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UniProtKB - P0ADY3 (RL14_ECOLI)

Entry version 130 (08 May 2019)
Sequence version 1 (01 Apr 1988)
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Protein

50S ribosomal protein L14

Gene

rplN

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

This protein binds directly to 23S ribosomal RNA. In the E.coli 70S ribosome it has been modeled to make two contacts with the 16S rRNA of the 30S subunit, forming part of bridges B5 and B8, connecting the 2 subunits (PubMed:12809609). Although the protein undergoes significant rotation during the transition from an initiation to and EF-G bound state, the bridges remain stable. In the 3.5 A resolved structures L14 and L19 interact and together make contact with the 16S rRNA in bridges B5 and B8 (PubMed:16272117).3 Publications
Can also interact with RsfS, in this case bridge B8 probably cannot form, and the 30S and 50S ribosomal subunits do not associate, which represses translation.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

  • large ribosomal subunit rRNA binding Source: EcoCyc
  • structural constituent of ribosome Source: GO_Central
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 functionRibonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:EG10875-MONOMER
ECOL316407:JW3272-MONOMER
MetaCyc:EG10875-MONOMER

Protein family/group databases

MoonProt database of moonlighting proteins

More...MoonProti		P0ADY3

<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 L14UniRule annotation
Alternative name(s):
Large ribosomal subunit protein uL141 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:rplNUniRule annotation
Ordered Locus Names:b3310, JW3272
<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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<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		EG10875 rplN

<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

View the complete GO annotation on QuickGO ...

<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>Mutagenesisi97T → A: Reduced RsfS binding. 1 Publication1
Mutagenesisi98R → A: Reduced RsfS binding. 1 Publication1
Mutagenesisi114K → A: Reduced RsfS binding. 1 Publication1
Mutagenesisi117S → A: No change in RsfS binding. 1 Publication1

<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_00001285401 – 12350S ribosomal protein L14Add BLAST123

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P0ADY3

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P0ADY3

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

More...PaxDbi		P0ADY3

PRoteomics IDEntifications database

More...PRIDEi		P0ADY3

<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:352727, PubMed:7556101, PubMed:2665813, PubMed:10094780, PubMed:10756104, PubMed:12809609, PubMed:16272117, PubMed:25310980, PubMed:24844575, PubMed:27934701, PubMed:27906160, PubMed:27906161). Contacts L19 (PubMed:2665813, PubMed:16272117). Forms two bridges to the 30S subunit in the 70S ribosome, contacting the 16S rRNA. Can also contact RsfS, which then probably inhibits ribosomal subunit association.12 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		852121, 1 interactor

