IDHG1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: IDHG1_MOUSE
• UniProt AC: P70404
• Protein Name: Isocitrate dehydrogenase [NAD] subunit gamma 1, mitochondrial
• Gene Name: Idh3g
• Organism: Mus musculus (Mouse).
• Sequence Length: 393
• Subcellular Localization: Mitochondrion.
• Protein Description: Regulatory subunit which plays a role in the allosteric regulation of the enzyme catalyzing the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal activity but the full activity of the heterotetramer (containing two subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly and cooperative function of both heterodimers..
• Protein Sequence: MALKVAIAAGGAAKAMLKPTLLCRPWEVLAAHVAPRRSISSQQTIPPSAKYGGRHTVTMIPGDGIGPELMLHVKSVFRHACVPVDFEEVHVSSNADEEDIRNAIMAIRRNRVALKGNIETNHNLPPSHKSRNNILRTSLDLYANVIHCKSLPGVVTRHKDIDILIVRENTEGEYSSLEHESVAGVVESLKIITKAKSLRIAEYAFKLAQESGRKKVTAVHKANIMKLGDGLFLQCCREVAAHYPQITFDSMIVDNTTMQLVSRPQQFDVMVMPNLYGNIVNNVCAGLVGGPGLVAGANYGHVYAVFETATRNTGKSIANKNIANPTATLLASCMMLDHLKLHSYATSIRKAVLASMDNENMHTPDIGGQGTTSQAIQDIIRHIRIINGRAVEA

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
81	S-nitrosocysteine	KSVFRHACVPVDFEE HHHHHHCCCCCCHHE	2.65	-
81	S-palmitoylation	KSVFRHACVPVDFEE HHHHHHCCCCCCHHE	2.65	28526873
130	Phosphorylation	NLPPSHKSRNNILRT CCCCCHHHHCCHHHH	34.51	23737553
148	S-nitrosocysteine	LYANVIHCKSLPGVV HHHCEEECCCCCCCE	1.89	-
148	S-palmitoylation	LYANVIHCKSLPGVV HHHCEEECCCCCCCE	1.89	26165157
149	Acetylation	YANVIHCKSLPGVVT HHCEEECCCCCCCEE	40.65	23864654
159	Acetylation	PGVVTRHKDIDILIV CCCEECCCCCEEEEE	53.76	23864654
170	Phosphorylation	ILIVRENTEGEYSSL EEEEECCCCCCCCCC	40.38	22324799
174	Phosphorylation	RENTEGEYSSLEHES ECCCCCCCCCCCHHH	17.89	29472430
175	Phosphorylation	ENTEGEYSSLEHESV CCCCCCCCCCCHHHH	24.93	29899451
176	Phosphorylation	NTEGEYSSLEHESVA CCCCCCCCCCHHHHH	36.55	23737553
181	Phosphorylation	YSSLEHESVAGVVES CCCCCHHHHHHHHHH	21.12	29472430
188	Phosphorylation	SVAGVVESLKIITKA HHHHHHHHHHHHHHH	24.29	22324799
206	Succinylation	RIAEYAFKLAQESGR HHHHHHHHHHHHHCC	34.44	26388266
206	Acetylation	RIAEYAFKLAQESGR HHHHHHHHHHHHHCC	34.44	23576753
226	Acetylation	VHKANIMKLGDGLFL HHHCCHHHHCCCHHH	45.59	23806337
226	Succinylation	VHKANIMKLGDGLFL HHHCCHHHHCCCHHH	45.59	-
226	Succinylation	VHKANIMKLGDGLFL HHHCCHHHHCCCHHH	45.59	23806337
235	S-palmitoylation	GDGLFLQCCREVAAH CCCHHHHHHHHHHHH	2.28	28526873
333	S-palmitoylation	TATLLASCMMLDHLK HHHHHHHHHHHHHHH	1.22	28526873
333	S-nitrosocysteine	TATLLASCMMLDHLK HHHHHHHHHHHHHHH	1.22	-
343	Phosphorylation	LDHLKLHSYATSIRK HHHHHHHHHHHHHHH	27.22	22817900
363	Phosphorylation	MDNENMHTPDIGGQG CCCCCCCCCCCCCCC	16.34	22817900

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

Oops, there are no upstream regulatory protein records of IDHG1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of IDHG1_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of IDHG1_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of IDHG1_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Proteomic analysis of in vivo phosphorylated synaptic proteins.";
Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,Blackstock W.P., Choudhary J.S., Grant S.G.;
J. Biol. Chem. 280:5972-5982(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-363, AND MASSSPECTROMETRY.
PubMed: 15572359