dbPTM

G6PD_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	G6PD_HUMAN
UniProt AC	P11413
Protein Name	Glucose-6-phosphate 1-dehydrogenase
Gene Name	G6PD
Organism	Homo sapiens (Human).
Sequence Length	515
Subcellular Localization
Protein 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..
Protein Sequence	MAEQVALSRTQVCGILREELFQGDAFHQSDTHIFIIMGASGDLAKKKIYPTIWWLFRDGLLPENTFIVGYARSRLTVADIRKQSEPFFKATPEEKLKLEDFFARNSYVAGQYDDAASYQRLNSHMNALHLGSQANRLFYLALPPTVYEAVTKNIHESCMSQIGWNRIIVEKPFGRDLQSSDRLSNHISSLFREDQIYRIDHYLGKEMVQNLMVLRFANRIFGPIWNRDNIACVILTFKEPFGTEGRGGYFDEFGIIRDVMQNHLLQMLCLVAMEKPASTNSDDVRDEKVKVLKCISEVQANNVVLGQYVGNPDGEGEATKGYLDDPTVPRGSTTATFAAVVLYVENERWDGVPFILRCGKALNERKAEVRLQFHDVAGDIFHQQCKRNELVIRVQPNEAVYTKMMTKKPGMFFNPEESELDLTYGNRYKNVKLPDAYERLILDVFCGSQMHFVRSDELREAWRIFTPLLHQIELEKPKPIPYIYGSRGPTEADELMKRVGFQYEGTYKWVNPHKL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAEQVALSR ------CHHHHHHHH	18.87	19413330
6	Phosphorylation	--MAEQVALSRTQVC --CHHHHHHHHHHHH	10.26	24719451
6 (in isoform 3)	Phosphorylation	-	10.26	24719451
8	Phosphorylation	MAEQVALSRTQVCGI CHHHHHHHHHHHHHH	24.44	29255136
9	Methylation	AEQVALSRTQVCGIL HHHHHHHHHHHHHHH	29.99	-
10	Phosphorylation	EQVALSRTQVCGILR HHHHHHHHHHHHHHH	23.21	25159151
26	Phosphorylation	ELFQGDAFHQSDTHI HHHCCCCCCCCCCEE	6.83	24719451
26 (in isoform 3)	Phosphorylation	-	6.83	23927012
29 (in isoform 3)	Phosphorylation	-	35.59	23927012
40	Phosphorylation	IFIIMGASGDLAKKK EEEEEECCCHHHHCC	27.40	-
40 (in isoform 3)	Phosphorylation	-	27.40	20068231
76	Phosphorylation	GYARSRLTVADIRKQ EEECCCEEHHHHHHH	16.73	21406692
82	Malonylation	LTVADIRKQSEPFFK EEHHHHHHHCCCHHH	59.52	26320211
82	Ubiquitination	LTVADIRKQSEPFFK EEHHHHHHHCCCHHH	59.52	-
82 (in isoform 2)	Ubiquitination	-	59.52	-
84	O-linked_Glycosylation	VADIRKQSEPFFKAT HHHHHHHCCCHHHCC	50.72	23301498
84	Phosphorylation	VADIRKQSEPFFKAT HHHHHHHCCCHHHCC	50.72	28450419
89	Acetylation	KQSEPFFKATPEEKL HHCCCHHHCCHHHHH	52.29	19608861
89	Malonylation	KQSEPFFKATPEEKL HHCCCHHHCCHHHHH	52.29	26320211
89	Ubiquitination	KQSEPFFKATPEEKL HHCCCHHHCCHHHHH	52.29	19608861
89 (in isoform 1)	Ubiquitination	-	52.29	21890473
89 (in isoform 2)	Ubiquitination	-	52.29	21890473
95	Acetylation	FKATPEEKLKLEDFF HHCCHHHHHCHHHHH	49.62	23749302
95	Ubiquitination	FKATPEEKLKLEDFF HHCCHHHHHCHHHHH	49.62	-
95 (in isoform 2)	Ubiquitination	-	49.62	-
97	Acetylation	ATPEEKLKLEDFFAR CCHHHHHCHHHHHHC	61.98	23749302
97	Ubiquitination	ATPEEKLKLEDFFAR CCHHHHHCHHHHHHC	61.98	21890473
