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P11413

- G6PD_HUMAN

UniProt

P11413 - G6PD_HUMAN

Protein

Glucose-6-phosphate 1-dehydrogenase

Gene

G6PD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 198 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei72 – 721NADP 12 Publications
    Binding sitei147 – 1471NADP 12 Publications
    Binding sitei171 – 1711NADP 1; via carbonyl oxygen2 Publications
    Binding sitei171 – 1711Substrate
    Binding sitei239 – 2391Substrate
    Binding sitei258 – 2581Substrate
    Active sitei263 – 2631Proton acceptorBy similarity
    Binding sitei357 – 3571NADP 22 Publications
    Binding sitei360 – 3601Substrate
    Binding sitei365 – 3651Substrate
    Binding sitei366 – 3661NADP 22 Publications
    Binding sitei370 – 3701NADP 22 Publications
    Binding sitei393 – 3931NADP 22 Publications
    Binding sitei395 – 3951Substrate
    Binding sitei487 – 4871NADP 22 Publications
    Binding sitei503 – 5031NADP 22 Publications
    Binding sitei509 – 5091NADP 22 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi38 – 458NADP 12 Publications
    Nucleotide bindingi401 – 4033NADP 22 Publications
    Nucleotide bindingi421 – 4233NADP 22 Publications

    GO - Molecular functioni

    1. glucose-6-phosphate dehydrogenase activity Source: UniProtKB
    2. glucose binding Source: BHF-UCL
    3. NADP binding Source: BHF-UCL
    4. protein binding Source: IntAct
    5. protein homodimerization activity Source: BHF-UCL

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. cellular response to oxidative stress Source: BHF-UCL
    3. cholesterol biosynthetic process Source: BHF-UCL
    4. cytokine production Source: BHF-UCL
    5. erythrocyte maturation Source: BHF-UCL
    6. glucose 6-phosphate metabolic process Source: UniProtKB
    7. glutathione metabolic process Source: BHF-UCL
    8. lipid metabolic process Source: BHF-UCL
    9. NADPH regeneration Source: BHF-UCL
    10. NADP metabolic process Source: UniProtKB
    11. negative regulation of protein glutathionylation Source: BHF-UCL
    12. oxidation-reduction process Source: BHF-UCL
    13. pentose biosynthetic process Source: BHF-UCL
    14. pentose-phosphate shunt Source: BHF-UCL
    15. pentose-phosphate shunt, oxidative branch Source: BHF-UCL
    16. regulation of neuron apoptotic process Source: Ensembl
    17. response to ethanol Source: Ensembl
    18. response to food Source: Ensembl
    19. response to organic cyclic compound Source: Ensembl
    20. ribose phosphate biosynthetic process Source: BHF-UCL
    21. small molecule metabolic process Source: Reactome
    22. substantia nigra development Source: UniProt

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Carbohydrate metabolism, Glucose metabolism

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:HS08467-MONOMER.
    ReactomeiREACT_1859. Pentose phosphate pathway (hexose monophosphate shunt).
    SABIO-RKP11413.
    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
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:4057. G6PD.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: LIFEdb
    2. cytoplasmic side of plasma membrane Source: BHF-UCL
    3. cytosol Source: BHF-UCL
    4. extracellular vesicular exosome Source: UniProt
    5. membrane Source: UniProtKB
    6. nucleus Source: Ensembl

    Pathology & Biotechi

    Involvement in diseasei

    Anemia, non-spherocytic hemolytic, due to G6PD deficiency (NSHA) [MIM:300908]: A 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.1 Publication
    Note: 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.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti35 – 351Missing in NSHA; Sunderland; class I.
    VAR_002452
    Natural varianti198 – 1981R → P in NSHA; Santiago; class I.
    VAR_002475
    Natural varianti387 – 3871R → C in NSHA; Guadajalara and Mount Sinai; class I. 2 Publications
    VAR_002498
    Natural varianti394 – 3941V → L in NSHA; Alhambra; class I. 1 Publication
    VAR_002500
    Natural varianti410 – 4101G → D in NSHA; Japan; class I. 1 Publication
    VAR_002504
    Natural varianti439 – 4391R → P in NSHA; Pawnee; class I. 1 Publication
    VAR_002506

