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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-Experimental evidence at protein leveli

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

Catalytic activityi

D-glucose 6-phosphate + NADP+ = 6-phospho-D-glucono-1,5-lactone + NADPH.1 Publication

Kineticsi

  1. KM=7.07 µM for NADP1 Publication
  2. KM=52 µM for glucose 6-phosphate1 Publication

    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 (G6PD), Glucose-6-phosphate 1-dehydrogenase, 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 (G6PD), Glucose-6-phosphate 1-dehydrogenase (G6PD), Glucose-6-phosphate 1-dehydrogenase
    2. 6-phosphogluconolactonase (PGLS)
    3. 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
    Binding sitei72NADP 12 Publications1
    Binding sitei147NADP 12 Publications1
    Binding sitei171NADP 1; via carbonyl oxygen2 Publications1
    Binding sitei171Substrate1
    Binding sitei239Substrate1
    Binding sitei258Substrate1
    Active sitei263Proton acceptorBy similarity1
    Binding sitei357NADP 22 Publications1
    Binding sitei360Substrate1
    Binding sitei365Substrate1
    Binding sitei366NADP 22 Publications1
    Binding sitei370NADP 22 Publications1
    Binding sitei393NADP 22 Publications1
    Binding sitei395Substrate1
    Binding sitei487NADP 22 Publications1
    Binding sitei503NADP 22 Publications1
    Binding sitei509NADP 22 Publications1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi38 – 45NADP 12 Publications8
    Nucleotide bindingi401 – 403NADP 22 Publications3
    Nucleotide bindingi421 – 423NADP 22 Publications3

    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

    • cellular response to oxidative stress Source: BHF-UCL
    • cholesterol biosynthetic process Source: BHF-UCL
    • erythrocyte maturation Source: BHF-UCL
    • glucose 6-phosphate metabolic process Source: UniProtKB
    • glucose metabolic process Source: UniProtKB-KW
    • glutathione metabolic process Source: BHF-UCL
    • lipid metabolic process Source: BHF-UCL
    • NADPH regeneration Source: BHF-UCL
    • NADP metabolic process Source: UniProtKB
    • negative regulation of cell growth involved in cardiac muscle cell development Source: Ensembl
    • negative regulation of protein glutathionylation Source: BHF-UCL
    • negative regulation of reactive oxygen species metabolic process Source: Ensembl
    • oxidation-reduction process Source: BHF-UCL
    • pentose biosynthetic process Source: BHF-UCL
    • pentose-phosphate shunt Source: BHF-UCL
    • pentose-phosphate shunt, oxidative branch Source: BHF-UCL
    • positive regulation of calcium ion transmembrane transport via high voltage-gated calcium channel Source: Ensembl
    • regulation of neuron apoptotic process Source: Ensembl
    • response to ethanol Source: Ensembl
    • response to food Source: Ensembl
    • response to iron(III) ion Source: Ensembl
    • response to organic cyclic compound Source: Ensembl
    • ribose phosphate biosynthetic process Source: BHF-UCL
    • substantia nigra development Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Carbohydrate metabolism, Glucose metabolism

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:HS08467-MONOMER.
    ZFISH:HS08467-MONOMER.
    BRENDAi1.1.1.49. 2681.
    ReactomeiR-HSA-5628897. TP53 Regulates Metabolic Genes.
    R-HSA-71336. Pentose phosphate pathway (hexose monophosphate shunt).
    SABIO-RKP11413.
    SIGNORiP11413.
    UniPathwayiUPA00115; UER00408.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glucose-6-phosphate 1-dehydrogenase (EC:1.1.1.49)
    Short name:
    G6PD
    Gene namesi
    Name:G6PD
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome X

    Organism-specific databases

    HGNCiHGNC:4057. G6PD.