97 (in isoform 1)	Ubiquitination	-	61.98	21890473
97 (in isoform 2)	Ubiquitination	-	61.98	21890473
106	Phosphorylation	EDFFARNSYVAGQYD HHHHHCCCCCCCCCC	18.54	28152594
107	Phosphorylation	DFFARNSYVAGQYDD HHHHCCCCCCCCCCC	9.62	28152594
112	Phosphorylation	NSYVAGQYDDAASYQ CCCCCCCCCCHHHHH	18.18	27273156
112 (in isoform 2)	Phosphorylation	-	18.18	25147952
117	Phosphorylation	GQYDDAASYQRLNSH CCCCCHHHHHHHHHH	24.42	28152594
118	Phosphorylation	QYDDAASYQRLNSHM CCCCHHHHHHHHHHH	7.91	28152594
119	Acetylation	YDDAASYQRLNSHMN CCCHHHHHHHHHHHC	40.67	19608861
119	Ubiquitination	YDDAASYQRLNSHMN CCCHHHHHHHHHHHC	40.67	19608861
123	Phosphorylation	ASYQRLNSHMNALHL HHHHHHHHHHCHHHH	28.80	20068231
127 (in isoform 3)	Ubiquitination	-	6.70	21890473
132	Phosphorylation	MNALHLGSQANRLFY HCHHHHCCCCCHHHH	32.26	20068231
139	Phosphorylation	SQANRLFYLALPPTV CCCCHHHHHHCCHHH	8.82	-
142	Phosphorylation	NRLFYLALPPTVYEA CHHHHHHCCHHHHHH	4.88	-
147	Phosphorylation	LALPPTVYEAVTKNI HHCCHHHHHHHHHHH	10.72	-
153	Phosphorylation	VYEAVTKNIHESCMS HHHHHHHHHHHHHHH	31.33	-
157	Phosphorylation	VTKNIHESCMSQIGW HHHHHHHHHHHHHCC	10.85	20873877
160	Phosphorylation	NIHESCMSQIGWNRI HHHHHHHHHHCCCEE	23.99	20873877
171	Acetylation	WNRIIVEKPFGRDLQ CCEEEEECCCCCCCC	34.45	19608861
171	Ubiquitination	WNRIIVEKPFGRDLQ CCEEEEECCCCCCCC	34.45	21890473
171 (in isoform 1)	Ubiquitination	-	34.45	21890473
171 (in isoform 2)	Ubiquitination	-	34.45	21890473
179	Phosphorylation	PFGRDLQSSDRLSNH CCCCCCCCHHHHHHH	41.31	23186163
180	Phosphorylation	FGRDLQSSDRLSNHI CCCCCCCHHHHHHHH	17.49	20873877
182	Methylation	RDLQSSDRLSNHISS CCCCCHHHHHHHHHH	41.80	-
184	Phosphorylation	LQSSDRLSNHISSLF CCCHHHHHHHHHHHH	27.53	23186163
188	Phosphorylation	DRLSNHISSLFREDQ HHHHHHHHHHHHHHC	17.28	23186163
189	Phosphorylation	RLSNHISSLFREDQI HHHHHHHHHHHHHCH	30.81	24719451
201	Acetylation	DQIYRIDHYLGKEMV HCHHHHHHHCCHHHH	19.83	19608861
201	Ubiquitination	DQIYRIDHYLGKEMV HCHHHHHHHCCHHHH	19.83	19608861
201 (in isoform 3)	Ubiquitination	-	19.83	21890473
202	Phosphorylation	QIYRIDHYLGKEMVQ CHHHHHHHCCHHHHH	17.25	28152594
202 (in isoform 2)	Phosphorylation	-	17.25	25147952
205	Glycation	RIDHYLGKEMVQNLM HHHHHCCHHHHHHHH	39.79	-
205	Ubiquitination	RIDHYLGKEMVQNLM HHHHHCCHHHHHHHH	39.79	-
205 (in isoform 2)	Ubiquitination	-	39.79	-
207	Sulfoxidation	DHYLGKEMVQNLMVL HHHCCHHHHHHHHHH	4.24	21406390
210	Phosphorylation	LGKEMVQNLMVLRFA CCHHHHHHHHHHHHH	20.77	-
232	S-palmitoylation	WNRDNIACVILTFKE CCCCCEEEEEEEECC	1.41	29575903
