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Protein

Glucose-6-phosphate 1-dehydrogenase

Gene

G6PD

Organism
Homo sapiens (Human)
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 rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis.2 Publications

Miscellaneous

Binds two molecules of NADP. The first one is a cosubstrate (bound to the N-terminal domain), the second is bound to the C-terminal domain and functions as a structural element.

<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 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=7.07 µM for NADP1 Publication
  2. KM=52 µM for glucose 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: pentose phosphate pathway

    This protein is involved in step 1 of the subpathway that synthesizes D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage).
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. Glucose-6-phosphate 1-dehydrogenase, Glucose-6-phosphate 1-dehydrogenase (zwf), Glucose-6-phosphate 1-dehydrogenase (G6PD), Glucose-6-phosphate 1-dehydrogenase (G6PD), Glucose-6-phosphate 1-dehydrogenase (G6PD), Glucose-6-phosphate 1-dehydrogenase (G6PD), Glucose-6-phosphate 1-dehydrogenase, Glucose-6-phosphate 1-dehydrogenase (zwf), Glucose-6-phosphate 1-dehydrogenase (G6PD), Glucose-6-phosphate 1-dehydrogenase (G6PD), Glucose-6-phosphate 1-dehydrogenase (G6PD)
    2. 6-phosphogluconolactonase (PGLS)
    3. 6-phosphogluconate dehydrogenase, decarboxylating (gntZ), 6-phosphogluconate dehydrogenase, decarboxylating, 6-phosphogluconate dehydrogenase, decarboxylating, 6-phosphogluconate dehydrogenase, decarboxylating (PGD)
    This subpathway is part of the pathway pentose phosphate pathway, 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-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage), the pathway pentose phosphate pathway 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 sitei72NADP 1Combined sources2 Publications1
    Binding sitei147NADP 1Combined sources2 Publications1
    Binding sitei171NADP 1; via carbonyl oxygenCombined sources2 Publications1
    Binding sitei171SubstrateCombined sources1 Publication1
    Binding sitei239SubstrateCombined sources1 Publication1
    Binding sitei258SubstrateCombined sources1 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 sitei263Proton acceptorBy similarity1
    Binding sitei357NADP 2Combined sources2 Publications1
    Binding sitei360SubstrateCombined sources1 Publication1
    Binding sitei365SubstrateCombined sources1 Publication1
    Binding sitei366NADP 2Combined sources2 Publications1
    Binding sitei370NADP 2Combined sources2 Publications1
    Binding sitei393NADP 2Combined sources2 Publications1
    Binding sitei395SubstrateCombined sources1 Publication1
    Binding sitei487NADP 2Combined sources2 Publications1
    Binding sitei503NADP 2Combined sources2 Publications1
    Binding sitei509NADP 2Combined sources2 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 bindingi38 – 45NADP 1Combined sources2 Publications8
    Nucleotide bindingi401 – 403NADP 2Combined sources2 Publications3
    Nucleotide bindingi421 – 423NADP 2Combined sources2 Publications3

    <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

    • glucose-6-phosphate dehydrogenase activity Source: UniProtKB
    • glucose binding Source: BHF-UCL
    • identical protein binding Source: IntAct
    • NADP binding Source: BHF-UCL
    • protein homodimerization activity Source: BHF-UCL

    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 processCarbohydrate metabolism, Glucose metabolism
    LigandNADP

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:HS08467-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.1.1.49 2681

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-5628897 TP53 Regulates Metabolic Genes
    R-HSA-71336 Pentose phosphate pathway

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P11413

    SIGNOR Signaling Network Open Resource

    More...
    SIGNORi
    P11413

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

    More...
    UniPathwayi
    UPA00115;UER00408

    <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:
    Glucose-6-phosphate 1-dehydrogenase (EC:1.1.1.49)
    Short name:
    G6PD
    <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:G6PD
    <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>OrganismiHomo sapiens (Human)
    <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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    <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
    • UP000005640 <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 X

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    HostDB:ENSG00000160211.15

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:4057 G6PD

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    305900 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_P11413