ComplexPortal: manually curated resource of macromolecular complexes

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

Database of interacting proteins

More...DIPi		DIP-35798N

Protein interaction database and analysis system

More...IntActi		P0ADY3, 53 interactors

STRING: functional protein association networks

More...STRINGi		511145.b3310

<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

1123
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
1ML5electron microscopy14.00n1-122[»]
2J28electron microscopy8.00K2-122[»]
2RDOelectron microscopy9.10K1-123[»]
3BBXelectron microscopy10.00K1-123[»]
3IY9electron microscopy14.10K2-122[»]
3IZZelectron microscopy10.80G2-122[»]
3J5Lelectron microscopy6.60K1-122[»]
3J7Zelectron microscopy3.90K1-123[»]
3J8Gelectron microscopy5.00K1-123[»]
3J9Yelectron microscopy3.90K1-123[»]
3J9Zelectron microscopy3.60LG1-123[»]
3JA1electron microscopy3.60LM1-123[»]
3JBUelectron microscopy3.64k1-123[»]
3JBVelectron microscopy3.32k1-123[»]
3JCDelectron microscopy3.70K1-123[»]
3JCEelectron microscopy3.20K1-123[»]
3JCJelectron microscopy3.70J1-123[»]
3JCNelectron microscopy4.60K1-123[»]
487Delectron microscopy7.50M1-122[»]
4CSUelectron microscopy5.50K1-123[»]
4U1UX-ray2.95BK/DK1-122[»]
4U1VX-ray3.00BK/DK1-122[»]
4U20X-ray2.90BK/DK1-122[»]
4U24X-ray2.90BK/DK1-122[»]
4U25X-ray2.90BK/DK1-122[»]
4U26X-ray2.80BK/DK1-122[»]
4U27X-ray2.80BK/DK1-122[»]
4UY8electron microscopy3.80K1-122[»]
4V47electron microscopy12.30AI1-123[»]
4V48electron microscopy11.50AI1-123[»]
4V4HX-ray3.46BK/DK1-123[»]
4V4QX-ray3.46BK/DK1-123[»]
4V4Velectron microscopy15.00BI2-123[»]
4V4Welectron microscopy15.00BI2-123[»]
4V50X-ray3.22BK/DK1-123[»]
4V52X-ray3.21BK/DK1-123[»]
4V53X-ray3.54BK/DK1-123[»]
4V54X-ray3.30BK/DK1-123[»]
4V55X-ray4.00BK/DK1-123[»]
4V56X-ray3.93BK/DK1-123[»]
4V57X-ray3.50BK/DK1-123[»]
4V5BX-ray3.74AK/CK1-123[»]
4V5Helectron microscopy5.80BK1-121[»]
4V5YX-ray4.45BK/DK1-123[»]
4V64X-ray3.50BK/DK1-123[»]
4V65electron microscopy9.00BD1-123[»]
4V66electron microscopy9.00BD1-123[»]
4V69electron microscopy6.70BK2-122[»]
4V6CX-ray3.19BK/DK1-123[»]
4V6DX-ray3.81BK/DK1-123[»]
4V6EX-ray3.71BK/DK1-123[»]
4V6Kelectron microscopy8.25AL1-123[»]
4V6Lelectron microscopy13.20BL1-123[»]
4V6Melectron microscopy7.10BK1-123[»]
4V6Nelectron microscopy12.10AM1-123[»]
4V6Oelectron microscopy14.70BM1-123[»]
4V6Pelectron microscopy13.50BM1-123[»]
4V6Qelectron microscopy11.50BM1-123[»]
4V6Relectron microscopy11.50BM1-123[»]
4V6Selectron microscopy13.10AM1-123[»]
4V6Telectron microscopy8.30BK1-122[»]
4V6Velectron microscopy9.80BO1-123[»]
4V6Yelectron microscopy12.00BK1-122[»]
4V6Zelectron microscopy12.00BK1-122[»]
4V70electron microscopy17.00BK1-122[»]
4V71electron microscopy20.00BK1-122[»]
4V72electron microscopy13.00BK1-122[»]
4V73electron microscopy15.00BK1-122[»]
4V74electron microscopy17.00BK1-122[»]
4V75electron microscopy12.00BK1-122[»]
4V76electron microscopy17.00BK1-122[»]
4V77electron microscopy17.00BK1-122[»]
4V78electron microscopy20.00BK1-122[»]
4V79electron microscopy15.00BK1-122[»]
4V7Aelectron microscopy9.00BK1-122[»]
4V7Belectron microscopy6.80BK1-123[»]
4V7Celectron microscopy7.60BM1-123[»]
4V7Delectron microscopy7.60AN1-123[»]
4V7Ielectron microscopy9.60AK1-123[»]
4V7SX-ray3.25BK/DK1-122[»]
4V7TX-ray3.19BK/DK1-122[»]
4V7UX-ray3.10BK/DK1-122[»]
4V7VX-ray3.29BK/DK1-122[»]
4V85X-ray3.20BO1-123[»]
4V89X-ray3.70BO1-123[»]
4V9CX-ray3.30BK/DK1-123[»]
4V9DX-ray3.00CK/DK1-122[»]
4V9OX-ray2.90AK/CK/EK/GK1-123[»]
4V9PX-ray2.90AK/CK/EK/GK1-123[»]
4WF1X-ray3.09BK/DK1-122[»]
4WOIX-ray3.00BK/CK1-123[»]
4WWWX-ray3.10RK/YK1-122[»]
4YBBX-ray2.10CL/DL1-123[»]
5ADYelectron microscopy4.50K1-123[»]
5AFIelectron microscopy2.90K1-123[»]
5AKAelectron microscopy5.70K1-123[»]
5GADelectron microscopy3.70L1-123[»]
5GAEelectron microscopy3.33L1-123[»]
5GAFelectron microscopy4.30L1-123[»]
5GAGelectron microscopy3.80L1-123[»]
5GAHelectron microscopy3.80L1-123[»]
5H5Uelectron microscopy3.00L1-123[»]
5IQRelectron microscopy3.00K1-123[»]
5IT8X-ray3.12CL/DL1-123[»]
5J5BX-ray2.80CL/DL1-123[»]
5J7LX-ray3.00CL/DL1-123[»]
5J88X-ray3.32CL/DL1-123[»]
5J8AX-ray3.10CL/DL1-123[»]
5J91X-ray2.96CL/DL1-123[»]
5JC9X-ray3.03CL/DL1-123[»]
5JTEelectron microscopy3.60BK1-123[»]
5JU8electron microscopy3.60BK1-123[»]
5KCRelectron microscopy3.601O1-123[»]
5KCSelectron microscopy3.901O1-123[»]
5KPSelectron microscopy3.90K1-123[»]
5KPVelectron microscopy4.10J1-123[»]
5KPWelectron microscopy3.90J1-123[»]
5KPXelectron microscopy3.90J1-123[»]
5L3Pelectron microscopy3.70O1-123[»]
5LZAelectron microscopy3.60K1-122[»]
5LZBelectron microscopy5.30K1-122[»]
5LZCelectron microscopy4.80K1-122[»]
5LZDelectron microscopy3.40K1-122[»]
5LZEelectron microscopy3.50K1-122[»]
5LZFelectron microscopy4.60K1-122[»]
5MDVelectron microscopy2.97K1-123[»]
5MDWelectron microscopy3.06K1-123[»]
5MDYelectron microscopy3.35K1-123[»]
5MDZelectron microscopy3.10K1-123[»]
5MGPelectron microscopy3.10K1-122[»]
5NCOelectron microscopy4.80L1-123[»]
5NP6electron microscopy3.60i1-122[»]
5NWYelectron microscopy2.93X1-123[»]
5O2Relectron microscopy3.40K1-122[»]
5U4Ielectron microscopy3.50L1-123[»]
5U9Felectron microscopy3.20131-123[»]
5U9Gelectron microscopy3.20131-123[»]
5UYKelectron microscopy3.90131-122[»]
5UYLelectron microscopy3.60131-122[»]
5UYMelectron microscopy3.20131-122[»]
5UYNelectron microscopy4.00131-122[»]
5UYPelectron microscopy3.90131-122[»]
5UYQelectron microscopy3.80131-122[»]
5WDTelectron microscopy3.00K1-122[»]
5WE4electron microscopy3.10K1-122[»]
5WFKelectron microscopy3.40K1-122[»]
6BU8electron microscopy3.50131-122[»]
6BY1X-ray3.94CK/DK1-122[»]
6C4Ielectron microscopy3.24L1-123[»]
6ENFelectron microscopy3.20K1-122[»]
6ENJelectron microscopy3.70K1-122[»]
6ENUelectron microscopy3.10K1-122[»]
6GBZelectron microscopy3.80K1-122[»]
6GC0electron microscopy3.80K1-122[»]
6GC4electron microscopy4.30K1-122[»]
6GC6electron microscopy4.30K1-122[»]
6GC7electron microscopy4.30K1-122[»]
6GC8electron microscopy3.80K1-122[»]
6GWTelectron microscopy3.80K1-122[»]
6GXMelectron microscopy3.80K1-122[»]
6GXNelectron microscopy3.90K1-122[»]
6GXOelectron microscopy3.90K1-122[»]
6GXPelectron microscopy4.40K1-122[»]
6H4Nelectron microscopy3.00K1-122[»]
6H58electron microscopy7.90K/KK1-122[»]
6HRMelectron microscopy2.96K1-123[»]
6I0Yelectron microscopy3.20K1-122[»]
6I7VX-ray2.90CL/DL1-123[»]
6Q98electron microscopy4.30K1-123[»]

