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UniProtKB - P0A7K2 (RL7_ECOLI)

Entry version 134 (11 Dec 2019)
Sequence version 2 (23 Jan 2007)
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Protein

50S ribosomal protein L7/L12

Gene

rplL

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

The binding site for several of the GTPase factors involved in protein synthesis (IF-2, EF-Tu, EF-G and RF3). Is thus essential for accurate translation. Deletion of 1 of the L12 dimers from the ribosome (by deleting the binding site on L10) leads to decreased IF-2 association with the 70S ribosome and decreased stimulation of the GTPase activity of EF-G.2 Publications

Miscellaneous

Ribosomal protein L8 appears to be an aggregate of ribosomal proteins L7/L12 and L10.1 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

Complete GO annotation on QuickGO ...

GO - Biological processi

  • translation Source: CAFA
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

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:EG10873-MONOMER
ECOL316407:JW3949-MONOMER
MetaCyc:EG10873-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 L7/L12UniRule annotation
Alternative name(s):
L8
Large ribosomal subunit protein bL121 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:rplLUniRule annotation
Ordered Locus Names:b3986, JW3949
<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

<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

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>Mutagenesisi66K → A: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. 1 Publication1
Mutagenesisi67V → D: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. 1 Publication1
Mutagenesisi70I → A: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. 1 Publication1
Mutagenesisi71K → A: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. 1 Publication1
Mutagenesisi74R → M: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. 1 Publication1
Mutagenesisi85K → A: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. 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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved5 Publications
<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_00001575282 – 12150S ribosomal protein L7/L12Add BLAST120

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserine; in L71 Publication1
Modified residuei82N6-methyllysine; partial1 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

Acetylation of Ser-2 converts L12 to L7.
Lys-82 was found to be 50% monomethylated.1 Publication

Keywords - PTMi

Acetylation, Methylation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P0A7K2

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P0A7K2

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

More...PaxDbi		P0A7K2

PRoteomics IDEntifications database

More...PRIDEi		P0A7K2

2D gel databases

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

More...SWISS-2DPAGEi		P0A7K2

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P0A7K2

<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

Homodimer. Part of the 50S ribosomal subunit; present in 4 copies per ribosome. L7/L12 forms dimers with an elongated shape. Two dimers associate with a copy of L10 to form part of the ribosomal stalk (called L8). The ribosomal stalk helps the ribosome interact with GTP-bound translation factors.

Forms a pentameric L10(L12)2(L12)2 complex, where L10 forms an elongated spine to which 2 L12 dimers bind in a sequential fashion.

2 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

Show more details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		852783, 3 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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

Database of interacting proteins

More...DIPi		DIP-36009N

Protein interaction database and analysis system

More...IntActi		P0A7K2, 135 interactors

STRING: functional protein association networks

More...STRINGi		511145.b3986

<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

1121
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P0A7K2

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P0A7K2

<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>Regioni54 – 121Required for recruitment of EF-Tu and EF-G, and for EF-Tu and EF-G-promoted GTP hydrolysisAdd BLAST68

<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 bacterial ribosomal protein bL12 family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4105KBC Bacteria
COG0222 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000248813

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0A7K2

KEGG Orthology (KO)

More...KOi		K02935

Database for complete collections of gene phylogenies

More...PhylomeDBi		P0A7K2

Family and domain databases

Conserved Domains Database

More...CDDi		cd00387 Ribosomal_L7_L12, 1 hit

Database of protein disorder

More...DisProti		DP01650

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.20.5.710, 1 hit
3.30.1390.10, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00368 Ribosomal_L7_L12, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR000206 Ribosomal_L7/12
IPR014719 Ribosomal_L7/12_C/ClpS-like
IPR013823 Ribosomal_L7/L12_C
IPR008932 Ribosomal_L7/L12_oligo
IPR036235 Ribosomal_L7/L12_oligo_N_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00542 Ribosomal_L12, 1 hit
PF16320 Ribosomal_L12_N, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48300 SSF48300, 1 hit
SSF54736 SSF54736, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00855 L12, 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>. The information is filed in different subsections. The current subsections and their content are listed below:<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.

