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P11413 (G6PD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 196. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucose-6-phosphate 1-dehydrogenase

Short name=G6PD
EC=1.1.1.49
Gene names
Name:G6PD
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length515 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.30

Catalytic activity

D-glucose 6-phosphate + NADP+ = 6-phospho-D-glucono-1,5-lactone + NADPH. Ref.30

Pathway

Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3. HAMAP-Rule MF_00966

Subunit structure

Homotetramer; dimer of dimers. Ref.27 Ref.30

Tissue specificity

Isoform Long is found in lymphoblasts, granulocytes and sperm.

Polymorphism

The sequence shown is that of variant B, the most common variant. HAMAP-Rule MF_00966

Involvement in disease

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. Ref.34

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.

Sequence similarities

Belongs to the glucose-6-phosphate dehydrogenase family.

Biophysicochemical properties

Kinetic parameters:

KM=7.07 µM for NADP Ref.30

KM=52 µM for glucose 6-phosphate

Sequence caution

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

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Glucose metabolism
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Hereditary hemolytic anemia
   LigandNADP
   Molecular functionOxidoreductase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processNADP metabolic process

Inferred from direct assay Ref.30. Source: UniProtKB

NADPH regeneration

Inferred from mutant phenotype PubMed 17516514. Source: BHF-UCL

carbohydrate metabolic process

Traceable author statement. Source: Reactome

cellular response to oxidative stress

Inferred from mutant phenotype PubMed 17516514. Source: BHF-UCL

cholesterol biosynthetic process

Inferred from mutant phenotype PubMed 12027950. Source: BHF-UCL

cytokine production

Inferred from mutant phenotype PubMed 17361089. Source: BHF-UCL

erythrocyte maturation

Inferred from mutant phenotype PubMed 5643703. Source: BHF-UCL

glucose 6-phosphate metabolic process

Inferred from direct assay Ref.30. Source: UniProtKB

glutathione metabolic process

Inferred from mutant phenotype PubMed 17516514PubMed 2420826. Source: BHF-UCL

lipid metabolic process

Traceable author statement PubMed 17361089. Source: BHF-UCL

negative regulation of protein glutathionylation

Inferred from mutant phenotype PubMed 17516514. Source: BHF-UCL

oxidation-reduction process

Inferred from mutant phenotype PubMed 2420826. Source: BHF-UCL

pentose biosynthetic process

Inferred from direct assay PubMed 5643703. Source: BHF-UCL

pentose-phosphate shunt

Inferred from direct assay PubMed 2297768. Source: BHF-UCL

pentose-phosphate shunt, oxidative branch

Inferred from mutant phenotype PubMed 2420826. Source: BHF-UCL

regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to food

Inferred from electronic annotation. Source: Ensembl

response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

ribose phosphate biosynthetic process

Inferred from mutant phenotype PubMed 2420826. Source: BHF-UCL

small molecule metabolic process

Traceable author statement. Source: Reactome

substantia nigra development

Inferred from expression pattern PubMed 22926577. Source: UniProt

   Cellular_componentcytoplasm

Inferred from direct assay. Source: LIFEdb

cytoplasmic side of plasma membrane

Inferred from direct assay PubMed 743300. Source: BHF-UCL

cytosol

Inferred from direct assay PubMed 743300. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

nucleus

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionNADP binding

Inferred from direct assay Ref.30. Source: BHF-UCL

glucose binding

Inferred from direct assay Ref.30. Source: BHF-UCL

glucose-6-phosphate dehydrogenase activity

Inferred from direct assay Ref.30. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 21157431. Source: IntAct

protein homodimerization activity

Inferred from physical interaction Ref.30. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HSPB1P047922EBI-4289891,EBI-352682

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform Short (identifier: P11413-1)

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.
Isoform Long (identifier: P11413-2)