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

More...SMRi		P0ADY3

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		P0ADY3

<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

Belongs to the universal ribosomal protein uL14 family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4108UNN Bacteria
COG0093 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000183702

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0ADY3

KEGG Orthology (KO)

More...KOi		K02874

Database for complete collections of gene phylogenies

More...PhylomeDBi		P0ADY3

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.40.150.20, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_01367 Ribosomal_L14, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR036853 Ribosomal_L14_sf
IPR000218 Ribosomal_L14P
IPR005745 Ribosomal_L14P_bac-type
IPR019972 Ribosomal_L14P_CS

The PANTHER Classification System

More...PANTHERi		PTHR11761 PTHR11761, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00238 Ribosomal_L14, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM01374 Ribosomal_L14, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50193 SSF50193, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01067 rplN_bact, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00049 RIBOSOMAL_L14, 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.

P0ADY3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MIQEQTMLNV ADNSGARRVM CIKVLGGSHR RYAGVGDIIK ITIKEAIPRG 
        60         70         80         90        100
KVKKGDVLKA VVVRTKKGVR RPDGSVIRFD GNACVLLNNN SEQPIGTRIF 
       110        120 
GPVTRELRSE KFMKIISLAP EVL
Length:123
Mass (Da):13,541
Last modified:April 1, 1988 - 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:i192ACB1623979510
GO

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 conflicti63Missing AA sequence (PubMed:352727).Curated1
Sequence conflicti84C → S AA sequence (PubMed:352727).Curated1
Sequence conflicti90 – 91NS → TD AA sequence (PubMed:352727).Curated2
Sequence conflicti97Missing AA sequence (PubMed:352727).Curated1
Sequence conflicti115I → L AA sequence (PubMed:352727).Curated1
Sequence conflicti123Missing AA sequence (PubMed:352727).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 13540.2 Da from positions 1 - 123. Determined by MALDI. 1 Publication

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
X01563 Genomic DNA Translation: CAA25715.1
U18997 Genomic DNA Translation: AAA58107.1
U00096 Genomic DNA Translation: AAC76335.1
AP009048 Genomic DNA Translation: BAE77981.1
V00357 Genomic DNA Translation: CAA23653.1

Protein sequence database of the Protein Information Resource

More...PIRi		A65124 R5EC14

NCBI Reference Sequences

More...RefSeqi		NP_417769.1, NC_000913.3
WP_000613955.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC76335; AAC76335; b3310
BAE77981; BAE77981; BAE77981

