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 75 (03 Jul 2019)
Sequence version 1 (19 Jul 2005)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Fumarate hydratase 1, mitochondrial

Gene

FH1

Organism
Leishmania major
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 reversible hydration of fumarate to (S)-malate (PubMed:22569531, PubMed:30645090). Catalyzes the hydration of fumarate to L-malate in the tricarboxylic acid (TCA) cycle to facilitate a transition step in the production of energy in the form of NADH (Probable).Curated2 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

[4Fe-4S] cluster1 PublicationNote: Binds 1 [4Fe-4S] cluster per subunit.1 Publication

<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

Specifically inhibited by 2-thiomalate, which coordinates with the catalytic [4Fe-4S] cluster.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 28.3 sec(-1) for fumarate (in anaerobic conditions) (PubMed:22569531). Kcat is 1.9 sec(-1) for fumarate (in aerobic conditions) (PubMed:22569531). Kcat is 12.9 sec(-1) for (S)-malate (in anaerobic conditions) (PubMed:22569531). Kcat is 0.55 sec(-1) for (S)-malate (in aerobic conditions) (PubMed:22569531).1 Publication
  1. KM=1.3 mM for fumarate (in anaerobic conditions)1 Publication
  2. KM=2.5 mM for fumarate (in aerobic conditions)1 Publication
  3. KM=2.3 mM for (S)-malate (in anaerobic conditions)1 Publication
  4. KM=1.2 mM for (S)-malate (in aerobic conditions)1 Publication
  1. Vmax=26.4 µmol/min/mg enzyme with fumarate as substrate (in anaerobic conditions)
  2. Vmax=1.8 µmol/min/mg enzyme with fumarate as substrate (in aerobic conditions)
  3. Vmax=11.8 µmol/min/mg enzyme with (S)-malate as substrate (in anaerobic conditions)
  4. Vmax=0.5 µmol/min/mg enzyme with (S)-malate as substrate (in aerobic conditions)

pH dependencei

Optimum pH is 8.7.1 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: tricarboxylic acid cycle

This protein is involved in step 1 of the subpathway that synthesizes (S)-malate from fumarate.By similarity
Proteins known to be involved in this subpathway in this organism are:
  1. Fumarate hydratase 1, mitochondrial (FH1)
This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-malate from fumarate, the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

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 bindingi114Iron-sulfur (4Fe-4S)Combined sources1 Publication1
<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 sitei154(S)-malate 1By similarity1
Binding sitei1542-Thiomalate inhibitorCombined sources1 Publication1
Binding sitei197(S)-malate 1; via amide nitrogenBy similarity1
Binding sitei1972-Thiomalate inhibitor; via the backbone amideBy similarity1
Metal bindingi233Iron-sulfur (4Fe-4S)Combined sources1 Publication1
Metal bindingi328Iron-sulfur (4Fe-4S)Combined sources1 Publication1
Binding sitei404(S)-malate 1By similarity1
Binding sitei4042-Thiomalate inhibitorCombined sources1 Publication1
Binding sitei474(S)-malate 1By similarity1
Binding sitei4742-Thiomalate inhibitorCombined sources1 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 functionLyase
Biological processTricarboxylic acid cycle
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

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

More...
UniPathwayi
UPA00223;UER01007

<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:
Fumarate hydratase 1, mitochondrial (EC:4.2.1.22 Publications)
Short name:
Fumarase 11 Publication
Short name:
LmFH-11 Publication
<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:FH11 Publication
ORF Names:LMJF_24_0320Imported
<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>OrganismiLeishmania major
<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 identifieri5664 [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 lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania
<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
  • UP000000542 <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 24

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
TriTrypDB:LmjF.24.0320

<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

GO - Cellular componenti

Keywords - Cellular componenti

Mitochondrion

<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 transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – ?MitochondrionSequence analysis
<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_0000447005? – 549Fumarate hydratase 1, mitochondrial

<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

Homodimer.

1 Publication

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
5664.LmjF.24.0320

<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

1549
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
Q4QAU9

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

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>Regioni115 – 116(S)-malate 1 bindingBy similarity2
Regioni115 – 1162-Thiomalate inhibitor bindingCombined sources1 Publication2
Regioni200 – 206(S)-malate 2 bindingBy similarity7
Regioni450 – 454(S)-malate 1 bindingBy similarity5
Regioni450 – 4542-Thiomalate inhibitorCombined sources1 Publication5

<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 class-I fumarase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IE1I Eukaryota
ENOG410K472 Eukaryota
COG1838 LUCA
COG1951 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000009338

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q4QAU9

KEGG Orthology (KO)

More...
KOi
K01676

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.20.130.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR004646 Fe-S_hydro-lyase_TtdA-typ_cat
IPR004647 Fe-S_hydro-lyase_TtdB-typ_cat
IPR036660 Fe-S_hydroAse_TtdB_cat_sf
IPR011167 Fe_dep_fumarate_hydratase
IPR020557 Fumarate_lyase_CS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF05681 Fumerase, 1 hit
PF05683 Fumerase_C, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF001394 Fe_dep_fumar_hy, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF117457 SSF117457, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00723 ttdB_fumA_fumB, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00163 FUMARATE_LYASES, 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.

