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UniProtKB - P11413 (G6PD_HUMAN)

Protein

Glucose-6-phosphate 1-dehydrogenase

Gene

G6PD

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

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.

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, Glucose-6-phosphate 1-dehydrogenase (G6PD), 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 (zwf)
    2. 6-phosphogluconolactonase (PGLS)
    3. 6-phosphogluconate dehydrogenase, decarboxylating (PGD), 6-phosphogluconate dehydrogenase, decarboxylating, 6-phosphogluconate dehydrogenase, decarboxylating, 6-phosphogluconate dehydrogenase, decarboxylating (gntZ)
    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 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
    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
    Nucleotide bindingi38 – 45NADP 1Combined sources2 Publications8
    Nucleotide bindingi401 – 403NADP 2Combined sources2 Publications3
    Nucleotide bindingi421 – 423NADP 2Combined sources2 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
    View the complete GO annotation on QuickGO ...

    GO - Biological processi

    View the complete GO annotation on QuickGO ...

    Keywordsi

    Molecular functionOxidoreductase
    Biological processCarbohydrate metabolism, Glucose metabolism
    LigandNADP

    Enzyme and pathway databases

    BioCyciMetaCyc:HS08467-MONOMER
    BRENDAi1.1.1.49 2681
    ReactomeiR-HSA-5628897 TP53 Regulates Metabolic Genes
    R-HSA-71336 Pentose phosphate pathway
    SABIO-RKiP11413
    SIGNORiP11413
    UniPathwayi
    UPA00115;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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
    Proteomesi
    • UP000005640 Componenti: Chromosome X

    Organism-specific databases

    EuPathDBiHostDB:ENSG00000160211.15
    HGNCiHGNC:4057 G6PD
    MIMi305900 gene
    neXtProtiNX_P11413

    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

    Pathology & Biotechi

    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
    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
    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
    Orphaneti466026 Class I glucose-6-phosphate dehydrogenase deficiency
    362 NON RARE IN EUROPE: Glucose-6-phosphate-dehydrogenase deficiency
    PharmGKBiPA28469

    Chemistry databases

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

    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
    ProteomicsDBi52771
    52772 [P11413-2]
    52773 [P11413-3]

    2D gel databases

    REPRODUCTION-2DPAGEiIPI00289800
    SWISS-2DPAGEiP11413

    PTM databases

    iPTMnetiP11413
    PhosphoSitePlusiP11413
    SwissPalmiP11413

    Expressioni

    Tissue specificityi

    Isoform Long is found in lymphoblasts, granulocytes and sperm.

    Gene expression databases

    BgeeiENSG00000160211 Expressed in 170 organ(s), highest expression level in blood
    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

    GO - Molecular functioni

    View the complete GO annotation on QuickGO ...

    Protein-protein interaction databases

    BioGridi108814, 67 interactors
    IntActiP11413, 8 interactors
    MINTiP11413
    STRINGi9606.ENSP00000377192

    Chemistry databases

    BindingDBiP11413

    Structurei

    Secondary structure

    1515
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    ProteinModelPortaliP11413
    SMRiP11413
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11413

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni201 – 205Substrate bindingCombined sources1 Publication5

    Sequence similaritiesi

    Belongs to the glucose-6-phosphate dehydrogenase family.Curated

    Phylogenomic databases

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

    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

    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

    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
    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

    Computationally mapped potential isoform sequencesi

    There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    		Gene namesLengthAnnotation
    E7EUI8E7EUI8_HUMAN
    Glucose-6-phosphate 1-dehydrogenase
    G6PD
    		338Annotation score:
    E7EM57E7EM57_HUMAN
    Glucose-6-phosphate 1-dehydrogenase
    G6PD
    		320Annotation score:
    E9PD92E9PD92_HUMAN
    Glucose-6-phosphate 1-dehydrogenase
    G6PD
    		256Annotation score:

    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 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
    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
    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

    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

    Similar proteinsi

    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
    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:
    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[»]
    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, 67 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

    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
    EuPathDBiHostDB:ENSG00000160211.15
    GeneCardsiG6PD
    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
    GenAtlasiSearch...

    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

    ChiTaRSiG6PD human
    EvolutionaryTraceiP11413
    GeneWikiiGlucose-6-phosphate_dehydrogenase
    GenomeRNAii2539
    PROiPR:P11413
    SOURCEiSearch...

    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
    ProtoNetiSearch...

    Entry informationi

    Entry nameiG6PD_HUMAN
    AccessioniPrimary (citable) accession number: P11413
    Secondary accession number(s): D3DWX9
    , Q16000, Q16765, Q8IU70, Q8IU88, Q8IUA6, Q96PQ2
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: January 23, 2007
    Last modified: November 7, 2018
    This is version 238 of the entry and version 4 of the sequence. See 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

    Keywords - Technical termi

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

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    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. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    7. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    UniProt is an ELIXIR core data resource
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