P11413 (G6PD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glucose-6-phosphate 1-dehydrogenase
Short name=G6PD
EC=1.1.1.49

Gene names

Name:

G6PD

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	515 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Produces pentose sugars for nucleic acid synthesis and main producer of NADPH reducing power.
Catalytic activity	D-glucose 6-phosphate + NADP+ = 6-phospho-D-glucono-1,5-lactone + NADPH.
Pathway	Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.
Subunit structure	Homodimer or homotetramer. Ref.23
Tissue specificity	Isoform Long is found in lymphoblasts, granulocytes and sperm.
Polymorphism	The sequence shown is that of variant B, the most common variant.
Involvement in disease	Chronic non-spherocytic hemolytic anemia (CNSHA) [MIM:305900]: 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 CNSHA 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.29
Miscellaneous	Has NADP both as cofactor (bound to the N-terminal domain) and as structural element bound to the C-terminal domain.
Sequence similarities	Belongs to the glucose-6-phosphate dehydrogenase family.
Sequence caution	The sequence AAA63175.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Hereditary hemolytic anemia
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	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 mutant phenotype PubMed 5643703. Source: BHF-UCL glutathione metabolic process Inferred from mutant phenotype PubMed 17516514PubMed 2420826. Source: BHF-UCL negative regulation of protein glutathionylation Inferred from mutant phenotype PubMed 17516514. Source: BHF-UCL pentose biosynthetic process Inferred from direct assay PubMed 5643703. Source: BHF-UCL pentose-phosphate shunt, oxidative branch Inferred from mutant phenotype PubMed 2420826. Source: BHF-UCL response to ethanol Inferred from electronic annotation. Source: Compara response to food Inferred from electronic annotation. Source: Compara response to organic cyclic compound Inferred from electronic annotation. Source: Compara ribose phosphate biosynthetic process Inferred from mutant phenotype PubMed 2420826. Source: BHF-UCL
Cellular_component	centrosome Inferred from direct assay. Source: HPA cytosol Inferred from direct assay PubMed 743300. Source: BHF-UCL internal side of plasma membrane Inferred from direct assay PubMed 743300. Source: BHF-UCL intracellular membrane-bounded organelle Inferred from direct assay. Source: HPA nucleus Inferred from electronic annotation. Source: Compara
Molecular_function	NADP binding Inferred from direct assay PubMed 15858258. Source: BHF-UCL glucose binding Inferred from direct assay PubMed 15858258. Source: BHF-UCL glucose-6-phosphate dehydrogenase activity Inferred from mutant phenotype PubMed 2420826PubMed 5643703PubMed 743300. Source: BHF-UCL
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.12

Chain

2 – 515

514

Glucose-6-phosphate 1-dehydrogenase

PRO_0000068083

Regions

Nucleotide binding

39 – 45

7

NADP By similarity

Sites

Active site

263

1

Proton acceptor By similarity

Binding site

40

1

NADP By similarity

Binding site

72

1

NADP By similarity

Binding site

201

1

Substrate By similarity

Binding site

205

1

Substrate By similarity

Binding site

238

1

NADP

Binding site

357

1

NADP

Binding site

487

1

NADP

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.19

Modified residue

89

1

N6-acetyllysine Ref.21

Modified residue

171

1

N6-acetyllysine Ref.21

Modified residue

403

1

N6-acetyllysine Ref.21

Modified residue

432

1

N6-acetyllysine Ref.21

Modified residue

497

1

N6-acetyllysine Ref.21

Natural variations

Alternative sequence

1

1

M → MGRRGSAPGNGRTLRGCERG GRRRRSADSVM in isoform 3.

VSP_037802

Alternative sequence

257

1

R → RGPGRQGGSGSESCSLSLGS LVWGPHALEPGEQGGELRRA LASSVPR in isoform Long.

VSP_001592

Natural variant

12

1

V → L in Sinnai. Ref.40

VAR_002450

Natural variant

32

1

H → R in CSNA; Gahoe; class III; frequent in Chinese. Ref.13

VAR_002451

Natural variant

35

1

Missing in CNSHA; Sunderland; class I.

VAR_002452

Natural variant

44

1

A → G in Orissa; class III; frequent in Indian tribal populations. Ref.37

VAR_002453

Natural variant

48

1

I → T in Aures; class II. Ref.33

VAR_002454

Natural variant

58

1

D → N in Metaponto; class III.

VAR_002455

Natural variant

68

1

V → 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 variant

70

1

Y → H in Namoru; 4% activity.

VAR_002457

Natural variant

75

1

L → P in Swansea; class I. Ref.38

VAR_002458

Natural variant

81

1

R → C in Konan/Ube; class III.

VAR_002460

Natural variant

81

1

R → H in Lagosanto; class III.

VAR_002459

Natural variant

106

1

S → C in Vancouver; class I.

