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Entry version 47 (23 Feb 2022)
Sequence version 1 (16 Apr 2014)
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Protein

3-oxoacyl-[acyl-carrier-protein] synthase 2

Gene

kasB

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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

Part of the mycobacterial fatty acid elongation system FAS-II, which is involved in mycolic acid biosynthesis. Catalyzes the elongation of long chain acyl-ACP substrates by the addition of two carbons from malonyl-ACP to an acyl acceptor (PubMed:11600501, PubMed:12464486, PubMed:16873379).

Involved in extension of the mycolate chains to full lengths and produces longer chain multiunsaturated hydrocarbons averaging 54 carbons in length (PubMed:12464486).

Essential for resistance to macrophage antimicrobial activity (PubMed:12950920).

4 Publications

Miscellaneous

Identified as a drug target (PubMed:10747933, PubMed:12950920). Inhibited by isoniazid (INH), thiolactomycin (TLM) and related analogs (PubMed:10747933, PubMed:12464486).3 Publications

<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 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

Phosphorylation decreases the condensing activity of KasB and leads to the production of shorter mycolic acids, which is associated to dramatic phenotype changes, such as loss of acid-fastness, increase of cell wall permeability, severe attenuation in infected mice and defect in macrophage colonization.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 1.6 min(-1) with hexadecanoyl-[ACP] as substrate. kcat is 0.6 min(-1) with eicosanoyl-[ACP] as substrate. kcat is 1.4 min(-1) with malonyl-[ACP] as substrate.1 Publication
  1. KM=1.4 µM for hexadecanoyl-[ACP]1 Publication
  2. KM=13.1 µM for hexadecanoyl-[ACP]1 Publication
  3. KM=1.9 µM for eicosanoyl-[ACP]1 Publication
  4. KM=13.5 µM for malonyl-[ACP]1 Publication
  5. KM=35 µM for malonyl-[ACP]1 Publication

<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: mycolic acid biosynthesis

This protein is involved in the pathway mycolic acid biosynthesis, which is part of Lipid metabolism.1 Publication4 Publications
View all proteins of this organism that are known to be involved in the pathway mycolic acid biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei170By similarity1

<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 functionAcyltransferase, Transferase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

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

More...
UniPathwayi
UPA00915

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000000963

<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:
3-oxoacyl-[acyl-carrier-protein] synthase 2 (EC:2.3.1.2942 Publications)
Alternative name(s):
Beta-ketoacyl-ACP synthase 2
Short name:
KAS 2
Beta-ketoacyl-acyl carrier protein synthase KasB1 Publication
Meromycolic acid 3-oxoacyl-(acyl carrier protein) synthase II
<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:kasB1 Publication
Ordered Locus Names:Rv2246
ORF Names:MTCY427.27
<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>OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
<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 identifieri83332 [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 lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
<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
  • UP000001584 <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

Organism-specific databases

Mycobacterium tuberculosis strain H37Rv genome database

More...
TubercuListi
Rv2246

<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

Deletion of the gene results in loss of acid-fast staining, which is a simple and rapid diagnostic test for detecting M.tuberculosis (PubMed:17360388, PubMed:22516756). The region between the inner and outer membranes of the mutant, which is composed mainly of cell wall anchored mycolic acids, shows a significant decrease in electron density as compared to the wild type. It suggests that altered mycolic acids patterns in the mutant may have affected the packing of the lipid rich layer of the M.tuberculosis cell envelope, resulting in a reduced electron density of this layer and loss of acid-fastness in light microscopical observation (PubMed:22516756). Mutants synthesize mycolic acids that are 2-6 carbons shorter than wild type and show a significant reduction in the abundance of keto-mycolates (PubMed:12950920, PubMed:17360388). Deletion of the gene affects mycolic acid trans-cyclopropanation, alters the colony morphology and abolishes classic serpentine growth (PubMed:17360388). Mutants exhibit strikingly altered cell wall permeability, leading to a marked increase in susceptibility to lipophilic antibiotics and the host antimicrobial molecules defensin and lysozyme (PubMed:12950920). Deletion mutant can persist in infected immunocompetent mice for up to 600 days without causing disease or mortality (PubMed:17360388).3 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>Mutagenesisi313T → A: Decreases phosphorylation. Lack of phosphorylation; when associated with A-315. 1 Publication1
Mutagenesisi313T → D: Phosphomimetic mutant. Loss of acid-fast staining and reduced pathogenicity; when associated with D-315. 1 Publication1
Mutagenesisi315T → A: Decreases phosphorylation. Lack of phosphorylation; when associated with A-313. 1 Publication1
Mutagenesisi315T → D: Phosphomimetic mutant. Loss of acid-fast staining and reduced pathogenicity; when associated with D-313. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4543

<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_00001803341 – 4173-oxoacyl-[acyl-carrier-protein] synthase 2Add BLAST417

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei313Phosphothreonine1 Publication1
Modified residuei315Phosphothreonine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated on Thr-313 and Thr-315 (PubMed:24809459). Phosphorylated in vitro by several Ser/Thr protein kinases (STPKs) (PubMed:16873379).2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

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

More...
PaxDbi
P9WQD7

<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

Homodimer.

