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Entry version 134 (08 May 2019)
Sequence version 1 (21 Jul 1986)
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Protein

50S ribosomal protein L18

Gene

rplR

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:4 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

This is one of the proteins that mediates the attachment of the 5S rRNA subcomplex onto the large ribosomal subunit where it forms part of the central protuberance. Binds stably to 5S rRNA; increases binding abilities of L5 in a cooperative fashion; both proteins together confer 23S rRNA binding. The 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.5 Publications

<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

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

More...
BioCyci
EcoCyc:EG10879-MONOMER
ECOL316407:JW3266-MONOMER
MetaCyc:EG10879-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:
50S ribosomal protein L18
Alternative name(s):
Large ribosomal subunit protein uL181 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:rplR
Ordered Locus Names:b3304, JW3266
<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
EG10879 rplR

<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_00001312581 – 11750S ribosomal protein L18Add BLAST117

<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

The protein has been shown to contain a phosphoserine, which was required for the protein to bind to 5S rRNA (PubMed:10529214). However, the presence of this phosphoserine is controversial, and it has not been seen by mass spectrometry.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P0C018

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P0C018

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

More...
PaxDbi
P0C018

PRoteomics IDEntifications database

More...
PRIDEi
P0C018

<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 50S ribosomal subunit (PubMed:1098937, PubMed:10094780, PubMed:12809609, PubMed:16272117, PubMed:25310980, PubMed:24844575, PubMed:27934701, PubMed:27906160, PubMed:27906161); part of the 5S rRNA/L5/L18/L25 subcomplex (PubMed:354687, PubMed:353728, PubMed:109811, PubMed:6159586, PubMed:7038683, PubMed:8925931). Contacts the 5S and 23S rRNAs.15 Publications

Protein-protein interaction databases

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-3807 50S large ribosomal subunit

Database of interacting proteins

More...
DIPi
DIP-47908N

Protein interaction database and analysis system

More...
IntActi
P0C018, 38 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b3304

