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Entry version 181 (02 Jun 2021)
Sequence version 1 (01 Aug 1988)
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Protein

Phosphoribosylglycinamide formyltransferase

Gene

purN

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

Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate.

UniRule annotation2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by N10-(bromoacetyl)-5,8-dideazafolate.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 20.7 sec(-1) for (6R)-N10-formyltetrahydrofolate (at pH 8.5). kcat is 13.5 sec(-1) for (6R)-N10-formyltetrahydrofolate (at pH 7.5).1 Publication
  1. KM=77.5 µM for (6R)-N10-formyltetrahydrofolate (at pH 8.5)1 Publication
  2. KM=84.8 µM for (6R)-N10-formyltetrahydrofolate (at pH 7.5)1 Publication

pH dependencei

Optimum pH is 8.5.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: IMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route).UniRule annotation1 Publication This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route), the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei6410-formyltetrahydrofolateUniRule annotation1 Publication1
Binding sitei10610-formyltetrahydrofolateUniRule annotation1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei108Proton donorUniRule annotation1 Publication1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei144Raises pKa of active site HisUniRule annotation1 Publication1

<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 functionTransferase
Biological processPurine biosynthesis

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:GART-MONOMER
MetaCyc:GART-MONOMER

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

More...
UniPathwayi
UPA00074;UER00126

<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:
Phosphoribosylglycinamide formyltransferaseUniRule annotation (EC:2.1.2.2UniRule annotation2 Publications)
Alternative name(s):
5'-phosphoribosylglycinamide transformylaseUniRule annotation
GAR transformylaseUniRule annotation
Short name:
GARTUniRule annotation
<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:purN1 PublicationUniRule annotation
Ordered Locus Names:b2500, JW2485
<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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<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

<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>Mutagenesisi70E → A: Loss of homodimerization. No effect on activity. 1 Publication1
Mutagenesisi106N → A, D, G or S: Reduces activity about 2000-fold. 1 Publication1
Mutagenesisi106N → E, H, I, K, L or Y: Loss of activity. 1 Publication1
Mutagenesisi108H → A, G, M, N, Q or R: Loss of activity. 2 Publications1
Mutagenesisi108H → E, S or T: Reduces activity about 1000-fold. 1 Publication1
Mutagenesisi119H → A: No effect. 1 Publication1
Mutagenesisi121H → Q: Increases Km for 5'-phosphoribosylglycinamide 4-fold. 1 Publication1
Mutagenesisi135S → A or L: Reduces activity about 1000-fold. 1 Publication1
Mutagenesisi137H → F or Q: No effect. 1 Publication1
Mutagenesisi144D → A, E, S or Y: Reduces activity about 1000-fold. 2 Publications1
Mutagenesisi144D → C, F, H, K, L, N, P, Q, R, T or V: Loss of activity. 2 Publications1

Miscellaneous databases

Pathogen-Host Interaction database

More...
PHI-basei
PHI:8652

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB04264, (10R)-10-formyl-5,8,10-trideazafolic acid
DB02794, (2S)-2-({4-[(2S)-1-(2-Amino-4-oxo-1,4-dihydro-6-quinazolinyl)-3-{[2-({(2R,3R,4S,5R)-3,4-dihydroxy-5-[(phosphonooxy)methyl]tetrahydro-2-furanyl}amino)-2-oxoethyl]amino}-2-hydroxy-2-propanyl]benzoyl}ami no)pentanedioic acid
DB02540, 10-formyl-5,8,10-trideazafolic acid
DB02236, Glycinamide Ribonucleotide

<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_00000749431 – 212Phosphoribosylglycinamide formyltransferaseAdd BLAST212

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P08179

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

More...
PaxDbi
P08179

PRoteomics IDEntifications database

More...
PRIDEi
P08179

<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

Monomer. Homodimer below pH 6.8.

5 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4261440, 10 interactors
851312, 1 interactor

Protein interaction database and analysis system

More...
IntActi
P08179, 1 interactor

STRING: functional protein association networks

More...
STRINGi
511145.b2500

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P08179

<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

1212
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
P08179

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
P08179

<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>Regioni11 – 135'-phosphoribosylglycinamide bindingUniRule annotation2 Publications3
Regioni89 – 9210-formyltetrahydrofolate bindingUniRule annotation2 Publications4
Regioni140 – 14410-formyltetrahydrofolate binding2 Publications5
Regioni170 – 1735'-phosphoribosylglycinamide binding2 Publications4

<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 GART family.UniRule annotationCurated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0299, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_038395_1_1_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P08179

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P08179

Family and domain databases

Conserved Domains Database

More...
CDDi
cd08645, FMT_core_GART, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01930, PurN, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR002376, Formyl_transf_N
IPR036477, Formyl_transf_N_sf
IPR004607, GART
IPR001555, GART_AS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00551, Formyl_trans_N, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53328, SSF53328, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00639, PurN, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00373, GART, 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.