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi171 – 1711K → Q: Inhibits catalytic activity. Does not impair dimerization. 1 Publication
    Mutagenesisi171 – 1711K → R: Inhibits catalytic activity. Does not impair dimerization. 1 Publication
    Mutagenesisi386 – 3861K → Q: Impairs dimerization and reduces catalytic activity. 1 Publication
    Mutagenesisi386 – 3861K → R: Does not impair dimerization and catalytic activity. 1 Publication
    Mutagenesisi403 – 4031K → Q: Impairs dimerization and reduces catalytic activity in cells under oxidative stress. 1 Publication
    Mutagenesisi403 – 4031K → R: Does not impair dimerization and catalytic activity. 1 Publication

    Keywords - Diseasei

    Disease mutation, Hereditary hemolytic anemia

    Organism-specific databases

    MIMi300908. phenotype.
    Orphaneti362. Glucose-6-phosphate-dehydrogenase deficiency.
    PharmGKBiPA28469.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed5 Publications
    Chaini2 – 515514Glucose-6-phosphate 1-dehydrogenasePRO_0000068083Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine4 Publications
    Modified residuei89 – 891N6-acetyllysine1 Publication
    Modified residuei171 – 1711N6-acetyllysine1 Publication
    Modified residuei403 – 4031N6-acetyllysine2 Publications
    Modified residuei432 – 4321N6-acetyllysine1 Publication
    Modified residuei497 – 4971N6-acetyllysine1 Publication

    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.6 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP11413.
    PaxDbiP11413.
    PRIDEiP11413.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00289800.
    SWISS-2DPAGEP11413.

    PTM databases

    PhosphoSiteiP11413.

    Expressioni

    Tissue specificityi

    Isoform Long is found in lymphoblasts, granulocytes and sperm.

    Gene expression databases

    ArrayExpressiP11413.
    BgeeiP11413.
    CleanExiHS_G6PD.
    GenevestigatoriP11413.

    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
    HSPB1P047922EBI-4289891,EBI-352682

    Protein-protein interaction databases

    BioGridi108814. 39 interactions.
    IntActiP11413. 2 interactions.
    MINTiMINT-4716941.
    STRINGi9606.ENSP00000377192.

    Structurei

    Secondary structure

    1
    515
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi32 – 376
    Turni38 – 403
    Helixi42 – 465
    Helixi48 – 5710
    Beta strandi63 – 7311
    Helixi77 – 848
    Helixi85 – 873
    Helixi92 – 943
    Helixi95 – 1039
    Beta strandi105 – 1095
    Helixi115 – 12612
    Turni127 – 1337
    Beta strandi134 – 1407
    Turni144 – 1463
    Helixi147 – 15711
    Beta strandi161 – 1633
    Beta strandi165 – 1695
    Helixi177 – 18711
    Turni188 – 1903
    Helixi193 – 1953
    Beta strandi196 – 1983
    Helixi201 – 2044
    Helixi206 – 21611
    Helixi219 – 2213
    Beta strandi222 – 2265
    Turni227 – 2293
    Beta strandi230 – 2389
    Helixi247 – 2504
    Turni251 – 2533
    Helixi254 – 2585
    Turni259 – 2624
    Helixi263 – 27210
    Beta strandi277 – 2804
    Helixi281 – 29212
    Helixi300 – 3023
    Beta strandi303 – 3097
    Helixi317 – 3193
    Helixi322 – 3243
    Beta strandi326 – 3283
    Beta strandi336 – 3449
    Turni347 – 3515
    Beta strandi353 – 3619
    Beta strandi366 – 3738
    Beta strandi389 – 3979
    Beta strandi399 – 4079
    Turni409 – 4113
    Beta strandi414 – 42310
    Turni424 – 4263
    Beta strandi427 – 4315
    Helixi436 – 44611
    Helixi449 – 4513
    Helixi455 – 47521
    Beta strandi480 – 4834
    Beta strandi486 – 4883
    Helixi490 – 4989

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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. Positions 28-515.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11413.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni201 – 2055Substrate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0364.
    HOVERGENiHBG000856.
    KOiK00036.
    OMAiDSIMEAW.
    PhylomeDBiP11413.
    TreeFamiTF300584.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    HAMAPiMF_00966. G6PD.
    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.
    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. Align