P0A7K2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSITKDQIIE AVAAMSVMDV VELISAMEEK FGVSAAAAVA VAAGPVEAAE 
        60         70         80         90        100
EKTEFDVILK AAGANKVAVI KAVRGATGLG LKEAKDLVES APAALKEGVS 
       110        120 
KDDAEALKKA LEEAGAEVEV K
Length:121
Mass (Da):12,295
Last modified:January 23, 2007 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i08B051A0CDAA527E
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 conflicti6D → F 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 12206.7 Da. Determined by MALDI. Non-methylated.1 Publication
Molecular mass is 66643±13 Da. Determined by ESI. Isolated L10(L12)4.1 Publication
Molecular mass is 12223±1 Da. Determined by ESI. L7, acetylated Ser-2.1 Publication
Molecular mass is 12164±1 Da. Determined by ESI. L12, unacetylated.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
V00339 Genomic DNA Translation: CAA23624.1
M38301 Genomic DNA Translation: AAA24573.1
U00006 Genomic DNA Translation: AAC43084.1
U00096 Genomic DNA Translation: AAC76960.1
AP009048 Genomic DNA Translation: BAE77334.1

Protein sequence database of the Protein Information Resource

More...PIRi		S12575 R5EC7

NCBI Reference Sequences

More...RefSeqi		NP_418413.1, NC_000913.3
WP_000028878.1, NZ_STEB01000045.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC76960; AAC76960; b3986
BAE77334; BAE77334; BAE77334

Database of genes from NCBI RefSeq genomes

More...GeneIDi		948489

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW3949
eco:b3986

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.2726

<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
V00339 Genomic DNA Translation: CAA23624.1
M38301 Genomic DNA Translation: AAA24573.1
U00006 Genomic DNA Translation: AAC43084.1
U00096 Genomic DNA Translation: AAC76960.1
AP009048 Genomic DNA Translation: BAE77334.1
PIRiS12575 R5EC7
RefSeqiNP_418413.1, NC_000913.3
WP_000028878.1, NZ_STEB01000045.1

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
1CTFX-ray1.70A48-121[»]
1RQSNMR-A48-121[»]
1RQTNMR-A/B2-38[»]
1RQUNMR-A/B2-121[»]
1RQVNMR-A/B2-121[»]
2BCWelectron microscopy11.20B54-121[»]
3J7Zelectron microscopy3.9061-121[»]
4UY8electron microscopy3.8062-31[»]
4V4Velectron microscopy15.00B3/B53-121[»]
4V4Welectron microscopy15.00B3/B53-121[»]
4V5Melectron microscopy7.80BL1-121[»]
4V5Nelectron microscopy7.60BL1-121[»]
4V7Belectron microscopy6.80B61-121[»]
4V7Delectron microscopy7.60AL2-121[»]
4V85X-ray3.20BJ/BK/BL/BM1-121[»]
4V89X-ray3.70BJ/BK/BL/BM1-121[»]
4V9OX-ray2.90A61-121[»]
5KCSelectron microscopy3.901L1-121[»]
6I0Yelectron microscopy3.2061-121[»]
SMRiP0A7K2
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi852783, 3 interactors
ComplexPortaliCPX-3807 50S large ribosomal subunit
DIPiDIP-36009N
IntActiP0A7K2, 135 interactors
STRINGi511145.b3986

PTM databases

iPTMnetiP0A7K2

2D gel databases

SWISS-2DPAGEiP0A7K2

Proteomic databases

EPDiP0A7K2
jPOSTiP0A7K2
PaxDbiP0A7K2
PRIDEiP0A7K2

Genome annotation databases

EnsemblBacteriaiAAC76960; AAC76960; b3986
BAE77334; BAE77334; BAE77334
GeneIDi948489
KEGGiecj:JW3949
eco:b3986
PATRICifig|1411691.4.peg.2726

Organism-specific databases

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

More...EchoBASEi		EB0866

Phylogenomic databases

eggNOGiENOG4105KBC Bacteria
COG0222 LUCA
HOGENOMiHOG000248813
InParanoidiP0A7K2
KOiK02935
PhylomeDBiP0A7K2

Enzyme and pathway databases

BioCyciEcoCyc:EG10873-MONOMER
ECOL316407:JW3949-MONOMER
MetaCyc:EG10873-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0A7K2

Protein Ontology

More...PROi		PR:P0A7K2

Family and domain databases

CDDicd00387 Ribosomal_L7_L12, 1 hit
DisProtiDP01650
Gene3Di1.20.5.710, 1 hit
3.30.1390.10, 1 hit
HAMAPiMF_00368 Ribosomal_L7_L12, 1 hit
InterProiView protein in InterPro
IPR000206 Ribosomal_L7/12
IPR014719 Ribosomal_L7/12_C/ClpS-like
IPR013823 Ribosomal_L7/L12_C
IPR008932 Ribosomal_L7/L12_oligo
IPR036235 Ribosomal_L7/L12_oligo_N_sf
PfamiView protein in Pfam
PF00542 Ribosomal_L12, 1 hit
PF16320 Ribosomal_L12_N, 1 hit
SUPFAMiSSF48300 SSF48300, 1 hit
SSF54736 SSF54736, 1 hit
TIGRFAMsiTIGR00855 L12, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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 nameiRL7_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: P0A7K2
Secondary accession number(s): P02392, Q2M8S2
<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: January 23, 2007
Last modified: December 11, 2019
This is version 134 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation 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, 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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