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

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

    <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

    <p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

    Anemia, non-spherocytic hemolytic, due to G6PD deficiency (NSHA)18 Publications
    The disease is caused by mutations affecting the gene represented in this entry. Deficiency of G6PD is associated with hemolytic anemia in two different situations. First, in areas in which malaria has been endemic, G6PD-deficiency alleles have reached high frequencies (1% to 50%) and deficient individuals, though essentially asymptomatic in the steady state, have a high risk of acute hemolytic attacks. Secondly, sporadic cases of G6PD deficiency occur at a very low frequencies, and they usually present a more severe phenotype. Several types of NSHA are recognized. Class-I variants are associated with severe NSHA; class-II have an activity <10% of normal; class-III have an activity of 10% to 60% of normal; class-IV have near normal activity.
    Disease descriptionA disease characterized by G6PD deficiency, acute hemolytic anemia, fatigue, back pain, and jaundice. In most patients, the disease is triggered by an exogenous agent, such as some drugs, food, or infection. Increased unconjugated bilirubin, lactate dehydrogenase, and reticulocytosis are markers of the disorder. Although G6PD deficiency can be life-threatening, most patients are asymptomatic throughout their life.
    See also OMIM:300908
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_00245132H → R in NSHA; Gahoe; class III; frequent in Chinese. 1 PublicationCorresponds to variant dbSNP:rs137852340Ensembl.1
    Natural variantiVAR_00245235Missing in NSHA; Sunderland; class I. 1
    Natural variantiVAR_00245344A → G in NSHA; Orissa; class III; frequent in Indian tribal populations. 1 PublicationCorresponds to variant dbSNP:rs78478128Ensembl.1
    Natural variantiVAR_00245448I → T in NSHA; Aures; class II. 1 PublicationCorresponds to variant dbSNP:rs76645461Ensembl.1
    Natural variantiVAR_00245558D → N in NSHA; Metaponto; class III. Corresponds to variant dbSNP:rs137852315Ensembl.1
    Natural variantiVAR_00245668V → M in NSHA; A(-) type I; class III; frequent in African population. 4 PublicationsCorresponds to variant dbSNP:rs1050828Ensembl.1
    Natural variantiVAR_00245770Y → H in NSHA; Namoru; 4% activity. Corresponds to variant dbSNP:rs137852349Ensembl.1
    Natural variantiVAR_00245875L → P in NSHA; Swansea; class I. 1 Publication1
    Natural variantiVAR_00246081R → C in NSHA; Konan/Ube; class III. Corresponds to variant dbSNP:rs138687036Ensembl.1
    Natural variantiVAR_00245981R → H in NSHA; Lagosanto; class III. Corresponds to variant dbSNP:rs782308266Ensembl.1
    Natural variantiVAR_002461106S → C in NSHA; Vancouver; class I. Corresponds to variant dbSNP:rs267606835Ensembl.1
    Natural variantiVAR_002463128L → P in NSHA; Vanua Lava; 4% activity. Corresponds to variant dbSNP:rs78365220Ensembl.1
    Natural variantiVAR_002465156E → K in NSHA; Ilesha; class III. Corresponds to variant dbSNP:rs137852313Ensembl.1
    Natural variantiVAR_002467163G → D in NSHA; Plymouth; class I. 1 Publication1
    Natural variantiVAR_002466163G → S in NSHA; Mahidol; class III; associated with reduced density of Plasmodium vivax but not Plasmodium falciparum in Southeast Asians; reduced activity. Corresponds to variant dbSNP:rs137852314Ensembl.1
    Natural variantiVAR_002468165N → D in NSHA; Chinese-3; class II. Corresponds to variant dbSNP:rs137852331Ensembl.1
    Natural variantiVAR_002469166R → H in NSHA; Naone; 1% activity. 1
    Natural variantiVAR_002470176D → G in NSHA; Shinshu; class I. 1 Publication1
    Natural variantiVAR_002471181D → V in NSHA; Santa Maria; class I. Corresponds to variant dbSNP:rs5030872Ensembl.1
    Natural variantiVAR_002472182R → W in NSHA; Vancouver; class I. Corresponds to variant dbSNP:rs267606836Ensembl.1
    Natural variantiVAR_002473188S → F in NSHA; Sassari/Cagliari; class II; frequent in the Mediterranean. 1 PublicationCorresponds to variant dbSNP:rs5030868Ensembl.1
    Natural variantiVAR_002474198R → C in NSHA; Coimbra; class II. Corresponds to variant dbSNP:rs137852330Ensembl.1
    Natural variantiVAR_002475198R → P in NSHA; Santiago; class I. Corresponds to variant dbSNP:rs137852332Ensembl.1
    Natural variantiVAR_075555198R → S in NSHA; Herlev; no glucoshosphate dehydrogenase activity. 1 Publication1
    Natural variantiVAR_002476212M → V in NSHA; Sibari; class III. Corresponds to variant dbSNP:rs782754619Ensembl.1
    Natural variantiVAR_002477213V → L in NSHA; Minnesota; class I. Corresponds to variant dbSNP:rs137852326Ensembl.1
    Natural variantiVAR_002478216F → L in NSHA; Harilaou; class I. Corresponds to variant dbSNP:rs137852319Ensembl.1
    Natural variantiVAR_002480227R → L in NSHA; A- type 2; class III. Corresponds to variant dbSNP:rs137852328Ensembl.1
    Natural variantiVAR_002479227R → Q in NSHA; Mexico City; class III. 1 PublicationCorresponds to variant dbSNP:rs137852328Ensembl.1
    Natural variantiVAR_002481242 – 243Missing in NSHA; Stonybrook; class I. 2
    Natural variantiVAR_002482257R → G in NSHA; Wayne; class I. 1
    Natural variantiVAR_002483274E → K in NSHA; Corum; class I. 1 Publication1
    Natural variantiVAR_002484278S → F in NSHA; Wexham; class I. 1 Publication1
    Natural variantiVAR_002485279T → S in NSHA; Chinese-1; class II. 1
    Natural variantiVAR_002486282D → H in NSHA; Seattle; class III. 1 PublicationCorresponds to variant dbSNP:rs137852318Ensembl.1
    Natural variantiVAR_002487285R → H in NSHA; Montalbano; class III. Corresponds to variant dbSNP:rs74575103Ensembl.1
    Natural variantiVAR_002488291V → M in NSHA; Viangchan/Jammu; class II. Corresponds to variant dbSNP:rs137852327Ensembl.1
    Natural variantiVAR_002489317E → K in NSHA; Kalyan/Kerala; class III. 1 PublicationCorresponds to variant dbSNP:rs137852339Ensembl.1
    Natural variantiVAR_002490323L → P in NSHA; A- type 3; class III. Corresponds to variant dbSNP:rs76723693Ensembl.1
    Natural variantiVAR_002491335A → T in NSHA; Chatham; class III. Corresponds to variant dbSNP:rs5030869Ensembl.1
    Natural variantiVAR_002493353P → S in NSHA; Ierapetra; class II. 1 PublicationCorresponds to variant dbSNP:rs137852333Ensembl.1
    Natural variantiVAR_002494363N → K in NSHA; Loma Linda; class I. Corresponds to variant dbSNP:rs137852329Ensembl.1
    Natural variantiVAR_002495385C → R in NSHA; Tomah; class I. Corresponds to variant dbSNP:rs137852322Ensembl.1
    Natural variantiVAR_002496386K → E in NSHA; Iowa; class I. Corresponds to variant dbSNP:rs137852320Ensembl.1
    Natural variantiVAR_002498387R → C in NSHA; Guadajalara and Mount Sinai; class I. 2 PublicationsCorresponds to variant dbSNP:rs137852334Ensembl.1
    Natural variantiVAR_002497387R → H in NSHA; Beverly Hills; class I. Corresponds to variant dbSNP:rs137852321Ensembl.1
    Natural variantiVAR_002499393R → H in NSHA; Nashville/Anaheim; class I. 1 PublicationCorresponds to variant dbSNP:rs137852316Ensembl.1
    Natural variantiVAR_002500394V → L in NSHA; Alhambra; class I. 1 PublicationCorresponds to variant dbSNP:rs137852335Ensembl.1
    Natural variantiVAR_002501396P → L in NSHA; Bari; class I. 1 Publication1
    Natural variantiVAR_002502398E → K in NSHA; Puerto Limon; class I. Corresponds to variant dbSNP:rs137852325Ensembl.1
    Natural variantiVAR_002503410G → C in NSHA; Riverside; class I. Corresponds to variant dbSNP:rs137852323Ensembl.1
    Natural variantiVAR_002504410G → D in NSHA; Japan; class I. 1 PublicationCorresponds to variant dbSNP:rs137852336Ensembl.1
    Natural variantiVAR_002505416E → K in NSHA; Tokyo; class I. 1
    Natural variantiVAR_002506439R → P in NSHA; Pawnee; class I. 1 PublicationCorresponds to variant dbSNP:rs137852337Ensembl.1
    Natural variantiVAR_002507440L → F in NSHA; Telti/Kobe; class I. 1
    Natural variantiVAR_002508447G → R in NSHA; Santiago de Cuba; class I. Corresponds to variant dbSNP:rs137852317Ensembl.1
    Natural variantiVAR_002509449Q → H in NSHA; Cassano; class II. 1
    Natural variantiVAR_002510454R → C in NSHA; Chinese-II/Maewo/Union; class II; <1% activity. 1 PublicationCorresponds to variant dbSNP:rs398123546Ensembl.1
    Natural variantiVAR_002511454R → H in NSHA; Andalus; class I. Corresponds to variant dbSNP:rs137852324Ensembl.1
    Natural variantiVAR_002512459R → L in NSHA; Canton; class II; frequent in China. Corresponds to variant dbSNP:rs72554665Ensembl.1
    Natural variantiVAR_002513459R → P in NSHA; Cosenza; class II. Corresponds to variant dbSNP:rs72554665Ensembl.1
    Natural variantiVAR_002514463R → H in NSHA; Kaiping; class II. Corresponds to variant dbSNP:rs72554664Ensembl.1
    Natural variantiVAR_002515488G → V in NSHA; Campinas; class I. 1

