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Entry version 125 (07 Apr 2021)
Sequence version 2 (23 Jan 2007)
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Protein

30S ribosome-binding factor

Gene

rbfA

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

One of at least 4 proteins (Era, RbfA, RimM and RsgA/YjeQ) that assist in the late maturation steps of the functional core of the 30S subunit. Essential for efficient processing of pre-16S rRNA (PubMed:9422595, PubMed:12963368, PubMed:12628255). Probably part of the 30S subunit prior to or during the final step in the processing of 16S free 30S ribosomal subunits. Probably interacts with the 5'-terminal helix region of 16S rRNA (PubMed:7535280). Has affinity for free ribosomal 30S subunits but not for 70S ribosomes (PubMed:7535280, PubMed:12963368). Overexpression suppresses a cold-sensitive C23U 16S rRNA mutation (PubMed:7535280). Overexpression decreases the lag time following cold-shock by about half, leading to faster adaptation and increased protein synthesis (PubMed:8898389). Overexpression also partially suppresses a rimM deletion mutant and partially rescues its 16S rRNA processing deficiency (PubMed:9422595). Its function overlaps that of Era in ribosome biogenesis (PubMed:16825789). A number of RbfA mutants suppress RsgA/YjeQ deletions, in all cases less RbfA is bound to the 30S ribosome (PubMed:21102555). Released from 30S ribosomes by RsgA; stimulates the ribosome-associated GTPase activity of RsgA (PubMed:21102555).7 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

  • ribosomal small subunit binding Source: EcoCyc

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

Biological processRibosome biogenesis, Stress response

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG11178-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%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
30S ribosome-binding factor1 Publication
Alternative name(s):
Protein P15B1 Publication
Ribosome-binding factor A1 PublicationUniRule annotation
Short name:
RbfA1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:rbfA1 PublicationUniRule annotation
Synonyms:P15B1 Publication, yhbB
Ordered Locus Names:b3167, JW3136
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

Keywords - Cellular componenti

Cytoplasm

<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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Severe growth defect at 26 and 30 degrees Celsius, with poor growth at 37 and 42 degrees; has decreased amounts of 70S ribosomes and polysomes and increased amounts of 30S and 50S subunits (PubMed:7535280). Results in a constitutive induction of the cold-shock response; increased cold-shock and ribosomal protein synthesis continues in the presence of general translation inhibition (PubMed:8898389). Less efficient processing of 5' end of 16S rRNA, increased levels of precursor 17S rRNA; effect is more pronounced in cold-shocked cells (PubMed:9422595, PubMed:12963368). Both phenotypes are partially suppressed by overexpression of Era and completely suppressed by overexpression of Era-delta 'Ala-40-Gly-49' mutation (PubMed:12753192). Double rbfA-rsgA deletion mutants have the same phenotype as single mutants (PubMed:21102555).6 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi10R → H: Suppresses growth defects and restores maturation of the 30S subunit of an rsgA deletion. Decreased affinity for 30S ribosomes. 1 Publication1
Mutagenesisi30P → L: Suppresses growth defects and restores maturation of the 30S subunit of an rsgA deletion. Decreased affinity for 30S ribosomes. 1 Publication1
Mutagenesisi77G → D: Suppresses growth defects and restores maturation of the 30S subunit of an rsgA deletion. Decreased affinity for 30S ribosomes. 1 Publication1
Mutagenesisi84G → E: Suppresses growth defects and restores maturation of the 30S subunit of an rsgA deletion. Decreased affinity for 30S ribosomes. 1 Publication1
Mutagenesisi100D → G: Suppresses growth defects and restores maturation of the 30S subunit of an rsgA deletion. Decreased affinity for 30S ribosomes. 1 Publication1
Mutagenesisi109 – 133Missing : Complements small colony and slow growth phenotype of the deletion mutant at 15 degrees Celsius, growth is not quite wild-type. Restores pre-16S rRNA processing but does not suppress cold-sensitive C23U 16S rRNA mutation. 2 PublicationsAdd BLAST25
Mutagenesisi112 – 133LVTSV…DSKED → GDQRGQT: Suppresses growth defects and restores maturation of the 30S subunit of an rsgA deletion. Decreased affinity for 30S ribosomes. 1 PublicationAdd BLAST22
Mutagenesisi120D → N: Suppresses growth defects and restores maturation of the 30S subunit of an rsgA deletion. Decreased affinity for 30S ribosomes. 1 Publication1
Mutagenesisi122 – 133Missing : Suppresses growth defects and restores maturation of the 30S subunit of an rsgA deletion. Decreased affinity for 30S ribosomes. 1 PublicationAdd BLAST12

<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%5Fprocessing%5Fsection">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 methionineiRemoved1 Publication
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001026582 – 13330S ribosome-binding factorAdd BLAST132

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0A7G2

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

More...
PaxDbi
P0A7G2

PRoteomics IDEntifications database

More...
PRIDEi
P0A7G2

2D gel databases

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

More...
SWISS-2DPAGEi
P0A7G2

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Fairly strongly expressed in maxicells, part of the metY operon that extends to pnp (at protein level) (PubMed:2849753). Induced by cold shock (42 to 15 degrees Celsius) (at protein level) (PubMed:8898389).2 Publications

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer (PubMed:12628255). Binds 30S but not 50S or 70S ribosomes (PubMed:7535280, PubMed:12963368, PubMed:25904134). Binds equally well to mature and immature 30S ribosomes, but is more stably associated with immature 30S ribosomes (PubMed:21102555).