236	Phosphorylation	NIACVILTFKEPFGT CEEEEEEEECCCCCC	22.87	20068231
238	Ubiquitination	ACVILTFKEPFGTEG EEEEEEECCCCCCCC	60.28	-
249	Phosphorylation	GTEGRGGYFDEFGII CCCCCCCCCCCCCHH	15.64	28152594
249 (in isoform 2)	Phosphorylation	-	15.64	27642862
266	Phosphorylation	VMQNHLLQMLCLVAM HHHHHHHHHHHHHHH	29.21	-
293	Ubiquitination	DEKVKVLKCISEVQA HHHHHHHHHHHHHHC	32.29	-
296	Phosphorylation	VKVLKCISEVQANNV HHHHHHHHHHHCCCE	40.98	-
299 (in isoform 2)	Phosphorylation	-	34.03	22210691
300 (in isoform 2)	Phosphorylation	-	18.10	22210691
320	Ubiquitination	DGEGEATKGYLDDPT CCCCCCCCCCCCCCC	53.24	-
322	Phosphorylation	EGEATKGYLDDPTVP CCCCCCCCCCCCCCC	14.44	-
339 (in isoform 2)	Ubiquitination	-	6.43	-
386	Acetylation	DIFHQQCKRNELVIR HHHHHHCCCCCEEEE	54.65	19608861
386	Succinylation	DIFHQQCKRNELVIR HHHHHHCCCCCEEEE	54.65	23954790
386	Ubiquitination	DIFHQQCKRNELVIR HHHHHHCCCCCEEEE	54.65	19608861
401	Nitration	VQPNEAVYTKMMTKK ECCCHHHHHCCCCCC	14.00	-
401	Phosphorylation	VQPNEAVYTKMMTKK ECCCHHHHHCCCCCC	14.00	27273156
402	Phosphorylation	QPNEAVYTKMMTKKP CCCHHHHHCCCCCCC	13.08	25159151
403	Acetylation	PNEAVYTKMMTKKPG CCHHHHHCCCCCCCC	14.69	24769394
403	Ubiquitination	PNEAVYTKMMTKKPG CCHHHHHCCCCCCCC	14.69	19608861
403 (in isoform 1)	Ubiquitination	-	14.69	21890473
407	Ubiquitination	VYTKMMTKKPGMFFN HHHCCCCCCCCCCCC	38.79	-
408	Acetylation	YTKMMTKKPGMFFNP HHCCCCCCCCCCCCH	37.32	23954790
408	Ubiquitination	YTKMMTKKPGMFFNP HHCCCCCCCCCCCCH	37.32	21906983
408 (in isoform 1)	Ubiquitination	-	37.32	21890473
411	Sulfoxidation	MMTKKPGMFFNPEES CCCCCCCCCCCHHHC	4.74	30846556
416	Acetylation	PGMFFNPEESELDLT CCCCCCHHHCCCCCC	75.22	19608861
416	Ubiquitination	PGMFFNPEESELDLT CCCCCCHHHCCCCCC	75.22	19608861
418	Phosphorylation	MFFNPEESELDLTYG CCCCHHHCCCCCCCC	41.62	-
423	Phosphorylation	EESELDLTYGNRYKN HHCCCCCCCCCCCCC	29.11	26356563
424	Phosphorylation	ESELDLTYGNRYKNV HCCCCCCCCCCCCCC	21.50	26356563
428	Phosphorylation	DLTYGNRYKNVKLPD CCCCCCCCCCCCCCH	15.77	26356563
429	Acetylation	LTYGNRYKNVKLPDA CCCCCCCCCCCCCHH	52.61	25953088
431	Phosphorylation	YGNRYKNVKLPDAYE CCCCCCCCCCCHHHH	6.19	24719451
432	Acetylation	GNRYKNVKLPDAYER CCCCCCCCCCHHHHH	64.79	19608861
432	Malonylation	GNRYKNVKLPDAYER CCCCCCCCCCHHHHH	64.79	26320211
432	Ubiquitination	GNRYKNVKLPDAYER CCCCCCCCCCHHHHH	64.79	19608861
432 (in isoform 2)	Ubiquitination	-	64.79	-
433	Acetylation	NRYKNVKLPDAYERL CCCCCCCCCHHHHHH	3.95	19608861
433	Ubiquitination	NRYKNVKLPDAYERL CCCCCCCCCHHHHHH	3.95	19608861
