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Protein

30S ribosomal protein S6

Gene

rpsF

Organism
Escherichia coli (strain K12)
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

Binds together with S18 to 16S ribosomal RNA.

<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

  • mRNA 5'-UTR binding Source: EcoCyc
  • small ribosomal subunit rRNA binding Source: EcoCyc
  • structural constituent of ribosome Source: GO_Central

GO - Biological processi

<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 functionRibonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
EcoCyc:EG10905-MONOMER
MetaCyc:EG10905-MONOMER

<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:
30S ribosomal protein S6
Alternative name(s):
Small ribosomal subunit protein bS61 Publication
Cleaved into the following 2 chains:
<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:rpsF
Ordered Locus Names:b4200, JW4158
<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>OrganismiEscherichia coli (strain K12)
<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 identifieri83333 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<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
  • UP000000318 <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
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG10905 rpsF

<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

GO - Cellular componenti

<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 ‘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_00000306401 – 13530S ribosomal protein S6, fully modified isoform1 PublicationAdd BLAST135
ChainiPRO_00000306411 – 13130S ribosomal protein S6, non-modified isoformAdd BLAST131

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 residuei93N6-acetyllysine1 Publication1

<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

5 different forms of the protein, varying only in the number of C-terminal glutamate residues, were isolated. The sequence shown is form S6-6, which is the longest. The first two Glu are encoded by the rpsF gene, the other Glu are added post-translationally by the RimK enzyme.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P02358

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P02358

PRoteomics IDEntifications database

More...
PRIDEi
P02358

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
P02358

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P02358

<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

Part of the 30S ribosomal subunit (PubMed:328274, PubMed:10094780, PubMed:12809609, PubMed:16272117, PubMed:27934701, PubMed:12244297, PubMed:27906160, PubMed:27906161, PubMed:28077875). Interacts weakly with L2 in one of the 3.5 A resolved structures (PubMed:16272117).9 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

WithEntry#Exp.IntActNotes
rpsRP0A7T74EBI-543068,EBI-548844

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4259641, 276 interactors

Database of interacting proteins

More...
DIPi
DIP-10782N

Protein interaction database and analysis system

More...
IntActi
P02358, 65 interactors

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_4395

<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

1135
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P02358

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P02358

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
P02358

<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

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4108ZDX Bacteria
COG0360 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000040438

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P02358

KEGG Orthology (KO)

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KOi
K02990

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P02358

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00473 bS6, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.70.60, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00360 Ribosomal_S6, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000529 Ribosomal_S6
IPR020815 Ribosomal_S6_CS
IPR020814 Ribosomal_S6_plastid/chlpt
IPR035980 Ribosomal_S6_sf
IPR014717 Transl_elong_EF1B/ribosomal_S6

The PANTHER Classification System

More...
PANTHERi
PTHR21011 PTHR21011, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01250 Ribosomal_S6, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54995 SSF54995, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00166 S6, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01048 RIBOSOMAL_S6, 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>Sequencei

<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.

P02358-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRHYEIVFMV HPDQSEQVPG MIERYTAAIT GAEGKIHRLE DWGRRQLAYP
60 70 80 90 100
INKLHKAHYV LMNVEAPQEV IDELETTFRF NDAVIRSMVM RTKHAVTEAS
110 120 130
PMVKAKDERR ERRDDFANET ADDAEAGDSE EEEEE
Length:135
Mass (Da):15,703
Last modified:July 21, 1986 - v1
<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:iF4CC629711C1FD0E
GO

<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 AAA97096 differs from that shown. Up to 4 Glu residues can be added post-translationally.1 Publication
The sequence AAC77157 differs from that shown. Up to 4 Glu residues can be added post-translationally.1 Publication
The sequence BAE78201 differs from that shown. Up to 4 Glu residues can be added post-translationally.1 Publication
The sequence CAA27652 differs from that shown. Up to 4 Glu residues can be added post-translationally.1 Publication

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 conflicti14Q → T AA sequence (PubMed:9868784).Curated1
Sequence conflicti20G → A AA sequence (PubMed:9868784).Curated1

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 15187.2 Da from positions 1 - 131. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X04022 Genomic DNA Translation: CAA27652.1 Sequence problems.
U14003 Genomic DNA Translation: AAA97096.1 Sequence problems.
U00096 Genomic DNA Translation: AAC77157.5 Sequence problems.
AP009048 Genomic DNA Translation: BAE78201.1 Sequence problems.