    Subcellular locationi

    GO - Cellular componenti

    • centrosome Source: HPA
    • cytoplasm Source: LIFEdb
    • cytoplasmic side of plasma membrane Source: BHF-UCL
    • cytosol Source: BHF-UCL
    • extracellular exosome Source: UniProtKB
    • intracellular membrane-bounded organelle Source: HPA
    • membrane Source: UniProtKB
    • microtubule organizing center Source: HPA
    • nucleus Source: Ensembl
    Complete GO annotation...

    Pathology & Biotechi

    Involvement in diseasei

    Anemia, non-spherocytic hemolytic, due to G6PD deficiency (NSHA)2 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
    Natural variantiVAR_00245132H → R in NSHA; Gahoe; class III; frequent in Chinese. 1 PublicationCorresponds to variant rs137852340dbSNPEnsembl.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 rs78478128dbSNPEnsembl.1
    Natural variantiVAR_00245448I → T in NSHA; Aures; class II. 1 PublicationCorresponds to variant rs76645461dbSNPEnsembl.1
    Natural variantiVAR_00245558D → N in NSHA; Metaponto; class III. Corresponds to variant rs137852315dbSNPEnsembl.1
    Natural variantiVAR_00245668V → M in NSHA; A(-) type I; class III; frequent in African population. 4 PublicationsCorresponds to variant rs1050828dbSNPEnsembl.1
    Natural variantiVAR_00245770Y → H in NSHA; Namoru; 4% activity. Corresponds to variant rs137852349dbSNPEnsembl.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 rs138687036dbSNPEnsembl.1
    Natural variantiVAR_00245981R → H in NSHA; Lagosanto; class III. Corresponds to variant rs782308266dbSNPEnsembl.1
    Natural variantiVAR_002461106S → C in NSHA; Vancouver; class I. Corresponds to variant rs267606835dbSNPEnsembl.1
    Natural variantiVAR_002462126N → D in NSHA; Santa Maria and Mount Sinai; class IV and class I. 6 PublicationsCorresponds to variant rs1050829dbSNPEnsembl.1
    Natural variantiVAR_002463128L → P in NSHA; Vanua Lava; 4% activity. Corresponds to variant rs78365220dbSNPEnsembl.1
    Natural variantiVAR_002465156E → K in NSHA; Ilesha; class III. Corresponds to variant rs137852313dbSNPEnsembl.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 rs137852314dbSNPEnsembl.1
    Natural variantiVAR_002468165N → D in NSHA; Chinese-3; class II. Corresponds to variant rs137852331dbSNPEnsembl.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 rs5030872dbSNPEnsembl.1
    Natural variantiVAR_002472182R → W in NSHA; Vancouver; class I. Corresponds to variant rs267606836dbSNPEnsembl.1
    Natural variantiVAR_002473188S → F in NSHA; Sassari/Cagliari; class II; frequent in the Mediterranean. 1 PublicationCorresponds to variant rs5030868dbSNPEnsembl.1
    Natural variantiVAR_002474198R → C in NSHA; Coimbra; class II. Corresponds to variant rs137852330dbSNPEnsembl.1
    Natural variantiVAR_002475198R → P in NSHA; Santiago; class I. Corresponds to variant rs137852332dbSNPEnsembl.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 rs782754619dbSNPEnsembl.1
    Natural variantiVAR_002477213V → L in NSHA; Minnesota; class I. Corresponds to variant rs137852326dbSNPEnsembl.1
    Natural variantiVAR_002478216F → L in NSHA; Harilaou; class I. Corresponds to variant rs137852319dbSNPEnsembl.1