2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4262435, 190 interactors

Protein interaction database and analysis system

More...
IntActi
P0A7G2, 2 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b3167

<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

1133
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
P0A7G2

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
P0A7G2

<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>Regioni109 – 133Required for stable 30S ribosomal association in vitro1 PublicationAdd BLAST25

<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 C-terminus (residues 109-133) is required for stable association with the 30S ribosomal subunit in vitro.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

Belongs to the RbfA family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0858, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_089475_5_0_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0A7G2

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0A7G2

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.300.20, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00003, RbfA, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR015946, KH_dom-like_a/b
IPR000238, RbfA
IPR023799, RbfA_dom_sf
IPR020053, Ribosome-bd_factorA_CS

The PANTHER Classification System

More...
PANTHERi
PTHR33515, PTHR33515, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02033, RBFA, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF89919, SSF89919, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00082, rbfA, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01319, RBFA, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P0A7G2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAKEFGRPQR VAQEMQKEIA LILQREIKDP RLGMMTTVSG VEMSRDLAYA
60 70 80 90 100
KVYVTFLNDK DEDAVKAGIK ALQEASGFIR SLLGKAMRLR IVPELTFFYD
110 120 130
NSLVEGMRMS NLVTSVVKHD EERRVNPDDS KED
Length:133
Mass (Da):15,154
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:iC8EE4FBFD8C01F08
GO

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
X13270 Genomic DNA Translation: CAA31634.1
X13775 Genomic DNA Translation: CAA32020.1
U18997 Genomic DNA Translation: AAA57970.1
U00096 Genomic DNA Translation: AAC76201.1
AP009048 Genomic DNA Translation: BAE77213.1

Protein sequence database of the Protein Information Resource

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PIRi
S01915, Q9EC15

NCBI Reference Sequences

More...
RefSeqi
NP_417636.1, NC_000913.3
WP_001040205.1, NZ_STEB01000012.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC76201; AAC76201; b3167
BAE77213; BAE77213; BAE77213

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
58462835
947685

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW3136
eco:b3167

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.3563

<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
X13270 Genomic DNA Translation: CAA31634.1
X13775 Genomic DNA Translation: CAA32020.1
U18997 Genomic DNA Translation: AAA57970.1
U00096 Genomic DNA Translation: AAC76201.1
AP009048 Genomic DNA Translation: BAE77213.1
PIRiS01915, Q9EC15
RefSeqiNP_417636.1, NC_000913.3
WP_001040205.1, NZ_STEB01000012.1

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
1KKGNMR-A1-108[»]
SMRiP0A7G2
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4262435, 190 interactors
IntActiP0A7G2, 2 interactors
STRINGi511145.b3167

2D gel databases

SWISS-2DPAGEiP0A7G2

Proteomic databases

jPOSTiP0A7G2
PaxDbiP0A7G2
PRIDEiP0A7G2

Genome annotation databases

EnsemblBacteriaiAAC76201; AAC76201; b3167
BAE77213; BAE77213; BAE77213
GeneIDi58462835
947685
KEGGiecj:JW3136
eco:b3167
PATRICifig|1411691.4.peg.3563

Organism-specific databases

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

More...
EchoBASEi
EB1165

Phylogenomic databases

eggNOGiCOG0858, Bacteria
HOGENOMiCLU_089475_5_0_6
InParanoidiP0A7G2
PhylomeDBiP0A7G2

Enzyme and pathway databases

BioCyciEcoCyc:EG11178-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0A7G2

Protein Ontology

More...
PROi
PR:P0A7G2

Family and domain databases

Gene3Di3.30.300.20, 1 hit
HAMAPiMF_00003, RbfA, 1 hit
InterProiView protein in InterPro
IPR015946, KH_dom-like_a/b
IPR000238, RbfA
IPR023799, RbfA_dom_sf
IPR020053, Ribosome-bd_factorA_CS
PANTHERiPTHR33515, PTHR33515, 1 hit
PfamiView protein in Pfam
PF02033, RBFA, 1 hit
SUPFAMiSSF89919, SSF89919, 1 hit
TIGRFAMsiTIGR00082, rbfA, 1 hit
PROSITEiView protein in PROSITE
PS01319, RBFA, 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 nameiRBFA_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: P0A7G2
Secondary accession number(s): P09170, Q2M943
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: January 23, 2007
Last modified: April 7, 2021
This is version 125 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
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