Protein sequence database of the Protein Information Resource

More...
PIRi
C65231 R3EC6

NCBI Reference Sequences

More...
RefSeqi
NP_418621.5, NC_000913.3

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC77157; AAC77157; b4200
BAE78201; BAE78201; BAE78201

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
948723

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW4158
eco:b4200

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|511145.12.peg.4332

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04022 Genomic DNA Translation: CAA27652.1 Sequence problems.
U14003 Genomic DNA Translation: AAA97096.1 Sequence problems.
U00096 Genomic DNA Translation: AAC77157.5 Sequence problems.
AP009048 Genomic DNA Translation: BAE78201.1 Sequence problems.
PIRiC65231 R3EC6
RefSeqiNP_418621.5, NC_000913.3

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
1EG0electron microscopy11.50C1-97[»]
1M5Gmodel-F1-100[»]
2YKRelectron microscopy9.80F1-100[»]
3IY8electron microscopy14.10F2-100[»]
3J9Yelectron microscopy3.90f1-135[»]
3J9Zelectron microscopy3.60SF1-135[»]
3JA1electron microscopy3.60SF1-135[»]
3JBUelectron microscopy3.64F1-131[»]
3JBVelectron microscopy3.32F1-131[»]
3JCDelectron microscopy3.70f1-135[»]
3JCEelectron microscopy3.20f1-135[»]
3JCJelectron microscopy3.70n1-135[»]
3JCNelectron microscopy4.60i1-135[»]
4A2Ielectron microscopy16.50F1-100[»]
4ADVelectron microscopy13.50F1-135[»]
4U1UX-ray2.95AF/CF1-100[»]
4U1VX-ray3.00AF/CF1-100[»]
4U20X-ray2.90AF/CF1-100[»]
4U24X-ray2.90AF/CF1-100[»]
4U25X-ray2.90AF/CF1-100[»]
4U26X-ray2.80AF/CF1-100[»]
4U27X-ray2.80AF/CF1-100[»]
4V47electron microscopy12.30BF1-135[»]
4V48electron microscopy11.50BF1-135[»]
4V4HX-ray3.46AF/CF1-135[»]
4V4QX-ray3.46AF/CF1-135[»]
4V4Velectron microscopy15.00AF1-95[»]
4V4Welectron microscopy15.00AF1-95[»]
4V50X-ray3.22AF/CF1-135[»]
4V52X-ray3.21AF/CF1-135[»]
4V53X-ray3.54AF/CF1-135[»]
4V54X-ray3.30AF/CF1-135[»]
4V55X-ray4.00AF/CF1-135[»]
4V56X-ray3.93AF/CF1-135[»]
4V57X-ray3.50AF/CF1-135[»]
4V5BX-ray3.74BF/DF1-135[»]
4V5Helectron microscopy5.80AF1-100[»]
4V5YX-ray4.45AF/CF1-135[»]
4V64X-ray3.50AF/CF1-135[»]
4V65electron microscopy9.00AT1-135[»]
4V66electron microscopy9.00AT1-135[»]
4V69electron microscopy6.70AF1-100[»]
4V6CX-ray3.19AF/CF1-135[»]
4V6DX-ray3.81AF/CF1-135[»]
4V6EX-ray3.71AF/CF1-135[»]
4V6Kelectron microscopy8.25BJ1-135[»]
4V6Lelectron microscopy13.20AJ1-135[»]
4V6Melectron microscopy7.10AF1-135[»]
4V6Nelectron microscopy12.10BI1-135[»]
4V6Oelectron microscopy14.70AI1-135[»]
4V6Pelectron microscopy13.50AI1-135[»]
4V6Qelectron microscopy11.50AI1-135[»]
4V6Relectron microscopy11.50AI1-135[»]
4V6Selectron microscopy13.10BH1-135[»]
4V6Telectron microscopy8.30AF1-100[»]
4V6Velectron microscopy9.80AF1-135[»]
4V6Yelectron microscopy12.00AF1-100[»]
4V6Zelectron microscopy12.00AF1-100[»]
4V70electron microscopy17.00AF1-100[»]
4V71electron microscopy20.00AF1-100[»]
4V72electron microscopy13.00AF1-100[»]
4V73electron microscopy15.00AF1-100[»]
4V74electron microscopy17.00AF1-100[»]
4V75electron microscopy12.00AF1-100[»]
4V76electron microscopy17.00AF1-100[»]
4V77electron microscopy17.00AF1-100[»]
4V78electron microscopy20.00AF1-100[»]