    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>Mutagenesisi171K → Q: Inhibits catalytic activity. Does not impair dimerization. 1 Publication1
    Mutagenesisi171K → R: Inhibits catalytic activity. Does not impair dimerization. 1 Publication1
    Mutagenesisi386K → Q: Impairs dimerization and reduces catalytic activity. 1 Publication1
    Mutagenesisi386K → R: Does not impair dimerization and catalytic activity. 1 Publication1
    Mutagenesisi403K → Q: Impairs dimerization and reduces catalytic activity in cells under oxidative stress. 1 Publication1
    Mutagenesisi403K → R: Does not impair dimerization and catalytic activity. 1 Publication1

    Keywords - Diseasei

    Disease mutation, Hereditary hemolytic anemia

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    2539

    MalaCards human disease database

    More...
    MalaCardsi
    G6PD
    MIMi300908 phenotype

    Open Targets

    More...
    OpenTargetsi
    ENSG00000160211

    Orphanet; a database dedicated to information on rare diseases and orphan drugs

    More...
    Orphaneti
    466026 Class I glucose-6-phosphate dehydrogenase deficiency
    362 NON RARE IN EUROPE: Glucose-6-phosphate-dehydrogenase deficiency

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA28469

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL5347

    Drug and drug target database

    More...
    DrugBanki
    DB05107 16-Bromoepiandrosterone
    DB03461 2'-Monophosphoadenosine 5'-Diphosphoribose
    DB03085 Hydroxyacetic Acid

    Polymorphism and mutation databases

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    116242483

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

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources2 Publications
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000680832 – 515Glucose-6-phosphate 1-dehydrogenaseAdd BLAST514

    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 residuei2N-acetylalanineCombined sources1 Publication1
    Modified residuei8PhosphoserineCombined sources1
    Modified residuei10PhosphothreonineCombined sources1
    Modified residuei89N6-acetyllysineCombined sources1
    Modified residuei171N6-acetyllysineCombined sources1
    Modified residuei403N6-acetyllysineCombined sources1 Publication1
    Modified residuei432N6-acetyllysineCombined sources1
    Modified residuei497N6-acetyllysineCombined sources1
    Modified residuei503PhosphotyrosineCombined sources1
    Isoform 3 (identifier: P11413-3)
    Modified residuei26PhosphoserineCombined sources1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    Acetylated by ELP3 at Lys-403; acetylation inhibits its homodimerization and enzyme activity. Deacetylated by SIRT2 at Lys-403; deacetylation stimulates its enzyme activity.2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P11413

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P11413

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

    More...
    PaxDbi
    P11413

    PeptideAtlas

    More...
    PeptideAtlasi
    P11413

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P11413

    ProteomicsDB human proteome resource

    More...
    ProteomicsDBi
    52771
    52772 [P11413-2]
    52773 [P11413-3]

    2D gel databases

    REPRODUCTION-2DPAGE

    More...
    REPRODUCTION-2DPAGEi
    IPI00289800

    Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

    More...
    SWISS-2DPAGEi
    P11413

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P11413

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...
    PhosphoSitePlusi
    P11413

    SwissPalm database of S-palmitoylation events

    More...
    SwissPalmi
    P11413

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

    <p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

    Isoform Long is found in lymphoblasts, granulocytes and sperm.