    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

    MAEQVALSRT QVCGILREEL FQGDAFHQSD THIFIIMGAS GDLAKKKIYP    50
    TIWWLFRDGL LPENTFIVGY ARSRLTVADI RKQSEPFFKA TPEEKLKLED 100
    FFARNSYVAG QYDDAASYQR LNSHMNALHL GSQANRLFYL ALPPTVYEAV 150
    TKNIHESCMS QIGWNRIIVE KPFGRDLQSS DRLSNHISSL FREDQIYRID 200
    HYLGKEMVQN LMVLRFANRI FGPIWNRDNI ACVILTFKEP FGTEGRGGYF 250
    DEFGIIRDVM QNHLLQMLCL VAMEKPASTN SDDVRDEKVK VLKCISEVQA 300
    NNVVLGQYVG NPDGEGEATK GYLDDPTVPR GSTTATFAAV VLYVENERWD 350
    GVPFILRCGK ALNERKAEVR LQFHDVAGDI FHQQCKRNEL VIRVQPNEAV 400
    YTKMMTKKPG MFFNPEESEL DLTYGNRYKN VKLPDAYERL ILDVFCGSQM 450
    HFVRSDELRE AWRIFTPLLH QIELEKPKPI PYIYGSRGPT EADELMKRVG 500
    FQYEGTYKWV NPHKL 515
    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

    Note: Contains a phosphoserine at position 26.

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

    Sequence cautioni

    The sequence AAA63175.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti11 – 111Q → H in CAA27309. (PubMed:3515319)Curated
    Sequence conflicti11 – 111Q → H in AAA63175. (PubMed:2428611)Curated
    Sequence conflicti11 – 111Q → H in AAA52500. (PubMed:2836867)Curated
    Sequence conflicti435 – 4362DA → EP in AAA52499. (PubMed:3012556)Curated

