Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 89 (25 May 2022)
Sequence version 1 (05 Jul 2004)
Previous versions | rss
Add a publicationFeedback
Protein

Trans-2-enoyl-CoA reductase [NADH]

Gene

fabV

Organism
Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104)
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

Involved in the fatty acid synthesis (FAS II). Catalyzes the reduction of the carbon-carbon double bond of crotonyl-CoA to yield butyryl-CoA. In vitro it can also use hexenoyl-CoA and dodecenoyl-CoA as substrates (PubMed:22906002).

3 Publications

Miscellaneous

Possesses high activity for the reduction reaction, but no activity for the reverse oxidation reaction.1 Publication

<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

Inhibited by lauroyl-CoA.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 385.9 sec(-1) for reductase activity (at pH 6.2 and 25 degrees Celsius) (PubMed:23050861). kcat is 112 sec(-1) for reductase activity with hexenoyl-CoA as substrate (PubMed:22906002). kcat is 91 sec(-1) for reductase activity with crotonyl-CoA as substrate (PubMed:22906002). kcat is 90 sec(-1) for reductase activity with dodecenoyl-CoA as substrate (PubMed:22906002).2 Publications
  1. KM=2.7 µM for crotonyl-CoA (at pH 6.2 and 30 degrees Celsius)1 Publication
  2. KM=5.2 µM for NAD1 Publication
  3. KM=12 µM for dodecenoyl-CoA1 Publication
  4. KM=12 µM for hexenoyl-CoA1 Publication
  5. KM=69.7 µM for NAD (at pH 6.2 and 25 degrees Celsius)1 Publication
  6. KM=70 µM for crotonyl-CoA1 Publication
  7. KM=190 µM for NADP1 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: fatty acid biosynthesis

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Sitei80Plays an important role in discriminating NADH against NADPH1 Publication1
<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 sitei230Substrate1 Publication1
<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 sitei240Proton donorUniRule annotation2 Publications1
Binding sitei249NAD1 Publication1

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 bindingi53 – 58NAD1 Publication6
Nucleotide bindingi79 – 80NAD1 Publication2
Nucleotide bindingi116 – 117NAD1 Publication2
Nucleotide bindingi144 – 145NAD1 Publication2
Nucleotide bindingi276 – 278NAD1 Publication3

<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

  • NAD binding Source: UniProtKB
  • trans-2-enoyl-CoA reductase (NAD+) activity Source: UniProtKB

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 functionOxidoreductase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandNAD

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.3.1.44, 6426

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

More...
UniPathwayi
UPA00094

<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:
Trans-2-enoyl-CoA reductase [NADH]1 Publication (EC:1.3.1.443 Publications)
Short name:
TER1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:fabV1 Publication
Ordered Locus Names:TDE_0597
<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>OrganismiTreponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104)
<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 identifieri243275 [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 lineageiBacteriaSpirochaetesSpirochaetalesTreponemataceaeTreponema
<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
  • UP000008212 <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

<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 use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Used in the biosynthesis of medium-chain volatile alcohols as biofuels engineered by microorganisms. The switch from the native flavin-dependent enoyl-CoA reductase used in the production of n-butanol, a key second-generation biofuel, to a flavin-independent trans-enoyl-CoA reductase from T.denticola leads to an order of magnitude increase in product yield in engineered E.coli.1 Publication

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>Mutagenesisi240Y → F: Loss of reductase activity, but no significant change in the affinity for crotonyl-CoA. 1 Publication1
Mutagenesisi276L → A: Significant decrease of the catalytic efficiency; when associated with A-277. The catalytic efficiency is slightly reduces and the affinity is relatively similar to wild-type; when associated with A-277 and A-295. 1 Publication1
Mutagenesisi277V → A: Significant decrease of the catalytic efficiency; when associated with A-276. The catalytic efficiency is slightly reduces and the affinity is relatively similar to wild-type; when associated with A-276 and A-295. 1 Publication1
Mutagenesisi287I → A: Shows 7-, 13- and 15-fold decrease of catalytic efficiency of the reductase activity for hexenoyl-CoA, crotonyl-CoA and dodecenoyl-CoA, respectively. The affinity is relatively similar to wild-type. This mutation may increase the accessibility of the longer acyl chain to the active site pocket. 1 Publication1
Mutagenesisi291L → A: The catalytic efficiency and affinity are relatively similar to wild-type toward crotonyl-CoA and hexenoyl-CoA. 1 Publication1
Mutagenesisi295F → A: The catalytic efficiency and affinity are relatively similar to wild-type toward crotonyl-CoA and hexenoyl-CoA. The catalytic efficiency is slightly reduces and the affinity is relatively similar to wild-type; when associated with A-276 and A-277. 1 Publication1
Mutagenesisi370Y → A: The catalytic efficiency and affinity are relatively similar to wild-type toward crotonyl-CoA and hexenoyl-CoA. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002200501 – 397Trans-2-enoyl-CoA reductase [NADH]Add BLAST397

<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

Monomer.

