07650 KH_2, 1 hit PF00189 Ribosomal_S3_C, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF54814 SSF54814, 1 hit SSF54821 SSF54821, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR01008 uS3_euk_arch, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50823 KH_TYPE_2, 1 hit PS00548 RIBOSOMAL_S3, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basket
Isoform 1 (identifier: P23396-1) [UniParc]FASTAAdd to basketAdded to basketShow »
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.
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
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i6ECBB34A8EE04AAF
Isoform 2 (identifier: P23396-2) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
85-85: E → ELKIMVMVTGYPLLPLK
10 20 30 40 50
MAVQISKKRK FVADGIFKAE LNEFLTRELA EDGYSGVEVR VTPTRTEIII
60 70 80 90 100
LATRTQNVLG EKGRRIRELT AVVQKRFGFP EGSVELKIMV MVTGYPLLPL
110 120 130 140 150
KLYAEKVATR GLCAIAQAES LRYKLLGGLA VRRACYGVLR FIMESGAKGC
160 170 180 190 200
EVVVSGKLRG QRAKSMKFVD GLMIHSGDPV NYYVDTAVRH VLLRQGVLGI
210 220 230 240 250
KVKIMLPWDP TGKIGPKKPL PDHVSIVEPK DEILPTTPIS EQKGGKPEPP
AMPQPVPTA
Note: No experimental confirmation available. Gene prediction based on EST data.
Show »Length:259
Mass (Da):28,487
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i68FF5C2DF8769693
<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni
The sequence BAB93471 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 8 | K → R in AAB19349 (PubMed:1712897).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 104 | S → C in CAA39248 (PubMed:2129557).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 233 | P → L in CAA39248 (PubMed:2129557).Curated | 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_046667 | 85 | E → ELKIMVMVTGYPLLPLK in isoform 2. Curated | 1 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks 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. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS58161.1 [P23396-2] CCDS8236.1 [P23396-1] |
Protein sequence database of the Protein Information Resource More...PIRi | A41247 R3HUS3 |
NCBI Reference Sequences More...RefSeqi | NP_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 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.546286 Hs.740358 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000278572; ENSP00000278572; ENSG00000149273 [P23396-2] ENST00000524851; ENSP00000433821; ENSG00000149273 [P23396-1] ENST00000527446; ENSP00000436971; ENSG00000149273 [P23396-1] ENST00000531188; ENSP00000434643; ENSG00000149273 [P23396-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 6188 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:6188 |
UCSC genome browser More...UCSCi | uc001owh.5 human [P23396-1] |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityi
Alternative splicing<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P23396 | 40S ribosomal protein S3 | 243 | |||
| 40S ribosomal protein S3 | ) | 243 | |||
| 40S ribosomal protein S3 | 243 | ||||
| 40S ribosomal protein S3 | 243 | ||||
| Ribosomal protein S3 | 243 | ||||
| +20 | |||||
| P23396-2 | RPS3 isoform 9 | 259 | |||
| RPS3 isoform 8 | 259 | ||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P23396 | 40S ribosomal protein S3 | 243 | |||
| 40S ribosomal protein S3 | ) | 243 | |||
| 40S ribosomal protein S3 | 243 | ||||
| 40S ribosomal protein S3 | 243 | ||||
| Ribosomal protein S3 | 243 | ||||
| +55 | |||||
| P23396-2 | Ribosomal protein S3 | 259 | |||
| Uncharacterized protein | 259 | ||||
| Uncharacterized protein | 319 | ||||
| Putative ribosomal protein S3 | 243 | ||||
| 40S ribosomal protein S3 | 243 | ||||
| +21 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P23396 | 40S ribosomal protein S3 | 243 | |||
| 40S ribosomal protein S3 | ) | 243 | |||
| 40S ribosomal protein S3 | 243 | ||||
| 40S ribosomal protein S3 | 243 | ||||
| Ribosomal protein S3 | 243 | ||||
| +772 | |||||
| P23396-2 | 40S ribosomal protein S3 | 253 | |||
| UPI00051E1EB7 | 314 | ||||
| UPI000442115E | 254 | ||||
| UPI0004F48F89 | 254 | ||||
| LOW QUALITY PROTEIN: 40S ribosomal protein S3-like | 378 | ||||
| +30 | |||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
| NIEHS-SNPs |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks 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. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS58161.1 [P23396-2] CCDS8236.1 [P23396-1] |
Protein sequence database of the Protein Information Resource More...PIRi | A41247 R3HUS3 |
NCBI Reference Sequences More...RefSeqi | NP_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 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.546286 Hs.740358 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1WH9 | NMR | - | A | 17-95 | [»] | |
| 4UG0 | electron microscopy | - | SD | 1-243 | [»] | |
| 4V6X | electron microscopy | 5.00 | AD | 1-243 | [»] | |
| 5A2Q | electron microscopy | 3.90 | D | 1-243 | [»] | |
| 5AJ0 | electron microscopy | 3.50 | BD | 1-243 | [»] | |
| 5FLX | electron microscopy | 3.90 | D | 1-243 | [»] | |
| 5LKS | electron microscopy | 3.60 | SD | 1-243 | [»] | |
| 5OA3 | electron microscopy | 4.30 | D | 1-243 | [»] | |
| 5T2C | electron microscopy | 3.60 | Aq | 1-243 | [»] | |
| 5VYC | X-ray | 6.00 | D1/D2/D3/D4/D5/D6 | 1-243 | [»] | |
| 6EK0 | electron microscopy | 2.90 | SD | 1-243 | [»] | |
| 6FEC | electron microscopy | 6.30 | g | 1-227 | [»] | |
| 6G51 | electron microscopy | 4.10 | D | 1-243 | [»] | |
| 6G53 | electron microscopy | 4.50 | D | 1-243 | [»] | |
| 6G5H | electron microscopy | 3.60 | D | 1-243 | [»] | |
