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Entry version 104 (26 Feb 2020)
Sequence version 1 (19 Jul 2004)
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Protein

Glyceraldehyde-3-phosphate dehydrogenase 1

Gene

gapA1

Organism
Staphylococcus aureus (strain MRSA252)
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 oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.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 '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 70 sec(-1) for dehydrogenase activity.1 Publication
  1. KM=0.31 mM for G3P1 Publication
  2. KM=316 mM for NAD1 Publication

    pH dependencei

    Optimum pH is 8.7.1 Publication

    Temperature dependencei

    Optimum temperature is 25 degrees Celsius.1 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: glycolysis

    This protein is involved in step 1 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.1 Publication
    Proteins known to be involved in the 5 steps of the subpathway in this organism are:
    1. Glyceraldehyde-3-phosphate dehydrogenase 1 (gapA1), Glyceraldehyde-3-phosphate dehydrogenase 2 (gapA2)
    2. Phosphoglycerate kinase (pgk)
    3. 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA)
    4. Enolase (eno)
    5. Pyruvate kinase (pyk)
    This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 sitei34NAD2 Publications1
    Binding sitei120NAD2 Publications1
    <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 sitei151Nucleophile1 Publication1
    <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>Sitei178Activates thiol group during catalysis1 Publication1
    Binding sitei181Glyceraldehyde 3-phosphate1 Publication1
    Binding sitei198Glyceraldehyde 3-phosphateBy similarity1
    Binding sitei234Glyceraldehyde 3-phosphate1 Publication1
    Binding sitei316NAD1 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 bindingi12 – 13NAD2 Publications2

    <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

    • glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity Source: UniProtKB
    • NAD binding Source: UniProtKB
    • NADP binding Source: InterPro

    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 processGlycolysis
    LigandNAD, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    SAUR282458:G1G3O-883-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.2.1.12 3352

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

    More...
    UniPathwayi
    UPA00109;UER00184

    Protein family/group databases

    MoonProt database of moonlighting proteins

    More...
    MoonProti
    Q6GIL8

    <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:
    Glyceraldehyde-3-phosphate dehydrogenase 11 Publication (EC:1.2.1.121 Publication)
    Short name:
    GAPDH 11 Publication
    Alternative name(s):
    NAD-dependent glyceraldehyde-3-phosphate dehydrogenase1 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:gapA1
    Synonyms:gap, gapA
    Ordered Locus Names:SAR0828
    <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>OrganismiStaphylococcus aureus (strain MRSA252)
    <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 identifieri282458 [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 lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

    <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

    Cytoplasm

    <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%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>Mutagenesisi151C → S: Loss of dehydrogenase activity. 1 Publication1
    Mutagenesisi178H → N: Loss of dehydrogenase activity. 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001456851 – 336Glyceraldehyde-3-phosphate dehydrogenase 1Add BLAST336

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q6GIL8

    <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

    Homotetramer.

    2 Publications

    <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

    1336
    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
    Q6GIL8

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    Q6GIL8

    <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>Regioni150 – 152Glyceraldehyde 3-phosphate binding1 Publication3
    Regioni211 – 212Glyceraldehyde 3-phosphate binding1 Publication2

    <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

    Phylogenomic databases

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_030140_0_0_9

    KEGG Orthology (KO)

    More...
    KOi
    K00134

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    NCVAPMA

    Database of Orthologous Groups

    More...
    OrthoDBi
    944149at2

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR020831 GlycerAld/Erythrose_P_DH
    IPR020830 GlycerAld_3-P_DH_AS
    IPR020829 GlycerAld_3-P_DH_cat
    IPR020828 GlycerAld_3-P_DH_NAD(P)-bd
    IPR006424 Glyceraldehyde-3-P_DH_1
    IPR036291 NAD(P)-bd_dom_sf

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF02800 Gp_dh_C, 1 hit
    PF00044 Gp_dh_N, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF000149 GAP_DH, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00078 G3PDHDRGNASE

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00846 Gp_dh_N, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51735 SSF51735, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01534 GAPDH-I, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00071 GAPDH, 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.