    Polymorphismi

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

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti12 – 121V → L in Sinnai. 1 Publication
    VAR_002450
    Natural varianti32 – 321H → R in CSNA; Gahoe; class III; frequent in Chinese. 1 Publication
    VAR_002451
    Natural varianti35 – 351Missing in NSHA; Sunderland; class I.
    VAR_002452
    Natural varianti44 – 441A → G in Orissa; class III; frequent in Indian tribal populations. 1 Publication
    VAR_002453
    Natural varianti48 – 481I → T in Aures; class II. 1 Publication
    VAR_002454
    Natural varianti58 – 581D → N in Metaponto; class III.
    VAR_002455
    Natural varianti68 – 681V → M in A(-) type I; class III; frequent in African population. 4 Publications
    Corresponds to variant rs1050828 [ dbSNP | Ensembl ].
    VAR_002456
    Natural varianti70 – 701Y → H in Namoru; 4% activity.
    VAR_002457
    Natural varianti75 – 751L → P in Swansea; class I. 1 Publication
    VAR_002458
    Natural varianti81 – 811R → C in Konan/Ube; class III.
    Corresponds to variant rs138687036 [ dbSNP | Ensembl ].
    VAR_002460
    Natural varianti81 – 811R → H in Lagosanto; class III.
    VAR_002459
    Natural varianti106 – 1061S → C in Vancouver; class I.
    VAR_002461
    Natural varianti126 – 1261N → D in A(+), A(-), Santa Maria; class IV and in Mount Sinai; class I. 6 Publications
    Corresponds to variant rs1050829 [ dbSNP | Ensembl ].
    VAR_002462
    Natural varianti128 – 1281L → P in Vanua Lava; 4% activity.
    VAR_002463
    Natural varianti131 – 1311G → V in Chinese-4.
    Corresponds to variant rs137852341 [ dbSNP | Ensembl ].
    VAR_002464
    Natural varianti156 – 1561E → K in Ilesha; class III.
    VAR_002465
    Natural varianti163 – 1631G → D in Plymouth; class I. 1 Publication
    VAR_002467
    Natural varianti163 – 1631G → S in Mahidol; class III; reduced activity; associated with reduced density of Plasmodium vivax but not Plasmodium falciparum in Southeast Asians.
    VAR_002466
    Natural varianti165 – 1651N → D in Chinese-3; class II.
    VAR_002468
    Natural varianti166 – 1661R → H in Naone; 1% activity.
    VAR_002469
    Natural varianti176 – 1761D → G in Shinshu; class I. 1 Publication
    VAR_002470
    Natural varianti181 – 1811D → V in Santa Maria; class I.
    Corresponds to variant rs5030872 [ dbSNP | Ensembl ].
    VAR_002471
    Natural varianti182 – 1821R → W in Vancouver; class I.
    VAR_002472
    Natural varianti188 – 1881S → F in Sassari/Cagliari; class II; frequent in the Mediterranean. 1 Publication
    Corresponds to variant rs5030868 [ dbSNP | Ensembl ].
    VAR_002473
    Natural varianti198 – 1981R → C in Coimbra; class II.
    VAR_002474
    Natural varianti198 – 1981R → P in NSHA; Santiago; class I.
    VAR_002475
    Natural varianti212 – 2121M → V in Sibari; class III.
    VAR_002476
    Natural varianti213 – 2131V → L in Minnesota; class I.
    VAR_002477
    Natural varianti216 – 2161F → L in Harilaou; class I.
    VAR_002478
    Natural varianti227 – 2271R → L in A- type 2; class III.
    VAR_002480
    Natural varianti227 – 2271R → Q in Mexico City; class III. 1 Publication
    VAR_002479
    Natural varianti242 – 2432Missing in Stonybrook; class I.
    VAR_002481
    Natural varianti257 – 2571R → G in Wayne; class I.
    VAR_002482
    Natural varianti274 – 2741E → K in Corum; class I. 1 Publication
    VAR_002483
    Natural varianti278 – 2781S → F in Wexham; class I. 1 Publication
    VAR_002484
    Natural varianti279 – 2791T → S in Chinese-1; class II.
    VAR_002485
    Natural varianti282 – 2821D → H in Seattle; class III. 1 Publication
    VAR_002486
    Natural varianti285 – 2851R → H in Montalbano; class III.
    VAR_002487
    Natural varianti291 – 2911V → M in Viangchan/Jammu; class II.
    VAR_002488
    Natural varianti317 – 3171E → K in Kalyan/Kerala; class III. 1 Publication
    VAR_002489
    Natural varianti322 – 3221Y → H in Rehovot. 1 Publication
    VAR_020535
    Natural varianti323 – 3231L → P in A- type 3; class III.
    Corresponds to variant rs76723693 [ dbSNP | Ensembl ].
    VAR_002490
    Natural varianti335 – 3351A → T in Chatham; class III.
    Corresponds to variant rs5030869 [ dbSNP | Ensembl ].
    VAR_002491
    Natural varianti342 – 3421L → F in Chinese-5.
    VAR_002492
    Natural varianti353 – 3531P → S in Ierapetra; class II. 1 Publication
    VAR_002493
    Natural varianti363 – 3631N → K in Loma Linda; class I.
    VAR_002494
    Natural varianti385 – 3851C → R in Tomah; class I.
    VAR_002495
    Natural varianti386 – 3861K → E in Iowa; class I.
    VAR_002496
    Natural varianti387 – 3871R → C in NSHA; Guadajalara and Mount Sinai; class I. 2 Publications
    VAR_002498
    Natural varianti387 – 3871R → H in Beverly Hills; class I.
    VAR_002497
    Natural varianti393 – 3931R → H in Nashville/Anaheim; class I. 1 Publication
    VAR_002499
    Natural varianti394 – 3941V → L in NSHA; Alhambra; class I. 1 Publication
    VAR_002500
    Natural varianti396 – 3961P → L in Bari; class I. 1 Publication
    VAR_002501
    Natural varianti398 – 3981E → K in Puerto Limon; class I.
    VAR_002502
    Natural varianti410 – 4101G → C in Riverside; class I.
    VAR_002503
    Natural varianti410 – 4101G → D in NSHA; Japan; class I. 1 Publication
    VAR_002504
    Natural varianti416 – 4161E → K in Tokyo; class I.
    VAR_002505
    Natural varianti439 – 4391R → P in NSHA; Pawnee; class I. 1 Publication
    VAR_002506
    Natural varianti440 – 4401L → F in Telti/Kobe; class I.
    VAR_002507
    Natural varianti447 – 4471G → R in Santiago de Cuba; class I.
    VAR_002508
    Natural varianti449 – 4491Q → H in Cassano; class II.
    VAR_002509
    Natural varianti454 – 4541R → C in Chinese-II/Maewo/Union; class II, <1% activity. 1 Publication
    VAR_002510
    Natural varianti454 – 4541R → H in Andalus; class I.
    VAR_002511
    Natural varianti459 – 4591R → L in Canton; class II; frequent in China.
    Corresponds to variant rs72554665 [ dbSNP | Ensembl ].
    VAR_002512
    Natural varianti459 – 4591R → P in Cosenza; class II.
    Corresponds to variant rs72554665 [ dbSNP | Ensembl ].
    VAR_002513
    Natural varianti463 – 4631R → H in Kaiping; class II.
    VAR_002514
    Natural varianti488 – 4881G → V in Campinas; class I.
    VAR_002515

