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UniProtKB - P23396 (RS3_HUMAN)

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>

<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>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. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Endonuclease activity is inhibited by MgCl2 on apurinic/apyrimidinic DNA but not on UV-irradiated DNA.1 Publication

<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>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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<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 functionDNA-binding, Lyase, Ribonucleoprotein, Ribosomal protein, RNA-binding
Biological processApoptosis, 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)
Alternative name(s):
Small ribosomal subunit protein uS31 Publication
<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>OrganismiHomo 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 identifieri9606 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 11

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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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 keyPosition(s)DescriptionActionsGraphical viewLength
<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>Mutagenesisi6S → A: No effect on phosphorylation by CDK1. Greatly reduced phosphorylation by PRKCD. Abolishes phosphorylation by PRKCD; when associated with A-221. 2 Publications1
Mutagenesisi18K → R: No effect on sumoylation. Abolishes sumoylation; when associated with R-214 and R-230. 1 Publication1
Mutagenesisi35S → A: No effect on phosphorylation by PRKCD. 1 Publication1
Mutagenesisi42T → 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 Publications1
Mutagenesisi42T → D: Phosphomimetic mutant which is detected exclusively in the nucleus. 1 Publication1
Mutagenesisi70T → A: No effect on phosphorylation by PRKCD. Abolishes phosphorylation by PKB. 2 Publications1
Mutagenesisi70T → D, E or R: Abolishes phosphorylation by PKB. 1 Publication1
Mutagenesisi132K → A: Does not affect ability to cleave DNA but abolishes binding to 8-oxoG. 1 Publication1
Mutagenesisi139S → A: No effect on phosphorylation by PRKCD. 1 Publication1
Mutagenesisi149S → A: No effect on phosphorylation by PRKCD. 1 Publication1
Mutagenesisi195T → A: No effect on phosphorylation by PRKCD. 1 Publication1
Mutagenesisi209S → A: Reduced phosphorylation by IKKB. 1 Publication1
Mutagenesisi214K → R: No effect on sumoylation. Abolishes sumoylation; when associated with R-18 and R-230. 1 Publication1
Mutagenesisi221T → 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 Publications1
Mutagenesisi230K → R: No effect on sumoylation. Abolishes sumoylation; when associated with R-18 and R-214. 1 Publication1

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 keyPosition(s)DescriptionActionsGraphical viewLength
<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 methionineiRemovedCombined sources1 Publication
<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_00001303202 – 24340S ribosomal protein S3Add BLAST242

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei6Phosphoserine; by PKC/PRKCD1 Publication1
Modified residuei35PhosphoserineCombined sources1
Modified residuei42Phosphothreonine; by MAPK1 Publication1
Modified residuei62N6-acetyllysineCombined sources1
Modified residuei64Asymmetric dimethylarginine; by PRMT11 Publication1
Modified residuei65Asymmetric dimethylarginine; by PRMT11 Publication1
Modified residuei67Asymmetric dimethylarginine; by PRMT11 Publication1
Modified residuei70Phosphothreonine; by PKB1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, 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-linki90Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residuei104PhosphoserineCombined sources1
Modified residuei132N6-succinyllysineBy similarity1
Cross-linki202Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residuei209Phosphoserine; by IKKB1 Publication1
Cross-linki214Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki214Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate2 Publications
Modified residuei220PhosphothreonineCombined sources1
Modified residuei221Phosphothreonine; by CDK1 and PKC/PRKCDCombined sources3 Publications1
Modified residuei224PhosphoserineCombined sources1
Cross-linki230Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei242PhosphothreonineCombined sources1

<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
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
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
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

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P23396

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		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 Expressed in 229 organ(s), highest expression level in female gonad

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 PublicationBy similarity19 Publications

<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

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		112102, 308 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, 82 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

1243
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WH9NMR-A17-95[»]
4UG0electron microscopy-SD1-243[»]
4V6Xelectron microscopy5.00AD1-243[»]
5A2Qelectron microscopy3.90D1-243[»]
5AJ0electron microscopy3.50BD1-243[»]
5FLXelectron microscopy3.90D1-243[»]
5LKSelectron microscopy3.60SD1-243[»]
5OA3electron microscopy4.30D1-243[»]
5T2Celectron microscopy3.60Aq1-243[»]
5VYCX-ray6.00D1/D2/D3/D4/D5/D61-243[»]
6EK0electron microscopy2.90SD1-243[»]
6FECelectron microscopy6.30g1-227[»]
6G51electron microscopy4.10D1-243[»]
6G53electron microscopy4.50D1-243[»]
6G5Helectron microscopy3.60D1-243[»]
6G5Ielectron microscopy3.50D1-243[»]

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...

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 keyPosition(s)DescriptionActionsGraphical viewLength
<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>Domaini21 – 92KH type-2PROSITE-ProRule annotationAdd BLAST72

<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		873694at2759

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 basket

This entry has 2 described isoforms and 13 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P23396-1) [UniParc]FASTAAdd to basket

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.