4V79electron microscopy15.00AF1-100[»]
4V7Aelectron microscopy9.00AF1-100[»]
4V7Belectron microscopy6.80AF1-135[»]
4V7Celectron microscopy7.60AF1-131[»]
4V7Delectron microscopy7.60BF1-131[»]
4V7Ielectron microscopy9.60BF1-135[»]
4V7SX-ray3.25AF/CF1-100[»]
4V7TX-ray3.19AF/CF1-100[»]
4V7UX-ray3.10AF/CF1-100[»]
4V7VX-ray3.29AF/CF1-100[»]
4V85X-ray3.20F1-131[»]
4V89X-ray3.70AF1-135[»]
4V9CX-ray3.30AF/CF1-135[»]
4V9DX-ray3.00AF/BF1-100[»]
4V9OX-ray2.90BF/DF/FF/HF1-135[»]
4V9PX-ray2.90BF/DF/FF/HF1-135[»]
4WF1X-ray3.09AF/CF1-100[»]
4WOIX-ray3.00AF/DF1-135[»]
4WWWX-ray3.10QF/XF1-100[»]
4YBBX-ray2.10AF/BF1-106[»]
5AFIelectron microscopy2.90f1-135[»]
5H5Uelectron microscopy3.00m1-135[»]
5IQRelectron microscopy3.00k1-135[»]
5IT8X-ray3.12AF/BF1-106[»]
5J5BX-ray2.80AF/BF1-106[»]
5J7LX-ray3.00AF/BF1-106[»]
5J88X-ray3.32AF/BF1-106[»]
5J8AX-ray3.10AF/BF1-106[»]
5J91X-ray2.96AF/BF1-106[»]
5JC9X-ray3.03AF/BF1-106[»]
5JTEelectron microscopy3.60AF1-135[»]
5JU8electron microscopy3.60AF1-135[»]
5KCRelectron microscopy3.601f1-135[»]
5KCSelectron microscopy3.901f1-135[»]
5KPSelectron microscopy3.90111-135[»]
5KPVelectron microscopy4.10101-135[»]
5KPWelectron microscopy3.90101-135[»]
5KPXelectron microscopy3.90101-135[»]
5L3Pelectron microscopy3.70f1-135[»]
5LZAelectron microscopy3.60f1-100[»]
5LZBelectron microscopy5.30f1-100[»]
5LZCelectron microscopy4.80f1-100[»]
5LZDelectron microscopy3.40f1-100[»]
5LZEelectron microscopy3.50f1-100[»]
5LZFelectron microscopy4.60f1-100[»]
5MDVelectron microscopy2.97k1-135[»]
5MDWelectron microscopy3.06k1-135[»]
5MDYelectron microscopy3.35k1-135[»]
5MDZelectron microscopy3.10k1-135[»]
5ME0electron microscopy13.50F1-131[»]
5ME1electron microscopy13.50F1-131[»]
5MGPelectron microscopy3.10f1-100[»]
5MY1electron microscopy7.60F1-135[»]
5NO2electron microscopy5.16F1-106[»]
5NO3electron microscopy5.16F1-106[»]
5NO4electron microscopy5.16F1-106[»]
5NP6electron microscopy3.60I1-100[»]
5NWYelectron microscopy2.9351-131[»]
5O2Relectron microscopy3.40f1-100[»]
5U4Ielectron microscopy3.50f1-135[»]
5U9Felectron microscopy3.20F1-131[»]
5U9Gelectron microscopy3.20F1-131[»]
5UYKelectron microscopy3.90F1-100[»]
5UYLelectron microscopy3.60F1-100[»]
5UYMelectron microscopy3.20F1-100[»]
5UYNelectron microscopy4.00F1-100[»]
5UYPelectron microscopy3.90F1-100[»]
5UYQelectron microscopy3.80F1-100[»]
5UZ4electron microscopy5.80F1-131[»]
5WDTelectron microscopy3.00f1-100[»]
5WE4electron microscopy3.10f1-100[»]
5WE6electron microscopy3.40f1-100[»]
5WFKelectron microscopy3.40f1-100[»]
6BU8electron microscopy3.50F1-126[»]
6C4Ielectron microscopy3.24f1-135[»]
6DNCelectron microscopy3.70SA1-131[»]
6ENFelectron microscopy3.20f1-100[»]
6ENJelectron microscopy3.70f1-100[»]
6ENUelectron microscopy3.10f1-100[»]
6GWTelectron microscopy3.80f1-100[»]
6GXMelectron microscopy3.80f1-100[»]
6GXNelectron microscopy3.90f1-100[»]
6GXOelectron microscopy3.90f1-100[»]
6GXPelectron microscopy4.40f1-100[»]
6H4Nelectron microscopy3.00f1-100[»]
6H58electron microscopy7.90f/ff1-100[»]
ProteinModelPortaliP02358
SMRiP02358
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259641, 276 interactors
DIPiDIP-10782N
IntActiP02358, 65 interactors
STRINGi316385.ECDH10B_4395

