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P11413

- G6PD_HUMAN

UniProt

P11413 - G6PD_HUMAN

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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

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.1 Publication

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-phosphate

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei72 – 721NADP 1
Binding sitei147 – 1471NADP 1
Binding sitei171 – 1711NADP 1; via carbonyl oxygen
Binding sitei171 – 1711Substrate
Binding sitei239 – 2391Substrate
Binding sitei258 – 2581Substrate
Active sitei263 – 2631Proton acceptor By similarity
Binding sitei357 – 3571NADP 2
Binding sitei360 – 3601Substrate
Binding sitei365 – 3651Substrate
Binding sitei366 – 3661NADP 2
Binding sitei370 – 3701NADP 2
Binding sitei393 – 3931NADP 2
Binding sitei395 – 3951Substrate
Binding sitei487 – 4871NADP 2
Binding sitei503 – 5031NADP 2
Binding sitei509 – 5091NADP 2

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi38 – 458NADP 1UniRule annotation
Nucleotide bindingi401 – 4033NADP 2UniRule annotation
Nucleotide bindingi421 – 4233NADP 2UniRule annotation

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
Complete GO annotation...

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. nucleus Source: Ensembl
Complete GO annotation...

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.
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.1 Publication
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.
Mutagenesisi171 – 1711K → R: Inhibits catalytic activity. Does not impair dimerization.
Mutagenesisi386 – 3861K → Q: Impairs dimerization and reduces catalytic activity.
Mutagenesisi386 – 3861K → R: Does not impair dimerization and catalytic activity.
Mutagenesisi403 – 4031K → Q: Impairs dimerization and reduces catalytic activity in cells under oxidative stress.
Mutagenesisi403 – 4031K → R: Does not impair dimerization and catalytic activity.

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 – 11Removed1 Publication
Chaini2 – 515514Glucose-6-phosphate 1-dehydrogenaseUniRule annotationPRO_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-acetyllysine1 Publication
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.

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.2 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.

Miscellaneous databases

EvolutionaryTraceiP11413.

Family & Domainsi

Region

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

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.

Polymorphismi

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

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. 1 Publication
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. VSP_037802
Alternative sequencei257 – 2571R → RGPGRQGGSGSESCSLSLGS LVWGPHALEPGEQGGELRRA LASSVPR in isoform Long. VSP_001592

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111Q → H in CAA27309. 1 Publication
Sequence conflicti11 – 111Q → H in AAA63175. 1 Publication
Sequence conflicti11 – 111Q → H in AAA52500. 1 Publication
Sequence conflicti435 – 4362DA → EP in AAA52499. 1 Publication

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]
ENST00000593787; ENSP00000471208; ENSG00000269087. [P11413-1]
ENST00000594771; ENSP00000470721; ENSG00000269087. [P11413-3]
ENST00000595441; ENSP00000469988; ENSG00000269087. [P11413-2]
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 ]
ENST00000593787 ; ENSP00000471208 ; ENSG00000269087 . [P11413-1 ]
ENST00000594771 ; ENSP00000470721 ; ENSG00000269087 . [P11413-3 ]
ENST00000595441 ; ENSP00000469988 ; ENSG00000269087 . [P11413-2 ]
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 197 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

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