« Hide
        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
GO
Isoform 2 (identifier: P23396-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     85-85: E → ELKIMVMVTGYPLLPLK

Note: No experimental confirmation available. Gene prediction based on EST data.
Show »
Length:259
Mass (Da):28,487
Checksum:i68FF5C2DF8769693
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 13 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9PL09E9PL09_HUMAN
40S ribosomal protein S3
RPS3
231Annotation score:

Annotation score:2 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>
H0YEU2H0YEU2_HUMAN
40S ribosomal protein S3
RPS3
171Annotation score:

Annotation score:2 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>
E9PSF4E9PSF4_HUMAN
40S ribosomal protein S3
RPS3
103Annotation score:

Annotation score:2 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>
E9PPU1E9PPU1_HUMAN
40S ribosomal protein S3
RPS3
158Annotation score:

Annotation score:2 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>
H0YCJ7H0YCJ7_HUMAN
40S ribosomal protein S3
RPS3
135Annotation score:

Annotation score:1 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>
F2Z2S8F2Z2S8_HUMAN
40S ribosomal protein S3
RPS3
117Annotation score:

Annotation score:1 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>
H0YF32H0YF32_HUMAN
40S ribosomal protein S3
RPS3
123Annotation score:

Annotation score:1 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>
E9PJN9E9PJN9_HUMAN
40S ribosomal protein S3
RPS3
36Annotation score:

Annotation score:1 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>
E9PK82E9PK82_HUMAN
40S ribosomal protein S3
RPS3
128Annotation score:

Annotation score:1 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>
E9PQ96E9PQ96_HUMAN
40S ribosomal protein S3
RPS3
91Annotation score:

Annotation score:1 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>
There are more potential isoformsShow all

<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 keyPosition(s)DescriptionActionsGraphical viewLength
<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 conflicti8K → R in AAB19349 (PubMed:1712897).Curated1
Sequence conflicti104S → C in CAA39248 (PubMed:2129557).Curated1
Sequence conflicti233P → L in CAA39248 (PubMed:2129557).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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_04666785E → ELKIMVMVTGYPLLPLK in isoform 2. Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links 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]

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

<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:
EMBLi
GenBanki
DDBJi
Links 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.
CCDSiCCDS58161.1 [P23396-2]
CCDS8236.1 [P23396-1]
PIRiA41247 R3HUS3
RefSeqiNP_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
UniGeneiHs.546286
Hs.740358

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WH9NMR-A17-95[»]
4UG0electron microscopy-SD1-243[»]
4V6Xelectron microscopy5.00AD1-243[»]
5A2Qelectron microscopy3.90D1-243[»]
5AJ0electron microscopy3.50BD1-243[»]
5FLXelectron microscopy3.90D1-243[»]
5LKSelectron microscopy3.60SD1-243[»]
5OA3electron microscopy4.30D1-243[»]
5T2Celectron microscopy3.60Aq1-243[»]
5VYCX-ray6.00D1/D2/D3/D4/D5/D61-243[»]
6EK0electron microscopy2.90SD1-243[»]
6FECelectron microscopy6.30g1-227[»]
6G51electron microscopy4.10D1-243[»]
6G53electron microscopy4.50D1-243[»]
6G5Helectron microscopy3.60D1-243[»]
6G5Ielectron microscopy3.50D1-243[»]
ProteinModelPortaliP23396
SMRiP23396
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112102, 308 interactors
CORUMiP23396
DIPiDIP-33177N
ELMiP23396
IntActiP23396, 82 interactors
MINTiP23396
STRINGi9606.ENSP00000433821

Protein family/group databases

MoonProtiP23396

PTM databases

iPTMnetiP23396
PhosphoSitePlusiP23396
SwissPalmiP23396

Polymorphism and mutation databases

BioMutaiRPS3
DMDMi417719

Proteomic databases

EPDiP23396
jPOSTiP23396
MaxQBiP23396
PaxDbiP23396
PeptideAtlasiP23396
PRIDEiP23396
ProteomicsDBi54087

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		6188
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000278572; ENSP00000278572; ENSG00000149273 [P23396-2]
ENST00000524851; ENSP00000433821; ENSG00000149273 [P23396-1]
ENST00000527446; ENSP00000436971; ENSG00000149273 [P23396-1]
ENST00000531188; ENSP00000434643; ENSG00000149273 [P23396-1]
GeneIDi6188
KEGGihsa:6188
UCSCiuc001owh.5 human [P23396-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		6188
DisGeNETi6188
EuPathDBiHostDB:ENSG00000149273.14

GeneCards: human genes, protein and diseases

More...GeneCardsi		RPS3
HGNCiHGNC:10420 RPS3
HPAiHPA063339
MIMi600454 gene
neXtProtiNX_P23396
OpenTargetsiENSG00000149273
PharmGKBiPA34829

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG3181 Eukaryota
COG0092 LUCA
GeneTreeiENSGT00390000008610
HOGENOMiHOG000210611
HOVERGENiHBG002195
InParanoidiP23396
KOiK02985
OMAiAVRHVLM
OrthoDBi873694at2759
PhylomeDBiP23396
TreeFamiTF300901

Enzyme and pathway databases

ReactomeiR-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)
SIGNORiP23396

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		RPS3 human
EvolutionaryTraceiP23396

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

BgeeiENSG00000149273 Expressed in 229 organ(s), highest expression level in female gonad
CleanExiHS_RPS3
ExpressionAtlasiP23396 baseline and differential
GenevisibleiP23396 HS

Family and domain databases

Gene3Di3.30.1140.32, 1 hit
3.30.300.20, 1 hit
InterProiView 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
PfamiView protein in Pfam
PF07650 KH_2, 1 hit
PF00189 Ribosomal_S3_C, 1 hit
SUPFAMiSSF54814 SSF54814, 1 hit
SSF54821 SSF54821, 1 hit
TIGRFAMsiTIGR01008 uS3_euk_arch, 1 hit
PROSITEiView 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 nameiRS3_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>AccessioniPrimary (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 historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: October 1, 1993
Last modified: January 16, 2019
This is version 215 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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Ribosomal proteins
    Ribosomal proteins families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
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