<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

1117
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00q2-117[»]
2J28electron microscopy8.00O1-117[»]
2RDOelectron microscopy9.10O1-117[»]
3BBXelectron microscopy10.00O1-117[»]
3J5Lelectron microscopy6.60O2-117[»]
3J7Zelectron microscopy3.90O1-117[»]
3J8Gelectron microscopy5.00O1-117[»]
3J9Yelectron microscopy3.90O1-117[»]
3J9Zelectron microscopy3.60LK1-117[»]
3JA1electron microscopy3.60LQ1-117[»]
3JBUelectron microscopy3.64o1-117[»]
3JBVelectron microscopy3.32o1-117[»]
3JCDelectron microscopy3.70O1-117[»]
3JCEelectron microscopy3.20O1-117[»]
3JCJelectron microscopy3.70N1-117[»]
3JCNelectron microscopy4.60O1-117[»]
4CSUelectron microscopy5.50O2-117[»]
4U1UX-ray2.95BO/DO2-117[»]
4U1VX-ray3.00BO/DO2-117[»]
4U20X-ray2.90BO/DO2-117[»]
4U24X-ray2.90BO/DO2-117[»]
4U25X-ray2.90BO/DO2-117[»]
4U26X-ray2.80BO/DO2-117[»]
4U27X-ray2.80BO/DO2-117[»]
4UY8electron microscopy3.80O2-117[»]
4V47electron microscopy12.30AM1-117[»]
4V48electron microscopy11.50AM1-117[»]
4V4HX-ray3.46BO/DO1-117[»]
4V4QX-ray3.46BO/DO1-117[»]
4V4Velectron microscopy15.00BM3-115[»]
4V4Welectron microscopy15.00BM3-115[»]
4V50X-ray3.22BO/DO1-117[»]
4V52X-ray3.21BO/DO1-117[»]
4V53X-ray3.54BO/DO1-117[»]
4V54X-ray3.30BO/DO1-117[»]
4V55X-ray4.00BO/DO1-117[»]
4V56X-ray3.93BO/DO1-117[»]
4V57X-ray3.50BO/DO1-117[»]
4V5BX-ray3.74AO/CO1-117[»]
4V5Helectron microscopy5.80BO2-117[»]
4V5YX-ray4.45BO/DO1-117[»]
4V64X-ray3.50BO/DO1-117[»]
4V65electron microscopy9.00BH1-117[»]
4V66electron microscopy9.00BH1-117[»]
4V69electron microscopy6.70BO2-117[»]
4V6CX-ray3.19BO/DO1-117[»]
4V6DX-ray3.81BO/DO1-117[»]
4V6EX-ray3.71BO/DO1-117[»]
4V6Kelectron microscopy8.25AP1-117[»]
4V6Lelectron microscopy13.20BP1-117[»]
4V6Melectron microscopy7.10BO1-117[»]
4V6Nelectron microscopy12.10AQ1-117[»]
4V6Oelectron microscopy14.70BQ1-117[»]
4V6Pelectron microscopy13.50BQ1-117[»]
4V6Qelectron microscopy11.50BQ1-117[»]
4V6Relectron microscopy11.50BQ1-117[»]
4V6Selectron microscopy13.10AQ1-117[»]
4V6Telectron microscopy8.30BO2-117[»]
4V6Velectron microscopy9.80BS1-117[»]
4V6Yelectron microscopy12.00BO1-117[»]
4V6Zelectron microscopy12.00BO1-117[»]
4V70electron microscopy17.00BO1-117[»]
4V71electron microscopy20.00BO1-117[»]
4V72electron microscopy13.00BO1-117[»]
4V73electron microscopy15.00BO1-117[»]
4V74electron microscopy17.00BO1-117[»]
4V75electron microscopy12.00BO1-117[»]
4V76electron microscopy17.00BO1-117[»]
4V77electron microscopy17.00BO1-117[»]
4V78electron microscopy20.00BO1-117[»]
4V79electron microscopy15.00BO1-117[»]
4V7Aelectron microscopy9.00BO1-117[»]
4V7Belectron microscopy6.80BO1-117[»]
4V7Celectron microscopy7.60BQ1-117[»]
4V7Delectron microscopy7.60AR1-117[»]
4V7Ielectron microscopy9.60AO1-117[»]
4V7SX-ray3.25BO/DO2-117[»]
4V7TX-ray3.19BO/DO2-117[»]
4V7UX-ray3.10BO/DO2-117[»]
4V7VX-ray3.29BO/DO2-117[»]
4V85X-ray3.20BS1-117[»]
4V89X-ray3.70BS1-117[»]
4V9CX-ray3.30BO/DO1-117[»]
4V9DX-ray3.00CO/DO2-117[»]
4V9OX-ray2.90AO/CO/EO/GO1-117[»]
4V9PX-ray2.90AO/CO/EO/GO1-117[»]
4WF1X-ray3.09BO/DO2-117[»]
4WOIX-ray3.00BO/CO1-117[»]
4WWWX-ray3.10RO/YO2-117[»]
4YBBX-ray2.10CP/DP1-117[»]
5ADYelectron microscopy4.50O1-117[»]
5AFIelectron microscopy2.90O1-117[»]
5AKAelectron microscopy5.70O1-117[»]
5GADelectron microscopy3.70P1-117[»]
5GAEelectron microscopy3.33P1-117[»]
5GAFelectron microscopy4.30P1-117[»]
5GAGelectron microscopy3.80P1-117[»]
5GAHelectron microscopy3.80P1-117[»]
5H5Uelectron microscopy3.00P1-117[»]
5IQRelectron microscopy3.00O1-117[»]
5IT8X-ray3.12CP/DP1-117[»]
5J5BX-ray2.80CP/DP1-117[»]
5J7LX-ray3.00CP/DP1-117[»]
5J88X-ray3.32CP/DP1-117[»]
5J8AX-ray3.10CP/DP1-117[»]
5J91X-ray2.96CP/DP1-117[»]
5JC9X-ray3.03CP/DP1-117[»]
5JTEelectron microscopy3.60BO1-117[»]
5JU8electron microscopy3.60BO1-117[»]
5KCRelectron microscopy3.601S1-117[»]
5KCSelectron microscopy3.901S1-117[»]
5KPSelectron microscopy3.90O1-117[»]
5KPVelectron microscopy4.10N1-117[»]
5KPWelectron microscopy3.90N1-117[»]
5KPXelectron microscopy3.90N1-117[»]
5L3Pelectron microscopy3.70S1-117[»]
5LZAelectron microscopy3.60O2-117[»]
5LZBelectron microscopy5.30O2-117[»]
5LZCelectron microscopy4.80O2-117[»]
5LZDelectron microscopy3.40O2-117[»]
5LZEelectron microscopy3.50O2-117[»]
5LZFelectron microscopy4.60O2-117[»]
5MDVelectron microscopy2.97O1-117[»]
5MDWelectron microscopy3.06O1-117[»]
5MDYelectron microscopy3.35O1-117[»]
5MDZelectron microscopy3.10O1-117[»]
5MGPelectron microscopy3.10O2-117[»]
5NCOelectron microscopy4.80P1-117[»]
5NP6electron microscopy3.60m2-117[»]
5NWYelectron microscopy2.93b1-117[»]
5O2Relectron microscopy3.40O2-117[»]
5U4Ielectron microscopy3.50P1-117[»]
5U9Felectron microscopy3.20171-117[»]
5U9Gelectron microscopy3.20171-117[»]
5UYKelectron microscopy3.90172-117[»]
5UYLelectron microscopy3.60172-117[»]
5UYMelectron microscopy3.20172-117[»]
5UYNelectron microscopy4.00172-117[»]
5UYPelectron microscopy3.90172-117[»]
5UYQelectron microscopy3.80172-117[»]
5WDTelectron microscopy3.00O2-117[»]
5WE4electron microscopy3.10O2-117[»]
5WE6electron microscopy3.40O2-117[»]
5WFKelectron microscopy3.40O2-117[»]
6BU8electron microscopy3.50172-117[»]
6BY1X-ray3.94CO/DO2-117[»]
6C4Ielectron microscopy3.24P1-117[»]
6ENFelectron microscopy3.20O2-117[»]
6ENJelectron microscopy3.70O2-117[»]
6ENUelectron microscopy3.10O2-117[»]
6GBZelectron microscopy3.80O2-117[»]
6GC0electron microscopy3.80O2-117[»]
6GC4electron microscopy4.30O2-117[»]
6GC8electron microscopy3.80O2-117[»]
6GWTelectron microscopy3.80O2-117[»]
6GXMelectron microscopy3.80O2-117[»]
6GXNelectron microscopy3.90O2-117[»]
6GXOelectron microscopy3.90O2-117[»]
6GXPelectron microscopy4.40O2-117[»]
6H4Nelectron microscopy3.00O2-117[»]
6H58electron microscopy7.90O/OO2-117[»]
6HRMelectron microscopy2.96O2-117[»]
6I0Yelectron microscopy3.20O2-117[»]
6I7VX-ray2.90CP/DP1-117[»]
6Q98electron microscopy4.30O1-117[»]