VAR_002461

Natural variant

126

1

N → D in A(+), A(-), Santa Maria; class IV and in Mount Sinai; class I. Ref.3 Ref.4 Ref.5 Ref.14 Ref.26 Ref.39
Corresponds to variant rs1050829 [ dbSNP | Ensembl ].

VAR_002462

Natural variant

128

1

L → P in Vanua Lava; 4% activity.

VAR_002463

Natural variant

131

1

G → V in Chinese-4.

VAR_002464

Natural variant

156

1

E → K in Ilesha; class III.

VAR_002465

Natural variant

163

1

G → D in Plymouth; class I. Ref.38

VAR_002467

Natural variant

163

1

G → S in Mahidol; class III; reduced activity; associated with reduced density of Plasmodium vivax but not Plasmodium falciparum in Southeast Asians. Ref.42

VAR_002466

Natural variant

165

1

N → D in Chinese-3; class II.

VAR_002468

Natural variant

166

1

R → H in Naone; 1% activity.

VAR_002469

Natural variant

176

1

D → G in Shinshu; class I. Ref.34

VAR_002470

Natural variant

181

1

D → V in Santa Maria; class I.
Corresponds to variant rs5030872 [ dbSNP | Ensembl ].

VAR_002471

Natural variant

182

1

R → W in Vancouver; class I.

VAR_002472

Natural variant

188

1

S → F in Sassari/Cagliari; class II; frequent in the Mediterranean. Ref.28
Corresponds to variant rs5030868 [ dbSNP | Ensembl ].

VAR_002473

Natural variant

198

1

R → C in Coimbra; class II.

VAR_002474

Natural variant

198

1

R → P in CNSHA; Santiago; class I.

VAR_002475

Natural variant

212

1

M → V in Sibari; class III.

VAR_002476

Natural variant

213

1

V → L in Minnesota; class I.

VAR_002477

Natural variant

216

1

F → L in Harilaou; class I.

VAR_002478

Natural variant

227

1

R → L in A- type 2; class III.

VAR_002480

Natural variant

227

1

R → Q in Mexico City; class III. Ref.29

VAR_002479

Natural variant

242 – 243

2

Missing in Stonybrook; class I.

VAR_002481

Natural variant

257

1

R → G in Wayne; class I.

VAR_002482

Natural variant

274

1

E → K in Corum; class I. Ref.38

VAR_002483

Natural variant

278

1

S → F in Wexham; class I. Ref.38

VAR_002484

Natural variant

279

1

T → S in Chinese-1; class II.

VAR_002485

Natural variant

282

1

D → H in Seattle; class III. Ref.28

VAR_002486

Natural variant

285

1

R → H in Montalbano; class III.

VAR_002487

Natural variant

291

1

V → M in Viangchan/Jammu; class II.

VAR_002488

Natural variant

317

1

E → K in Kalyan/Kerala; class III. Ref.32

VAR_002489

Natural variant

322

1

Y → H in Rehovot. Ref.41

VAR_020535

Natural variant

323

1

L → P in A- type 3; class III.

VAR_002490

Natural variant

335

1

A → T in Chatham; class III.
Corresponds to variant rs5030869 [ dbSNP | Ensembl ].

VAR_002491

Natural variant

342

1

L → F in Chinese-5.

VAR_002492

Natural variant

353

1

P → S in Ierapetra; class II. Ref.29

VAR_002493

Natural variant

363

1

N → K in Loma Linda; class I.

VAR_002494

Natural variant

385

1

C → R in Tomah; class I.

VAR_002495

Natural variant

386

1

K → E in Iowa; class I.

VAR_002496

Natural variant

387

1

R → C in CNSHA; Guadajalara and Mount Sinai; class I. Ref.29 Ref.39

VAR_002498

Natural variant

387

1

R → H in Beverly Hills; class I.

VAR_002497

Natural variant

393

1

R → H in Nashville/Anaheim; class I. Ref.30

VAR_002499

Natural variant

394

1

V → L in CNSHA; Alhambra; class I. Ref.29

VAR_002500

Natural variant

396

1

P → L in Bari; class I. Ref.35

VAR_002501

Natural variant

398

1

E → K in Puerto Limon; class I.

VAR_002502

Natural variant

410

1

G → C in Riverside; class I.

VAR_002503

Natural variant

410

1

G → D in CNSHA; Japan; class I. Ref.29

VAR_002504

Natural variant

416

1

E → K in Tokyo; class I.

VAR_002505

Natural variant

439

1

R → P in CNSHA; Pawnee; class I. Ref.29

VAR_002506

Natural variant

440

1

L → F in Telti/Kobe; class I.

VAR_002507

Natural variant

447

1

G → R in Santiago de Cuba; class I.

VAR_002508

Natural variant

449

1

Q → H in Cassano; class II.