    Natural variantiVAR_002480227R → L in NSHA; A- type 2; class III. Corresponds to variant rs137852328dbSNPEnsembl.1
    Natural variantiVAR_002479227R → Q in NSHA; Mexico City; class III. 1 PublicationCorresponds to variant rs137852328dbSNPEnsembl.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 rs137852318dbSNPEnsembl.1
    Natural variantiVAR_002487285R → H in NSHA; Montalbano; class III. Corresponds to variant rs74575103dbSNPEnsembl.1
    Natural variantiVAR_002488291V → M in NSHA; Viangchan/Jammu; class II. Corresponds to variant rs137852327dbSNPEnsembl.1
    Natural variantiVAR_002489317E → K in NSHA; Kalyan/Kerala; class III. 1 PublicationCorresponds to variant rs137852339dbSNPEnsembl.1
    Natural variantiVAR_002490323L → P in NSHA; A- type 3; class III. Corresponds to variant rs76723693dbSNPEnsembl.1
    Natural variantiVAR_002491335A → T in NSHA; Chatham; class III. Corresponds to variant rs5030869dbSNPEnsembl.1
    Natural variantiVAR_002493353P → S in NSHA; Ierapetra; class II. 1 PublicationCorresponds to variant rs137852333dbSNPEnsembl.1
    Natural variantiVAR_002494363N → K in NSHA; Loma Linda; class I. Corresponds to variant rs137852329dbSNPEnsembl.1
    Natural variantiVAR_002495385C → R in NSHA; Tomah; class I. Corresponds to variant rs137852322dbSNPEnsembl.1
    Natural variantiVAR_002496386K → E in NSHA; Iowa; class I. Corresponds to variant rs137852320dbSNPEnsembl.1
    Natural variantiVAR_002498387R → C in NSHA; Guadajalara and Mount Sinai; class I. 2 PublicationsCorresponds to variant rs137852334dbSNPEnsembl.1
    Natural variantiVAR_002497387R → H in NSHA; Beverly Hills; class I. Corresponds to variant rs137852321dbSNPEnsembl.1
    Natural variantiVAR_002499393R → H in NSHA; Nashville/Anaheim; class I. 1 PublicationCorresponds to variant rs137852316dbSNPEnsembl.1
    Natural variantiVAR_002500394V → L in NSHA; Alhambra; class I. 1 PublicationCorresponds to variant rs137852335dbSNPEnsembl.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 rs137852325dbSNPEnsembl.1
    Natural variantiVAR_002503410G → C in NSHA; Riverside; class I. Corresponds to variant rs137852323dbSNPEnsembl.1
    Natural variantiVAR_002504410G → D in NSHA; Japan; class I. 1 PublicationCorresponds to variant rs137852336dbSNPEnsembl.1
    Natural variantiVAR_002505416E → K in NSHA; Tokyo; class I. 1
    Natural variantiVAR_002506439R → P in NSHA; Pawnee; class I. 1 PublicationCorresponds to variant rs137852337dbSNPEnsembl.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 rs137852317dbSNPEnsembl.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 rs398123546dbSNPEnsembl.1
    Natural variantiVAR_002511454R → H in NSHA; Andalus; class I. Corresponds to variant rs137852324dbSNPEnsembl.1
    Natural variantiVAR_002512459R → L in NSHA; Canton; class II; frequent in China. Corresponds to variant rs72554665dbSNPEnsembl.1
    Natural variantiVAR_002513459R → P in NSHA; Cosenza; class II. Corresponds to variant rs72554665dbSNPEnsembl.1
    Natural variantiVAR_002514463R → H in NSHA; Kaiping; class II. Corresponds to variant rs72554664dbSNPEnsembl.1
    Natural variantiVAR_002515488G → V in NSHA; Campinas; class I. 1