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

More...
SMRi
P0C018

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P0C018

<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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 17Required for binding of the 5S rRNA/L5/L18 complex to the 23S rRNA1 PublicationAdd BLAST17

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The basic N-terminus is not necessary for binding to 5S rRNA. It is however required for cooperative binding of L5 and L18 to 5S rRNA as well as for binding of the 5S rRNA/L5/L18 complex to the 23S rRNA.1 Publication

<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
COG0256 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000248742

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0C018

KEGG Orthology (KO)

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KOi
K02881

Database for complete collections of gene phylogenies

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PhylomeDBi
P0C018

Family and domain databases

HAMAP database of protein families

More...
HAMAPi
MF_01337_B Ribosomal_L18_B, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR005484 Ribosomal_L18
IPR004389 Ribosomal_L18_bac-type

The PANTHER Classification System

More...
PANTHERi
PTHR12899 PTHR12899, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00861 Ribosomal_L18p, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00060 L18_bact, 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.

P0C018-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDKKSARIRR ATRARRKLQE LGATRLVVHR TPRHIYAQVI APNGSEVLVA
60 70 80 90 100
ASTVEKAIAE QLKYTGNKDA AAAVGKAVAE RALEKGIKDV SFDRSGFQYH
110
GRVQALADAA REAGLQF
Length:117
Mass (Da):12,770
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:iCA1082FF9B5D9697
GO

<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 12769.8 Da from positions 1 - 117. 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
X01563 Genomic DNA Translation: CAA25721.1
U18997 Genomic DNA Translation: AAA58101.1
U00096 Genomic DNA Translation: AAC76329.1
AP009048 Genomic DNA Translation: BAE77987.1

Protein sequence database of the Protein Information Resource

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PIRi
A02803 R5EC18

NCBI Reference Sequences

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RefSeqi
NP_417763.1, NC_000913.3
WP_000358960.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

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EnsemblBacteriai
AAC76329; AAC76329; b3304
BAE77987; BAE77987; BAE77987