The sequence of this isoform differs from the canonical sequence as follows:
     257-257: R → RGPGRQGGSGSESCSLSLGSLVWGPHALEPGEQGGELRRALASSVPR
Isoform 3 (identifier: P11413-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGRRGSAPGNGRTLRGCERGGRRRRSADSVM
Note: Contains a phosphoserine at position 26.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12
Chain2 – 515514Glucose-6-phosphate 1-dehydrogenase HAMAP-Rule MF_00966
PRO_0000068083

Regions

Nucleotide binding38 – 458NADP 1 HAMAP-Rule MF_00966
Nucleotide binding401 – 4033NADP 2 HAMAP-Rule MF_00966
Nucleotide binding421 – 4233NADP 2 HAMAP-Rule MF_00966
Region201 – 2055Substrate binding HAMAP-Rule MF_00966

Sites

Active site2631Proton acceptor By similarity
Binding site721NADP 1
Binding site1471NADP 1
Binding site1711NADP 1; via carbonyl oxygen
Binding site1711Substrate
Binding site2391Substrate
Binding site2581Substrate
Binding site3571NADP 2
Binding site3601Substrate
Binding site3651Substrate
Binding site3661NADP 2
Binding site3701NADP 2
Binding site3931NADP 2
Binding site3951Substrate
Binding site4871NADP 2
Binding site5031NADP 2
Binding site5091NADP 2

Amino acid modifications

Modified residue21N-acetylalanine Ref.19 Ref.21 Ref.25 Ref.26
Modified residue891N6-acetyllysine Ref.22
Modified residue1711N6-acetyllysine Ref.22
Modified residue4031N6-acetyllysine Ref.22
Modified residue4321N6-acetyllysine Ref.22
Modified residue4971N6-acetyllysine Ref.22

