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Protein

ATP synthase subunit epsilon, mitochondrial

Gene

ATP5F1E

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score:

Annotation score:4 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

Mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F1 - containing the extramembraneous catalytic core, and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F1 domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.

<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

Biological processATP synthesis, Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-BTA-163210 Formation of ATP by chemiosmotic coupling
R-BTA-8949613 Cristae formation

<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:
ATP synthase subunit epsilon, mitochondrialCurated
Short name:
ATPase subunit epsilon
Alternative name(s):
ATP synthase F1 subunit epsilonBy similarity
<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:ATP5F1EBy similarity
Synonyms:ATP5E
<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>OrganismiBos taurus (Bovine)
<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 identifieri9913 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
<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
  • UP000009136 <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> Componentsi: Chromosome 13, Chromosome 22

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

CF(1), Membrane, Mitochondrion, Mitochondrion inner membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL612444

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved2 Publications
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000716612 – 51ATP synthase subunit epsilon, mitochondrialAdd BLAST50

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 residuei21N6-acetyllysine; alternateBy similarity1
Modified residuei21N6-succinyllysine; alternateBy similarity1
Modified residuei32N6-acetyllysine; alternateBy similarity1
Modified residuei32N6-succinyllysine; alternateBy similarity1
Modified residuei37N6-acetyllysine; alternateBy similarity1
Modified residuei37N6-succinyllysine; alternateBy similarity1
Modified residuei44N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

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

More...
PaxDbi
P05632

PRoteomics IDEntifications database

More...
PRIDEi
P05632

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSBTAG00000032954 Expressed in 9 organ(s), highest expression level in adult mammalian kidney

<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

F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 seems to have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MD and MP68.2 Publications

Protein-protein interaction databases

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P05632

Database of interacting proteins

More...
DIPi
DIP-46312N

Protein interaction database and analysis system

More...
IntActi
P05632, 8 interactors

Molecular INTeraction database

More...
MINTi
P05632

STRING: functional protein association networks

More...
STRINGi
9913.ENSBTAP00000051455

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P05632

<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

151
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
1E79X-ray2.40I2-51[»]
1H8EX-ray2.00I2-51[»]
2CK3X-ray1.95I2-51[»]
2JDIX-ray1.90I2-51[»]
2V7QX-ray2.10I2-51[»]
2W6HX-ray5.00I1-51[»]
2W6IX-ray4.00I1-51[»]
2W6JX-ray3.84I1-51[»]
2WSSX-ray3.20I/R2-51[»]
2XNDX-ray3.50I2-48[»]
4ASUX-ray2.60I2-51[»]
4YXWX-ray3.10I2-51[»]
5ARAelectron microscopy6.70I2-51[»]
5AREelectron microscopy7.40I2-51[»]
5ARHelectron microscopy7.20I2-51[»]
5ARIelectron microscopy7.40I2-51[»]
5FIJelectron microscopy7.40I2-51[»]
5FIKelectron microscopy6.40I2-51[»]
5FILelectron microscopy7.10I2-51[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P05632

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

More...
SMRi
P05632

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P05632

<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 eukaryotic ATPase epsilon family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3495 Eukaryota
ENOG410Y5P5 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000015470

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000214506

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG050611

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P05632

KEGG Orthology (KO)

More...
KOi
K02135

Identification of Orthologs from Complete Genome Data

More...
OMAi
ANAMKTS

Database of Orthologous Groups

More...
OrthoDBi
1628103at2759

TreeFam database of animal gene trees

More...
TreeFami
TF300278

Family and domain databases

Conserved Domains Database

More...
CDDi
cd12153 F1-ATPase_epsilon, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.1620.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006721 ATP_synth_F1_esu_mt
IPR036742 ATP_synth_F1_esu_sf_mt

The PANTHER Classification System

More...
PANTHERi
PTHR12448 PTHR12448, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF04627 ATP-synt_Eps, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48690 SSF48690, 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>.<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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P05632-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVAYWRQAGL SYIRYSQICA KAVRDALKTE FKANAMKTSG STIKIVKVKK