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MGRRGSAPGNGRTLRGCERG GRRRRSADSVM in isoform 3. 1 PublicationVSP_037802
    Alternative sequencei257 – 2571R → RGPGRQGGSGSESCSLSLGS LVWGPHALEPGEQGGELRRA LASSVPR in isoform Long. CuratedVSP_001592

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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]
    GeneIDi2539.
    KEGGihsa:2539.
    UCSCiuc004flx.1. human. [P11413-3]
    uc004fly.1. human. [P11413-1]

    Polymorphism databases

    DMDMi116242483.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    G6PD

    G6PD deficiency resource

    G6PDdb

    G6PD mutation database

    SHMPD

    The Singapore human mutation and polymorphism database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS14756.2. [P11413-3 ]
    CCDS44023.1. [P11413-1 ]
    PIRi A40309. DEHUG6.
    RefSeqi NP_000393.4. NM_000402.4. [P11413-3 ]
    NP_001035810.1. NM_001042351.2. [P11413-1 ]
    UniGenei Hs.461047.
    Hs.684904.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1QKI X-ray 3.00 A/B/C/D/E/F/G/H 2-515 [» ]
    2BH9 X-ray 2.50 A 27-515 [» ]
    2BHL X-ray 2.90 A/B 28-515 [» ]
    ProteinModelPortali P11413.
    SMRi P11413. Positions 28-515.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108814. 39 interactions.
    IntActi P11413. 2 interactions.
    MINTi MINT-4716941.
    STRINGi 9606.ENSP00000377192.

    Chemistry

    BindingDBi P11413.
    ChEMBLi CHEMBL5347.

    PTM databases

    PhosphoSitei P11413.

    Polymorphism databases

    DMDMi 116242483.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00289800.
    SWISS-2DPAGE P11413.

    Proteomic databases

    MaxQBi P11413.
    PaxDbi P11413.
    PRIDEi P11413.

    Protocols and materials databases

    DNASUi 2539.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000369620 ; ENSP00000358633 ; ENSG00000160211 . [P11413-2 ]
    ENST00000393562 ; ENSP00000377192 ; ENSG00000160211 . [P11413-3 ]
    ENST00000393564 ; ENSP00000377194 ; ENSG00000160211 . [P11413-1 ]
    GeneIDi 2539.
    KEGGi hsa:2539.
    UCSCi uc004flx.1. human. [P11413-3 ]
    uc004fly.1. human. [P11413-1 ]

    Organism-specific databases

    CTDi 2539.
    GeneCardsi GC0XM153759.
    HGNCi HGNC:4057. G6PD.
    HPAi HPA000247.
    HPA000834.
    MIMi 300908. phenotype.
    305900. gene.
    neXtProti NX_P11413.
    Orphaneti 362. Glucose-6-phosphate-dehydrogenase deficiency.
    PharmGKBi PA28469.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0364.
    HOVERGENi HBG000856.
    KOi K00036.
    OMAi DSIMEAW.
    PhylomeDBi P11413.
    TreeFami TF300584.

    Enzyme and pathway databases

    UniPathwayi UPA00115 ; UER00408 .
    BioCyci MetaCyc:HS08467-MONOMER.
    Reactomei REACT_1859. Pentose phosphate pathway (hexose monophosphate shunt).
    SABIO-RK P11413.