Database of genes from NCBI RefSeq genomes

More...GeneIDi		947809

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW3272
eco:b3310

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.3421

<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: CAA25715.1
U18997 Genomic DNA Translation: AAA58107.1
U00096 Genomic DNA Translation: AAC76335.1
AP009048 Genomic DNA Translation: BAE77981.1
V00357 Genomic DNA Translation: CAA23653.1
PIRiA65124 R5EC14
RefSeqiNP_417769.1, NC_000913.3
WP_000613955.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00n1-122[»]
2J28electron microscopy8.00K2-122[»]
2RDOelectron microscopy9.10K1-123[»]
3BBXelectron microscopy10.00K1-123[»]
3IY9electron microscopy14.10K2-122[»]
3IZZelectron microscopy10.80G2-122[»]
3J5Lelectron microscopy6.60K1-122[»]
3J7Zelectron microscopy3.90K1-123[»]
3J8Gelectron microscopy5.00K1-123[»]
3J9Yelectron microscopy3.90K1-123[»]
3J9Zelectron microscopy3.60LG1-123[»]
3JA1electron microscopy3.60LM1-123[»]
3JBUelectron microscopy3.64k1-123[»]
3JBVelectron microscopy3.32k1-123[»]
3JCDelectron microscopy3.70K1-123[»]
3JCEelectron microscopy3.20K1-123[»]
3JCJelectron microscopy3.70J1-123[»]
3JCNelectron microscopy4.60K1-123[»]
487Delectron microscopy7.50M1-122[»]
4CSUelectron microscopy5.50K1-123[»]
4U1UX-ray2.95BK/DK1-122[»]
4U1VX-ray3.00BK/DK1-122[»]
4U20X-ray2.90BK/DK1-122[»]
4U24X-ray2.90BK/DK1-122[»]
4U25X-ray2.90BK/DK1-122[»]
4U26X-ray2.80BK/DK1-122[»]
4U27X-ray2.80BK/DK1-122[»]
4UY8electron microscopy3.80K1-122[»]
4V47electron microscopy12.30AI1-123[»]
4V48electron microscopy11.50AI1-123[»]
4V4HX-ray3.46BK/DK1-123[»]
4V4QX-ray3.46BK/DK1-123[»]
4V4Velectron microscopy15.00BI2-123[»]
4V4Welectron microscopy15.00BI2-123[»]
4V50X-ray3.22BK/DK1-123[»]
4V52X-ray3.21BK/DK1-123[»]
4V53X-ray3.54BK/DK1-123[»]
4V54X-ray3.30BK/DK1-123[»]
4V55X-ray4.00BK/DK1-123[»]
4V56X-ray3.93BK/DK1-123[»]
4V57X-ray3.50BK/DK1-123[»]
4V5BX-ray3.74AK/CK1-123[»]
4V5Helectron microscopy5.80BK1-121[»]
4V5YX-ray4.45BK/DK1-123[»]
4V64X-ray3.50BK/DK1-123[»]
4V65electron microscopy9.00BD1-123[»]
4V66electron microscopy9.00BD1-123[»]
4V69electron microscopy6.70BK2-122[»]
4V6CX-ray3.19BK/DK1-123[»]
4V6DX-ray3.81BK/DK1-123[»]
4V6EX-ray3.71BK/DK1-123[»]
4V6Kelectron microscopy8.25AL1-123[»]
4V6Lelectron microscopy13.20BL1-123[»]
4V6Melectron microscopy7.10BK1-123[»]
4V6Nelectron microscopy12.10AM1-123[»]
4V6Oelectron microscopy14.70BM1-123[»]
4V6Pelectron microscopy13.50BM1-123[»]
4V6Qelectron microscopy11.50BM1-123[»]
4V6Relectron microscopy11.50BM1-123[»]
4V6Selectron microscopy13.10AM1-123[»]
4V6Telectron microscopy8.30BK1-122[»]
4V6Velectron microscopy9.80BO1-123[»]
4V6Yelectron microscopy12.00BK1-122[»]
4V6Zelectron microscopy12.00BK1-122[»]
4V70electron microscopy17.00BK1-122[»]
4V71electron microscopy20.00BK1-122[»]
4V72electron microscopy13.00BK1-122[»]
4V73electron microscopy15.00BK1-122[»]
4V74electron microscopy17.00BK1-122[»]
4V75electron microscopy12.00BK1-122[»]
4V76electron microscopy17.00BK1-122[»]
4V77electron microscopy17.00BK1-122[»]
4V78electron microscopy20.00BK1-122[»]
4V79electron microscopy15.00BK1-122[»]
4V7Aelectron microscopy9.00BK1-122[»]
4V7Belectron microscopy6.80BK1-123[»]
4V7Celectron microscopy7.60BM1-123[»]
4V7Delectron microscopy7.60AN1-123[»]
4V7Ielectron microscopy9.60AK1-123[»]
4V7SX-ray3.25BK/DK1-122[»]