Natural variations

Alternative sequence11M → MGRRGSAPGNGRTLRGCERG GRRRRSADSVM in isoform 3.
VSP_037802
Alternative sequence2571R → RGPGRQGGSGSESCSLSLGS LVWGPHALEPGEQGGELRRA LASSVPR in isoform Long.
VSP_001592
Natural variant121V → L in Sinnai. Ref.45
VAR_002450
Natural variant321H → R in CSNA; Gahoe; class III; frequent in Chinese. Ref.13
VAR_002451
Natural variant351Missing in NSHA; Sunderland; class I.
VAR_002452
Natural variant441A → G in Orissa; class III; frequent in Indian tribal populations. Ref.42
VAR_002453
Natural variant481I → T in Aures; class II. Ref.38
VAR_002454
Natural variant581D → N in Metaponto; class III.
VAR_002455
Natural variant681V → M in A(-) type I; class III; frequent in African population. Ref.3 Ref.4 Ref.5 Ref.14
Corresponds to variant rs1050828 [ dbSNP | Ensembl ].
VAR_002456
Natural variant701Y → H in Namoru; 4% activity.
VAR_002457
Natural variant751L → P in Swansea; class I. Ref.43
VAR_002458
Natural variant811R → C in Konan/Ube; class III.
Corresponds to variant rs138687036 [ dbSNP | Ensembl ].
VAR_002460
Natural variant811R → H in Lagosanto; class III.
VAR_002459
Natural variant1061S → C in Vancouver; class I.
VAR_002461
Natural variant1261N → D in A(+), A(-), Santa Maria; class IV and in Mount Sinai; class I. Ref.3 Ref.4 Ref.5 Ref.14 Ref.31 Ref.44
Corresponds to variant rs1050829 [ dbSNP | Ensembl ].
VAR_002462
Natural variant1281L → P in Vanua Lava; 4% activity.
VAR_002463
Natural variant1311G → V in Chinese-4.
Corresponds to variant rs137852341 [ dbSNP | Ensembl ].
VAR_002464
Natural variant1561E → K in Ilesha; class III.
VAR_002465
Natural variant1631G → D in Plymouth; class I. Ref.43
VAR_002467
Natural variant1631G → S in Mahidol; class III; reduced activity; associated with reduced density of Plasmodium vivax but not Plasmodium falciparum in Southeast Asians. Ref.47
VAR_002466
Natural variant1651N → D in Chinese-3; class II.
VAR_002468
Natural variant1661R → H in Naone; 1% activity.
VAR_002469
Natural variant1761D → G in Shinshu; class I. Ref.39
VAR_002470
Natural variant1811D → V in Santa Maria; class I.
Corresponds to variant rs5030872 [ dbSNP | Ensembl ].
VAR_002471
Natural variant1821R → W in Vancouver; class I.
VAR_002472
Natural variant1881S → F in Sassari/Cagliari; class II; frequent in the Mediterranean. Ref.33
Corresponds to variant rs5030868 [ dbSNP | Ensembl ].
VAR_002473
Natural variant1981R → C in Coimbra; class II.
VAR_002474
Natural variant1981R → P in NSHA; Santiago; class I.
VAR_002475
Natural variant2121M → V in Sibari; class III.
VAR_002476
Natural variant2131V → L in Minnesota; class I.
VAR_002477
Natural variant2161F → L in Harilaou; class I.
VAR_002478
Natural variant2271R → L in A- type 2; class III.
VAR_002480
Natural variant2271R → Q in Mexico City; class III. Ref.34
VAR_002479
Natural variant242 – 2432Missing in Stonybrook; class I.
VAR_002481
Natural variant2571R → G in Wayne; class I.
VAR_002482
Natural variant2741E → K in Corum; class I. Ref.43
VAR_002483
Natural variant2781S → F in Wexham; class I. Ref.43
VAR_002484
Natural variant2791T → S in Chinese-1; class II.
VAR_002485
Natural variant2821D → H in Seattle; class III. Ref.33
VAR_002486
Natural variant2851R → H in Montalbano; class III.
VAR_002487
Natural variant2911V → M in Viangchan/Jammu; class II.
VAR_002488
Natural variant3171E → K in Kalyan/Kerala; class III. Ref.37
VAR_002489
Natural variant3221Y → H in Rehovot. Ref.46
VAR_020535
Natural variant3231L → P in A- type 3; class III.
Corresponds to variant rs76723693 [ dbSNP | Ensembl ].
VAR_002490
Natural variant3351A → T in Chatham; class III.
Corresponds to variant rs5030869 [ dbSNP | Ensembl ].
VAR_002491
Natural variant3421L → F in Chinese-5.
VAR_002492
Natural variant3531P → S in Ierapetra; class II. Ref.34
VAR_002493
Natural variant3631N → K in Loma Linda; class I.
VAR_002494
Natural variant3851C → R in Tomah; class I.
VAR_002495
Natural variant3861K → E in Iowa; class I.
VAR_002496
Natural variant3871R → C in NSHA; Guadajalara and Mount Sinai; class I. Ref.34 Ref.44
VAR_002498
Natural variant3871R → H in Beverly Hills; class I.
VAR_002497
Natural variant3931R → H in Nashville/Anaheim; class I. Ref.35
VAR_002499
Natural variant3941V → L in NSHA; Alhambra; class I. Ref.34
VAR_002500
Natural variant3961P → L in Bari; class I. Ref.40
VAR_002501
Natural variant3981E → K in Puerto Limon; class I.
VAR_002502
Natural variant4101G → C in Riverside; class I.
VAR_002503
Natural variant4101G → D in NSHA; Japan; class I. Ref.34
VAR_002504
Natural variant4161E → K in Tokyo; class I.
VAR_002505
Natural variant4391R → P in NSHA; Pawnee; class I. Ref.34
VAR_002506
Natural variant4401L → F in Telti/Kobe; class I.
VAR_002507
Natural variant4471G → R in Santiago de Cuba; class I.
VAR_002508
Natural variant4491Q → H in Cassano; class II.
VAR_002509
Natural variant4541R → C in Chinese-II/Maewo/Union; class II, <1% activity. Ref.36
VAR_002510
Natural variant4541R → H in Andalus; class I.
VAR_002511
Natural variant4591R → L in Canton; class II; frequent in China.
Corresponds to variant rs72554665 [ dbSNP | Ensembl ].
VAR_002512
Natural variant4591R → P in Cosenza; class II.
Corresponds to variant rs72554665 [ dbSNP | Ensembl ].
VAR_002513
Natural variant4631R → H in Kaiping; class II.
VAR_002514
Natural variant4881G → V in Campinas; class I.
VAR_002515

