UniProt Accession

 G6PD_HUMAN; P11413; D3DWX9; Q16000; Q16765; Q8IU70; Q8IU88; Q8IUA6; Q96PQ2 

Genbank Protein ID

 X03674; M65234; M26749; M26750; M65225; M65226; M65227; M65228; M65229; M65230; M65231; M65233; M65232; M21248; M19866; X55448; L44140; AF277315; CH471172; CH471172; BC000337; M27940; S58359; X53815; S64462; AY158096; AY158097; AY158098; AY158099; AY158100; AY158101; AY158102; AY158103; AY158104; AY158105; AY158106; AY158107; AY158108; AY158109; AY158110; AY158111; AY158112; AY158113; AY158114; AY158115; AY158116; AY158117; AY158118; AY158119; AY158120; AY158121; AY158122; AY158123; AY158124; AY158125; AY158126; AY158127; AY158128; AY158129; AY158130; AY158131; AY158132; AY158133; AY158134; AY158135; AY158136; AY158137; AY158138; AY158139; AY158140; AY158141; AY158142; M12996; M23423 

Genbank Nucleotide ID

 CAA27309.1; AAA63175.1; AAA63175.1; AAA63175.1; AAA63175.1; AAA63175.1; AAA63175.1; AAA63175.1; AAA63175.1; AAA63175.1; AAA63175.1; AAA63175.1; AAA63175.1; AAA52500.1; AAA52501.1; CAA39089.1; AAA92653.1; AAL27011.1; EAW72682.1; EAW72686.1; AAH00337.1; AAA52504.1; AAB26169.1; CAA37811.1; AAB20299.1; AAN76367.1; AAN76368.1; AAN76369.1; AAN76370.1; AAN76371.1; AAN76372.1; AAN76373.1; AAN76374.1; AAN76375.1; AAN76376.1; AAN76377.1; AAN76378.1; AAN76379.1; AAN76380.1; AAN76381.1; AAN76382.1; AAN76383.1; AAN76384.1; AAN76385.1; AAN76386.1; AAN76387.1; AAN76388.1; AAN76389.1; AAN76390.1; AAN76391.1; AAN76392.1; AAN76393.1; AAN76394.1; AAN76395.1; AAN76396.1; AAN76397.1; AAN76398.1; AAN76399.1; AAN76400.1; AAN76401.1; AAN76402.1; AAN76403.1; AAN76404.1; AAN76405.1; AAN76406.1; AAN76407.1; AAN76408.1; AAN76409.1; AAN76410.1; AAN76411.1; AAN76412.1; AAN76413.1; AAA52499.1; AAB59390.1 

Protein Name

 Glucose-6-phosphate 1-dehydrogenase 

Protein Synonyms/Alias

 G6PD 

Gene Name

 G6PD 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
82	LTVADIRKQSEPFFK	ubiquitination	[1]
89	KQSEPFFKATPEEKL	ubiquitination	[1]
95	FKATPEEKLKLEDFF	ubiquitination	[1]
97	ATPEEKLKLEDFFAR	ubiquitination	[1, 2, 3]
171	WNRIIVEKPFGRDLQ	ubiquitination	[1, 2, 3]
205	RIDHYLGKEMVQNLM	ubiquitination	[1]
339	DEKVKVLKCISEVQA	ubiquitination	[1]
432	DIFHQQCKRNELVIR	ubiquitination	[1, 2]
449	PNEAVYTKMMTKKPG	ubiquitination	[1, 4]
453	VYTKMMTKKPGMFFN	ubiquitination	[1]
454	YTKMMTKKPGMFFNP	ubiquitination	[1]
478	GNRYKNVKLPDAYER	ubiquitination	[1]
522	LHQIELEKPKPIPYI	ubiquitination	[1]
524	QIELEKPKPIPYIYG	ubiquitination	[1]
543	TEADELMKRVGFQYE	ubiquitination	[1]
560	YKWVNPHKL******	ubiquitination	[1]

Reference

 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 

Functional Description

 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. 

Sequence Annotation

 NP_BIND 38 45 NADP 1.
 NP_BIND 401 403 NADP 2.
 NP_BIND 421 423 NADP 2.
 REGION 201 205 Substrate binding.
 ACT_SITE 263 263 Proton acceptor (By similarity).
 BINDING 72 72 NADP 1.
 BINDING 147 147 NADP 1.
 BINDING 171 171 NADP 1; via carbonyl oxygen.
 BINDING 171 171 Substrate.
 BINDING 239 239 Substrate.
 BINDING 258 258 Substrate.
 BINDING 357 357 NADP 2.
 BINDING 360 360 Substrate.
 BINDING 365 365 Substrate.
 BINDING 366 366 NADP 2.
 BINDING 370 370 NADP 2.
 BINDING 393 393 NADP 2.
 BINDING 395 395 Substrate.
 BINDING 487 487 NADP 2.
 BINDING 503 503 NADP 2.
 BINDING 509 509 NADP 2.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 89 89 N6-acetyllysine.
 MOD_RES 171 171 N6-acetyllysine.
 MOD_RES 403 403 N6-acetyllysine.
 MOD_RES 432 432 N6-acetyllysine.
 MOD_RES 497 497 N6-acetyllysine.  

Keyword

 3D-structure; Acetylation; Alternative splicing; Carbohydrate metabolism; Complete proteome; Direct protein sequencing; Disease mutation; Glucose metabolism; Hereditary hemolytic anemia; NADP; Oxidoreductase; Phosphoprotein; Polymorphism; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 515 AA 

Protein Sequence

Gene Ontology

 GO:0005813; C:centrosome; IDA:HPA.
 GO:0005829; C:cytosol; IDA:BHF-UCL.
 GO:0009898; C:internal side of plasma membrane; IDA:BHF-UCL.
 GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0005536; F:glucose binding; IDA:BHF-UCL.
 GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IDA:UniProtKB.
 GO:0050661; F:NADP binding; IDA:BHF-UCL.
 GO:0034599; P:cellular response to oxidative stress; IMP:BHF-UCL.
 GO:0006695; P:cholesterol biosynthetic process; IMP:BHF-UCL.
 GO:0001816; P:cytokine production; IMP:BHF-UCL.
 GO:0043249; P:erythrocyte maturation; IMP:BHF-UCL.
 GO:0051156; P:glucose 6-phosphate metabolic process; IDA:UniProtKB.
 GO:0006749; P:glutathione metabolic process; IMP:BHF-UCL.
 GO:0010734; P:negative regulation of protein glutathionylation; IMP:BHF-UCL.
 GO:0019322; P:pentose biosynthetic process; IDA:BHF-UCL.
 GO:0009051; P:pentose-phosphate shunt, oxidative branch; IMP:BHF-UCL.
 GO:0045471; P:response to ethanol; IEA:Compara.
 GO:0032094; P:response to food; IEA:Compara.
 GO:0014070; P:response to organic cyclic compound; IEA:Compara.
 GO:0046390; P:ribose phosphate biosynthetic process; IMP:BHF-UCL. 

Interpro

 IPR001282; G6P_DH.
 IPR019796; G6P_DH_AS.
 IPR022675; G6P_DH_C.
 IPR022674; G6P_DH_NAD-bd.
 IPR016040; NAD(P)-bd_dom. 

Pfam

 PF02781; G6PD_C
 PF00479; G6PD_N 

SMART

  

PROSITE

 PS00069; G6P_DEHYDROGENASE 

PRINTS

 PR00079; G6PDHDRGNASE.