VAR_002509

Natural variant

454

1

R → C in Chinese-II/Maewo/Union; class II, <1% activity. Ref.31

VAR_002510

Natural variant

454

1

R → H in Andalus; class I.

VAR_002511

Natural variant

459

1

R → L in Canton; class II; frequent in China.

VAR_002512

Natural variant

459

1

R → P in Cosenza; class II.

VAR_002513

Natural variant

463

1

R → H in Kaiping; class II.

VAR_002514

Natural variant

488

1

G → V in Campinas; class I.

VAR_002515

Experimental info

Sequence conflict

11

1

Q → H in CAA27309. Ref.1

Sequence conflict

11

1

Q → H in AAA63175. Ref.2

Sequence conflict

11

1

Q → H in AAA52500. Ref.3

Sequence conflict

435 – 436

2

DA → EP in AAA52499. Ref.15

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

515

Helix Strand Turn

Details...

Beta strand

32 – 37

6

Turn

38 – 40

3

Helix

42 – 46

5

Helix

48 – 57

10

Beta strand

63 – 73

11

Helix

77 – 84

8

Helix

85 – 87

3

Helix

92 – 94

3

Helix

95 – 103

9

Beta strand

105 – 109

5

Helix

115 – 126

12

Turn

127 – 133

7

Beta strand

134 – 140

7

Turn

144 – 146

3

Helix

147 – 157

11

Beta strand

161 – 163

3

Beta strand

165 – 169

5

Helix

177 – 187

11

Turn

188 – 190

3

Helix

193 – 195

3

Beta strand

196 – 198

3

Helix

201 – 204

4

Helix

206 – 216

11

Helix

219 – 221

3

Beta strand

222 – 226

5

Turn

227 – 229

3

Beta strand

230 – 238

9

Helix

247 – 250

4

Turn

251 – 253

3

Helix

254 – 258

5

Turn

259 – 262

4

Helix

263 – 272

10

Beta strand

277 – 280

4

Helix

281 – 292

12

Helix

300 – 302

3

Beta strand

303 – 309

7

Helix

317 – 319

3

Helix

322 – 324

3

Beta strand

326 – 328

3

Beta strand

336 – 344

9

Turn

347 – 351

5

Beta strand

353 – 361

9

Beta strand

366 – 373

8

Beta strand

389 – 397

9

Beta strand

399 – 407

9

Turn

409 – 411

3

Beta strand

414 – 423

10

Turn

424 – 426

3

Beta strand

427 – 431

5

Helix

436 – 446

11

Helix

449 – 451

3

Helix

455 – 475

21

Beta strand

480 – 483

4

Beta strand

486 – 488

3

Helix

490 – 498

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform Short [UniParc]. Last modified January 23, 2007. Version 4. Checksum: F2B775340640A96F	FASTA	515	59,257
	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
	Isoform Long [UniParc]. Checksum: A6759ACCB3CDF921	FASTA	561	63,827
	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 DEFGIIRGPG RQGGSGSESC SLSLGSLVWG PHALEPGEQG GELRRALASS 310 320 330 340 350 360 VPRDVMQNHL LQMLCLVAME KPASTNSDDV RDEKVKVLKC ISEVQANNVV LGQYVGNPDG 370 380 390 400 410 420 EGEATKGYLD DPTVPRGSTT ATFAAVVLYV ENERWDGVPF ILRCGKALNE RKAEVRLQFH 430 440 450 460 470 480 DVAGDIFHQQ CKRNELVIRV QPNEAVYTKM MTKKPGMFFN PEESELDLTY GNRYKNVKLP 490 500 510 520 530 540 DAYERLILDV FCGSQMHFVR SDELREAWRI FTPLLHQIEL EKPKPIPYIY GSRGPTEADE 550 560 LMKRVGFQYE GTYKWVNPHK L
	Isoform 3 [UniParc]. Checksum: CFE3675547A5672F	FASTA	545	62,468
	10 20 30 40 50 60 MGRRGSAPGN GRTLRGCERG GRRRRSADSV MAEQVALSRT QVCGILREEL FQGDAFHQSD 70 80 90 100 110 120 THIFIIMGAS GDLAKKKIYP TIWWLFRDGL LPENTFIVGY ARSRLTVADI RKQSEPFFKA 130 140 150 160 170 180 TPEEKLKLED FFARNSYVAG QYDDAASYQR LNSHMNALHL GSQANRLFYL ALPPTVYEAV 190 200 210 220 230 240 TKNIHESCMS QIGWNRIIVE KPFGRDLQSS DRLSNHISSL FREDQIYRID HYLGKEMVQN 250 260 270 280 290 300 LMVLRFANRI FGPIWNRDNI ACVILTFKEP FGTEGRGGYF DEFGIIRDVM QNHLLQMLCL 310 320 330 340 350 360 VAMEKPASTN SDDVRDEKVK VLKCISEVQA NNVVLGQYVG NPDGEGEATK GYLDDPTVPR 370 380 390 400 410 420 GSTTATFAAV VLYVENERWD GVPFILRCGK ALNERKAEVR LQFHDVAGDI FHQQCKRNEL 430 440 450 460 470 480 VIRVQPNEAV YTKMMTKKPG MFFNPEESEL DLTYGNRYKN VKLPDAYERL ILDVFCGSQM 490 500 510 520 530 540 HFVRSDELRE AWRIFTPLLH QIELEKPKPI PYIYGSRGPT EADELMKRVG FQYEGTYKWV NPHKL