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000160211 Expressed in 170 organ(s), highest expression level in blood

    CleanEx database of gene expression profiles

    More...
    CleanExi
    HS_G6PD

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    P11413 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P11413 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    HPA000247
    HPA000834

    <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; dimer of dimers. Interacts with SIRT2; the interaction is enhanced by H2O2 treatment.3 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    108814, 69 interactors

    Protein interaction database and analysis system

    More...
    IntActi
    P11413, 8 interactors

    Molecular INTeraction database

    More...
    MINTi
    P11413

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000377192

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P11413

    <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

    1515
    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
    P11413

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

    More...
    SMRi
    P11413

    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
    P11413

    <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>Regioni201 – 205Substrate bindingCombined 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

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG0563 Eukaryota
    COG0364 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00530000063435

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...
    HOVERGENi
    HBG000856

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P11413

    KEGG Orthology (KO)

    More...
    KOi
    K00036

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    VEICVYE

    Database of Orthologous Groups

    More...
    OrthoDBi
    EOG091G06FN

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P11413

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF300584

    Family and domain databases

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00966 G6PD, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR001282 G6P_DH
    IPR019796 G6P_DH_AS
    IPR022675 G6P_DH_C
    IPR022674 G6P_DH_NAD-bd
    IPR036291 NAD(P)-bd_dom_sf

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR23429 PTHR23429, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF02781 G6PD_C, 1 hit
    PF00479 G6PD_N, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF000110 G6PD, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00079 G6PDHDRGNASE

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51735 SSF51735, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00871 zwf, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00069 G6P_DEHYDROGENASE, 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>Sequences (3+)i

    <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.

    This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

    This entry has 3 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

    Isoform Short (identifier: P11413-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide
            10         20         30         40         50
    MAEQVALSRT QVCGILREEL FQGDAFHQSD THIFIIMGAS GDLAKKKIYP
    60 70 80 90 100
    TIWWLFRDGL LPENTFIVGY ARSRLTVADI RKQSEPFFKA TPEEKLKLED
    110 120 130 140 150
    FFARNSYVAG QYDDAASYQR LNSHMNALHL GSQANRLFYL ALPPTVYEAV
    160 170 180 190 200
    TKNIHESCMS QIGWNRIIVE KPFGRDLQSS DRLSNHISSL FREDQIYRID
    210 220 230 240 250
    HYLGKEMVQN LMVLRFANRI FGPIWNRDNI ACVILTFKEP FGTEGRGGYF
    260 270 280 290 300
    DEFGIIRDVM QNHLLQMLCL VAMEKPASTN SDDVRDEKVK VLKCISEVQA
    310 320 330 340 350
    NNVVLGQYVG NPDGEGEATK GYLDDPTVPR GSTTATFAAV VLYVENERWD
    360 370 380 390 400
    GVPFILRCGK ALNERKAEVR LQFHDVAGDI FHQQCKRNEL VIRVQPNEAV
    410 420 430 440 450
    YTKMMTKKPG MFFNPEESEL DLTYGNRYKN VKLPDAYERL ILDVFCGSQM
    460 470 480 490 500
    HFVRSDELRE AWRIFTPLLH QIELEKPKPI PYIYGSRGPT EADELMKRVG
    510
    FQYEGTYKWV NPHKL
    Length:515
    Mass (Da):59,257
    Last modified:January 23, 2007 - v4
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iF2B775340640A96F
    GO
    Isoform Long (identifier: P11413-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         257-257: R → RGPGRQGGSGSESCSLSLGSLVWGPHALEPGEQGGELRRALASSVPR

    Show »
    Length:561
    Mass (Da):63,827
    Checksum:iA6759ACCB3CDF921
    GO
    Isoform 3 (identifier: P11413-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MGRRGSAPGNGRTLRGCERGGRRRRSADSVM

    Show »
    Length:545
    Mass (Da):62,468
    Checksum:iCFE3675547A5672F
    GO

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    E7EM57E7EM57_HUMAN
    Glucose-6-phosphate 1-dehydrogenase
    G6PD
    320Annotation score:

    Annotation score:2 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>
    E7EUI8E7EUI8_HUMAN
    Glucose-6-phosphate 1-dehydrogenase
    G6PD
    338Annotation score:

    Annotation score:2 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>
    E9PD92E9PD92_HUMAN
    Glucose-6-phosphate 1-dehydrogenase
    G6PD
    256Annotation score:

    Annotation score:1 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>

    <p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence AAA63175 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    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 conflicti11Q → H in CAA27309 (PubMed:3515319).Curated1
    Sequence conflicti11Q → H in AAA63175 (PubMed:2428611).Curated1
    Sequence conflicti11Q → H in AAA52500 (PubMed:2836867).Curated1
    Sequence conflicti435 – 436DA → EP in AAA52499 (PubMed:3012556).Curated2

    <p>This subsection of the ‘Sequence’ section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement_in_disease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi

    The sequence shown is that of variant B, the most common variant.