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    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

    DisGeNETi2539.
    MalaCardsiG6PD.
    MIMi300908. phenotype.
    OpenTargetsiENSG00000160211.
    Orphaneti362. Glucose-6-phosphate-dehydrogenase deficiency.
    PharmGKBiPA28469.

    Chemistry databases

    ChEMBLiCHEMBL5347.

    Polymorphism and mutation databases

    DMDMi116242483.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemovedCombined sources2 Publications
    ChainiPRO_00000680832 – 515Glucose-6-phosphate 1-dehydrogenaseAdd BLAST514

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    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

    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

    EPDiP11413.
    MaxQBiP11413.
    PaxDbiP11413.
    PeptideAtlasiP11413.
    PRIDEiP11413.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00289800.
    SWISS-2DPAGEP11413.

    PTM databases

    iPTMnetiP11413.
    PhosphoSitePlusiP11413.
    SwissPalmiP11413.

    Expressioni

    Tissue specificityi

    Isoform Long is found in lymphoblasts, granulocytes and sperm.

    Gene expression databases

    BgeeiENSG00000160211.
    CleanExiHS_G6PD.
    ExpressionAtlasiP11413. baseline and differential.
    GenevisibleiP11413. HS.

    Organism-specific databases

    HPAiHPA000247.
    HPA000834.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself5EBI-4289891,EBI-4289891
    HSPB1P047922EBI-4289891,EBI-352682
    SIRT2Q8IXJ63EBI-4289891,EBI-477232

    GO - Molecular functioni

    • identical protein binding Source: IntAct
    • protein homodimerization activity Source: BHF-UCL

    Protein-protein interaction databases

    BioGridi108814. 65 interactors.
    IntActiP11413. 6 interactors.
    MINTiMINT-4716941.
    STRINGi9606.ENSP00000377192.

    Chemistry databases

    BindingDBiP11413.

    Structurei

    Secondary structure

    1515
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi32 – 37Combined sources6
    Turni38 – 40Combined sources3
    Helixi42 – 46Combined sources5
    Helixi48 – 57Combined sources10
    Beta strandi63 – 73Combined sources11
    Helixi77 – 84Combined sources8
    Helixi85 – 87Combined sources3
    Helixi92 – 94Combined sources3
    Helixi95 – 103Combined sources9
    Beta strandi105 – 109Combined sources5
    Helixi115 – 126Combined sources12
    Turni127 – 133Combined sources7
    Beta strandi134 – 140Combined sources7
    Turni144 – 146Combined sources3
    Helixi147 – 157Combined sources11
    Beta strandi161 – 163Combined sources3
    Beta strandi165 – 169Combined sources5
    Helixi177 – 187Combined sources11
    Turni188 – 190Combined sources3
    Helixi193 – 195Combined sources3
    Beta strandi196 – 198Combined sources3
    Helixi201 – 204Combined sources4
    Helixi206 – 216Combined sources11
    Helixi219 – 221Combined sources3
    Beta strandi222 – 226Combined sources5
    Turni227 – 229Combined sources3
    Beta strandi230 – 238Combined sources9
    Helixi247 – 250Combined sources4
    Turni251 – 253Combined sources3
    Helixi254 – 258Combined sources5
    Turni259 – 262Combined sources4
    Helixi263 – 272Combined sources10
    Beta strandi277 – 280Combined sources4
    Helixi281 – 292Combined sources12
    Helixi300 – 302Combined sources3
    Beta strandi303 – 309Combined sources7
    Helixi317 – 319Combined sources3
    Helixi322 – 324Combined sources3
    Beta strandi326 – 328Combined sources3
    Beta strandi336 – 344Combined sources9
    Turni347 – 351Combined sources5
    Beta strandi353 – 361Combined sources9
    Beta strandi366 – 373Combined sources8
    Beta strandi389 – 397Combined sources9
    Beta strandi399 – 407Combined sources9
    Turni409 – 411Combined sources3
    Beta strandi414 – 423Combined sources10
    Turni424 – 426Combined sources3
    Beta strandi427 – 431Combined sources5
    Helixi436 – 446Combined sources11
    Helixi449 – 451Combined sources3
    Helixi455 – 475Combined sources21
    Beta strandi480 – 483Combined sources4
    Beta strandi486 – 488Combined sources3
    Helixi490 – 498Combined sources9

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    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[»]
    ProteinModelPortaliP11413.
    SMRiP11413.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11413.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni201 – 205Substrate binding5