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, 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), MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"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, MASS SPECTROMETRY.
[22]	"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].
[23]	"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, HOMOTETRAMERIZATION.
[24]	"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.
[25]	"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.
[26]	"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.
[27]	"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.
[28]	"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.
[29]	"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 CNSHA CYS-387; LEU-394; ASP-410 AND PRO-439.
[30]	"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.
[31]	"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.
[32]	"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.
[33]	"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.
[34]	"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.
[35]	"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.
[36]	"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.
[37]	"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.
[38]	"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.
[39]	"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.
[40]	"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.
[41]	"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.
[42]	"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

GeneReviews

SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00216008.
IPI00289800.
IPI00853547.

PIR

DEHUG6. A40309.

RefSeq

NP_000393.4. NM_000402.3.
NP_001035810.1. NM_001042351.1.

UniGene

Hs.461047.
Hs.684904.

3D structure databases

PDBe
RCSB PDB
PDBj

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	28-514	[»]
2BHL	X-ray	2.90	A/B	28-515	[»]

ProteinModelPortal

P11413.

ModBase

Search...

Protein-protein interaction databases

IntAct

P11413. 1 interaction.

STRING

9606.ENSP00000377192.

PTM databases

PhosphoSite

P11413.

Polymorphism databases

DMDM

116242483.

2D gel databases

REPRODUCTION-2DPAGE

IPI00289800.

SWISS-2DPAGE

P11413.

Proteomic databases

PaxDb

P11413.

PRIDE

P11413.

Protocols and materials databases

DNASU

2539.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000291567; ENSP00000291567; ENSG00000160211.
ENST00000369620; ENSP00000358633; ENSG00000160211.
ENST00000393562; ENSP00000377192; ENSG00000160211.
ENST00000393564; ENSP00000377194; ENSG00000160211.
ENST00000593787; ENSP00000471208; ENSG00000269087.
ENST00000594771; ENSP00000470721; ENSG00000269087.
ENST00000595441; ENSP00000469988; ENSG00000269087.
ENST00000600069; ENSP00000470353; ENSG00000269087.

GeneID

2539.

KEGG

hsa:2539.

UCSC

uc004flx.1. human.
uc004fly.1. human.

Organism-specific databases

CTD

2539.

GeneCards

GC0XM153759.

HGNC

HGNC:4057. G6PD.

HPA

HPA000247.
HPA000834.

MIM

305900. gene+phenotype.

neXtProt

NX_P11413.

Orphanet

362. Glucose-6-phosphate-dehydrogenase deficiency.

PharmGKB

PA28469.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0364.

HOVERGEN

HBG000856.

KO

K00036.

OMA

KSPGITF.

OrthoDB

EOG4VHK69.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

SABIO-RK

P11413.

UniPathway

UPA00115; UER00408.

Gene expression databases

ArrayExpress

P11413.

Bgee

P11413.

CleanEx

HS_G6PD.

Genevestigator

P11413.

GermOnline

ENSG00000160211. Homo sapiens.

Family and domain databases

Gene3D

3.40.50.720. 1 hit.

InterPro

IPR001282. G6P_DH.
IPR019796. G6P_DH_AS.
IPR022675. G6P_DH_C.
IPR022674. G6P_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

PANTHER

PTHR23429. PTHR23429. 1 hit.

Pfam

PF02781. G6PD_C. 1 hit.
PF00479. G6PD_N. 1 hit.
[Graphical view]

PIRSF

PIRSF000110. G6PD. 1 hit.

PRINTS

PR00079. G6PDHDRGNASE.

TIGRFAMs

TIGR00871. zwf. 1 hit.

PROSITE

PS00069. G6P_DEHYDROGENASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P11413.

ChEMBL

CHEMBL5347.

ChiTaRS

G6PD. human.

EvolutionaryTrace

P11413.

GenomeRNAi

2539.

NextBio

10021.

SOURCE

Search...

Entry information

Entry name

G6PD_HUMAN

Accession

Primary (citable) accession number: P11413
Secondary accession number(s): D3DWX9 , Q16000, Q16765, Q8IU70, Q8IU88, Q8IUA6, Q96PQ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 182 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.