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_00245012V → L in Sinnai. 1 Publication1
    Natural variantiVAR_00245132H → R in NSHA; Gahoe; class III; frequent in Chinese. 1 PublicationCorresponds to variant dbSNP:rs137852340Ensembl.1
    Natural variantiVAR_00245235Missing in NSHA; Sunderland; class I. 1
    Natural variantiVAR_00245344A → G in NSHA; Orissa; class III; frequent in Indian tribal populations. 1 PublicationCorresponds to variant dbSNP:rs78478128Ensembl.1
    Natural variantiVAR_00245448I → T in NSHA; Aures; class II. 1 PublicationCorresponds to variant dbSNP:rs76645461Ensembl.1
    Natural variantiVAR_00245558D → N in NSHA; Metaponto; class III. Corresponds to variant dbSNP:rs137852315Ensembl.1
    Natural variantiVAR_00245668V → M in NSHA; A(-) type I; class III; frequent in African population. 4 PublicationsCorresponds to variant dbSNP:rs1050828Ensembl.1
    Natural variantiVAR_00245770Y → H in NSHA; Namoru; 4% activity. Corresponds to variant dbSNP:rs137852349Ensembl.1
    Natural variantiVAR_00245875L → P in NSHA; Swansea; class I. 1 Publication1
    Natural variantiVAR_00246081R → C in NSHA; Konan/Ube; class III. Corresponds to variant dbSNP:rs138687036Ensembl.1
    Natural variantiVAR_00245981R → H in NSHA; Lagosanto; class III. Corresponds to variant dbSNP:rs782308266Ensembl.1
    Natural variantiVAR_002461106S → C in NSHA; Vancouver; class I. Corresponds to variant dbSNP:rs267606835Ensembl.1
    Natural variantiVAR_002462126N → D Polymorphism; found in Santa Maria and Mount Sinai; associated with C-387 in Mount Sinai; class IV and class I. 7 PublicationsCorresponds to variant dbSNP:rs1050829Ensembl.1
    Natural variantiVAR_002463128L → P in NSHA; Vanua Lava; 4% activity. Corresponds to variant dbSNP:rs78365220Ensembl.1
    Natural variantiVAR_002464131G → V in Chinese-4. Corresponds to variant dbSNP:rs137852341Ensembl.1
    Natural variantiVAR_002465156E → K in NSHA; Ilesha; class III. Corresponds to variant dbSNP:rs137852313Ensembl.1
    Natural variantiVAR_002467163G → D in NSHA; Plymouth; class I. 1 Publication1
    Natural variantiVAR_002466163G → S in NSHA; Mahidol; class III; associated with reduced density of Plasmodium vivax but not Plasmodium falciparum in Southeast Asians; reduced activity. Corresponds to variant dbSNP:rs137852314Ensembl.1
    Natural variantiVAR_002468165N → D in NSHA; Chinese-3; class II. Corresponds to variant dbSNP:rs137852331Ensembl.1
    Natural variantiVAR_002469166R → H in NSHA; Naone; 1% activity. 1
    Natural variantiVAR_002470176D → G in NSHA; Shinshu; class I. 1 Publication1
    Natural variantiVAR_002471181D → V in NSHA; Santa Maria; class I. Corresponds to variant dbSNP:rs5030872Ensembl.1
    Natural variantiVAR_002472182R → W in NSHA; Vancouver; class I. Corresponds to variant dbSNP:rs267606836Ensembl.1
    Natural variantiVAR_002473188S → F in NSHA; Sassari/Cagliari; class II; frequent in the Mediterranean. 1 PublicationCorresponds to variant dbSNP:rs5030868Ensembl.1
    Natural variantiVAR_002474198R → C in NSHA; Coimbra; class II. Corresponds to variant dbSNP:rs137852330Ensembl.1
    Natural variantiVAR_002475198R → P in NSHA; Santiago; class I. Corresponds to variant dbSNP:rs137852332Ensembl.1
    Natural variantiVAR_075555198R → S in NSHA; Herlev; no glucoshosphate dehydrogenase activity. 1 Publication1
    Natural variantiVAR_002476212M → V in NSHA; Sibari; class III. Corresponds to variant dbSNP:rs782754619Ensembl.1
    Natural variantiVAR_002477213V → L in NSHA; Minnesota; class I. Corresponds to variant dbSNP:rs137852326Ensembl.1
    Natural variantiVAR_002478216F → L in NSHA; Harilaou; class I. Corresponds to variant dbSNP:rs137852319Ensembl.1
    Natural variantiVAR_002480227R → L in NSHA; A- type 2; class III. Corresponds to variant dbSNP:rs137852328Ensembl.1
    Natural variantiVAR_002479227R → Q in NSHA; Mexico City; class III. 1 PublicationCorresponds to variant dbSNP:rs137852328Ensembl.1
    Natural variantiVAR_002481242 – 243Missing in NSHA; Stonybrook; class I. 2
    Natural variantiVAR_002482257R → G in NSHA; Wayne; class I. 1
    Natural variantiVAR_002483274E → K in NSHA; Corum; class I. 1 Publication1
    Natural variantiVAR_002484278S → F in NSHA; Wexham; class I. 1 Publication1
    Natural variantiVAR_002485279T → S in NSHA; Chinese-1; class II. 1
    Natural variantiVAR_002486282D → H in NSHA; Seattle; class III. 1 PublicationCorresponds to variant dbSNP:rs137852318Ensembl.1
    Natural variantiVAR_002487285R → H in NSHA; Montalbano; class III. Corresponds to variant dbSNP:rs74575103Ensembl.1
    Natural variantiVAR_002488291V → M in NSHA; Viangchan/Jammu; class II. Corresponds to variant dbSNP:rs137852327Ensembl.1
    Natural variantiVAR_002489317E → K in NSHA; Kalyan/Kerala; class III. 1 PublicationCorresponds to variant dbSNP:rs137852339Ensembl.1
    Natural variantiVAR_020535322Y → H in Rehovot. 1 PublicationCorresponds to variant dbSNP:rs137852347Ensembl.1
    Natural variantiVAR_002490323L → P in NSHA; A- type 3; class III. Corresponds to variant dbSNP:rs76723693Ensembl.1
    Natural variantiVAR_002491335A → T in NSHA; Chatham; class III. Corresponds to variant dbSNP:rs5030869Ensembl.1
    Natural variantiVAR_002492342L → F in Chinese-5. Corresponds to variant dbSNP:rs137852342Ensembl.1
    Natural variantiVAR_002493353P → S in NSHA; Ierapetra; class II. 1 PublicationCorresponds to variant dbSNP:rs137852333Ensembl.1
    Natural variantiVAR_002494363N → K in NSHA; Loma Linda; class I. Corresponds to variant dbSNP:rs137852329Ensembl.1
    Natural variantiVAR_002495385C → R in NSHA; Tomah; class I. Corresponds to variant dbSNP:rs137852322Ensembl.1