Database of genes from NCBI RefSeq genomes

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GeneIDi
29379200
947804

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW3266
eco:b3304

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.3427

<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
X01563 Genomic DNA Translation: CAA25721.1
U18997 Genomic DNA Translation: AAA58101.1
U00096 Genomic DNA Translation: AAC76329.1
AP009048 Genomic DNA Translation: BAE77987.1
PIRiA02803 R5EC18
RefSeqiNP_417763.1, NC_000913.3
WP_000358960.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00q2-117[»]
2J28electron microscopy8.00O1-117[»]
2RDOelectron microscopy9.10O1-117[»]
3BBXelectron microscopy10.00O1-117[»]
3J5Lelectron microscopy6.60O2-117[»]
3J7Zelectron microscopy3.90O1-117[»]
3J8Gelectron microscopy5.00O1-117[»]
3J9Yelectron microscopy3.90O1-117[»]
3J9Zelectron microscopy3.60LK1-117[»]
3JA1electron microscopy3.60LQ1-117[»]
3JBUelectron microscopy3.64o1-117[»]
3JBVelectron microscopy3.32o1-117[»]
3JCDelectron microscopy3.70O1-117[»]
3JCEelectron microscopy3.20O1-117[»]
3JCJelectron microscopy3.70N1-117[»]
3JCNelectron microscopy4.60O1-117[»]
4CSUelectron microscopy5.50O2-117[»]
4U1UX-ray2.95BO/DO2-117[»]
4U1VX-ray3.00BO/DO2-117[»]
4U20X-ray2.90BO/DO2-117[»]
4U24X-ray2.90BO/DO2-117[»]
4U25X-ray2.90BO/DO2-117[»]
4U26X-ray2.80BO/DO2-117[»]
4U27X-ray2.80BO/DO2-117[»]
4UY8electron microscopy3.80O2-117[»]
4V47electron microscopy12.30AM1-117[»]
4V48electron microscopy11.50AM1-117[»]
4V4HX-ray3.46BO/DO1-117[»]
4V4QX-ray3.46BO/DO1-117[»]
4V4Velectron microscopy15.00BM3-115[»]
4V4Welectron microscopy15.00BM3-115[»]
4V50X-ray3.22BO/DO1-117[»]
4V52X-ray3.21BO/DO1-117[»]
4V53X-ray3.54BO/DO1-117[»]
4V54X-ray3.30BO/DO1-117[»]
4V55X-ray4.00BO/DO1-117[»]
4V56X-ray3.93BO/DO1-117[»]
4V57X-ray3.50BO/DO1-117[»]
4V5BX-ray3.74AO/CO1-117[»]
4V5Helectron microscopy5.80BO2-117[»]
4V5YX-ray4.45BO/DO1-117[»]
4V64X-ray3.50BO/DO1-117[»]
4V65electron microscopy9.00BH1-117[»]
4V66electron microscopy9.00BH1-117[»]
4V69electron microscopy6.70BO2-117[»]
4V6CX-ray3.19BO/DO1-117[»]
4V6DX-ray3.81BO/DO1-117[»]
4V6EX-ray3.71BO/DO1-117[»]
4V6Kelectron microscopy8.25AP1-117[»]
4V6Lelectron microscopy13.20BP1-117[»]
4V6Melectron microscopy7.10BO1-117[»]
4V6Nelectron microscopy12.10AQ1-117[»]
4V6Oelectron microscopy14.70BQ1-117[»]
4V6Pelectron microscopy13.50BQ1-117[»]
4V6Qelectron microscopy11.50BQ1-117[»]
4V6Relectron microscopy11.50BQ1-117[»]
4V6Selectron microscopy13.10AQ1-117[»]
4V6Telectron microscopy8.30BO2-117[»]
4V6Velectron microscopy9.80BS1-117[»]
4V6Yelectron microscopy12.00BO1-117[»]
4V6Zelectron microscopy12.00BO1-117[»]
4V70electron microscopy17.00BO1-117[»]
4V71electron microscopy20.00BO1-117[»]
4V72electron microscopy13.00BO1-117[»]
4V73electron microscopy15.00BO1-117[»]
4V74electron microscopy17.00BO1-117[»]
4V75electron microscopy12.00BO1-117[»]
4V76electron microscopy17.00BO1-117[»]
4V77electron microscopy17.00BO1-117[»]
4V78electron microscopy20.00BO1-117[»]
4V79electron microscopy15.00BO1-117[»]
4V7Aelectron microscopy9.00BO1-117[»]
4V7Belectron microscopy6.80BO1-117[»]
4V7Celectron microscopy7.60BQ1-117[»]
4V7Delectron microscopy7.60AR1-117[»]