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiKOG0563. Eukaryota.
    COG0364. LUCA.
    GeneTreeiENSGT00530000063435.
    HOVERGENiHBG000856.
    InParanoidiP11413.
    KOiK00036.
    OMAiTIFEPIW.
    OrthoDBiEOG091G06FN.
    PhylomeDBiP11413.
    TreeFamiTF300584.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    HAMAPiMF_00966. G6PD. 1 hit.
    InterProiIPR001282. G6P_DH.
    IPR019796. G6P_DH_AS.
    IPR022675. G6P_DH_C.
    IPR022674. G6P_DH_NAD-bd.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR23429. PTHR23429. 1 hit.
    PfamiPF02781. G6PD_C. 1 hit.
    PF00479. G6PD_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000110. G6PD. 1 hit.
    PRINTSiPR00079. G6PDHDRGNASE.
    SUPFAMiSSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR00871. zwf. 1 hit.
    PROSITEiPS00069. G6P_DEHYDROGENASE. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

    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
    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

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    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

    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 rs137852340dbSNPEnsembl.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 rs78478128dbSNPEnsembl.1
    Natural variantiVAR_00245448I → T in NSHA; Aures; class II. 1 PublicationCorresponds to variant rs76645461dbSNPEnsembl.1
    Natural variantiVAR_00245558D → N in NSHA; Metaponto; class III. Corresponds to variant rs137852315dbSNPEnsembl.1
    Natural variantiVAR_00245668V → M in NSHA; A(-) type I; class III; frequent in African population. 4 PublicationsCorresponds to variant rs1050828dbSNPEnsembl.1
    Natural variantiVAR_00245770Y → H in NSHA; Namoru; 4% activity. Corresponds to variant rs137852349dbSNPEnsembl.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 rs138687036dbSNPEnsembl.1
    Natural variantiVAR_00245981R → H in NSHA; Lagosanto; class III. Corresponds to variant rs782308266dbSNPEnsembl.1
    Natural variantiVAR_002461106S → C in NSHA; Vancouver; class I. Corresponds to variant rs267606835dbSNPEnsembl.1
    Natural variantiVAR_002462126N → D in NSHA; Santa Maria and Mount Sinai; class IV and class I. 6 PublicationsCorresponds to variant rs1050829dbSNPEnsembl.1
    Natural variantiVAR_002463128L → P in NSHA; Vanua Lava; 4% activity. Corresponds to variant rs78365220dbSNPEnsembl.1
    Natural variantiVAR_002464131G → V in Chinese-4. Corresponds to variant rs137852341dbSNPEnsembl.1
    Natural variantiVAR_002465156E → K in NSHA; Ilesha; class III. Corresponds to variant rs137852313dbSNPEnsembl.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 rs137852314dbSNPEnsembl.1
    Natural variantiVAR_002468165N → D in NSHA; Chinese-3; class II. Corresponds to variant rs137852331dbSNPEnsembl.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 rs5030872dbSNPEnsembl.1
    Natural variantiVAR_002472182R → W in NSHA; Vancouver; class I. Corresponds to variant rs267606836dbSNPEnsembl.1
    Natural variantiVAR_002473188S → F in NSHA; Sassari/Cagliari; class II; frequent in the Mediterranean. 1 PublicationCorresponds to variant rs5030868dbSNPEnsembl.1
    Natural variantiVAR_002474198R → C in NSHA; Coimbra; class II. Corresponds to variant rs137852330dbSNPEnsembl.1
    Natural variantiVAR_002475198R → P in NSHA; Santiago; class I. Corresponds to variant rs137852332dbSNPEnsembl.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 rs782754619dbSNPEnsembl.1
    Natural variantiVAR_002477213V → L in NSHA; Minnesota; class I. Corresponds to variant rs137852326dbSNPEnsembl.1
    Natural variantiVAR_002478216F → L in NSHA; Harilaou; class I. Corresponds to variant rs137852319dbSNPEnsembl.1