    Natural variantiVAR_002496386K → E in NSHA; Iowa; class I. Corresponds to variant dbSNP:rs137852320Ensembl.1
    Natural variantiVAR_002498387R → C in NSHA; Guadajalara and Mount Sinai; class I. 2 PublicationsCorresponds to variant dbSNP:rs137852334Ensembl.1
    Natural variantiVAR_002497387R → H in NSHA; Beverly Hills; class I. Corresponds to variant dbSNP:rs137852321Ensembl.1
    Natural variantiVAR_002499393R → H in NSHA; Nashville/Anaheim; class I. 1 PublicationCorresponds to variant dbSNP:rs137852316Ensembl.1
    Natural variantiVAR_002500394V → L in NSHA; Alhambra; class I. 1 PublicationCorresponds to variant dbSNP:rs137852335Ensembl.1
    Natural variantiVAR_002501396P → L in NSHA; Bari; class I. 1 Publication1
    Natural variantiVAR_002502398E → K in NSHA; Puerto Limon; class I. Corresponds to variant dbSNP:rs137852325Ensembl.1
    Natural variantiVAR_002503410G → C in NSHA; Riverside; class I. Corresponds to variant dbSNP:rs137852323Ensembl.1
    Natural variantiVAR_002504410G → D in NSHA; Japan; class I. 1 PublicationCorresponds to variant dbSNP:rs137852336Ensembl.1
    Natural variantiVAR_002505416E → K in NSHA; Tokyo; class I. 1
    Natural variantiVAR_002506439R → P in NSHA; Pawnee; class I. 1 PublicationCorresponds to variant dbSNP:rs137852337Ensembl.1
    Natural variantiVAR_002507440L → F in NSHA; Telti/Kobe; class I. 1
    Natural variantiVAR_002508447G → R in NSHA; Santiago de Cuba; class I. Corresponds to variant dbSNP:rs137852317Ensembl.1
    Natural variantiVAR_002509449Q → H in NSHA; Cassano; class II. 1
    Natural variantiVAR_002510454R → C in NSHA; Chinese-II/Maewo/Union; class II; <1% activity. 1 PublicationCorresponds to variant dbSNP:rs398123546Ensembl.1
    Natural variantiVAR_002511454R → H in NSHA; Andalus; class I. Corresponds to variant dbSNP:rs137852324Ensembl.1
    Natural variantiVAR_002512459R → L in NSHA; Canton; class II; frequent in China. Corresponds to variant dbSNP:rs72554665Ensembl.1
    Natural variantiVAR_002513459R → P in NSHA; Cosenza; class II. Corresponds to variant dbSNP:rs72554665Ensembl.1
    Natural variantiVAR_002514463R → H in NSHA; Kaiping; class II. Corresponds to variant dbSNP:rs72554664Ensembl.1
    Natural variantiVAR_002515488G → V in NSHA; Campinas; class I. 1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0378021M → MGRRGSAPGNGRTLRGCERG GRRRRSADSVM in isoform 3. 1 Publication1
    Alternative sequenceiVSP_001592257R → RGPGRQGGSGSESCSLSLGS LVWGPHALEPGEQGGELRRA LASSVPR in isoform Long. 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
    X03674 mRNA Translation: CAA27309.1
    M65234
    , M26749, M26750, M65225, M65226, M65227, M65228, M65229, M65230, M65231, M65233, M65232 Genomic DNA Translation: AAA63175.1 Different initiation.
    M21248 mRNA Translation: AAA52500.1
    M19866 mRNA Translation: AAA52501.1
    X55448 Genomic DNA Translation: CAA39089.1
    L44140 Genomic DNA Translation: AAA92653.1
    AF277315 Genomic DNA Translation: AAL27011.1
    CH471172 Genomic DNA Translation: EAW72682.1
    CH471172 Genomic DNA Translation: EAW72686.1
    BC000337 mRNA Translation: AAH00337.1
    M27940 mRNA Translation: AAA52504.1
    S58359 mRNA Translation: AAB26169.1
    X53815 Genomic DNA Translation: CAA37811.1
    S64462 Genomic DNA Translation: AAB20299.1
    AY158096 Genomic DNA Translation: AAN76367.1
    AY158097 Genomic DNA Translation: AAN76368.1
    AY158098 Genomic DNA Translation: AAN76369.1
    AY158099 Genomic DNA Translation: AAN76370.1
    AY158100 Genomic DNA Translation: AAN76371.1
    AY158101 Genomic DNA Translation: AAN76372.1
    AY158102 Genomic DNA Translation: AAN76373.1
    AY158103 Genomic DNA Translation: AAN76374.1
    AY158104 Genomic DNA Translation: AAN76375.1
    AY158105 Genomic DNA Translation: AAN76376.1
    AY158106 Genomic DNA Translation: AAN76377.1
    AY158107 Genomic DNA Translation: AAN76378.1
    AY158108 Genomic DNA Translation: AAN76379.1
    AY158109 Genomic DNA Translation: AAN76380.1
    AY158110 Genomic DNA Translation: AAN76381.1
    AY158111 Genomic DNA Translation: AAN76382.1
    AY158112 Genomic DNA Translation: AAN76383.1
    AY158113 Genomic DNA Translation: AAN76384.1
    AY158114 Genomic DNA Translation: AAN76385.1
    AY158115 Genomic DNA Translation: AAN76386.1
    AY158116 Genomic DNA Translation: AAN76387.1
    AY158117 Genomic DNA Translation: AAN76388.1
    AY158118 Genomic DNA Translation: AAN76389.1
    AY158119 Genomic DNA Translation: AAN76390.1
    AY158120 Genomic DNA Translation: AAN76391.1
    AY158121 Genomic DNA Translation: AAN76392.1
    AY158122 Genomic DNA Translation: AAN76393.1
    AY158123 Genomic DNA Translation: AAN76394.1
    AY158124 Genomic DNA Translation: AAN76395.1
    AY158125 Genomic DNA Translation: AAN76396.1
    AY158126 Genomic DNA Translation: AAN76397.1
    AY158127 Genomic DNA Translation: AAN76398.1
    AY158128 Genomic DNA Translation: AAN76399.1
    AY158129 Genomic DNA Translation: AAN76400.1
    AY158130 Genomic DNA Translation: AAN76401.1
    AY158131 Genomic DNA Translation: AAN76402.1
    AY158132 Genomic DNA Translation: AAN76403.1
    AY158133 Genomic DNA Translation: AAN76404.1
    AY158134 Genomic DNA Translation: AAN76405.1
    AY158135 Genomic DNA Translation: AAN76406.1
    AY158136 Genomic DNA Translation: AAN76407.1
    AY158137 Genomic DNA Translation: AAN76408.1
    AY158138 Genomic DNA Translation: AAN76409.1
    AY158139 Genomic DNA Translation: AAN76410.1
    AY158140 Genomic DNA Translation: AAN76411.1
    AY158141 Genomic DNA Translation: AAN76412.1
    AY158142 Genomic DNA Translation: AAN76413.1
    M12996 mRNA Translation: AAA52499.1
    M23423 Genomic DNA Translation: AAB59390.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS44023.1 [P11413-1]