    Miscellaneous databases

    ChiTaRSi G6PD. human.
    EvolutionaryTracei P11413.
    GeneWikii Glucose-6-phosphate_dehydrogenase.
    GenomeRNAii 2539.
    NextBioi 10021.
    PROi P11413.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P11413.
    Bgeei P11413.
    CleanExi HS_G6PD.
    Genevestigatori P11413.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    HAMAPi MF_00966. G6PD.
    InterProi IPR001282. G6P_DH.
    IPR019796. G6P_DH_AS.
    IPR022675. G6P_DH_C.
    IPR022674. G6P_DH_NAD-bd.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    PANTHERi PTHR23429. PTHR23429. 1 hit.
    Pfami PF02781. G6PD_C. 1 hit.
    PF00479. G6PD_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000110. G6PD. 1 hit.
    PRINTSi PR00079. G6PDHDRGNASE.
    TIGRFAMsi TIGR00871. zwf. 1 hit.
    PROSITEi PS00069. G6P_DEHYDROGENASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation of human glucose-6-phosphate dehydrogenase (G6PD) cDNA clones: primary structure of the protein and unusual 5' non-coding region."
      Persico M.G., Viglietto G., Martini G., Toniolo D., Paonessa G., Moscatelli C., Dono R., Vulliamy T.J., Luzzatto L., D'Urso M.
      Nucleic Acids Res. 14:2511-2522(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
    2. "Structural analysis of the X-linked gene encoding human glucose 6-phosphate dehydrogenase."
      Martini G., Toniolo D., Vulliamy T., Luzzatto L., Dono R., Viglietto G., Paonessa G., D'Urso M., Persico M.G.
      EMBO J. 5:1849-1855(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Molecular cloning and nucleotide sequence of cDNA for human glucose-6-phosphate dehydrogenase variant A(-)."
      Hirono A., Beutler E.
      Proc. Natl. Acad. Sci. U.S.A. 85:3951-3954(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), VARIANTS MET-68 AND ASP-126.
    4. "Sequence of human glucose-6-phosphate dehydrogenase cloned in plasmids and a yeast artificial chromosome."
      Chen E.Y., Cheng A., Lee A., Kuang W., Hillier L., Green P., Schlessinger D., Ciccodicola A., D'Urso M.
      Genomics 10:792-800(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS MET-68 AND ASP-126.
    5. "Long-range sequence analysis in Xq28: thirteen known and six candidate genes in 219.4 kb of high GC DNA between the RCP/GCP and G6PD loci."
      Chen E.Y., Zollo M., Mazzarella R.A., Ciccodicola A., Chen C.-N., Zuo L., Heiner C., Burough F.W., Ripetto M., Schlessinger D., D'Urso M.
      Hum. Mol. Genet. 5:659-668(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS MET-68 AND ASP-126.
    6. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
      Tissue: Lung.
    9. "Two structural genes on different chromosomes are required for encoding the major subunit of human red cell glucose-6-phosphate dehydrogenase."
      Kanno H., Huang I.Y., Kan Y.W., Yoshida A.
      Cell 58:595-606(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-71.
    10. "5' structure and expression of human glucose-6-phosphate dehydrogenase mRNA."
      Kanno H., Kondoh T., Yoshida A.
      DNA Cell Biol. 12:209-215(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-71 (ISOFORM 3).
    11. "The CpG island in the 5' region of the G6PD gene of man and mouse."
      Toniolo D., Filippi M., Dono R., Lettieri T., Martini G.
      Gene 102:197-203(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
    12. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-9.
      Tissue: Platelet.
    13. "A to G substitution identified in exon 2 of the G6PD gene among G6PD deficient Chinese."
      Chao L.T., Du C.S., Louie E., Zuo L., Chen E., Lubin B., Chiu D.T.
      Nucleic Acids Res. 19:6056-6056(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-34, VARIANT CSNA ARG-32.
    14. "Nucleotide variability at G6pd and the signature of malarial selection in humans."
      Saunders M.A., Hammer M.F., Nachman M.W.
      Genetics 162:1849-1861(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-515 (ISOFORM SHORT), VARIANTS MET-68 AND ASP-126.
    15. "Human glucose-6-phosphate dehydrogenase: primary structure and cDNA cloning."
      Takizawa T., Huang I.-Y., Ikuta T., Yoshida A.
      Proc. Natl. Acad. Sci. U.S.A. 83:4157-4161(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 154-515 (ISOFORM SHORT).
