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Entry version 136 (12 Aug 2020)
Sequence version 2 (23 Jan 2007)
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Protein

Argininosuccinate synthase

Gene

argG

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-arginine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-arginine from L-ornithine and carbamoyl phosphate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Ornithine carbamoyltransferase subunit F (argF), Ornithine carbamoyltransferase (argF), Ornithine carbamoyltransferase subunit I (argI)
  2. Argininosuccinate synthase (argG), Argininosuccinate synthase (argG)
  3. Argininosuccinate lyase (argH), Argininosuccinate lyase (argH)
This subpathway is part of the pathway L-arginine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-arginine from L-ornithine and carbamoyl phosphate, the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei43ATP; via amide nitrogen and carbonyl oxygen1 Publication1
Binding sitei99Citrulline2 Publications1
Binding sitei129ATP; via amide nitrogen1 Publication1
Binding sitei131Aspartate1 Publication1
Binding sitei131ATP1 Publication1
Binding sitei135Aspartate1 Publication1
Binding sitei135Citrulline2 Publications1
Binding sitei136Aspartate1 Publication1
Binding sitei136ATP1 Publication1
Binding sitei139Citrulline2 Publications1
Binding sitei192Citrulline2 Publications1
Binding sitei194ATP1 Publication1
Binding sitei201Citrulline2 Publications1
Binding sitei203Citrulline2 Publications1
Binding sitei280Citrulline2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bindingi17 – 25ATP1 Publication9

<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

  • argininosuccinate synthase activity Source: GO_Central
  • ATP binding Source: UniProtKB-UniRule
  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: InterPro

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 functionLigase
Biological processAmino-acid biosynthesis, Arginine biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:ARGSUCCINSYN-MONOMER
ECOL316407:JW3140-MONOMER

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00068;UER00113

<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:
Argininosuccinate synthase (EC:6.3.4.5)
Alternative name(s):
Citrulline--aspartate ligase
<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:argG
Ordered Locus Names:b3172, JW3140
<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

GO - Cellular componenti

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

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB09462, Glycerin
DB00536, Guanidine

<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 methionineiRemoved2 Publications
<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_00001486952 – 447Argininosuccinate synthaseAdd BLAST446

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0A6E4

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

More...
PaxDbi
P0A6E4

PRoteomics IDEntifications database

More...
PRIDEi
P0A6E4

2D gel databases

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

More...
SWISS-2DPAGEi
P0A6E4

<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

Homotetramer.

2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4263121, 37 interactors
851906, 1 interactor

Database of interacting proteins

More...
DIPi
DIP-35842N

Protein interaction database and analysis system

More...
IntActi
P0A6E4, 14 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b3172

<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

1447
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
P0A6E4

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
P0A6E4

<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 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 monomer is composed of two major structural domains: a nucleotide-binding domain and a catalytic/multimerization domain. Binding of ATP results in a large rigid body conformational change of the nucleotide binding domain.

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0137, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_032784_4_1_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0A6E4

KEGG Orthology (KO)

More...
KOi
K01940

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0A6E4

Family and domain databases

Conserved Domains Database

More...
CDDi
cd01999, Argininosuccinate_Synthase, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.287.400, 1 hit
3.40.50.620, 1 hit
3.90.1260.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00581, Arg_succ_synth_type2, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR023437, Arg_succ_synth_type2_subfam
IPR001518, Arginosuc_synth
IPR018223, Arginosuc_synth_CS
IPR023434, Arginosuc_synth_type_1_subfam
IPR024074, AS_cat/multimer_dom_body
IPR024073, AS_multimer_C_tail
IPR014729, Rossmann-like_a/b/a_fold

The PANTHER Classification System

More...
PANTHERi
PTHR11587, PTHR11587, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00764, Arginosuc_synth, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF69864, SSF69864, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00032, argG, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00564, ARGININOSUCCIN_SYN_1, 1 hit
PS00565, ARGININOSUCCIN_SYN_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.

<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.