447 (in isoform 2)	Phosphorylation	-	14.95	25147952
448	Phosphorylation	ILDVFCGSQMHFVRS HHHHHCCCCCCCCCC	26.05	-
449 (in isoform 2)	Ubiquitination	-	18.04	21890473
453 (in isoform 2)	Ubiquitination	-	3.30	-
454	Phosphorylation	GSQMHFVRSDELREA CCCCCCCCCHHHHHH	37.13	-
454 (in isoform 2)	Ubiquitination	-	37.13	21890473
462	Acetylation	SDELREAWRIFTPLL CHHHHHHHHHHHHHH	6.80	19608861
470 (in isoform 2)	Phosphorylation	-	33.97	27642862
476	Acetylation	LHQIELEKPKPIPYI HHHHHCCCCCCCCEE	71.60	25953088
476	Ubiquitination	LHQIELEKPKPIPYI HHHHHCCCCCCCCEE	71.60	-
478	Ubiquitination	QIELEKPKPIPYIYG HHHCCCCCCCCEECC	67.65	-
478 (in isoform 2)	Ubiquitination	-	67.65	-
490	Phosphorylation	IYGSRGPTEADELMK ECCCCCCCHHHHHHH	46.78	-
496	Sulfoxidation	PTEADELMKRVGFQY CCHHHHHHHHHCCCE	2.15	30846556
497	Acetylation	TEADELMKRVGFQYE CHHHHHHHHHCCCEE	57.46	19608861
497	Malonylation	TEADELMKRVGFQYE CHHHHHHHHHCCCEE	57.46	33225896
497	Ubiquitination	TEADELMKRVGFQYE CHHHHHHHHHCCCEE	57.46	2190698
497 (in isoform 1)	Ubiquitination	-	57.46	21890473
503	Phosphorylation	MKRVGFQYEGTYKWV HHHHCCCEECCEEEC	17.67	12524354
506	Phosphorylation	VGFQYEGTYKWVNPH HCCCEECCEEECCCC	15.24	21945579
507	Phosphorylation	GFQYEGTYKWVNPHK CCCEECCEEECCCCC	17.45	21945579
514	Acetylation	YKWVNPHKL------ EEECCCCCC------	58.09	19608861
514	Ubiquitination	YKWVNPHKL------ EEECCCCCC------	58.09	19608861
522 (in isoform 2)	Ubiquitination	-		-
524 (in isoform 2)	Ubiquitination	-		-
527	Acetylation	------------------- -------------------		19608861
527	Ubiquitination	------------------- -------------------		19608861
533	Phosphorylation	------------------------- -------------------------		27251275
537	Phosphorylation	----------------------------- -----------------------------		27251275
543 (in isoform 2)	Ubiquitination	-		21890473
544	Acetylation	------------------------------------ ------------------------------------		19608861
549 (in isoform 2)	Phosphorylation	-		27642862
553 (in isoform 2)	Phosphorylation	-		27642862
560 (in isoform 2)	Ubiquitination	-		-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
210	S	Phosphorylation	Kinase	PRKCD	Q05655	GPS
266	T	Phosphorylation	Kinase	PRKCD	Q05655	GPS
428	Y	Phosphorylation	Kinase	SRC	P12931	PSP
507	Y	Phosphorylation	Kinase	SRC	P12931	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
403	K	Acetylation	19608861
Acetylated by ELP3 at Lys-403; acetylation inhibits its homodimerization and enzyme activity.
