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Entry version 130 (18 Sep 2019)
Sequence version 1 (01 Aug 1998)
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Protein

UDP-3-O-acyl-N-acetylglucosamine deacetylase

Gene

lpxC

Organism
Aquifex aeolicus (strain VF5)
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 hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis.UniRule annotation1 Publication

<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 ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+UniRule annotation1 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: lipid IV(A) biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine.UniRule annotation
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase (lpxA)
  2. UDP-3-O-acyl-N-acetylglucosamine deacetylase (lpxC)
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  5. Lipid-A-disaccharide synthase (lpxB)
  6. Tetraacyldisaccharide 4'-kinase (lpxK)
This subpathway is part of the pathway lipid IV(A) biosynthesis, which is itself part of Glycolipid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine, the pathway lipid IV(A) biosynthesis and in Glycolipid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi74Zinc; via tele nitrogenUniRule annotationCombined sources2 Publications1
Metal bindingi226Zinc; via tele nitrogenUniRule annotationCombined sources2 Publications1
Metal bindingi230ZincUniRule annotationCombined sources2 Publications1
<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 sitei253Proton donorUniRule 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 functionHydrolase
Biological processLipid A biosynthesis, Lipid biosynthesis, Lipid metabolism
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
AAEO224324:G1G15-1266-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.5.1.108 396

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

More...
UniPathwayi
UPA00359;UER00478

<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:
UDP-3-O-acyl-N-acetylglucosamine deacetylaseUniRule annotation (EC:3.5.1.108UniRule annotation2 Publications)
Short name:
UDP-3-O-acyl-GlcNAc deacetylaseUniRule annotation
Alternative name(s):
UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylaseUniRule 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:lpxCUniRule annotation
Synonyms:envA
Ordered Locus Names:aq_1772
<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>OrganismiAquifex aeolicus (strain VF5)
<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 identifieri224324 [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 lineageiBacteriaAquificaeAquificalesAquificaceaeAquifex
<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
  • UP000000798 <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

<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>Mutagenesisi19H → A: 20-fold decrease in activity. 2-fold decrease in zinc content. 1 Publication1
Mutagenesisi19H → Q: 2-fold decrease in activity. 1 Publication1
Mutagenesisi19H → Y: 22-fold decrease in activity. 1 Publication1
Mutagenesisi73E → A: 10-fold decrease in activity. 3.6-fold decrease in zinc content. 1 Publication1
Mutagenesisi73E → Q: Loss of activity. 1 Publication1
Mutagenesisi74H → A: Almost loss of activity. 10-fold decrease in zinc content. 1 Publication1
Mutagenesisi74H → Q: Almost loss of activity. 1 Publication1
Mutagenesisi95E → A, N or S: Almost no change in activity. 1 Publication1
Mutagenesisi100D → A, N or S: Almost no change in activity. 1 Publication1
Mutagenesisi222E → A: 20-fold decrease in activity. 1 Publication1
Mutagenesisi222E → N: Loss of activity. 1 Publication1
Mutagenesisi222E → S: 15-fold decrease in activity. 1 Publication1
Mutagenesisi226H → A: 720-fold decrease in activity. 16.6-fold decrease in zinc content. 1 Publication1
Mutagenesisi234D → A: Almost loss of activity. 1.5-fold decrease in zinc content. 1 Publication1
Mutagenesisi234D → N: 29-fold decrease in activity. 1 Publication1
Mutagenesisi234D → S: Loss of activity. 1 Publication1
Mutagenesisi253H → A: Loss of activity. 4.3-fold decrease in zinc content. 1 Publication1
Mutagenesisi253H → Q: Loss of activity. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1075040

Drug and drug target database

More...
DrugBanki
DB07355 3-(heptyloxy)benzoic acid
DB08231 Myristic acid
DB07536 N-{(1S,2R)-2-hydroxy-1-[(hydroxyamino)carbonyl]propyl}-4-{[4-(morpholin-4-ylmethyl)phenyl]ethynyl}benzamide
DB04257 Palmitoleic Acid
DB01991 Tu-514

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001919171 – 282UDP-3-O-acyl-N-acetylglucosamine deacetylaseAdd BLAST282

<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

STRING: functional protein association networks

More...
STRINGi
224324.aq_1772

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
O67648

<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

1282
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
O67648

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
O67648

<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

Belongs to the LpxC family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105C7C Bacteria
COG0774 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000256664

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O67648

KEGG Orthology (KO)

More...
KOi
K02535

Identification of Orthologs from Complete Genome Data

More...
OMAi
IVFYRSD

Database of Orthologous Groups

More...
OrthoDBi
428602at2

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.1700.10, 1 hit
3.30.230.20, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00388 LpxC, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR020568 Ribosomal_S5_D2-typ_fold
IPR004463 UDP-acyl_GlcNac_deAcase
IPR011334 UDP-acyl_GlcNac_deAcase_C
IPR015870 UDP-acyl_N-AcGlcN_deAcase_N

The PANTHER Classification System

More...
PANTHERi
PTHR33694 PTHR33694, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03331 LpxC, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54211 SSF54211, 2 hits

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00325 lpxC, 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.