Experimental info

Sequence conflict111Q → H in CAA27309. Ref.1
Sequence conflict111Q → H in AAA63175. Ref.2
Sequence conflict111Q → H in AAA52500. Ref.3
Sequence conflict435 – 4362DA → EP in AAA52499. Ref.15

Secondary structure

............................................................................................ 515
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Short [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: F2B775340640A96F

FASTA51559,257
        10         20         30         40         50         60 
MAEQVALSRT QVCGILREEL FQGDAFHQSD THIFIIMGAS GDLAKKKIYP TIWWLFRDGL 

        70         80         90        100        110        120 
LPENTFIVGY ARSRLTVADI RKQSEPFFKA TPEEKLKLED FFARNSYVAG QYDDAASYQR 

       130        140        150        160        170        180 
LNSHMNALHL GSQANRLFYL ALPPTVYEAV TKNIHESCMS QIGWNRIIVE KPFGRDLQSS 

       190        200        210        220        230        240 
DRLSNHISSL FREDQIYRID HYLGKEMVQN LMVLRFANRI FGPIWNRDNI ACVILTFKEP 

       250        260        270        280        290        300 
FGTEGRGGYF DEFGIIRDVM QNHLLQMLCL VAMEKPASTN SDDVRDEKVK VLKCISEVQA 

       310        320        330        340        350        360 
NNVVLGQYVG NPDGEGEATK GYLDDPTVPR GSTTATFAAV VLYVENERWD GVPFILRCGK 

       370        380        390        400        410        420 
ALNERKAEVR LQFHDVAGDI FHQQCKRNEL VIRVQPNEAV YTKMMTKKPG MFFNPEESEL 

       430        440        450        460        470        480 
DLTYGNRYKN VKLPDAYERL ILDVFCGSQM HFVRSDELRE AWRIFTPLLH QIELEKPKPI 

       490        500        510 
PYIYGSRGPT EADELMKRVG FQYEGTYKWV NPHKL 

« Hide

Isoform Long [UniParc].

Checksum: A6759ACCB3CDF921
Show »

FASTA56163,827
Isoform 3 [UniParc].

Checksum: CFE3675547A5672F
Show »

FASTA54562,468

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"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.
[28]"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.
[29]"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.
[30]"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.
[31]"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.
[32]"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.
[33]"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.
[34]"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.
[35]"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.
[36]"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.
[37]"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.
[38]"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.
[39]"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.
[40]"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.
[41]"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.
[42]"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.
[43]"New glucose-6-phosphate dehydrogenase mutations associated with chronic anemia."
Mason P.J., Sonati M.F., Macdonald D., Lanza C., Busutil D., Town M., Corcoran C.M., Kaeda J.S., Stevens D.J., Al-Ismail S., Altay C., Hatton C., Lewis D.S., McMullin M.F., Meloni T., Paul B., Pippard M., Prentice A.G., Vulliamy T.J., Luzzatto L.
Blood 85:1377-1380(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SWANSEA PRO-75; PLYMOUTH ASP-163; CORUM LYS-274 AND WEXHAM PHE-278.
[44]"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.
[45]"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.
[46]"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.
[47]"Positively selected G6PD-Mahidol mutation reduces Plasmodium vivax density in Southeast Asians."
Louicharoen C., Patin E., Paul R., Nuchprayoon I., Witoonpanich B., Peerapittayamongkol C., Casademont I., Sura T., Laird N.M., Singhasivanon P., Quintana-Murci L., Sakuntabhai A.
Science 326:1546-1549(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION OF VARIANT MAHIDOL SER-163 WITH REDUCED DENSITY OF PLASMODIUM VIVAX.
+Additional computationally mapped references.