    Q6GIL8-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MAVKVAINGF GRIGRLAFRR IQEVEGLEVV AVNDLTDDDM LAHLLKYDTM
    60 70 80 90 100
    QGRFTGEVEV VDGGFRVNGK EVKSFSEPDA SKLPWKDLNI DVVLECTGFY
    110 120 130 140 150
    TDKDKAQAHI EAGAKKVLIS APATGDLKTI VFNTNHQELD GSETVVSGAS
    160 170 180 190 200
    CTTNSLAPVA KVLNDDFGLV EGLMTTIHAY TGDQNTQDAP HRKGDKRRAR
    210 220 230 240 250
    AAAENIIPNS TGAAKAIGKV IPEIDGKLDG GAQRVPVATG SLTELTVVLE
    260 270 280 290 300
    KQDVTVEQVN EAMKNASNES FGYTEDEIVS SDVVGMTYGS LFDATQTRVM
    310 320 330
    SVGDRQLVKV AAWYDNEMSY TAQLVRTLAY LAELSK
    Length:336
    Mass (Da):36,281
    Last modified:July 19, 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:i37A6CEA9376779E5
    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
    BX571856 Genomic DNA Translation: CAG39837.1

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_000279414.1, NC_002952.2

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    CAG39837; CAG39837; SAR0828

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    sar:SAR0828

    <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
    BX571856 Genomic DNA Translation: CAG39837.1
    RefSeqiWP_000279414.1, NC_002952.2

    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
    3HQ4X-ray2.20O/P/Q/R1-336[»]
    3K73X-ray2.50O/P/Q/R1-336[»]
    3K9QX-ray2.50O/P/Q/R1-336[»]
    3KSDX-ray2.20O/P/Q/R1-336[»]
    3KSZX-ray2.60O/P/Q/R1-336[»]
    3KV3X-ray2.50O/P/Q/R1-336[»]
    3L4SX-ray2.20O/P/Q/R1-336[»]
    3L6OX-ray2.20O/P/Q/R1-336[»]
    3LC1X-ray2.00O/P/Q/R1-336[»]
    3LC2X-ray2.80O/P/Q/R1-336[»]
    3LC7X-ray2.50O/P/Q/R1-336[»]
    3LVFX-ray1.70O/P/Q/R1-336[»]
    3VAZX-ray3.19A/B/O/P/Q/R1-336[»]
    5T73X-ray2.60A/B/C/D1-336[»]
    SMRiQ6GIL8
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein family/group databases

    MoonProtiQ6GIL8

    Proteomic databases

    PRIDEiQ6GIL8

    Genome annotation databases

    EnsemblBacteriaiCAG39837; CAG39837; SAR0828
    KEGGisar:SAR0828

    Phylogenomic databases

    HOGENOMiCLU_030140_0_0_9
    KOiK00134
    OMAiNCVAPMA
    OrthoDBi944149at2

    Enzyme and pathway databases

    UniPathwayiUPA00109;UER00184
    BioCyciSAUR282458:G1G3O-883-MONOMER
    BRENDAi1.2.1.12 3352

    Miscellaneous databases

    EvolutionaryTraceiQ6GIL8

    Family and domain databases

    InterProiView protein in InterPro
    IPR020831 GlycerAld/Erythrose_P_DH
    IPR020830 GlycerAld_3-P_DH_AS
    IPR020829 GlycerAld_3-P_DH_cat
    IPR020828 GlycerAld_3-P_DH_NAD(P)-bd
    IPR006424 Glyceraldehyde-3-P_DH_1
    IPR036291 NAD(P)-bd_dom_sf
    PfamiView protein in Pfam
    PF02800 Gp_dh_C, 1 hit
    PF00044 Gp_dh_N, 1 hit
    PIRSFiPIRSF000149 GAP_DH, 1 hit
    PRINTSiPR00078 G3PDHDRGNASE
    SMARTiView protein in SMART
    SM00846 Gp_dh_N, 1 hit
    SUPFAMiSSF51735 SSF51735, 1 hit
    TIGRFAMsiTIGR01534 GAPDH-I, 1 hit
    PROSITEiView protein in PROSITE
    PS00071 GAPDH, 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 nameiG3P1_STAAR
    <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: Q6GIL8
    <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 1, 2005
    Last sequence update: July 19, 2004
    Last modified: February 26, 2020
    This is version 104 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

    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
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