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Entry version 166 (12 Aug 2020)
Sequence version 1 (01 Mar 1992)
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Protein

DNA repair protein RadA

Gene

radA

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

DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function (PubMed:26845522). Genetic experiments involving combination of radA mutations with mutations in recA, recB, recG, recJ, recQ, ruvA and ruvC show it plays a role in recombination and recombinational repair, probably involving stabilizing or processing branched DNA or blocked replication forks. Is genetically synergistic to RecG and RuvABC (PubMed:12446634, PubMed:25484163). May be involved in recovery of genetic rearrangements during replication fork breakdown (PubMed:16904387). In combination with RadD is important in recovery from double-strand DNA breaks (DSB) (PubMed:25425430).5 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri11 – 28C4-typeUniRule annotation1 PublicationAdd BLAST18
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi102 – 109ATPUniRule annotation1 Publication8

<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 functionDNA-binding, Hydrolase
Biological processDNA damage, DNA repair, Stress response
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG11296-MONOMER
ECOL316407:JW4352-MONOMER

Protein family/group databases

MEROPS protease database

More...
MEROPSi
S16.A04

<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:
DNA repair protein RadA1 PublicationUniRule annotation (EC:3.6.4.-1 Publication)
Alternative name(s):
Branch migration protein RadA1 Publication
DNA repair protein Sms1 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:radA1 PublicationUniRule annotation
Synonyms:sms1 Publication
Ordered Locus Names:b4389, JW4352
<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 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

Increased sensitivity to methyl methanesulfonate, mitomycin C, phleomycin (PubMed:1327967, PubMed:12446634). Has a modest defect in RecA-mediated conjugational DNA recombination; double radA-radD mutants have wild-type levels (PubMed:25425430, PubMed:12446634). 10- to 1000-fold decrease in survival after ionising irradiation (IR) (PubMed:25049088, PubMed:25425430). Double radA-radD deletions have nearly 106-fold lower survival against IR and the double mutant is more severely affected by UV radiation than either of the single mutants alone. The single mutation is more sensitive to dsDNA breaks induced by ciprofloxacin (CFX), the double radA-radD mutant is inviable upon CFX treatment; the SOS response is slightly induced in the single and more induced in the double mutant (PubMed:25425430). Another group showed very slight sensitivity to CFX, UV and azidothymidine (AZT) in single deletion mutants, a radA-recG deletion is extremely sensitive to CFX and AZT, less so to UV. The SOS response is induced in the radA-recG double mutant, indicating spontaneous DNA damage. AZT sensitivity is suppressed by further recA or recF deletions, suggesting AZT-induced DNA gaps are processed into lethal intermediates in a RecA-dependent fashion mediated by RecF. RuvAB suppresses UV, CFX and AZT sensitivity to vaarying degrees. Similarly, radA-uvrD double deletions are also more sensitive to UV, CFX and AZT. Adding a recF mutation almost completely suppresses AZT and partially suppresses UV and CFX sensitivity, suggesting RadA processes a class of intermediates that accumulates in uvrD mutants (PubMed:25484163).5 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>Mutagenesisi28C → Y in radA100; rich medium-grown cells are sensitive to gamma, X-ray and UV radiation as well as methyl methanesulfonate and hydroxyurea, impaired in repair of dsDNA breaks. Decreased resistance to ciprofloxacin (CFX). 4 Publications1
Mutagenesisi108K → R: Decreased resistance to CFX, semi-dominant to wild-type. 1 Publication1
Mutagenesisi228 – 460Missing : Decreased resistance to CFX. 1 PublicationAdd BLAST233
Mutagenesisi258K → R: Decreased resistance to CFX, semi-dominant to wild-type. 1 Publication1
Mutagenesisi275 – 460Missing : Decreased resistance to CFX. 1 PublicationAdd BLAST186
Mutagenesisi372S → A: Wild-type resistance to CFX; equivalent to the active site Ser of Lon protease. 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001879261 – 460DNA repair protein RadAAdd BLAST460

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P24554

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

More...
PaxDbi
P24554

PRoteomics IDEntifications database

More...
PRIDEi
P24554

<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

Part of the serB-radA operon (PubMed:1327967).1 Publication

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4262780, 171 interactors
853189, 1 interactor

Database of interacting proteins

More...
DIPi
DIP-10635N

Protein interaction database and analysis system

More...
IntActi
P24554, 5 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b4389

<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

3D structure databases

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

More...
SMRi
P24554

Database of comparative protein structure models

More...
ModBasei
Search...

<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>Regioni357 – 460Lon-protease-likeUniRule annotation1 PublicationAdd BLAST104

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi258 – 262RadA KNRFG motifUniRule annotation1 Publication5

<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

Has a putative N-terminal zinc-finger, a region with homology to RecA with ATPase motifs including the RadA KNRFG motif (approximately residues 60-290), while the C-terminus is homologous to Lon protease (from about residue 290 to the end, the ribosomal S5 domain). In this organism the Lon protease active site Ser-372 is conserved, but not all other bacteria encode Ser at this position (PubMed:1327967, PubMed:8759876). Mutation of Ser-372 has no discernible effect on RadA function, suggesting RadA is not a protease (PubMed:25484163).UniRule annotation2 Publications1 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 RecA family. RadA subfamily.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri11 – 28C4-typeUniRule annotation1 PublicationAdd BLAST18

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG1066, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_018264_0_1_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P24554

KEGG Orthology (KO)

More...
KOi
K04485

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P24554

Family and domain databases

Conserved Domains Database

More...
CDDi
cd01121, Sms, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.230.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01498, RadA_bact, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003593, AAA+_ATPase
IPR004504, DNA_repair_RadA
IPR027417, P-loop_NTPase
IPR020588, RecA_ATP-bd
IPR020568, Ribosomal_S5_D2-typ_fold
IPR014721, Ribosomal_S5_D2-typ_fold_subgr
IPR041166, Rubredoxin_2

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF18073, Rubredoxin_2, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00382, AAA, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540, SSF52540, 1 hit
SSF54211, SSF54211, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00416, sms, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50162, RECA_2, 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.