4V7Ielectron microscopy9.60AO1-117[»]
4V7SX-ray3.25BO/DO2-117[»]
4V7TX-ray3.19BO/DO2-117[»]
4V7UX-ray3.10BO/DO2-117[»]
4V7VX-ray3.29BO/DO2-117[»]
4V85X-ray3.20BS1-117[»]
4V89X-ray3.70BS1-117[»]
4V9CX-ray3.30BO/DO1-117[»]
4V9DX-ray3.00CO/DO2-117[»]
4V9OX-ray2.90AO/CO/EO/GO1-117[»]
4V9PX-ray2.90AO/CO/EO/GO1-117[»]
4WF1X-ray3.09BO/DO2-117[»]
4WOIX-ray3.00BO/CO1-117[»]
4WWWX-ray3.10RO/YO2-117[»]
4YBBX-ray2.10CP/DP1-117[»]
5ADYelectron microscopy4.50O1-117[»]
5AFIelectron microscopy2.90O1-117[»]
5AKAelectron microscopy5.70O1-117[»]
5GADelectron microscopy3.70P1-117[»]
5GAEelectron microscopy3.33P1-117[»]
5GAFelectron microscopy4.30P1-117[»]
5GAGelectron microscopy3.80P1-117[»]
5GAHelectron microscopy3.80P1-117[»]
5H5Uelectron microscopy3.00P1-117[»]
5IQRelectron microscopy3.00O1-117[»]
5IT8X-ray3.12CP/DP1-117[»]
5J5BX-ray2.80CP/DP1-117[»]
5J7LX-ray3.00CP/DP1-117[»]
5J88X-ray3.32CP/DP1-117[»]
5J8AX-ray3.10CP/DP1-117[»]
5J91X-ray2.96CP/DP1-117[»]
5JC9X-ray3.03CP/DP1-117[»]
5JTEelectron microscopy3.60BO1-117[»]
5JU8electron microscopy3.60BO1-117[»]
5KCRelectron microscopy3.601S1-117[»]
5KCSelectron microscopy3.901S1-117[»]
5KPSelectron microscopy3.90O1-117[»]
5KPVelectron microscopy4.10N1-117[»]
5KPWelectron microscopy3.90N1-117[»]
5KPXelectron microscopy3.90N1-117[»]
5L3Pelectron microscopy3.70S1-117[»]
5LZAelectron microscopy3.60O2-117[»]
5LZBelectron microscopy5.30O2-117[»]
5LZCelectron microscopy4.80O2-117[»]
5LZDelectron microscopy3.40O2-117[»]
5LZEelectron microscopy3.50O2-117[»]
5LZFelectron microscopy4.60O2-117[»]
5MDVelectron microscopy2.97O1-117[»]
5MDWelectron microscopy3.06O1-117[»]
5MDYelectron microscopy3.35O1-117[»]
5MDZelectron microscopy3.10O1-117[»]
5MGPelectron microscopy3.10O2-117[»]
5NCOelectron microscopy4.80P1-117[»]
5NP6electron microscopy3.60m2-117[»]
5NWYelectron microscopy2.93b1-117[»]
5O2Relectron microscopy3.40O2-117[»]
5U4Ielectron microscopy3.50P1-117[»]
5U9Felectron microscopy3.20171-117[»]
5U9Gelectron microscopy3.20171-117[»]
5UYKelectron microscopy3.90172-117[»]
5UYLelectron microscopy3.60172-117[»]
5UYMelectron microscopy3.20172-117[»]
5UYNelectron microscopy4.00172-117[»]
5UYPelectron microscopy3.90172-117[»]
5UYQelectron microscopy3.80172-117[»]
5WDTelectron microscopy3.00O2-117[»]
5WE4electron microscopy3.10O2-117[»]
5WE6electron microscopy3.40O2-117[»]
5WFKelectron microscopy3.40O2-117[»]
6BU8electron microscopy3.50172-117[»]
6BY1X-ray3.94CO/DO2-117[»]
6C4Ielectron microscopy3.24P1-117[»]
6ENFelectron microscopy3.20O2-117[»]
6ENJelectron microscopy3.70O2-117[»]
6ENUelectron microscopy3.10O2-117[»]
6GBZelectron microscopy3.80O2-117[»]
6GC0electron microscopy3.80O2-117[»]
6GC4electron microscopy4.30O2-117[»]
6GC8electron microscopy3.80O2-117[»]
6GWTelectron microscopy3.80O2-117[»]
6GXMelectron microscopy3.80O2-117[»]
6GXNelectron microscopy3.90O2-117[»]
6GXOelectron microscopy3.90O2-117[»]
6GXPelectron microscopy4.40O2-117[»]
6H4Nelectron microscopy3.00O2-117[»]
6H58electron microscopy7.90O/OO2-117[»]
6HRMelectron microscopy2.96O2-117[»]
6I0Yelectron microscopy3.20O2-117[»]
6I7VX-ray2.90CP/DP1-117[»]
6Q98electron microscopy4.30O1-117[»]
SMRiP0C018
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