PTM databases

iPTMnetiP02358

2D gel databases

SWISS-2DPAGEiP02358

Proteomic databases

EPDiP02358
PaxDbiP02358
PRIDEiP02358

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77157; AAC77157; b4200
BAE78201; BAE78201; BAE78201
GeneIDi948723
KEGGiecj:JW4158
eco:b4200
PATRICifig|511145.12.peg.4332

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB0898
EcoGeneiEG10905 rpsF

Phylogenomic databases

eggNOGiENOG4108ZDX Bacteria
COG0360 LUCA
HOGENOMiHOG000040438
InParanoidiP02358
KOiK02990
PhylomeDBiP02358

Enzyme and pathway databases

BioCyciEcoCyc:EG10905-MONOMER
MetaCyc:EG10905-MONOMER

Miscellaneous databases

EvolutionaryTraceiP02358

Protein Ontology

More...
PROi
PR:P02358

Family and domain databases

CDDicd00473 bS6, 1 hit
Gene3Di3.30.70.60, 1 hit
HAMAPiMF_00360 Ribosomal_S6, 1 hit
InterProiView protein in InterPro
IPR000529 Ribosomal_S6
IPR020815 Ribosomal_S6_CS
IPR020814 Ribosomal_S6_plastid/chlpt
IPR035980 Ribosomal_S6_sf
IPR014717 Transl_elong_EF1B/ribosomal_S6
PANTHERiPTHR21011 PTHR21011, 1 hit
PfamiView protein in Pfam
PF01250 Ribosomal_S6, 1 hit
SUPFAMiSSF54995 SSF54995, 1 hit
TIGRFAMsiTIGR00166 S6, 1 hit
PROSITEiView protein in PROSITE
PS01048 RIBOSOMAL_S6, 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 nameiRS6_ECOLI
<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: P02358
Secondary accession number(s): Q2M6A5
<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: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 7, 2018
This is version 197 of the entry and version 1 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 programProkaryotic Protein Annotation Program

<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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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