UniProt ID | IDH3A_MOUSE | |
---|---|---|
UniProt AC | Q9D6R2 | |
Protein Name | Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial | |
Gene Name | Idh3a | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 366 | |
Subcellular Localization | Mitochondrion. | |
Protein Description | Catalytic subunit of the enzyme which catalyzes 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 | MAGSAWVSKVSRLLGAFHNTKQVTRGFAGGVQTVTLIPGDGIGPEISASVMKIFDAAKAPIQWEERNVTAIQGPGGKWMIPPEAKESMDKNKMGLKGPLKTPIAAGHPSMNLLLRKTFDLYANVRPCVSIEGYKTPYTDVNIVTIRENTEGEYSGIEHVIVDGVVQSIKLITEEASKRIAEFAFEYARNNHRSNVTAVHKANIMRMSDGLFLQKCREVAENCKDIKFNEMYLDTVCLNMVQDPSQFDVLVMPNLYGDILSDLCAGLIGGLGVTPSGNIGANGVAIFESVHGTAPDIAGKDMANPTALLLSAVMMLRHMGLFDHAAKIEAACFATIKDGKSLTKDLGGNAKCSDFTEEICRRVKDLD | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
4 | Phosphorylation | ----MAGSAWVSKVS ----CCCHHHHHHHH | 14.93 | 20495213 | |
58 | Acetylation | MKIFDAAKAPIQWEE HHHHHHHCCCCCEEC | 57.31 | 23864654 | |
58 | Ubiquitination | MKIFDAAKAPIQWEE HHHHHHHCCCCCEEC | 57.31 | - | |
58 | Succinylation | MKIFDAAKAPIQWEE HHHHHHHCCCCCEEC | 57.31 | 23806337 | |
77 | Acetylation | AIQGPGGKWMIPPEA EEECCCCCEECCHHH | 39.23 | 23864654 | |
77 | Succinylation | AIQGPGGKWMIPPEA EEECCCCCEECCHHH | 39.23 | - | |
77 | Succinylation | AIQGPGGKWMIPPEA EEECCCCCEECCHHH | 39.23 | 23806337 | |
85 | Acetylation | WMIPPEAKESMDKNK EECCHHHHHCCCCCC | 48.97 | 23864654 | |
90 | Acetylation | EAKESMDKNKMGLKG HHHHCCCCCCCCCCC | 50.23 | 23201123 | |
96 | Acetylation | DKNKMGLKGPLKTPI CCCCCCCCCCCCCCC | 53.40 | 2395061 | |
100 | Acetylation | MGLKGPLKTPIAAGH CCCCCCCCCCCCCCC | 56.22 | 24062335 | |
100 | Ubiquitination | MGLKGPLKTPIAAGH CCCCCCCCCCCCCCC | 56.22 | - | |
100 | Succinylation | MGLKGPLKTPIAAGH CCCCCCCCCCCCCCC | 56.22 | - | |
100 | Malonylation | MGLKGPLKTPIAAGH CCCCCCCCCCCCCCC | 56.22 | 26320211 | |
100 | Glutarylation | MGLKGPLKTPIAAGH CCCCCCCCCCCCCCC | 56.22 | 24703693 | |
101 | Phosphorylation | GLKGPLKTPIAAGHP CCCCCCCCCCCCCCC | 27.84 | 19060867 | |
127 | S-nitrosocysteine | LYANVRPCVSIEGYK HHCCCCCCEEECCCC | 2.35 | - | |
127 | S-nitrosylation | LYANVRPCVSIEGYK HHCCCCCCEEECCCC | 2.35 | 21278135 | |
167 | Phosphorylation | IVDGVVQSIKLITEE EECHHHHHHHHHCHH | 15.30 | 23140645 | |
177 | Succinylation | LITEEASKRIAEFAF HHCHHHHHHHHHHHH | 55.67 | 26388266 | |
177 | Ubiquitination | LITEEASKRIAEFAF HHCHHHHHHHHHHHH | 55.67 | 27667366 | |
177 | Acetylation | LITEEASKRIAEFAF HHCHHHHHHHHHHHH | 55.67 | 21728379 | |