1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
83332.Rv2246

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P9WQD7

<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

1417
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
P9WQD7

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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

<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
COG0304, Bacteria

Identification of Orthologs from Complete Genome Data

More...
OMAi
QIGHCLG

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00834, KAS_I_II, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.47.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000794, Beta-ketoacyl_synthase
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR020841, PKS_Beta-ketoAc_synthase_dom
IPR016039, Thiolase-like

The PANTHER Classification System

More...
PANTHERi
PTHR11712, PTHR11712, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00109, ketoacyl-synt, 1 hit
PF02801, Ketoacyl-synt_C, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00825, PKS_KS, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53901, SSF53901, 2 hits

<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.

P9WQD7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTELVTGKAF PYVVVTGIAM TTALATDAET TWKLLLDRQS GIRTLDDPFV
60 70 80 90 100
EEFDLPVRIG GHLLEEFDHQ LTRIELRRMG YLQRMSTVLS RRLWENAGSP
110 120 130 140 150
EVDTNRLMVS IGTGLGSAEE LVFSYDDMRA RGMKAVSPLT VQKYMPNGAA
160 170 180 190 200
AAVGLERHAK AGVMTPVSAC ASGAEAIARA WQQIVLGEAD AAICGGVETR
210 220 230 240 250
IEAVPIAGFA QMRIVMSTNN DDPAGACRPF DRDRDGFVFG EGGALLLIET
260 270 280 290 300
EEHAKARGAN ILARIMGASI TSDGFHMVAP DPNGERAGHA ITRAIQLAGL
310 320 330 340 350
APGDIDHVNA HATGTQVGDL AEGRAINNAL GGNRPAVYAP KSALGHSVGA
360 370 380 390 400
VGAVESILTV LALRDQVIPP TLNLVNLDPE IDLDVVAGEP RPGNYRYAIN
410
NSFGFGGHNV AIAFGRY
Length:417
Mass (Da):44,277
Last modified:April 16, 2014 - 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:i239F7D19A6380F66
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence CCP45026 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

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
AL123456 Genomic DNA Translation: CCP45026.1 Different initiation.

Protein sequence database of the Protein Information Resource

More...
PIRi
B70779

NCBI Reference Sequences

More...
RefSeqi
NP_216762.1, NC_000962.3
WP_003411576.1, NC_018143.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
45426226
887539

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mtu:Rv2246

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|83332.12.peg.2504

<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
AL123456 Genomic DNA Translation: CCP45026.1 Different initiation.
PIRiB70779
RefSeqiNP_216762.1, NC_000962.3
WP_003411576.1, NC_018143.2

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
2GP6X-ray2.40A/B5-417[»]
SMRiP9WQD7
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv2246

Chemistry databases

BindingDBiP9WQD7
ChEMBLiCHEMBL4543
SwissLipidsiSLP:000000963

Proteomic databases

PaxDbiP9WQD7

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
887539

Genome annotation databases

GeneIDi45426226
887539
KEGGimtu:Rv2246
PATRICifig|83332.12.peg.2504

Organism-specific databases

TubercuListiRv2246

Phylogenomic databases

eggNOGiCOG0304, Bacteria
OMAiQIGHCLG

Enzyme and pathway databases

UniPathwayiUPA00915

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P9WQD7

Family and domain databases

CDDicd00834, KAS_I_II, 1 hit
Gene3Di3.40.47.10, 2 hits
InterProiView protein in InterPro
IPR000794, Beta-ketoacyl_synthase
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR020841, PKS_Beta-ketoAc_synthase_dom
IPR016039, Thiolase-like
PANTHERiPTHR11712, PTHR11712, 1 hit
PfamiView protein in Pfam
PF00109, ketoacyl-synt, 1 hit
PF02801, Ketoacyl-synt_C, 1 hit
SMARTiView protein in SMART
SM00825, PKS_KS, 1 hit
SUPFAMiSSF53901, SSF53901, 2 hits

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 nameiKASB_MYCTU
<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: P9WQD7
Secondary accession number(s): L0TBY1, P63456, Q10525
<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: April 16, 2014
Last sequence update: April 16, 2014
Last modified: February 23, 2022
This is version 47 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, 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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