    Natural variantiVAR_002480227R → L in NSHA; A- type 2; class III. Corresponds to variant rs137852328dbSNPEnsembl.1
    Natural variantiVAR_002479227R → Q in NSHA; Mexico City; class III. 1 PublicationCorresponds to variant rs137852328dbSNPEnsembl.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 rs137852318dbSNPEnsembl.1
    Natural variantiVAR_002487285R → H in NSHA; Montalbano; class III. Corresponds to variant rs74575103dbSNPEnsembl.1
    Natural variantiVAR_002488291V → M in NSHA; Viangchan/Jammu; class II. Corresponds to variant rs137852327dbSNPEnsembl.1
    Natural variantiVAR_002489317E → K in NSHA; Kalyan/Kerala; class III. 1 PublicationCorresponds to variant rs137852339dbSNPEnsembl.1
    Natural variantiVAR_020535322Y → H in Rehovot. 1 PublicationCorresponds to variant rs137852347dbSNPEnsembl.1
    Natural variantiVAR_002490323L → P in NSHA; A- type 3; class III. Corresponds to variant rs76723693dbSNPEnsembl.1
    Natural variantiVAR_002491335A → T in NSHA; Chatham; class III. Corresponds to variant rs5030869dbSNPEnsembl.1
    Natural variantiVAR_002492342L → F in Chinese-5. Corresponds to variant rs137852342dbSNPEnsembl.1
    Natural variantiVAR_002493353P → S in NSHA; Ierapetra; class II. 1 PublicationCorresponds to variant rs137852333dbSNPEnsembl.1
    Natural variantiVAR_002494363N → K in NSHA; Loma Linda; class I. Corresponds to variant rs137852329dbSNPEnsembl.1
    Natural variantiVAR_002495385C → R in NSHA; Tomah; class I. Corresponds to variant rs137852322dbSNPEnsembl.1
    Natural variantiVAR_002496386K → E in NSHA; Iowa; class I. Corresponds to variant rs137852320dbSNPEnsembl.1
    Natural variantiVAR_002498387R → C in NSHA; Guadajalara and Mount Sinai; class I. 2 PublicationsCorresponds to variant rs137852334dbSNPEnsembl.1
    Natural variantiVAR_002497387R → H in NSHA; Beverly Hills; class I. Corresponds to variant rs137852321dbSNPEnsembl.1
    Natural variantiVAR_002499393R → H in NSHA; Nashville/Anaheim; class I. 1 PublicationCorresponds to variant rs137852316dbSNPEnsembl.1
    Natural variantiVAR_002500394V → L in NSHA; Alhambra; class I. 1 PublicationCorresponds to variant rs137852335dbSNPEnsembl.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 rs137852325dbSNPEnsembl.1
    Natural variantiVAR_002503410G → C in NSHA; Riverside; class I. Corresponds to variant rs137852323dbSNPEnsembl.1
    Natural variantiVAR_002504410G → D in NSHA; Japan; class I. 1 PublicationCorresponds to variant rs137852336dbSNPEnsembl.1
    Natural variantiVAR_002505416E → K in NSHA; Tokyo; class I. 1
    Natural variantiVAR_002506439R → P in NSHA; Pawnee; class I. 1 PublicationCorresponds to variant rs137852337dbSNPEnsembl.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 rs137852317dbSNPEnsembl.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 rs398123546dbSNPEnsembl.1
    Natural variantiVAR_002511454R → H in NSHA; Andalus; class I. Corresponds to variant rs137852324dbSNPEnsembl.1
    Natural variantiVAR_002512459R → L in NSHA; Canton; class II; frequent in China. Corresponds to variant rs72554665dbSNPEnsembl.1
    Natural variantiVAR_002513459R → P in NSHA; Cosenza; class II. Corresponds to variant rs72554665dbSNPEnsembl.1
    Natural variantiVAR_002514463R → H in NSHA; Kaiping; class II. Corresponds to variant rs72554664dbSNPEnsembl.1
    Natural variantiVAR_002515488G → V in NSHA; Campinas; class I. 1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    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:
    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.
    CCDSiCCDS14756.2. [P11413-3]
    CCDS44023.1. [P11413-1]
    PIRiA40309. DEHUG6.
    RefSeqiNP_000393.4. NM_000402.4. [P11413-3]
    NP_001035810.1. NM_001042351.2. [P11413-1]
    UniGeneiHs.461047.
    Hs.684904.