<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.

Q4QAU9-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLRRLAPLLA EFNFVPLVSK VSHKETKYRL LTKDYVSVVQ PGAGLPEMLR
60 70 80 90 100
VDPAALTLLS STAFDDVEHL LRSSHLMSLR KIFDDPEASD NDKFVALQLL
110 120 130 140 150
KNANISSARL LPGCQDTGTA IIAGYRGDQV FVPGNDEEAL SRGVYDIFQK
160 170 180 190 200
RNFRYSQNVP LSMYDEKNTG TNLPAQIDLY ASKGMEYSFM FVAKGGGSAN
210 220 230 240 250
KSFLLQETKS VLNPKSLRNF LKEKLAMFGT SACPPYHVAV VIGGTSAEMT
260 270 280 290 300
MKVLKYASCH YYDDLITKPD MKTGYTFRDL ELEEEVLKVC QNIGMGAQFG
310 320 330 340 350
GKYYAHDVRV IRMPRHGASC PIGIGVSCSA DRQALGKINK DGVWLEELEM
360 370 380 390 400
EPSQYLPDLK EDELLKTPAV MVNLNRPMPE VLQELSKHPV RTRLSLTGTI
410 420 430 440 450
IVARDSAHAR MREMLEAGKP LPQYMKEHPV YYAGPAKQPD GLPSGSFGPT
460 470 480 490 500
TAGRMDPFVD LFQSHGGSMV MLAKGNRSKQ VTKACHKYGG FYLGSIGGPA
510 520 530 540
AVLAQNAIKK VECLDMKDLG MEAVWRIEVE NFPAFIVVDD KGNDFFEQL
Length:549
Mass (Da):60,808
Last modified:July 19, 2005 - 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:i608C35DB92700C1A
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
FR796420 Genomic DNA Translation: CAJ04118.1

NCBI Reference Sequences

More...
RefSeqi
XP_001683549.1, XM_001683497.1

Genome annotation databases

Ensembl protists genome annotation project

More...
EnsemblProtistsi
CAJ04118; CAJ04118; LMJF_24_0320

GeneDB pathogen genome database from Sanger Institute

More...
GeneDBi
LmjF.24.0320:pep

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5652198

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
lma:LMJF_24_0320

<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
FR796420 Genomic DNA Translation: CAJ04118.1
RefSeqiXP_001683549.1, XM_001683497.1

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
6MSOX-ray2.05A/B/C/D10-549[»]
SMRiQ4QAU9
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi5664.LmjF.24.0320

Genome annotation databases

EnsemblProtistsiCAJ04118; CAJ04118; LMJF_24_0320
GeneDBiLmjF.24.0320:pep
GeneIDi5652198
KEGGilma:LMJF_24_0320

Organism-specific databases

EuPathDBiTriTrypDB:LmjF.24.0320

Phylogenomic databases

eggNOGiENOG410IE1I Eukaryota
ENOG410K472 Eukaryota
COG1838 LUCA
COG1951 LUCA
HOGENOMiHOG000009338
InParanoidiQ4QAU9
KOiK01676

Enzyme and pathway databases

UniPathwayiUPA00223;UER01007

Family and domain databases

Gene3Di3.20.130.10, 1 hit
InterProiView protein in InterPro
IPR004646 Fe-S_hydro-lyase_TtdA-typ_cat
IPR004647 Fe-S_hydro-lyase_TtdB-typ_cat
IPR036660 Fe-S_hydroAse_TtdB_cat_sf
IPR011167 Fe_dep_fumarate_hydratase
IPR020557 Fumarate_lyase_CS
PfamiView protein in Pfam
PF05681 Fumerase, 1 hit
PF05683 Fumerase_C, 1 hit
PIRSFiPIRSF001394 Fe_dep_fumar_hy, 1 hit
SUPFAMiSSF117457 SSF117457, 1 hit
TIGRFAMsiTIGR00723 ttdB_fumA_fumB, 1 hit
PROSITEiView protein in PROSITE
PS00163 FUMARATE_LYASES, 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 nameiFUM1_LEIMA
<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: Q4QAU9
<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: May 8, 2019
Last sequence update: July 19, 2005
Last modified: July 3, 2019
This is version 75 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)

<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
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