P0A6E4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTTILKHLPV GQRIGIAFSG GLDTSAALLW MRQKGAVPYA YTANLGQPDE
60 70 80 90 100
EDYDAIPRRA MEYGAENARL IDCRKQLVAE GIAAIQCGAF HNTTGGLTYF
110 120 130 140 150
NTTPLGRAVT GTMLVAAMKE DGVNIWGDGS TYKGNDIERF YRYGLLTNAE
160 170 180 190 200
LQIYKPWLDT DFIDELGGRH EMSEFMIACG FDYKMSVEKA YSTDSNMLGA
210 220 230 240 250
THEAKDLEYL NSSVKIVNPI MGVKFWDESV KIPAEEVTVR FEQGHPVALN
260 270 280 290 300
GKTFSDDVEM MLEANRIGGR HGLGMSDQIE NRIIEAKSRG IYEAPGMALL
310 320 330 340 350
HIAYERLLTG IHNEDTIEQY HAHGRQLGRL LYQGRWFDSQ ALMLRDSLQR
360 370 380 390 400
WVASQITGEV TLELRRGNDY SILNTVSENL TYKPERLTME KGDSVFSPDD
410 420 430 440
RIGQLTMRNL DITDTREKLF GYAKTGLLSS SAASGVPQVE NLENKGQ
Length:447
Mass (Da):49,898
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:iD5E7E51BD06E1813
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 conflicti220I → N in AAA23482 (PubMed:2123815).Curated1
Sequence conflicti328G → D in AAA23482 (PubMed:2123815).Curated1

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
M35236 Genomic DNA Translation: AAA23482.1
U18997 Genomic DNA Translation: AAA57974.1
U00096 Genomic DNA Translation: AAC76205.1
AP009048 Genomic DNA Translation: BAE77217.1

Protein sequence database of the Protein Information Resource

More...
PIRi
G65107, AJECRS

NCBI Reference Sequences

More...
RefSeqi
NP_417640.1, NC_000913.3
WP_000207680.1, NZ_SSZK01000007.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC76205; AAC76205; b3172
BAE77217; BAE77217; BAE77217

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
947590

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW3140
eco:b3172

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.3559

<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
M35236 Genomic DNA Translation: AAA23482.1
U18997 Genomic DNA Translation: AAA57974.1
U00096 Genomic DNA Translation: AAC76205.1
AP009048 Genomic DNA Translation: BAE77217.1
PIRiG65107, AJECRS
RefSeqiNP_417640.1, NC_000913.3
WP_000207680.1, NZ_SSZK01000007.1

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
1K92X-ray1.60A2-447[»]
1K97X-ray2.00A2-447[»]
1KP2X-ray2.00A2-447[»]
1KP3X-ray2.00A2-447[»]
SMRiP0A6E4
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4263121, 37 interactors
851906, 1 interactor
DIPiDIP-35842N
IntActiP0A6E4, 14 interactors
STRINGi511145.b3172

Chemistry databases

DrugBankiDB09462, Glycerin
DB00536, Guanidine

2D gel databases

SWISS-2DPAGEiP0A6E4

Proteomic databases

jPOSTiP0A6E4
PaxDbiP0A6E4
PRIDEiP0A6E4

Genome annotation databases

EnsemblBacteriaiAAC76205; AAC76205; b3172
BAE77217; BAE77217; BAE77217
GeneIDi947590
KEGGiecj:JW3140
eco:b3172
PATRICifig|1411691.4.peg.3559

Organism-specific databases

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

More...
EchoBASEi
EB0066

Phylogenomic databases

eggNOGiCOG0137, Bacteria
HOGENOMiCLU_032784_4_1_6
InParanoidiP0A6E4
KOiK01940
PhylomeDBiP0A6E4

Enzyme and pathway databases

UniPathwayiUPA00068;UER00113
BioCyciEcoCyc:ARGSUCCINSYN-MONOMER
ECOL316407:JW3140-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0A6E4

Protein Ontology

More...
PROi
PR:P0A6E4

Family and domain databases

CDDicd01999, Argininosuccinate_Synthase, 1 hit
Gene3Di1.10.287.400, 1 hit
3.40.50.620, 1 hit
3.90.1260.10, 1 hit
HAMAPiMF_00581, Arg_succ_synth_type2, 1 hit
InterProiView protein in InterPro
IPR023437, Arg_succ_synth_type2_subfam
IPR001518, Arginosuc_synth
IPR018223, Arginosuc_synth_CS
IPR023434, Arginosuc_synth_type_1_subfam
IPR024074, AS_cat/multimer_dom_body
IPR024073, AS_multimer_C_tail
IPR014729, Rossmann-like_a/b/a_fold
PANTHERiPTHR11587, PTHR11587, 1 hit
PfamiView protein in Pfam
PF00764, Arginosuc_synth, 1 hit
SUPFAMiSSF69864, SSF69864, 1 hit
TIGRFAMsiTIGR00032, argG, 1 hit
PROSITEiView protein in PROSITE
PS00564, ARGININOSUCCIN_SYN_1, 1 hit
PS00565, ARGININOSUCCIN_SYN_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 nameiASSY_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: P0A6E4
Secondary accession number(s): P22767, Q2M939
<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: August 12, 2020
This is version 136 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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