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Entry version 53 (29 Sep 2021)
Sequence version 1 (11 Jan 2011)
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Protein

D-ornithine 4,5-aminomutase subunit beta

Gene

oraE

Organism
Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF) (Clostridium sticklandii)
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

Component of a complex that catalyzes the reversible migration of the omega amino group of D-ornithine to C-4 to form (2R,4S)-2,4-diaminopentanoic acid. OraE may be the catalytic subunit. Active only on D-ornithine and 2,4-diaminopentanoic acid but not active on L-ornithine, L-beta-lysine, L-alpha-lysine or D-alpha-lysine.

3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the '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

Protein has several cofactor binding sites:

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

Increased activity in the presence of dithiothreitol (DTT) in vitro. Inhibited by 1 mM potassium phosphate and potassium chloride. Inhibited by L-alpha-ornithine, D,L-alpha-lysine, L-beta-lysine (50%-60%), L-alpha-lysine (26%) and by delta-amino-n-valeric acid to a lesser extent. Significant decrease in activity is observed in the presence of 0.2 mM p-chloromercuribenzoate, N-ethylmaleimide and also by 2 mM iodoacetate to a lesser extent but not inhibited by arsenite.2 Publications

<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 6.3 sec(-1). Values are measured for recombinant S and E components expressed together in E.coli to overcome the presence of corrinoids in native system.
  1. KM=44.5 µM for D-ornithine3 Publications
  2. KM=0.43 µM for adenosylcobalamin3 Publications
  3. KM=1.5 µM for pyridoxal phosphate3 Publications

pH dependencei

Optimum pH is 9.0 or between 8.5-8.7 (with Tris-HCl buffer). Half-maximal activity is observed at pH 7.4 and 9.7.3 Publications

Temperature dependencei

Optimum temperature is 37 degrees Celsius for native enzyme. Displays half-maximal activity at 23 degrees Celsius and 49 degrees Celsius. Rapidly inactivated at temperatures above 45 degrees Celsius. Loses more than 35% and 30% of its activity when stored at -20 degrees Celsius for 1 month and at 4 degrees Celsius for 48 hours, respectively.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei81Substrate1 Publication1
Binding sitei160Substrate1
Binding sitei182Substrate1 Publication1
<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 bindingi615Cobalt (adenosylcobalamin axial ligand); via tele nitrogen1 Publication1
Binding sitei700Adenosylcobalamin1
Binding sitei720Adenosylcobalamin1

<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

<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 functionIsomerase
LigandCobalamin, Cobalt, Metal-binding, Pyridoxal phosphate

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-12493

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
5.4.3.5, 1522

<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:
D-ornithine 4,5-aminomutase subunit beta (EC:5.4.3.53 Publications)
Alternative name(s):
D-ornithine aminomutase E component1 Publication
Short name:
OAM-E
<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:oraE
Ordered Locus Names:CLOST_1290
<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>OrganismiAcetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF) (Clostridium sticklandii)
<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 identifieri499177 [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 lineageiBacteriaFirmicutesClostridiaEubacterialesPeptostreptococcaceaeAcetoanaerobium
<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
  • UP000007041 <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>Mutagenesisi615H → G: Loss of corrinoid-binding ability. 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_00004218051 – 740D-ornithine 4,5-aminomutase subunit betaAdd BLAST740

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 residuei626N6-(pyridoxal phosphate)lysine1 Publication1

<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

Heterotetramer of 2 alpha (OraS) and 2 beta (OraE) subunits.

3 Publications

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
1511.CLOST_1290

<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

1740
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
E3PY95

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini602 – 739B12-bindingPROSITE-ProRule annotationAdd BLAST138

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni294 – 296Substrate binding3
Regioni614 – 616Adenosylcobalamin binding1 Publication3
Regioni664 – 669Adenosylcobalamin binding1 Publication6

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG5012, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_027795_0_0_9

Identification of Orthologs from Complete Genome Data

More...
OMAi
AWKVMPE

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.20.20.440, 1 hit
3.30.30.60, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR016176, Cbl-dep_enz_cat
IPR006158, Cobalamin-bd
IPR036724, Cobalamin-bd_sf
IPR028991, KamE_N
IPR036843, KamE_N_sf
IPR015130, Lys-AminoMut_A
IPR037086, Lys-AminoMut_asu_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02310, B12-binding, 1 hit
PF09043, Lys-AminoMut_A, 1 hit
PF16554, OAM_dimer, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51703, SSF51703, 1 hit
SSF52242, SSF52242, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51332, B12_BINDING, 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.