4V7TX-ray3.19BK/DK1-122[»]
4V7UX-ray3.10BK/DK1-122[»]
4V7VX-ray3.29BK/DK1-122[»]
4V85X-ray3.20BO1-123[»]
4V89X-ray3.70BO1-123[»]
4V9CX-ray3.30BK/DK1-123[»]
4V9DX-ray3.00CK/DK1-122[»]
4V9OX-ray2.90AK/CK/EK/GK1-123[»]
4V9PX-ray2.90AK/CK/EK/GK1-123[»]
4WF1X-ray3.09BK/DK1-122[»]
4WOIX-ray3.00BK/CK1-123[»]
4WWWX-ray3.10RK/YK1-122[»]
4YBBX-ray2.10CL/DL1-123[»]
5ADYelectron microscopy4.50K1-123[»]
5AFIelectron microscopy2.90K1-123[»]
5AKAelectron microscopy5.70K1-123[»]
5GADelectron microscopy3.70L1-123[»]
5GAEelectron microscopy3.33L1-123[»]
5GAFelectron microscopy4.30L1-123[»]
5GAGelectron microscopy3.80L1-123[»]
5GAHelectron microscopy3.80L1-123[»]
5H5Uelectron microscopy3.00L1-123[»]
5IQRelectron microscopy3.00K1-123[»]
5IT8X-ray3.12CL/DL1-123[»]
5J5BX-ray2.80CL/DL1-123[»]
5J7LX-ray3.00CL/DL1-123[»]
5J88X-ray3.32CL/DL1-123[»]
5J8AX-ray3.10CL/DL1-123[»]
5J91X-ray2.96CL/DL1-123[»]
5JC9X-ray3.03CL/DL1-123[»]
5JTEelectron microscopy3.60BK1-123[»]
5JU8electron microscopy3.60BK1-123[»]
5KCRelectron microscopy3.601O1-123[»]
5KCSelectron microscopy3.901O1-123[»]
5KPSelectron microscopy3.90K1-123[»]
5KPVelectron microscopy4.10J1-123[»]
5KPWelectron microscopy3.90J1-123[»]
5KPXelectron microscopy3.90J1-123[»]
5L3Pelectron microscopy3.70O1-123[»]
5LZAelectron microscopy3.60K1-122[»]
5LZBelectron microscopy5.30K1-122[»]
5LZCelectron microscopy4.80K1-122[»]
5LZDelectron microscopy3.40K1-122[»]
5LZEelectron microscopy3.50K1-122[»]
5LZFelectron microscopy4.60K1-122[»]
5MDVelectron microscopy2.97K1-123[»]
5MDWelectron microscopy3.06K1-123[»]
5MDYelectron microscopy3.35K1-123[»]
5MDZelectron microscopy3.10K1-123[»]
5MGPelectron microscopy3.10K1-122[»]
5NCOelectron microscopy4.80L1-123[»]
5NP6electron microscopy3.60i1-122[»]
5NWYelectron microscopy2.93X1-123[»]
5O2Relectron microscopy3.40K1-122[»]
5U4Ielectron microscopy3.50L1-123[»]
5U9Felectron microscopy3.20131-123[»]
5U9Gelectron microscopy3.20131-123[»]
5UYKelectron microscopy3.90131-122[»]
5UYLelectron microscopy3.60131-122[»]
5UYMelectron microscopy3.20131-122[»]
5UYNelectron microscopy4.00131-122[»]
5UYPelectron microscopy3.90131-122[»]
5UYQelectron microscopy3.80131-122[»]
5WDTelectron microscopy3.00K1-122[»]
5WE4electron microscopy3.10K1-122[»]
5WFKelectron microscopy3.40K1-122[»]
6BU8electron microscopy3.50131-122[»]
6BY1X-ray3.94CK/DK1-122[»]
6C4Ielectron microscopy3.24L1-123[»]
6ENFelectron microscopy3.20K1-122[»]
6ENJelectron microscopy3.70K1-122[»]
6ENUelectron microscopy3.10K1-122[»]
6GBZelectron microscopy3.80K1-122[»]
6GC0electron microscopy3.80K1-122[»]
6GC4electron microscopy4.30K1-122[»]
6GC6electron microscopy4.30K1-122[»]
6GC7electron microscopy4.30K1-122[»]
6GC8electron microscopy3.80K1-122[»]
6GWTelectron microscopy3.80K1-122[»]
6GXMelectron microscopy3.80K1-122[»]
6GXNelectron microscopy3.90K1-122[»]
6GXOelectron microscopy3.90K1-122[»]
6GXPelectron microscopy4.40K1-122[»]
6H4Nelectron microscopy3.00K1-122[»]
6H58electron microscopy7.90K/KK1-122[»]
6HRMelectron microscopy2.96K1-123[»]
6I0Yelectron microscopy3.20K1-122[»]
6I7VX-ray2.90CL/DL1-123[»]
6Q98electron microscopy4.30K1-123[»]
SMRiP0ADY3
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi852121, 1 interactor
ComplexPortaliCPX-3807 50S large ribosomal subunit
DIPiDIP-35798N
IntActiP0ADY3, 53 interactors
STRINGi511145.b3310

