dbPTM

G6PD1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	G6PD1_MOUSE
UniProt AC	Q00612
Protein Name	Glucose-6-phosphate 1-dehydrogenase X
Gene Name	G6pdx
Organism	Mus musculus (Mouse).
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 (By similarity)..
Protein Sequence	MAEQVALSRTQVCGILREELYQGDAFHQADTHIFIIMGASGDLAKKKIYPTIWWLFRDGLLPEDTFIVGYARSRLTVDDIRKQSEPFFKATPEERPKLEEFFARNSYVAGQYDDAASYKHLNSHMNALHQGMQANRLFYLALPPTVYEAVTKNIQETCMSQTGWNRIIVEKPFGRDLQSSNQLSNHISSLFREDQIYRIDHYLGKEMVQNLMVLRFANRIFGPIWNRDNIACVILTFKEPFGTEGRGGYFDEFGIIRDVMQNHLLQMLCLVAMEKPATTGSDDVRDEKVKVLKCISEVETDNVVLGQYVGNPNGEGEAANGYLDDPTVPHGSTTATFAAAVLYVENERWDGVPFILRCGKALNERKAEVRLQFRDVAGDIFHQQCKRNELVIRVQPNEAVYTKMMTKKPGMFFNPEESELDLTYGNRYKNVKLPDAYERLILDVFCGSQMHFVRSDELREAWRIFTPLLHKIDREKPQPIPYVYGSRGPTEADELMKRVGFQYEGTYKWVNPHKL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAEQVALSR ------CHHHHHHHH	18.87	-
8	Phosphorylation	MAEQVALSRTQVCGI CHHHHHHHHHHHHHH	24.44	28066266
10	Phosphorylation	EQVALSRTQVCGILR HHHHHHHHHHHHHHH	23.21	28066266
13	Glutathionylation	ALSRTQVCGILREEL HHHHHHHHHHHHHHH	1.70	24333276
89	Acetylation	KQSEPFFKATPEERP HHCCCHHHCCHHHCH	52.29	-
91	Phosphorylation	SEPFFKATPEERPKL CCCHHHCCHHHCHHH	31.65	-
112	Phosphorylation	NSYVAGQYDDAASYK CCCCCCCCCCHHHHH	18.18	22817900
117	Phosphorylation	GQYDDAASYKHLNSH CCCCCHHHHHHHHHH	36.11	30635358
158	S-palmitoylation	TKNIQETCMSQTGWN HHHHHHHHHHCCCCC	2.13	28680068
171	Acetylation	WNRIIVEKPFGRDLQ CCEEEEECCCCCCCH	34.45	23806337
202	Phosphorylation	QIYRIDHYLGKEMVQ HHHHHHHHCCHHHHH	17.25	22817900
385	Glutathionylation	GDIFHQQCKRNELVI HHHHHHHHCCCCEEE	3.44	24333276
401	Phosphorylation	VQPNEAVYTKMMTKK ECCCHHHHHHCCCCC	14.00	28418008
402	Phosphorylation	QPNEAVYTKMMTKKP CCCHHHHHHCCCCCC	13.08	22499769
403	Acetylation	PNEAVYTKMMTKKPG CCHHHHHHCCCCCCC	14.69	-
418	Phosphorylation	MFFNPEESELDLTYG CCCCHHHCCCCCCCC	41.62	26525534
423	Phosphorylation	EESELDLTYGNRYKN HHCCCCCCCCCCCCC	29.11	25367039
424	Phosphorylation	ESELDLTYGNRYKNV HCCCCCCCCCCCCCC	21.50	22817900
428	Phosphorylation	DLTYGNRYKNVKLPD CCCCCCCCCCCCCCH	15.77	25367039
432	Acetylation	GNRYKNVKLPDAYER CCCCCCCCCCHHHHH	64.79	-
446	Glutathionylation	RLILDVFCGSQMHFV HHHHHHHCCCCCCCC	5.28	24333276
497	Acetylation	TEADELMKRVGFQYE CHHHHHHHHHCCCEE	57.46	22826441
503	Phosphorylation	MKRVGFQYEGTYKWV HHHHCCCEECCEEEC	17.67	18034455
506	Phosphorylation	VGFQYEGTYKWVNPH HCCCEECCEEECCCC	15.24	28066266
507	Phosphorylation	GFQYEGTYKWVNPHK CCCEECCEEECCCCC	17.45	20116462

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
Oops, there are no upstream regulatory protein records of G6PD1_MOUSE !!

Functions of PTM Sites

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

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 G6PD1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of G6PD1_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of G6PD1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-401; TYR-503 ANDTYR-507, AND MASS SPECTROMETRY.	18034455 [Abstract]
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling."; Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.; J. Immunol. 179:5864-5876(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-507, AND MASSSPECTROMETRY.	17947660 [Abstract]

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