O67648-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGLEKTVKEK LSFEGVGIHT GEYSKLIIHP EKEGTGIRFF KNGVYIPARH
60 70 80 90 100
EFVVHTNHST DLGFKGQRIK TVEHILSVLH LLEITNVTIE VIGNEIPILD
110 120 130 140 150
GSGWEFYEAI RKNILNQNRE IDYFVVEEPI IVEDEGRLIK AEPSDTLEVT
160 170 180 190 200
YEGEFKNFLG RQKFTFVEGN EEEIVLARTF CFDWEIEHIK KVGLGKGGSL
210 220 230 240 250
KNTLVLGKDK VYNPEGLRYE NEPVRHKVFD LIGDLYLLGS PVKGKFYSFR
260 270 280
GGHSLNVKLV KELAKKQKLT RDLPHLPSVQ AL
Length:282
Mass (Da):32,145
Last modified:August 1, 1998 - 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:i38EFE076144B5F27
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
AE000657 Genomic DNA Translation: AAC07605.1

Protein sequence database of the Protein Information Resource

More...
PIRi
F70452

NCBI Reference Sequences

More...
RefSeqi
NP_214214.1, NC_000918.1
WP_010881151.1, NC_000918.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC07605; AAC07605; aq_1772

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
1193363

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
aae:aq_1772

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|224324.8.peg.1368

<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
AE000657 Genomic DNA Translation: AAC07605.1
PIRiF70452
RefSeqiNP_214214.1, NC_000918.1
WP_010881151.1, NC_000918.1

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
1P42X-ray2.00A/B2-271[»]
1XXENMR-A1-282[»]
1YH8X-ray2.70A/B2-271[»]
1YHCX-ray2.10A/B2-271[»]
2GO3X-ray2.00A/B1-267[»]
2GO4X-ray2.70A/B1-267[»]
2IERX-ray2.70A/B1-271[»]
2IESX-ray3.10A/B1-271[»]
2J65X-ray2.20A/B1-271[»]
2JT2NMR-A1-274[»]
2O3ZX-ray2.25A/B1-271[»]
3P3CX-ray1.25A2-275[»]
3P76X-ray1.93A1-271[»]
4OZEX-ray1.61A/B1-282[»]
4U3BX-ray1.34A1-271[»]
4U3DX-ray1.25A1-271[»]
5DROX-ray2.01A/B1-274[»]
5DRPX-ray1.89A/B1-274[»]
5U86X-ray1.62A1-275[»]
6IH0X-ray1.21A1-271[»]
SMRiO67648
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi224324.aq_1772

Chemistry databases

BindingDBiO67648
ChEMBLiCHEMBL1075040
DrugBankiDB07355 3-(heptyloxy)benzoic acid
DB08231 Myristic acid
DB07536 N-{(1S,2R)-2-hydroxy-1-[(hydroxyamino)carbonyl]propyl}-4-{[4-(morpholin-4-ylmethyl)phenyl]ethynyl}benzamide
DB04257 Palmitoleic Acid
DB01991 Tu-514

Genome annotation databases

EnsemblBacteriaiAAC07605; AAC07605; aq_1772
GeneIDi1193363
KEGGiaae:aq_1772
PATRICifig|224324.8.peg.1368

Phylogenomic databases

eggNOGiENOG4105C7C Bacteria
COG0774 LUCA
HOGENOMiHOG000256664
InParanoidiO67648
KOiK02535
OMAiIVFYRSD
OrthoDBi428602at2

Enzyme and pathway databases

UniPathwayiUPA00359;UER00478
BioCyciAAEO224324:G1G15-1266-MONOMER
BRENDAi3.5.1.108 396

Miscellaneous databases

EvolutionaryTraceiO67648

Family and domain databases

Gene3Di3.30.1700.10, 1 hit
3.30.230.20, 1 hit
HAMAPiMF_00388 LpxC, 1 hit
InterProiView protein in InterPro
IPR020568 Ribosomal_S5_D2-typ_fold
IPR004463 UDP-acyl_GlcNac_deAcase
IPR011334 UDP-acyl_GlcNac_deAcase_C
IPR015870 UDP-acyl_N-AcGlcN_deAcase_N
PANTHERiPTHR33694 PTHR33694, 1 hit
PfamiView protein in Pfam
PF03331 LpxC, 1 hit
SUPFAMiSSF54211 SSF54211, 2 hits
TIGRFAMsiTIGR00325 lpxC, 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 nameiLPXC_AQUAE
<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: O67648
<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: June 1, 2001
Last sequence update: August 1, 1998
Last modified: September 18, 2019
This is version 130 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, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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