    16. "Human erythrocyte glucose-6-phosphate dehydrogenase. Identification of a reactive lysyl residue labelled with pyridoxal 5'-phosphate."
      Camardella L., Caruso C., Rutigliano B., Romano M., di Prisco G., Descalzi-Cancedda F.
      Eur. J. Biochem. 171:485-489(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 199-215.
    17. "Amino acid sequence of the carboxy-terminal end of human erythrocyte glucose-6-phosphate dehydrogenase."
      Descalzi-Cancedda F., Caruso C., Romano M., di Prisco G., Camardella L.
      Biochem. Biophys. Res. Commun. 118:332-338(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 509-515.
    18. "Alternative splicing of human glucose-6-phosphate dehydrogenase messenger RNA in different tissues."
      Hirono A., Beutler E.
      J. Clin. Invest. 83:343-346(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING.
    19. "Glucose 6-phosphate dehydrogenase from human erythrocytes: identification of N-acetyl-alanine at the N-terminus of the mature protein."
      Camardella L., Damonte G., Carratore V., Benatti U., Tonetti M., Moneti G.
      Biochem. Biophys. Res. Commun. 207:331-338(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-89; LYS-171; LYS-403; LYS-432 AND LYS-497, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "Glucose-6-phosphate dehydrogenase, NADPH, and cell survival."
      Stanton R.C.
      IUBMB Life 64:362-369(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    25. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "Regulation of G6PD acetylation by KAT9/SIRT2 modulates NADPH homeostasis and cell survival during oxidative stress."
      Wang Y.P., Zhou L.S., Zhao Y.Z., Wang S.W., Chen L.L., Liu L.X., Ling Z.Q., Hu F.J., Sun Y.P., Zhang J.Y., Yang C., Yang Y., Xiong Y., Guan K.L., Ye D.
      EMBO J. 33:1304-1320(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ACETYLATION AT LYS-403 BY ELP3, DEACETYLATION AT LYS-403 BY SIRT2, INTERACTION WITH SIRT2, MUTAGENESIS OF LYS-171; LYS-386 AND LYS-403, SUBUNIT.
    28. "Human glucose-6-phosphate dehydrogenase: the crystal structure reveals a structural NADP(+) molecule and provides insights into enzyme deficiency."
      Au S.W., Gover S., Lam V.M., Adams M.J.
      Structure 8:293-303(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF VARIANT CANTON IN COMPLEX WITH NADP, SUBUNIT.
    29. "Variants of glucose-6-phosphate dehydrogenase are due to missense mutations spread throughout the coding region of the gene."
      Vulliamy T., Beutler E., Luzzatto L.
      Hum. Mutat. 2:159-167(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON VARIANTS.
    30. "G6PDdb, an integrated database of glucose-6-phosphate dehydrogenase (G6PD) mutations."
      Kwok C.J., Martin A.C., Au S.W., Lam V.M.
      Hum. Mutat. 19:217-224(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON VARIANTS.
    31. "Structural studies of glucose-6-phosphate and NADP+ binding to human glucose-6-phosphate dehydrogenase."
      Kotaka M., Gover S., Vandeputte-Rutten L., Au S.W., Lam V.M., Adams M.J.
      Acta Crystallogr. D 61:495-504(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 28-514 IN COMPLEX WITH NADP AND GLUCOSE 6-PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    32. "A single nucleotide base transition is the basis of the common human glucose-6-phosphate dehydrogenase variant A (+)."
      Takizawa T., Yoneyama Y., Miwa S., Yoshida A.
      Genomics 1:228-231(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT A(+) ASP-126.
    33. "Diverse point mutations in the human glucose-6-phosphate dehydrogenase gene cause enzyme deficiency and mild or severe hemolytic anemia."
      Vulliamy T.J., D'Urso M., Battistuzzi G., Estrada M., Foulkes N.S., Martini G., Calabro V., Poggi V., Giordano R., Town M., Luzzatto L., Persico M.G.
      Proc. Natl. Acad. Sci. U.S.A. 85:5171-5175(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS.
    34. "Two point mutations are responsible for G6PD polymorphism in Sardinia."
      de Vita G., Alcalay M., Sampietro M., Cappelini M.D., Fiorelli G., Toniolo D.
      Am. J. Hum. Genet. 44:233-240(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS SASSARI/CAGLIARI PHE-188 AND SEATTLE HIS-282.
    35. "New glucose-6-phosphate dehydrogenase mutations from various ethnic groups."
      Beutler E., Westwood B., Prchal J.T., Vaca C.S., Bartsocas C.S., Baronciani L.
