dbPTM

G6PD_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	G6PD_RAT
UniProt AC	P05370
Protein Name	Glucose-6-phosphate 1-dehydrogenase
Gene Name	G6pdx
Organism	Rattus norvegicus (Rat).
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	MAEQVALSRTQVCGILREELYQGDAFHQADTHIFIIMGASGDLAKKKIYPTIWWLFRDGLLPEDTFIVGYARSRLTVDDIRKQSEPFFKVTPEERPKLEEFFARNSYVAGQYDDPASYKHLNSHMNALHQGMQANRLFYLALPPTVYEAVTKNIQEICMSQTGWNRIIVEKPFGRDLQSSNQLSNHISSLFREDQIYRIDHYLGKEMVQNLMVLRFANRIFGPIWNRDNIACVILTFKEPFGTEGRGGYFDEFGIIRDVMQNHLLQMLCLVAMEKPASTDSDDVRDEKVKVLKCISEVETDNVVLGQYVGNPSGEGEATNGYLDDPTVPHGSTTATFAAAVLYVENERWDGVPFILRCGKALNERKAEVRLQFRDVAGDIFHQQCKRNELVIRVQPNEAVYTKMMTKKPGMFFNPEESELDLTYGNRYKNVKLPDAYERLILDVFCGSQMHFVRSDELREAWRIFTPLLHKIDREKPQPIPYVYGSRGPTEADELMKRVGFQYEGTYKWVNPHKL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAEQVALSR ------CHHHHHHHH	18.87	2606104
8	Phosphorylation	MAEQVALSRTQVCGI CHHHHHHHHHHHHHH	24.44	30181290
10	Phosphorylation	EQVALSRTQVCGILR HHHHHHHHHHHHHHH	23.21	-
89	Acetylation	KQSEPFFKVTPEERP HHCCCCCCCCHHHCH	45.65	-
91	Phosphorylation	SEPFFKVTPEERPKL CCCCCCCCHHHCHHH	26.10	25403869
119	Acetylation	YDDPASYKHLNSHMN CCCHHHHHHHHHHHH	38.84	22902405
171	Acetylation	WNRIIVEKPFGRDLQ CCEEEEECCCCCCCH	34.45	22902405
401	Phosphorylation	VQPNEAVYTKMMTKK ECCCHHHHHHCCCCC	14.00	22108457
403	Acetylation	PNEAVYTKMMTKKPG CCHHHHHHCCCCCCC	14.69	22902405
408	Acetylation	YTKMMTKKPGMFFNP HHHCCCCCCCCCCCH	37.32	22902405
432	Acetylation	GNRYKNVKLPDAYER CCCCCCCCCCHHHHH	64.79	22902405
497	Acetylation	TEADELMKRVGFQYE CHHHHHHHHHCCCEE	57.46	22902405
503	Phosphorylation	MKRVGFQYEGTYKWV HHHHCCCEECCEEEC	17.67	30181290
506	Phosphorylation	VGFQYEGTYKWVNPH HCCCEECCEEECCCC	15.24	30181290
507	Phosphorylation	GFQYEGTYKWVNPHK CCCEECCEEECCCCC	17.45	-

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 G6PD_RAT !!

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 G6PD_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of G6PD_RAT !!

Drug and Disease Associations

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

Regulatory Network of G6PD_RAT

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Glucose-6-phosphate dehydrogenase. Characteristics revealed by therat liver enzyme structure."; Jeffery J., Barros-Soederling J., Murray L., Wood I., Hansen R.,Szepesi B., Joernvall H.; Eur. J. Biochem. 186:551-556(1989). Cited for: PROTEIN SEQUENCE OF 2-514.	2606104 [Abstract]