P08179-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNIVVLISGN GSNLQAIIDA CKTNKIKGTV RAVFSNKADA FGLERARQAG
60 70 80 90 100
IATHTLIASA FDSREAYDRE LIHEIDMYAP DVVVLAGFMR ILSPAFVSHY
110 120 130 140 150
AGRLLNIHPS LLPKYPGLHT HRQALENGDE EHGTSVHFVT DELDGGPVIL
160 170 180 190 200
QAKVPVFAGD SEDDITARVQ TQEHAIYPLV ISWFADGRLK MHENAAWLDG
210
QRLPPQGYAA DE
Length:212
Mass (Da):23,238
Last modified:August 1, 1988 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iD38F326BCBA103FB
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
M13747 Genomic DNA Translation: AAA83899.1
U00096 Genomic DNA Translation: AAC75553.1
AP009048 Genomic DNA Translation: BAA16388.1
AF293167 Genomic DNA Translation: AAG14584.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A28486, XYECGF

NCBI Reference Sequences

More...
RefSeqi
NP_416995.1, NC_000913.3
WP_001028612.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC75553; AAC75553; b2500
BAA16388; BAA16388; BAA16388

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
946973

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW2485
eco:b2500

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.4238

<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
M13747 Genomic DNA Translation: AAA83899.1
U00096 Genomic DNA Translation: AAC75553.1
AP009048 Genomic DNA Translation: BAA16388.1
AF293167 Genomic DNA Translation: AAG14584.1
PIRiA28486, XYECGF
RefSeqiNP_416995.1, NC_000913.3
WP_001028612.1, NZ_LN832404.1

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
1C2TX-ray2.10A/B1-212[»]
1C3EX-ray2.10A/B1-209[»]
1CDDX-ray2.80A/B1-212[»]
1CDEX-ray2.50A/B/C/D1-212[»]
1GARX-ray1.96A/B1-212[»]
1GRCX-ray3.00A/B1-212[»]
1JKXX-ray1.60A/B/C/D1-212[»]
2GARX-ray1.80A1-212[»]
3GARX-ray1.90A1-212[»]
SMRiP08179
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4261440, 10 interactors
851312, 1 interactor
IntActiP08179, 1 interactor
STRINGi511145.b2500

Chemistry databases

BindingDBiP08179
DrugBankiDB04264, (10R)-10-formyl-5,8,10-trideazafolic acid
DB02794, (2S)-2-({4-[(2S)-1-(2-Amino-4-oxo-1,4-dihydro-6-quinazolinyl)-3-{[2-({(2R,3R,4S,5R)-3,4-dihydroxy-5-[(phosphonooxy)methyl]tetrahydro-2-furanyl}amino)-2-oxoethyl]amino}-2-hydroxy-2-propanyl]benzoyl}ami no)pentanedioic acid
DB02540, 10-formyl-5,8,10-trideazafolic acid
DB02236, Glycinamide Ribonucleotide

Proteomic databases

jPOSTiP08179
PaxDbiP08179
PRIDEiP08179

Genome annotation databases

EnsemblBacteriaiAAC75553; AAC75553; b2500
BAA16388; BAA16388; BAA16388
GeneIDi946973
KEGGiecj:JW2485
eco:b2500
PATRICifig|1411691.4.peg.4238

Organism-specific databases

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

More...
EchoBASEi
EB0792

Phylogenomic databases

eggNOGiCOG0299, Bacteria
HOGENOMiCLU_038395_1_1_6
InParanoidiP08179
PhylomeDBiP08179

Enzyme and pathway databases

UniPathwayiUPA00074;UER00126
BioCyciEcoCyc:GART-MONOMER
MetaCyc:GART-MONOMER

Miscellaneous databases

EvolutionaryTraceiP08179
PHI-baseiPHI:8652

Protein Ontology

More...
PROi
PR:P08179

Family and domain databases

CDDicd08645, FMT_core_GART, 1 hit
HAMAPiMF_01930, PurN, 1 hit
InterProiView protein in InterPro
IPR002376, Formyl_transf_N
IPR036477, Formyl_transf_N_sf
IPR004607, GART
IPR001555, GART_AS
PfamiView protein in Pfam
PF00551, Formyl_trans_N, 1 hit
SUPFAMiSSF53328, SSF53328, 1 hit
TIGRFAMsiTIGR00639, PurN, 1 hit
PROSITEiView protein in PROSITE
PS00373, GART, 1 hit

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 nameiPUR3_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: P08179
<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: August 1, 1988
Last sequence update: August 1, 1988
Last modified: June 2, 2021
This is version 181 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, 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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