E
Length:51
Mass (Da):5,783
Last modified:January 23, 2007 - v4
<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:iE0D70FA7C9191CAE
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 CAA34849 differs from that shown. Reason: Erroneous initiation.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
X16978 mRNA Translation: CAA34849.1 Different initiation.
BC108146 mRNA Translation: AAI08147.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S08239 PWBOE

NCBI Reference Sequences

More...
RefSeqi
NP_001137213.1, NM_001143741.1
XP_002697025.2, XM_002696979.4
XP_005193391.1, XM_005193334.3

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Bt.58312

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSBTAT00000035337; ENSBTAP00000035213; ENSBTAG00000032954
ENSBTAT00000056576; ENSBTAP00000051455; ENSBTAG00000039208

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
617230

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bta:617230

<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
X16978 mRNA Translation: CAA34849.1 Different initiation.
BC108146 mRNA Translation: AAI08147.1
PIRiS08239 PWBOE
RefSeqiNP_001137213.1, NM_001143741.1
XP_002697025.2, XM_002696979.4
XP_005193391.1, XM_005193334.3
UniGeneiBt.58312

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E79X-ray2.40I2-51[»]
1H8EX-ray2.00I2-51[»]
2CK3X-ray1.95I2-51[»]
2JDIX-ray1.90I2-51[»]
2V7QX-ray2.10I2-51[»]
2W6HX-ray5.00I1-51[»]
2W6IX-ray4.00I1-51[»]
2W6JX-ray3.84I1-51[»]
2WSSX-ray3.20I/R2-51[»]
2XNDX-ray3.50I2-48[»]
4ASUX-ray2.60I2-51[»]
4YXWX-ray3.10I2-51[»]
5ARAelectron microscopy6.70I2-51[»]
5AREelectron microscopy7.40I2-51[»]
5ARHelectron microscopy7.20I2-51[»]
5ARIelectron microscopy7.40I2-51[»]
5FIJelectron microscopy7.40I2-51[»]
5FIKelectron microscopy6.40I2-51[»]
5FILelectron microscopy7.10I2-51[»]
ProteinModelPortaliP05632
SMRiP05632
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

CORUMiP05632
DIPiDIP-46312N
IntActiP05632, 8 interactors
MINTiP05632
STRINGi9913.ENSBTAP00000051455

Chemistry databases

BindingDBiP05632
ChEMBLiCHEMBL612444

Proteomic databases

PaxDbiP05632
PRIDEiP05632

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000035337; ENSBTAP00000035213; ENSBTAG00000032954
ENSBTAT00000056576; ENSBTAP00000051455; ENSBTAG00000039208
GeneIDi617230
KEGGibta:617230

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
514

Phylogenomic databases

eggNOGiKOG3495 Eukaryota
ENOG410Y5P5 LUCA
GeneTreeiENSGT00390000015470
HOGENOMiHOG000214506
HOVERGENiHBG050611
InParanoidiP05632
KOiK02135
OMAiANAMKTS
OrthoDBi1628103at2759
TreeFamiTF300278

Enzyme and pathway databases

ReactomeiR-BTA-163210 Formation of ATP by chemiosmotic coupling
R-BTA-8949613 Cristae formation

Miscellaneous databases

EvolutionaryTraceiP05632

Protein Ontology

More...
PROi
PR:P05632

Gene expression databases

BgeeiENSBTAG00000032954 Expressed in 9 organ(s), highest expression level in adult mammalian kidney

Family and domain databases

CDDicd12153 F1-ATPase_epsilon, 1 hit
Gene3Di1.10.1620.20, 1 hit
InterProiView protein in InterPro
IPR006721 ATP_synth_F1_esu_mt
IPR036742 ATP_synth_F1_esu_sf_mt
PANTHERiPTHR12448 PTHR12448, 1 hit
PfamiView protein in Pfam
PF04627 ATP-synt_Eps, 1 hit
SUPFAMiSSF48690 SSF48690, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiATP5E_BOVIN
<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: P05632
Secondary accession number(s): Q32PE5
<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: November 1, 1988
Last sequence update: January 23, 2007
Last modified: January 16, 2019
This is version 165 of the entry and version 4 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 programChordata 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, Direct protein sequencing, Reference proteome

Documents

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