E3PY95-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEKDLQLRVN EKLDVENILK DLDKYTPKRR GWTWRQPAEN LQMGPFIYKD
60 70 80 90 100
ASTPLENSVA LPSAKYFGDI DPQPLPVITT EIASGRFEDD IRRMRMAAWH
110 120 130 140 150
GADHIMVIRT AGQSHYDGLI EGTPQGIGGV PITRKQVRAQ RKALDLIEEE
160 170 180 190 200
VGRPINYHSY VSGVAGPDIA VMFAEEGVNG AHQDPQYNVL YRNINMIRSF
210 220 230 240 250
IDACESKTIM AWADMAQIDG AHNANATARE AWKVMPELMV QHALNSIFSL
260 270 280 290 300
KVGMKKSNIC LSTVPPTAPP APSMYLDLPY AVALREMFEG YRMRAQMNTK
310 320 330 340 350
YMEASTREAT VTHVLNLLIS KLTRADIQST ITPDEGRNVP WHIYNIEACD
360 370 380 390 400
TAKQALIGMD GLMDMVQLKR EGVLGDTVRE LKERAVLFME EIIEAGGYFN
410 420 430 440 450
AVEQGFFVDS GYYPERNGDG IARQINGGIG AGTVFERDED YMAPVTAHFG
460 470 480 490 500
YNNVKQYDEA LVSEPSKLID GCTLEVPEKI VYIDELDEND NVNVRMEETK
510 520 530 540 550
EFRHSSMIKP EVEWQADGTV LLTMFLPTSK RVAEFAAIEF AKKMNLEEVE
560 570 580 590 600
VINREVMQEA EGTRIELKGR VPFSIDINSL VIPPEPEILS EDEIREDIEK
610 620 630 640 650
TPLKIVAATV GEDEHSVGLR EVIDIKHGGI EKYGVEVHYL GTSVPVEKLV
660 670 680 690 700
DAAIELKADA ILASTIISHD DIHYKNMKRI HELAVEKGIR DKIMIGCGGT
710 720 730 740
QVTPEVAVKQ GVDAGFGRGS KGIHVATFLV KKRREMREGK
Length:740
Mass (Da):82,765
Last modified:January 11, 2011 - 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:iA12B500F690213A9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti25Y → T AA sequence (PubMed:11577113).Curated1
Sequence conflicti220G → GIDG in AAK72502 (PubMed:11577113).Curated1

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
AY038595 Genomic DNA Translation: AAK72502.1
FP565809 Genomic DNA Translation: CBH21410.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CBH21410; CBH21410; CLOST_1290

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
cst:CLOST_1290

<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
AY038595 Genomic DNA Translation: AAK72502.1
FP565809 Genomic DNA Translation: CBH21410.1

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
3KOWX-ray2.90A/B/C/D1-740[»]
3KOXX-ray2.40A/B/C/D1-740[»]
3KOYX-ray2.80A/B/C/D1-740[»]
3KOZX-ray2.80A/B/C/D1-740[»]
3KP0X-ray2.80A/B/C/D1-740[»]
3KP1X-ray2.01A/B/C/D1-740[»]
SMRiE3PY95
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi1511.CLOST_1290

Genome annotation databases

EnsemblBacteriaiCBH21410; CBH21410; CLOST_1290
KEGGicst:CLOST_1290

Phylogenomic databases

eggNOGiCOG5012, Bacteria
HOGENOMiCLU_027795_0_0_9
OMAiAWKVMPE

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12493
BRENDAi5.4.3.5, 1522

Family and domain databases

Gene3Di3.20.20.440, 1 hit
3.30.30.60, 1 hit
InterProiView protein in InterPro
IPR016176, Cbl-dep_enz_cat
IPR006158, Cobalamin-bd
IPR036724, Cobalamin-bd_sf
IPR028991, KamE_N
IPR036843, KamE_N_sf
IPR015130, Lys-AminoMut_A
IPR037086, Lys-AminoMut_asu_sf
PfamiView protein in Pfam
PF02310, B12-binding, 1 hit
PF09043, Lys-AminoMut_A, 1 hit
PF16554, OAM_dimer, 1 hit
SUPFAMiSSF51703, SSF51703, 1 hit
SSF52242, SSF52242, 1 hit
PROSITEiView protein in PROSITE
PS51332, B12_BINDING, 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 nameiOAME_ACESD
<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: E3PY95
Secondary accession number(s): Q8VPJ5
<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: March 6, 2013
Last sequence update: January 11, 2011
Last modified: September 29, 2021
This is version 53 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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