P24554-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAKAPKRAFV CNECGADYPR WQGQCSACHA WNTITEVRLA ASPMVARNER
60 70 80 90 100
LSGYAGSAGV AKVQKLSDIS LEELPRFSTG FKEFDRVLGG GVVPGSAILI
110 120 130 140 150
GGNPGAGKST LLLQTLCKLA QQMKTLYVTG EESLQQVAMR AHRLGLPTDN
160 170 180 190 200
LNMLSETSIE QICLIAEEEQ PKLMVIDSIQ VMHMADVQSS PGSVAQVRET
210 220 230 240 250
AAYLTRFAKT RGVAIVMVGH VTKDGSLAGP KVLEHCIDCS VLLDGDADSR
260 270 280 290 300
FRTLRSHKNR FGAVNELGVF AMTEQGLREV SNPSAIFLSR GDEVTSGSSV
310 320 330 340 350
MVVWEGTRPL LVEIQALVDH SMMANPRRVA VGLEQNRLAI LLAVLHRHGG
360 370 380 390 400
LQMADQDVFV NVVGGVKVTE TSADLALLLA MVSSLRDRPL PQDLVVFGEV
410 420 430 440 450
GLAGEIRPVP SGQERISEAA KHGFRRAIVP AANVPKKAPE GMQIFGVKKL
460
SDALSVFDDL
Length:460
Mass (Da):49,472
Last modified:March 1, 1992 - 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:iC03C8BE5367E7BFF
GO

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
X63155 Genomic DNA Translation: CAA44856.1
U59449 Genomic DNA Translation: AAC44380.1
U14003 Genomic DNA Translation: AAA97285.1
U00096 Genomic DNA Translation: AAC77342.1
AP009048 Genomic DNA Translation: BAE78378.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JC1417

NCBI Reference Sequences

More...
RefSeqi
NP_418806.1, NC_000913.3
WP_001029687.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC77342; AAC77342; b4389
BAE78378; BAE78378; BAE78378

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
948912

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW4352
eco:b4389

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.2296

<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
X63155 Genomic DNA Translation: CAA44856.1
U59449 Genomic DNA Translation: AAC44380.1
U14003 Genomic DNA Translation: AAA97285.1
U00096 Genomic DNA Translation: AAC77342.1
AP009048 Genomic DNA Translation: BAE78378.1
PIRiJC1417
RefSeqiNP_418806.1, NC_000913.3
WP_001029687.1, NZ_LN832404.1

3D structure databases

SMRiP24554
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi4262780, 171 interactors
853189, 1 interactor
DIPiDIP-10635N
IntActiP24554, 5 interactors
STRINGi511145.b4389

Protein family/group databases

MEROPSiS16.A04

Proteomic databases

jPOSTiP24554
PaxDbiP24554
PRIDEiP24554

Genome annotation databases

EnsemblBacteriaiAAC77342; AAC77342; b4389
BAE78378; BAE78378; BAE78378
GeneIDi948912
KEGGiecj:JW4352
eco:b4389
PATRICifig|1411691.4.peg.2296

Organism-specific databases

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

More...
EchoBASEi
EB1273

Phylogenomic databases

eggNOGiCOG1066, Bacteria
HOGENOMiCLU_018264_0_1_6
InParanoidiP24554
KOiK04485
PhylomeDBiP24554

Enzyme and pathway databases

BioCyciEcoCyc:EG11296-MONOMER
ECOL316407:JW4352-MONOMER

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P24554

Family and domain databases

CDDicd01121, Sms, 1 hit
Gene3Di3.30.230.10, 1 hit
HAMAPiMF_01498, RadA_bact, 1 hit
InterProiView protein in InterPro
IPR003593, AAA+_ATPase
IPR004504, DNA_repair_RadA
IPR027417, P-loop_NTPase
IPR020588, RecA_ATP-bd
IPR020568, Ribosomal_S5_D2-typ_fold
IPR014721, Ribosomal_S5_D2-typ_fold_subgr
IPR041166, Rubredoxin_2
PfamiView protein in Pfam
PF18073, Rubredoxin_2, 1 hit
SMARTiView protein in SMART
SM00382, AAA, 1 hit
SUPFAMiSSF52540, SSF52540, 1 hit
SSF54211, SSF54211, 1 hit
TIGRFAMsiTIGR00416, sms, 1 hit
PROSITEiView protein in PROSITE
PS50162, RECA_2, 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 nameiRADA_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: P24554
Secondary accession number(s): Q2M5S8
<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: March 1, 1992
Last sequence update: March 1, 1992
Last modified: August 12, 2020
This is version 166 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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
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