403	K	Acetylation	19608861
Deacetylated by SIRT2 at Lys-403; deacetylation stimulates its enzyme activity.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of G6PD_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
G6PD_HUMAN	G6PD	physical	10745013
HSPB1_HUMAN	HSPB1	physical	21157431
SYHC_HUMAN	HARS	physical	22939629
TCPD_HUMAN	CCT4	physical	22939629
AL7A1_HUMAN	ALDH7A1	physical	22863883
CAN1_HUMAN	CAPN1	physical	22863883
IF4H_HUMAN	EIF4H	physical	22863883
IF5_HUMAN	EIF5	physical	22863883
ERP44_HUMAN	ERP44	physical	22863883
GBP2_HUMAN	GBP2	physical	22863883
AGAL_HUMAN	GLA	physical	22863883
ISOC1_HUMAN	ISOC1	physical	22863883
MAT2B_HUMAN	MAT2B	physical	22863883
6PGD_HUMAN	PGD	physical	22863883
IPP2_HUMAN	PPP1R2	physical	22863883
1433S_HUMAN	SFN	physical	22863883
UBFD1_HUMAN	UBFD1	physical	22863883
VINC_HUMAN	VCL	physical	22863883
1433B_HUMAN	YWHAB	physical	22863883
1433E_HUMAN	YWHAE	physical	22863883
1433G_HUMAN	YWHAG	physical	22863883
1433F_HUMAN	YWHAH	physical	22863883
1433T_HUMAN	YWHAQ	physical	22863883
1433Z_HUMAN	YWHAZ	physical	22863883
ANCHR_HUMAN	ZFYVE19	physical	22863883
ZN622_HUMAN	ZNF622	physical	22863883
G6PD_HUMAN	G6PD	physical	25416956
ARFP1_HUMAN	ARFIP1	physical	26344197
ARMT1_HUMAN	C6orf211	physical	26344197
CDD_HUMAN	CDA	physical	26344197
DUT_HUMAN	DUT	physical	26344197
FPPS_HUMAN	FDPS	physical	26344197
SYHC_HUMAN	HARS	physical	26344197
GRP75_HUMAN	HSPA9	physical	26344197
HSPB1_HUMAN	HSPB1	physical	26344197
IDHP_HUMAN	IDH2	physical	26344197
MYO6_HUMAN	MYO6	physical	26344197
PDXK_HUMAN	PDXK	physical	26344197
PGAM1_HUMAN	PGAM1	physical	26344197
RPE_HUMAN	RPE	physical	26344197
TNG2_HUMAN	TANGO2	physical	26344197
UFM1_HUMAN	UFM1	physical	26344197
UN13D_HUMAN	UNC13D	physical	26344197
XPO1_HUMAN	XPO1	physical	26344197

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
300908	Anemia, non-spherocytic hemolytic, due to G6PD deficiency (NSHA)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of G6PD_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Glucose 6-phosphate dehydrogenase from human erythrocytes:identification of N-acetyl-alanine at the N-terminus of the matureprotein."; Camardella L., Damonte G., Carratore V., Benatti U., Tonetti M.,Moneti G.; Biochem. Biophys. Res. Commun. 207:331-338(1995). Cited for: ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.	7857286 [Abstract]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-89; LYS-171; LYS-386;LYS-403; LYS-432; LYS-497 AND LYS-514, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-503, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-401; TYR-503 ANDTYR-507, AND MASS SPECTROMETRY.	18083107 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-401, AND MASSSPECTROMETRY.	15592455 [Abstract]
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules."; Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.; Mol. Cell. Proteomics 4:1240-1250(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-507, AND MASSSPECTROMETRY.	15951569 [Abstract]

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