      Blood 80:255-256(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GLN-227 AND SER-353, VARIANTS NSHA CYS-387; LEU-394; ASP-410 AND PRO-439.
    36. "Molecular basis of chronic non-spherocytic haemolytic anaemia: a new G6PD variant (393arg-to-his) with abnormal K(m) G6P and marked in vivo instability."
      Filosa S., Calabro V., Vallone D., Poggi V., Mason P., Pagnini D., Alfinito F., Rotoli B., Martini G., Luzzatto L., Battistuzzi G.
      Br. J. Haematol. 80:111-116(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT NASHVILLE/ANAHEIM HIS-393.
    37. "A novel C to T substitution at nucleotide 1360 of cDNA which abolishes a natural Hha I site accounts for a new G6PD deficiency gene in Chinese."
      Perng L.-I., Chiou S.-S., Liu T.-C., Chang J.-G.
      Hum. Mol. Genet. 1:205-205(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CHINESE-2/MAEWO CYS-454.
    38. "G6PD Kalyan and G6PD Kerala; two deficient variants in India caused by the same 317 Glu-->Lys mutation."
      Ahluwalia A., Corcoran C.M., Vulliamy T.J., Ishwad C.S., Naidu J.M., Stevens D.J., Mason P.J., Luzzatto L.
      Hum. Mol. Genet. 1:209-210(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT KALYAN/KERALA LYS-317.
    39. "G6PD Aures: a new mutation (48 Ile-->Thr) causing mild G6PD deficiency is associated with favism."
      Nafa K., Reghis A., Osmani N., Baghli L., Benabadji M., Kaplan J.-C., Vulliamy T.J., Luzzatto L.
      Hum. Mol. Genet. 2:81-82(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT AURES THR-48.
    40. "Molecular study of eight Japanese cases of glucose-6-phosphate dehydrogenase deficiency by nonradioisotopic single-strand conformation polymorphism analysis."
      Hirono A., Miwa S., Fujii H., Ishida F., Yamada K., Kubota K.
      Blood 83:3363-3368(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SHINSHU GLY-176.
    41. "A novel single-base mutation in the glucose 6-phosphate dehydrogenase gene is associated with chronic non-spherocytic haemolytic anaemia."
      Filosa S., Cai W., Galanello R., Cao A., de Mattia D., Schettini F., Martini G.
      Hum. Genet. 94:560-562(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BARI LEU-396.
    42. "Multiple glucose 6-phosphate dehydrogenase-deficient variants correlate with malaria endemicity in the Vanuatu archipelago (southwestern Pacific)."
      Ganczakowski M., Town M., Bowden D.K., Vulliamy T.J., Kaneko A., Clegg J.B., Weatherall D.J., Luzzatto L.
      Am. J. Hum. Genet. 56:294-301(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS NAMORU; VANUA LAVA; NAONE AND UNION.
    43. "A new glucose-6-phosphate dehydrogenase variant, G6PD Orissa (44 Ala-->Gly), is the major polymorphic variant in tribal populations in India."
      Kaeda J.S., Chhotray G.P., Ranjit M.R., Bautista J.M., Reddy P.H., Stevens D., Naidu J.M., Britt R.P., Vulliamy T.J., Luzzatto L., Mason P.J.
      Am. J. Hum. Genet. 57:1335-1341(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ORISSA GLY-44.
    44. Cited for: VARIANTS SWANSEA PRO-75; PLYMOUTH ASP-163; CORUM LYS-274 AND WEXHAM PHE-278.
    45. "G6PD Mount Sinai: a new severe hemolytic variant characterized by dual mutations at nucleotides 376G and 1159T (N126D)."
      Vlachos A., Westwood B., Lipton J.M., Beutler E.
      Hum. Mutat. Suppl. 1:S154-S155(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MOUNT SINAI ASP-126 AND CYS-387.
    46. "A new glucose 6 phosphate dehydrogenase variant, G6PD Sinnai (34 G->T)."
      Galanello R., Loi D., Sollaino C., Dessi S., Cao A., Melis M.A.
      Hum. Mutat. 12:72-73(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SINNAI LEU-12.
    47. "A new exon 9 glucose-6-phosphate dehydrogenase mutation (G6PD 'Rehovot') in a Jewish Ethiopian family with variable phenotypes."
      Iancovici-Kidon M., Sthoeger D., Abrahamov A., Volach B., Beutler E., Gelbart T., Barak Y.
      Blood Cells Mol. Dis. 26:567-571(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT REHOVOT HIS-322.
    48. Cited for: ASSOCIATION OF VARIANT MAHIDOL SER-163 WITH REDUCED DENSITY OF PLASMODIUM VIVAX.

    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: October 1, 2014
    This is version 198 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

    External Data

    Dasty 3