| 6G5I | electron microscopy | 3.50 | D | 1-243 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P23396 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P23396 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 112102, 282 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P23396 |
Database of interacting proteins More...DIPi | DIP-33177N |
The Eukaryotic Linear Motif resource for Functional Sites in Proteins More...ELMi | P23396 |
Protein interaction database and analysis system More...IntActi | P23396, 86 interactors |
Molecular INTeraction database More...MINTi | P23396 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000433821 |
Protein family/group databases
MoonProt database of moonlighting proteins More...MoonProti | P23396 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P23396 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P23396 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P23396 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | RPS3 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 417719 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P23396 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P23396 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P23396 |
PeptideAtlas More...PeptideAtlasi | P23396 |
PRoteomics IDEntifications database More...PRIDEi | P23396 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 54087 |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 6188 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000278572; ENSP00000278572; ENSG00000149273 [P23396-2] ENST00000524851; ENSP00000433821; ENSG00000149273 [P23396-1] ENST00000527446; ENSP00000436971; ENSG00000149273 [P23396-1] ENST00000531188; ENSP00000434643; ENSG00000149273 [P23396-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 6188 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:6188 |
UCSC genome browser More...UCSCi | uc001owh.5 human [P23396-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 6188 |
DisGeNET More...DisGeNETi | 6188 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000149273.14 |
GeneCards: human genes, protein and diseases More...GeneCardsi | RPS3 |
Human Gene Nomenclature Database More...HGNCi | HGNC:10420 RPS3 |
Human Protein Atlas More...HPAi | HPA063339 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 600454 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P23396 |
Open Targets More...OpenTargetsi | ENSG00000149273 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA34829 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG3181 Eukaryota COG0092 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000008610 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000210611 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG002195 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P23396 |
KEGG Orthology (KO) More...KOi | K02985 |
Identification of Orthologs from Complete Genome Data More...OMAi | AVRHVLM |
Database of Orthologous Groups More...OrthoDBi | EOG091G0I8D |
Database for complete collections of gene phylogenies More...PhylomeDBi | P23396 |
TreeFam database of animal gene trees More...TreeFami | TF300901 |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-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-9010553 Regulation of expression of SLITs and ROBOs 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) |
SIGNOR Signaling Network Open Resource More...SIGNORi | P23396 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | RPS3 human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P23396 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | RPS3 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 6188 |
Protein Ontology More...PROi | PR:P23396 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000149273 |
CleanEx database of gene expression profiles More...CleanExi | HS_RPS3 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P23396 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P23396 HS |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.30.1140.32, 1 hit 3.30.300.20, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR015946 KH_dom-like_a/b IPR004044 KH_dom_type_2 IPR009019 KH_sf_prok-type IPR001351 Ribosomal_S3_C IPR036419 Ribosomal_S3_C_sf IPR018280 Ribosomal_S3_CS IPR005703 Ribosomal_S3_euk/arc |
Pfam protein domain database More...Pfami | View protein in Pfam PF07650 KH_2, 1 hit PF00189 Ribosomal_S3_C, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF54814 SSF54814, 1 hit SSF54821 SSF54821, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR01008 uS3_euk_arch, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50823 KH_TYPE_2, 1 hit PS00548 RIBOSOMAL_S3, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | RS3_HUMAN | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P23396Primary (citable) accession number: P23396 Secondary accession number(s): B2R7N5 , J3KN86, Q498B5, Q8NI95 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1991 |
| Last sequence update: | October 1, 1993 | |
| Last modified: | July 18, 2018 | |
| This is version 210 of the entry and version 2 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| 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. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 11
Human chromosome 11: entries, gene names and cross-references to MIM - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - Ribosomal proteins
Ribosomal proteins families and list of entries - SIMILARITY comments
Index of protein domains and families