    Genome annotation databases

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

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    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.
    CCDSiCCDS14756.2. [P11413-3]
    CCDS44023.1. [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:
    PDBei
    RCSB PDBi
    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[»]
    ProteinModelPortaliP11413.
    SMRiP11413.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi108814. 65 interactors.
    IntActiP11413. 6 interactors.
    MINTiMINT-4716941.
    STRINGi9606.ENSP00000377192.

    Chemistry databases

    BindingDBiP11413.
    ChEMBLiCHEMBL5347.

    PTM databases

    iPTMnetiP11413.
    PhosphoSitePlusiP11413.
    SwissPalmiP11413.

    Polymorphism and mutation databases

    DMDMi116242483.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00289800.
    SWISS-2DPAGEP11413.

    Proteomic databases

    EPDiP11413.
    MaxQBiP11413.
    PaxDbiP11413.
    PeptideAtlasiP11413.
    PRIDEiP11413.

    Protocols and materials databases

    DNASUi2539.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    CTDi2539.
    DisGeNETi2539.
    GeneCardsiG6PD.
    HGNCiHGNC:4057. G6PD.
    HPAiHPA000247.
    HPA000834.
    MalaCardsiG6PD.
    MIMi300908. phenotype.
    305900. gene.
    neXtProtiNX_P11413.
    OpenTargetsiENSG00000160211.
    Orphaneti362. Glucose-6-phosphate-dehydrogenase deficiency.
    PharmGKBiPA28469.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG0563. Eukaryota.
    COG0364. LUCA.
    GeneTreeiENSGT00530000063435.
    HOVERGENiHBG000856.
    InParanoidiP11413.
    KOiK00036.
    OMAiTIFEPIW.
    OrthoDBiEOG091G06FN.
    PhylomeDBiP11413.
    TreeFamiTF300584.

    Enzyme and pathway databases

    UniPathwayiUPA00115; UER00408.
    BioCyciMetaCyc:HS08467-MONOMER.
    ZFISH:HS08467-MONOMER.
    BRENDAi1.1.1.49. 2681.
    ReactomeiR-HSA-5628897. TP53 Regulates Metabolic Genes.
    R-HSA-71336. Pentose phosphate pathway (hexose monophosphate shunt).
    SABIO-RKP11413.
    SIGNORiP11413.

    Miscellaneous databases

    ChiTaRSiG6PD. human.
    EvolutionaryTraceiP11413.
    GeneWikiiGlucose-6-phosphate_dehydrogenase.
    GenomeRNAii2539.
    PROiP11413.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000160211.
    CleanExiHS_G6PD.
    ExpressionAtlasiP11413. baseline and differential.
    GenevisibleiP11413. HS.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    HAMAPiMF_00966. G6PD. 1 hit.
    InterProiIPR001282. G6P_DH.
    IPR019796. G6P_DH_AS.
    IPR022675. G6P_DH_C.
    IPR022674. G6P_DH_NAD-bd.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR23429. PTHR23429. 1 hit.
    PfamiPF02781. G6PD_C. 1 hit.
    PF00479. G6PD_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000110. G6PD. 1 hit.
    PRINTSiPR00079. G6PDHDRGNASE.
    SUPFAMiSSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR00871. zwf. 1 hit.
    PROSITEiPS00069. G6P_DEHYDROGENASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiG6PD_HUMAN
    AccessioniPrimary (citable) accession number: P11413
    Secondary accession number(s): D3DWX9
    , Q16000, Q16765, Q8IU70, Q8IU88, Q8IUA6, Q96PQ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: January 23, 2007
    Last modified: November 30, 2016
    This is version 222 of the entry and version 4 of the sequence. [Complete history]
    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.

    Miscellaneousi

    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.

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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.