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A40309 DEHUG6

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_000393.4, NM_000402.4 [P11413-3]
    NP_001035810.1, NM_001042351.2 [P11413-1]

    UniGene gene-oriented nucleotide sequence clusters

    More...
    UniGenei
    Hs.461047
    Hs.684904

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000369620; ENSP00000358633; ENSG00000160211 [P11413-2]
    ENST00000393562; ENSP00000377192; ENSG00000160211 [P11413-1]
    ENST00000393564; ENSP00000377194; ENSG00000160211 [P11413-1]
    ENST00000621232; ENSP00000483686; ENSG00000160211 [P11413-1]

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    2539

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:2539

    UCSC genome browser

    More...
    UCSCi
    uc004flx.3 human [P11413-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    <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

    <p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

    G6PDdb

    G6PD mutation database

    SHMPD

    The Singapore human mutation and polymorphism database

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X03674 mRNA Translation: CAA27309.1
    M65234
    , M26749, M26750, M65225, M65226, M65227, M65228, M65229, M65230, M65231, M65233, M65232 Genomic DNA Translation: AAA63175.1 Different initiation.
    M21248 mRNA Translation: AAA52500.1
    M19866 mRNA Translation: AAA52501.1
    X55448 Genomic DNA Translation: CAA39089.1
    L44140 Genomic DNA Translation: AAA92653.1
    AF277315 Genomic DNA Translation: AAL27011.1
    CH471172 Genomic DNA Translation: EAW72682.1
    CH471172 Genomic DNA Translation: EAW72686.1
    BC000337 mRNA Translation: AAH00337.1
    M27940 mRNA Translation: AAA52504.1
    S58359 mRNA Translation: AAB26169.1
    X53815 Genomic DNA Translation: CAA37811.1
    S64462 Genomic DNA Translation: AAB20299.1
    AY158096 Genomic DNA Translation: AAN76367.1
    AY158097 Genomic DNA Translation: AAN76368.1
    AY158098 Genomic DNA Translation: AAN76369.1
    AY158099 Genomic DNA Translation: AAN76370.1
    AY158100 Genomic DNA Translation: AAN76371.1
    AY158101 Genomic DNA Translation: AAN76372.1
    AY158102 Genomic DNA Translation: AAN76373.1
    AY158103 Genomic DNA Translation: AAN76374.1
    AY158104 Genomic DNA Translation: AAN76375.1
    AY158105 Genomic DNA Translation: AAN76376.1
    AY158106 Genomic DNA Translation: AAN76377.1
    AY158107 Genomic DNA Translation: AAN76378.1
    AY158108 Genomic DNA Translation: AAN76379.1
    AY158109 Genomic DNA Translation: AAN76380.1
    AY158110 Genomic DNA Translation: AAN76381.1
    AY158111 Genomic DNA Translation: AAN76382.1
    AY158112 Genomic DNA Translation: AAN76383.1
    AY158113 Genomic DNA Translation: AAN76384.1
    AY158114 Genomic DNA Translation: AAN76385.1
    AY158115 Genomic DNA Translation: AAN76386.1
    AY158116 Genomic DNA Translation: AAN76387.1
    AY158117 Genomic DNA Translation: AAN76388.1
    AY158118 Genomic DNA Translation: AAN76389.1
    AY158119 Genomic DNA Translation: AAN76390.1
    AY158120 Genomic DNA Translation: AAN76391.1
    AY158121 Genomic DNA Translation: AAN76392.1
    AY158122 Genomic DNA Translation: AAN76393.1
    AY158123 Genomic DNA Translation: AAN76394.1
    AY158124 Genomic DNA Translation: AAN76395.1
    AY158125 Genomic DNA Translation: AAN76396.1
    AY158126 Genomic DNA Translation: AAN76397.1
    AY158127 Genomic DNA Translation: AAN76398.1
    AY158128 Genomic DNA Translation: AAN76399.1
    AY158129 Genomic DNA Translation: AAN76400.1
    AY158130 Genomic DNA Translation: AAN76401.1
    AY158131 Genomic DNA Translation: AAN76402.1
    AY158132 Genomic DNA Translation: AAN76403.1
    AY158133 Genomic DNA Translation: AAN76404.1
    AY158134 Genomic DNA Translation: AAN76405.1
    AY158135 Genomic DNA Translation: AAN76406.1
    AY158136 Genomic DNA Translation: AAN76407.1
    AY158137 Genomic DNA Translation: AAN76408.1
    AY158138 Genomic DNA Translation: AAN76409.1
    AY158139 Genomic DNA Translation: AAN76410.1
    AY158140 Genomic DNA Translation: AAN76411.1
    AY158141 Genomic DNA Translation: AAN76412.1
    AY158142 Genomic DNA Translation: AAN76413.1
    M12996 mRNA Translation: AAA52499.1
    M23423 Genomic DNA Translation: AAB59390.1
    CCDSiCCDS44023.1 [P11413-1]
    PIRiA40309 DEHUG6
    RefSeqiNP_000393.4, NM_000402.4 [P11413-3]
    NP_001035810.1, NM_001042351.2 [P11413-1]
    UniGeneiHs.461047
    Hs.684904

