CPLM-003921

Genbank Nucleotide ID

Glucose-6-phosphate 1-dehydrogenase

Protein Synonyms/Alias

Homo sapiens (Human)

Position	Peptide	Type	References
89	KQSEPFFKATPEEKL	acetylation	[1]
89	KQSEPFFKATPEEKL	ubiquitination	[2]
97	ATPEEKLKLEDFFAR	ubiquitination	[2, 3, 4]
171	WNRIIVEKPFGRDLQ	acetylation	[1]
171	WNRIIVEKPFGRDLQ	ubiquitination	[2, 3, 4]
205	RIDHYLGKEMVQNLM	glycation	[5]
238	ACVILTFKEPFGTEG	ubiquitination	[4]
320	DGEGEATKGYLDDPT	ubiquitination	[4]
386	DIFHQQCKRNELVIR	acetylation	[1]
386	DIFHQQCKRNELVIR	ubiquitination	[6, 7, 8]
403	PNEAVYTKMMTKKPG	acetylation	[1, 9]
403	PNEAVYTKMMTKKPG	ubiquitination	[2, 7, 8, 10]
407	VYTKMMTKKPGMFFN	ubiquitination	[7]
408	YTKMMTKKPGMFFNP	ubiquitination	[2, 7]
432	GNRYKNVKLPDAYER	acetylation	[1, 8, 9, 11]
432	GNRYKNVKLPDAYER	ubiquitination	[7]
476	LHQIELEKPKPIPYI	ubiquitination	[7]
478	QIELEKPKPIPYIYG	ubiquitination	[7]
497	TEADELMKRVGFQYE	acetylation	[1, 8, 9, 11]
497	TEADELMKRVGFQYE	ubiquitination	[2, 7, 8]
514	YKWVNPHKL******	acetylation	[1]
514	YKWVNPHKL******	ubiquitination	[7]

[1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
[2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[4] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
[5] Enhanced reactivity of Lys182 explains the limited efficacy of biogenic amines in preventing the inactivation of glucose-6-phosphate dehydrogenase by methylglyoxal.
Flores-Morales P, Diema C, Vilaseca M, Estelrich J, Luque FJ, Gutiérrez-Oliva S, Toro-Labbé A, Silva E.
Bioorg Med Chem. 2011 Mar 1;19(5):1613-22. [PMID: 21333543]
[6] Global identification of modular cullin-RING ligase substrates.
Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
[7] 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]
[8] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
[9] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
[10] 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]
[11] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
PLoS One. 2012;7(12):e50545. [PMID: 23236377]

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.

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.

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.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

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.

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

PF02781; G6PD_C
PF00479; G6PD_N

PS00069; G6P_DEHYDROGENASE

PR00079; G6PDHDRGNASE.