Protein family/group databases

MoonProtiP0ADY3

Proteomic databases

EPDiP0ADY3
jPOSTiP0ADY3
PaxDbiP0ADY3
PRIDEiP0ADY3

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76335; AAC76335; b3310
BAE77981; BAE77981; BAE77981
GeneIDi947809
KEGGiecj:JW3272
eco:b3310
PATRICifig|1411691.4.peg.3421

Organism-specific databases

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

More...EchoBASEi		EB0868
EcoGeneiEG10875 rplN

Phylogenomic databases

eggNOGiENOG4108UNN Bacteria
COG0093 LUCA
HOGENOMiHOG000183702
InParanoidiP0ADY3
KOiK02874
PhylomeDBiP0ADY3

Enzyme and pathway databases

BioCyciEcoCyc:EG10875-MONOMER
ECOL316407:JW3272-MONOMER
MetaCyc:EG10875-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0ADY3

Protein Ontology

More...PROi		PR:P0ADY3

Family and domain databases

Gene3Di2.40.150.20, 1 hit
HAMAPiMF_01367 Ribosomal_L14, 1 hit
InterProiView protein in InterPro
IPR036853 Ribosomal_L14_sf
IPR000218 Ribosomal_L14P
IPR005745 Ribosomal_L14P_bac-type
IPR019972 Ribosomal_L14P_CS
PANTHERiPTHR11761 PTHR11761, 1 hit
PfamiView protein in Pfam
PF00238 Ribosomal_L14, 1 hit
SMARTiView protein in SMART
SM01374 Ribosomal_L14, 1 hit
SUPFAMiSSF50193 SSF50193, 1 hit
TIGRFAMsiTIGR01067 rplN_bact, 1 hit
PROSITEiView protein in PROSITE
PS00049 RIBOSOMAL_L14, 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 nameiRL14_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: P0ADY3
Secondary accession number(s): P02411, Q2M6X5
<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: April 1, 1988
Last modified: May 8, 2019
This is version 130 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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