193 | Phosphorylation | YARNNHRSNVTAVHK HHHHCCCCCCHHHHH | 28.27 | 23684622 | |
200 | Succinylation | SNVTAVHKANIMRMS CCCHHHHHHHHHHHC | 36.21 | 23806337 | |
200 | Ubiquitination | SNVTAVHKANIMRMS CCCHHHHHHHHHHHC | 36.21 | - | |
200 | Acetylation | SNVTAVHKANIMRMS CCCHHHHHHHHHHHC | 36.21 | 23806337 | |
214 | Acetylation | SDGLFLQKCREVAEN CCCCHHHHHHHHHHH | 37.09 | 24062335 | |
216 | Methylation | GLFLQKCREVAENCK CCHHHHHHHHHHHCC | 48.75 | 58856157 | |
216 | Dimethylation | GLFLQKCREVAENCK CCHHHHHHHHHHHCC | 48.75 | - | |
222 | Glutathionylation | CREVAENCKDIKFNE HHHHHHHCCCCCCCH | 2.93 | 24333276 | |
222 | S-nitrosylation | CREVAENCKDIKFNE HHHHHHHCCCCCCCH | 2.93 | 21278135 | |
222 | S-nitrosocysteine | CREVAENCKDIKFNE HHHHHHHCCCCCCCH | 2.93 | - | |
223 | Succinylation | REVAENCKDIKFNEM HHHHHHCCCCCCCHH | 74.25 | 26388266 | |
223 | Acetylation | REVAENCKDIKFNEM HHHHHHCCCCCCCHH | 74.25 | 23576753 | |
326 | Acetylation | GLFDHAAKIEAACFA CCHHHHHHHHHHEEE | 41.69 | 24062335 | |
331 | S-nitrosylation | AAKIEAACFATIKDG HHHHHHHEEEEECCC | 2.84 | 24895380 | |
331 | S-nitrosocysteine | AAKIEAACFATIKDG HHHHHHHEEEEECCC | 2.84 | - | |
336 | Succinylation | AACFATIKDGKSLTK HHEEEEECCCCCCCC | 56.95 | 23806337 | |
336 | Acetylation | AACFATIKDGKSLTK HHEEEEECCCCCCCC | 56.95 | 23864654 | |
339 | Acetylation | FATIKDGKSLTKDLG EEEECCCCCCCCCCC | 53.04 | 23201123 | |
343 | Succinylation | KDGKSLTKDLGGNAK CCCCCCCCCCCCCCC | 57.14 | 23806337 | |
343 | Ubiquitination | KDGKSLTKDLGGNAK CCCCCCCCCCCCCCC | 57.14 | 27667366 | |
343 | Succinylation | KDGKSLTKDLGGNAK CCCCCCCCCCCCCCC | 57.14 | - | |
343 | Acetylation | KDGKSLTKDLGGNAK CCCCCCCCCCCCCCC | 57.14 | 24062335 | |
350 | Succinylation | KDLGGNAKCSDFTEE CCCCCCCCCCHHHHH | 37.97 | - | |
350 | Succinylation | KDLGGNAKCSDFTEE CCCCCCCCCCHHHHH | 37.97 | 23806337 | |
350 | Acetylation | KDLGGNAKCSDFTEE CCCCCCCCCCHHHHH | 37.97 | 23806337 | |
351 | S-nitrosylation | DLGGNAKCSDFTEEI CCCCCCCCCHHHHHH | 4.36 | 24895380 | |
359 | S-nitrosylation | SDFTEEICRRVKDLD CHHHHHHHHHHHCCC | 2.29 | 24895380 | |
363 | Acetylation | EEICRRVKDLD---- HHHHHHHHCCC---- | 51.25 | 2416169 |
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 IDH3A_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of IDH3A_MOUSE !! |
* 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 IDH3A_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of IDH3A_MOUSE !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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