Web resources

G6PD

G6PD deficiency resource

G6PDdb

G6PD mutation database

SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03674 mRNA. Translation: CAA27309.1.
M65234 expand/collapse EMBL AC list , 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.
CCDSCCDS14756.2. [P11413-3]
CCDS44023.1. [P11413-1]
PIRDEHUG6. A40309.
RefSeqNP_000393.4. NM_000402.4. [P11413-3]
NP_001035810.1. NM_001042351.2. [P11413-1]
UniGeneHs.461047.
Hs.684904.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QKIX-ray3.00A/B/C/D/E/F/G/H2-515[»]
2BH9X-ray2.50A27-515[»]
2BHLX-ray2.90A/B28-515[»]
ProteinModelPortalP11413.
SMRP11413. Positions 28-515.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108814. 38 interactions.
IntActP11413. 2 interactions.
MINTMINT-4716941.
STRING9606.ENSP00000377192.

Chemistry

BindingDBP11413.
ChEMBLCHEMBL5347.

PTM databases

PhosphoSiteP11413.

Polymorphism databases

DMDM116242483.

2D gel databases

REPRODUCTION-2DPAGEIPI00289800.
SWISS-2DPAGEP11413.

Proteomic databases

MaxQBP11413.
PaxDbP11413.
PRIDEP11413.

Protocols and materials databases

DNASU2539.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369620; 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]
GeneID2539.
KEGGhsa:2539.
UCSCuc004flx.1. human. [P11413-3]
uc004fly.1. human. [P11413-1]

Organism-specific databases

CTD2539.
GeneCardsGC0XM153759.
HGNCHGNC:4057. G6PD.
HPAHPA000247.
HPA000834.
MIM300908. phenotype.
305900. gene.
neXtProtNX_P11413.
Orphanet362. Glucose-6-phosphate-dehydrogenase deficiency.
PharmGKBPA28469.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0364.
HOVERGENHBG000856.
KOK00036.
OMADSIMEAW.
PhylomeDBP11413.
TreeFamTF300584.

Enzyme and pathway databases

BioCycMetaCyc:HS08467-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
SABIO-RKP11413.
UniPathwayUPA00115; UER00408.

Gene expression databases

ArrayExpressP11413.
BgeeP11413.
CleanExHS_G6PD.
GenevestigatorP11413.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_00966. G6PD.
InterProIPR001282. G6P_DH.
IPR019796. G6P_DH_AS.
IPR022675. G6P_DH_C.
IPR022674. G6P_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR23429. PTHR23429. 1 hit.
PfamPF02781. G6PD_C. 1 hit.
PF00479. G6PD_N. 1 hit.
[Graphical view]
PIRSFPIRSF000110. G6PD. 1 hit.
PRINTSPR00079. G6PDHDRGNASE.
TIGRFAMsTIGR00871. zwf. 1 hit.
PROSITEPS00069. G6P_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSG6PD. human.
EvolutionaryTraceP11413.
GeneWikiGlucose-6-phosphate_dehydrogenase.
GenomeRNAi2539.
NextBio10021.
PROP11413.
SOURCESearch...

Entry information

Entry nameG6PD_HUMAN
AccessionPrimary (citable) accession number: P11413
Secondary accession number(s): D3DWX9 expand/collapse secondary AC list , Q16000, Q16765, Q8IU70, Q8IU88, Q8IUA6, Q96PQ2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 196 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM