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Protein

ATP-dependent 6-phosphofructokinase

Gene

pfkA

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
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 phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.UniRule annotation1 Publication

Miscellaneous

In the R state the 6-P group of fructose 6-phosphate (F6P) is bound by His-249 from one chain and Arg-162 and Arg-243 from an adjacent chain. In the T state a conformation change moves Arg-162 away from the substrate. Glu-161 takes its place, hence repelling the phosphate of ATP.1 Publication

<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

Mg2+UniRule annotation1 Publication

<p>This subsection of the ‘Function’ 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

Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate.UniRule annotation1 Publication2 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

  1. KM=0.07 mM for ATP1 Publication
  2. KM=0.033 mM for fructose 6-phosphate1 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: glycolysis

    This protein is involved in step 3 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.UniRule annotation
    Proteins known to be involved in the 4 steps of the subpathway in this organism are:
    1. no protein annotated in this organism
    2. Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase (pgiB), Glucose-6-phosphate isomerase A (pgiA), Glucose-6-phosphate isomerase B (pgiB)
    3. ATP-dependent 6-phosphofructokinase (pfkA), ATP-dependent 6-phosphofructokinase (pfkA), ATP-dependent 6-phosphofructokinase (pfkA), ATP-dependent 6-phosphofructokinase (pfkA)
    4. Fructose-bisphosphate aldolase (fba)
    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 D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ 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 sitei11ATP; via amide nitrogenUniRule annotation1
    Binding sitei59Allosteric activator ADP; shared with dimeric partnerUniRule annotation1 Publication1
    <p>This subsection of the ‘Function’ 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 bindingi103Magnesium; catalyticUniRule annotation1 Publication1
    <p>This subsection of the ‘Function’ 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 sitei127Proton acceptorUniRule annotation1
    Binding sitei154Allosteric activator ADPUniRule annotation1 Publication1
    Binding sitei162Substrate; shared with dimeric partnerUniRule annotation1 Publication1
    Binding sitei211Allosteric activator ADPUniRule annotation1 Publication1
    Binding sitei222SubstrateUniRule annotation2 Publications1
    Binding sitei243Substrate; shared with dimeric partnerUniRule annotation2 Publications1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ 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 bindingi72 – 73ATPUniRule annotation1 Publication2
    Nucleotide bindingi102 – 105ATPUniRule annotation4

    <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 functionAllosteric enzyme, Kinase, Transferase
    Biological processGlycolysis
    LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.7.1.11 623

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P00512

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

    More...
    UniPathwayi
    UPA00109;UER00182

    <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-dependent 6-phosphofructokinaseUniRule annotation (EC:2.7.1.11UniRule annotation)
    Short name:
    ATP-PFKUniRule annotation
    Short name:
    PhosphofructokinaseUniRule annotation
    Alternative name(s):
    PhosphohexokinaseUniRule annotation
    <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:pfkAUniRule annotation
    Synonyms:pfk
    <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>OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
    <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 identifieri1422 [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 lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

    <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

    Chemistry databases

    Drug and drug target database

    More...
    DrugBanki
    DB02726 2-Phosphoglycolic Acid
    DB04493 Fructose-6-Phosphate

    <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_00001119351 – 319ATP-dependent 6-phosphofructokinaseAdd BLAST319

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P00512

    <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

    Homotetramer.UniRule annotation4 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

    1319
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P00512

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

    More...
    SMRi
    P00512

    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
    P00512

    <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>Regioni21 – 25Allosteric activator ADP binding; shared with dimeric partnerUniRule annotation1 Publication5
    Regioni125 – 127Substrate bindingUniRule annotation2 Publications3
    Regioni169 – 171Substrate bindingUniRule annotation2 Publications3
    Regioni185 – 187Allosteric activator ADP bindingUniRule annotation1 Publication3
    Regioni213 – 215Allosteric activator ADP bindingUniRule annotation1 Publication3
    Regioni249 – 252Substrate bindingUniRule annotation2 Publications4

    <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

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00763 Bacterial_PFK, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00339 Phosphofructokinase_I_B1, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR022953 ATP_PFK
    IPR012003 ATP_PFK_prok-type
    IPR012828 PFKA_ATP_prok
    IPR015912 Phosphofructokinase_CS
    IPR000023 Phosphofructokinase_dom
    IPR035966 PKF_sf

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00365 PFK, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF000532 ATP_PFK_prok, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00476 PHFRCTKINASE

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF53784 SSF53784, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR02482 PFKA_ATP, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00433 PHOSPHOFRUCTOKINASE, 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.

    P00512-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKRIGVLTSG GDSPGMNAAI RSVVRKAIYH GVEVYGVYHG YAGLIAGNIK
    60 70 80 90 100
    KLEVGDVGDI IHRGGTILYT ARCPEFKTEE GQKKGIEQLK KHGIEGLVVI
    110 120 130 140 150
    GGDGSYQGAK KLTEHGFPCV GVPGTIDNDI PGTDFTIGFD TALNTVIDAI
    160 170 180 190 200
    DKIRDTATSH ERTYVIEVMG RHAGDIALWS GLAGGAETIL IPEADYDMND
    210 220 230 240 250
    VIARLKRGHE RGKKHSIIIV AEGVGSGVDF GRQIQEATGF ETRVTVLGHV
    260 270 280 290 300
    QRGGSPTAFD RVLASRLGAR AVELLLEGKG GRCVGIQNNQ LVDHDIAEAL
    310
    ANKHTIDQRM YALSKELSI
    Length:319
    Mass (Da):34,119
    Last modified:July 1, 1989 - v2
    <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:iEE968D39BA30712B
    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 conflicti12D → N AA sequence (PubMed:6447595).Curated1
    Sequence conflicti35 – 37Missing AA sequence (PubMed:6447595).Curated3
    Sequence conflicti43G → V AA sequence (PubMed:6447595).Curated1
    Sequence conflicti82Q → E AA sequence (PubMed:6447595).Curated1
    Sequence conflicti95E → Q AA sequence (PubMed:6447595).Curated1
    Sequence conflicti225G → L AA sequence (PubMed:6447595).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
    M15643 Genomic DNA Translation: AAA22656.1
    D13095 Genomic DNA Translation: BAA02405.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A27474 KIBSFF

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_033014452.1, NZ_LUCR01000070.1

    <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
    M15643 Genomic DNA Translation: AAA22656.1
    D13095 Genomic DNA Translation: BAA02405.1
    PIRiA27474 KIBSFF
    RefSeqiWP_033014452.1, NZ_LUCR01000070.1

    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
    1MTOX-ray3.20A/B/C/D/E/F/G/H1-319[»]
    3PFKX-ray2.40A1-319[»]
    3U39X-ray2.79A/B/C/D1-319[»]
    4I36X-ray2.30A/B/C/D1-319[»]
    4I4IX-ray2.49A/B/C/D1-319[»]
    4I7EX-ray2.00A/B/C/D1-319[»]
    4PFKX-ray2.40A1-319[»]
    6PFKX-ray2.60A/B/C/D1-319[»]
    ProteinModelPortaliP00512
    SMRiP00512
    ModBaseiSearch...
    MobiDBiSearch...

    Chemistry databases

    DrugBankiDB02726 2-Phosphoglycolic Acid
    DB04493 Fructose-6-Phosphate

    Proteomic databases

    PRIDEiP00512

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayi
    UPA00109;UER00182

    BRENDAi2.7.1.11 623
    SABIO-RKiP00512

    Miscellaneous databases

    EvolutionaryTraceiP00512

    Family and domain databases

    CDDicd00763 Bacterial_PFK, 1 hit
    HAMAPiMF_00339 Phosphofructokinase_I_B1, 1 hit
    InterProiView protein in InterPro
    IPR022953 ATP_PFK
    IPR012003 ATP_PFK_prok-type
    IPR012828 PFKA_ATP_prok
    IPR015912 Phosphofructokinase_CS
    IPR000023 Phosphofructokinase_dom
    IPR035966 PKF_sf
    PfamiView protein in Pfam
    PF00365 PFK, 1 hit
    PIRSFiPIRSF000532 ATP_PFK_prok, 1 hit
    PRINTSiPR00476 PHFRCTKINASE
    SUPFAMiSSF53784 SSF53784, 1 hit
    TIGRFAMsiTIGR02482 PFKA_ATP, 1 hit
    PROSITEiView protein in PROSITE
    PS00433 PHOSPHOFRUCTOKINASE, 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 nameiPFKA_GEOSE
    <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: P00512
    <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: July 21, 1986
    Last sequence update: July 1, 1989
    Last modified: December 5, 2018
    This is version 145 of the entry and version 2 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

    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
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