    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
    1QKIX-ray3.00A/B/C/D/E/F/G/H2-515[»]
    2BH9X-ray2.50A27-515[»]
    2BHLX-ray2.90A/B28-515[»]
    5UKWX-ray2.65A29-511[»]
    6E07X-ray2.60B/C/F/L/N/Q/T/W1-515[»]
    6E08X-ray1.90L1-515[»]
    ProteinModelPortaliP11413
    SMRiP11413
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi108814, 69 interactors
    IntActiP11413, 8 interactors
    MINTiP11413
    STRINGi9606.ENSP00000377192

    Chemistry databases

    BindingDBiP11413
    ChEMBLiCHEMBL5347
    DrugBankiDB05107 16-Bromoepiandrosterone
    DB03461 2'-Monophosphoadenosine 5'-Diphosphoribose
    DB03085 Hydroxyacetic Acid

    PTM databases

    iPTMnetiP11413
    PhosphoSitePlusiP11413
    SwissPalmiP11413

    Polymorphism and mutation databases

    DMDMi116242483

    2D gel databases

    REPRODUCTION-2DPAGEiIPI00289800
    SWISS-2DPAGEiP11413

    Proteomic databases

    EPDiP11413
    MaxQBiP11413
    PaxDbiP11413
    PeptideAtlasiP11413
    PRIDEiP11413
    ProteomicsDBi52771
    52772 [P11413-2]
    52773 [P11413-3]

    Protocols and materials databases

    The DNASU plasmid repository

    More...
    DNASUi
    2539
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000369620; ENSP00000358633; ENSG00000160211 [P11413-2]
    ENST00000393562; ENSP00000377192; ENSG00000160211 [P11413-1]
    ENST00000393564; ENSP00000377194; ENSG00000160211 [P11413-1]
    ENST00000621232; ENSP00000483686; ENSG00000160211 [P11413-1]
    GeneIDi2539
    KEGGihsa:2539
    UCSCiuc004flx.3 human [P11413-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    2539
    DisGeNETi2539
    EuPathDBiHostDB:ENSG00000160211.15

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    G6PD
    HGNCiHGNC:4057 G6PD
    HPAiHPA000247
    HPA000834
    MalaCardsiG6PD
    MIMi300908 phenotype
    305900 gene
    neXtProtiNX_P11413
    OpenTargetsiENSG00000160211
    Orphaneti466026 Class I glucose-6-phosphate dehydrogenase deficiency
    362 NON RARE IN EUROPE: Glucose-6-phosphate-dehydrogenase deficiency
    PharmGKBiPA28469

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG0563 Eukaryota
    COG0364 LUCA
    GeneTreeiENSGT00530000063435
    HOVERGENiHBG000856
    InParanoidiP11413
    KOiK00036
    OMAiVEICVYE
    OrthoDBiEOG091G06FN
    PhylomeDBiP11413
    TreeFamiTF300584

    Enzyme and pathway databases

    UniPathwayi
    UPA00115;UER00408

    BioCyciMetaCyc:HS08467-MONOMER
    BRENDAi1.1.1.49 2681
    ReactomeiR-HSA-5628897 TP53 Regulates Metabolic Genes
    R-HSA-71336 Pentose phosphate pathway
    SABIO-RKiP11413
    SIGNORiP11413

    Miscellaneous databases

    ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

    More...
    ChiTaRSi
    G6PD human
    EvolutionaryTraceiP11413

    The Gene Wiki collection of pages on human genes and proteins

    More...
    GeneWikii
    Glucose-6-phosphate_dehydrogenase

    Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

    More...
    GenomeRNAii
    2539

    Protein Ontology

    More...
    PROi
    PR:P11413

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000160211 Expressed in 170 organ(s), highest expression level in blood
    CleanExiHS_G6PD
    ExpressionAtlasiP11413 baseline and differential
    GenevisibleiP11413 HS

    Family and domain databases

    HAMAPiMF_00966 G6PD, 1 hit
    InterProiView protein in InterPro
    IPR001282 G6P_DH
    IPR019796 G6P_DH_AS
    IPR022675 G6P_DH_C
    IPR022674 G6P_DH_NAD-bd
    IPR036291 NAD(P)-bd_dom_sf
    PANTHERiPTHR23429 PTHR23429, 1 hit
    PfamiView protein in Pfam
    PF02781 G6PD_C, 1 hit
    PF00479 G6PD_N, 1 hit
    PIRSFiPIRSF000110 G6PD, 1 hit
    PRINTSiPR00079 G6PDHDRGNASE
    SUPFAMiSSF51735 SSF51735, 1 hit
    TIGRFAMsiTIGR00871 zwf, 1 hit
    PROSITEiView protein in PROSITE
    PS00069 G6P_DEHYDROGENASE, 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 nameiG6PD_HUMAN
    <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: P11413
    Secondary accession number(s): D3DWX9
    , Q16000, Q16765, Q8IU70, Q8IU88, Q8IUA6, Q96PQ2
    <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: October 1, 1989
    Last sequence update: January 23, 2007
    Last modified: December 5, 2018
    This is version 239 of the entry and version 4 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    7. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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