ComplexPortaliCPX-3807 50S large ribosomal subunit
DIPiDIP-47908N
IntActiP0C018, 38 interactors
STRINGi511145.b3304

Proteomic databases

EPDiP0C018
jPOSTiP0C018
PaxDbiP0C018
PRIDEiP0C018

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76329; AAC76329; b3304
BAE77987; BAE77987; BAE77987
GeneIDi29379200
947804
KEGGiecj:JW3266
eco:b3304
PATRICifig|1411691.4.peg.3427

Organism-specific databases

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

More...
EchoBASEi
EB0872
EcoGeneiEG10879 rplR

Phylogenomic databases

eggNOGiCOG0256 LUCA
HOGENOMiHOG000248742
InParanoidiP0C018
KOiK02881
PhylomeDBiP0C018

Enzyme and pathway databases

BioCyciEcoCyc:EG10879-MONOMER
ECOL316407:JW3266-MONOMER
MetaCyc:EG10879-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0C018

Protein Ontology

More...
PROi
PR:P0C018

Family and domain databases

HAMAPiMF_01337_B Ribosomal_L18_B, 1 hit
InterProiView protein in InterPro
IPR005484 Ribosomal_L18
IPR004389 Ribosomal_L18_bac-type
PANTHERiPTHR12899 PTHR12899, 1 hit
PfamiView protein in Pfam
PF00861 Ribosomal_L18p, 1 hit
TIGRFAMsiTIGR00060 L18_bact, 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 nameiRL18_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: P0C018
Secondary accession number(s): P02419, Q2M6W9
<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: May 8, 2019
This is version 134 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
UniProt is an ELIXIR core data resource
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