3 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
243275.TDE_0597

<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

1397
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...
AlphaFoldDBi
Q73Q47

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

More...
SMRi
Q73Q47

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

Belongs to the TER reductase family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG3007, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_057698_1_0_12

Identification of Orthologs from Complete Genome Data

More...
OMAi
EGCIEQI

Database of Orthologous Groups

More...
OrthoDBi
678530at2

Family and domain databases

HAMAP database of protein families

More...
HAMAPi
MF_01838, FabV_reductase, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR024906, Eno_Rdtase_FAD-bd_dom
IPR024910, Enoyl-CoA_Rdtase_cat_dom
IPR010758, Trans-2-enoyl-CoA_reductase

The PANTHER Classification System

More...
PANTHERi
PTHR37480, PTHR37480, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF07055, Eno-Rase_FAD_bd, 1 hit
PF12242, Eno-Rase_NADH_b, 1 hit
PF12241, Enoyl_reductase, 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.

Q73Q47-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MIVKPMVRNN ICLNAHPQGC KKGVEDQIEY TKKRITAEVK AGAKAPKNVL
60 70 80 90 100
VLGCSNGYGL ASRITAAFGY GAATIGVSFE KAGSETKYGT PGWYNNLAFD
110 120 130 140 150
EAAKREGLYS VTIDGDAFSD EIKAQVIEEA KKKGIKFDLI VYSLASPVRT
160 170 180 190 200
DPDTGIMHKS VLKPFGKTFT GKTVDPFTGE LKEISAEPAN DEEAAATVKV
210 220 230 240 250
MGGEDWERWI KQLSKEGLLE EGCITLAYSY IGPEATQALY RKGTIGKAKE
260 270 280 290 300
HLEATAHRLN KENPSIRAFV SVNKGLVTRA SAVIPVIPLY LASLFKVMKE
310 320 330 340 350
KGNHEGCIEQ ITRLYAERLY RKDGTIPVDE ENRIRIDDWE LEEDVQKAVS
360 370 380 390
ALMEKVTGEN AESLTDLAGY RHDFLASNGF DVEGINYEAE VERFDRI
Length:397
Mass (Da):43,759
Last modified:July 5, 2004 - 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:i7D5916140E5A8F35
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
AE017226 Genomic DNA Translation: AAS11092.1

NCBI Reference Sequences

More...
RefSeqi
NP_971211.1, NC_002967.9
WP_002681770.1, NC_002967.9

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAS11092; AAS11092; TDE_0597

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
2741560

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
tde:TDE_0597

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|243275.7.peg.577

<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
AE017226 Genomic DNA Translation: AAS11092.1
RefSeqiNP_971211.1, NC_002967.9
WP_002681770.1, NC_002967.9

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
4FBGX-ray3.02A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-397[»]
4GGOX-ray2.00A/B/C/D1-397[»]
4GGPX-ray2.05A/B/C/D1-397[»]
AlphaFoldDBiQ73Q47
SMRiQ73Q47
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi243275.TDE_0597

Genome annotation databases

EnsemblBacteriaiAAS11092; AAS11092; TDE_0597
GeneIDi2741560
KEGGitde:TDE_0597
PATRICifig|243275.7.peg.577

Phylogenomic databases

eggNOGiCOG3007, Bacteria
HOGENOMiCLU_057698_1_0_12
OMAiEGCIEQI
OrthoDBi678530at2

Enzyme and pathway databases

UniPathwayiUPA00094
BRENDAi1.3.1.44, 6426

Family and domain databases

HAMAPiMF_01838, FabV_reductase, 1 hit
InterProiView protein in InterPro
IPR024906, Eno_Rdtase_FAD-bd_dom
IPR024910, Enoyl-CoA_Rdtase_cat_dom
IPR010758, Trans-2-enoyl-CoA_reductase
PANTHERiPTHR37480, PTHR37480, 1 hit
PfamiView protein in Pfam
PF07055, Eno-Rase_FAD_bd, 1 hit
PF12242, Eno-Rase_NADH_b, 1 hit
PF12241, Enoyl_reductase, 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 nameiFABV_TREDE
<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: Q73Q47
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: July 5, 2004
Last modified: May 25, 2022
This is version 89 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again