UniProt ID | MDHM_RAT | |
---|---|---|
UniProt AC | P04636 | |
Protein Name | Malate dehydrogenase, mitochondrial | |
Gene Name | Mdh2 | |
Organism | Rattus norvegicus (Rat). | |
Sequence Length | 338 | |
Subcellular Localization | Mitochondrion matrix . | |
Protein Description | ||
Protein Sequence | MLSALARPVGAALRRSFSTSAQNNAKVAVLGASGGIGQPLSLLLKNSPLVSRLTLYDIAHTPGVAADLSHIETRANVKGYLGPEQLPDCLKGCDVVVIPAGVPRKPGMTRDDLFNTNATIVATLTAACAQHCPEAMICIISNPVNSTIPITAEVFKKHGVYNPNKIFGVTTLDIVRANTFVAELKGLDPARVNVPVIGGHAGKTIIPLISQCTPKVDFPQDQLATLTGRIQEAGTEVVKAKAGAGSATLSMAYAGARFVFSLVDAMNGKEGVIECSFVQSKETECTYFSTPLLLGKKGLEKNLGIGKITPFEEKMIAEAIPELKASIKKGEDFVKNMK | |
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 |
---|---|---|---|---|---|
33 | O-linked_Glycosylation | KVAVLGASGGIGQPL EEEEEECCCCCCHHH | 35.44 | 27213235 | |
33 | Phosphorylation | KVAVLGASGGIGQPL EEEEEECCCCCCHHH | 35.44 | 23984901 | |
47 | Phosphorylation | LSLLLKNSPLVSRLT HHHHHHCCCCCEEEE | 20.30 | 23984901 | |
51 | Phosphorylation | LKNSPLVSRLTLYDI HHCCCCCEEEEHHHH | 29.29 | 23991683 | |
51 | O-linked_Glycosylation | LKNSPLVSRLTLYDI HHCCCCCEEEEHHHH | 29.29 | 27213235 | |
54 | Phosphorylation | SPLVSRLTLYDIAHT CCCCEEEEHHHHCCC | 23.35 | 23984901 | |
56 | Phosphorylation | LVSRLTLYDIAHTPG CCEEEEHHHHCCCCC | 10.48 | 23991683 | |
61 | Phosphorylation | TLYDIAHTPGVAADL EHHHHCCCCCHHHCC | 16.83 | 23984901 | |
69 | O-linked_Glycosylation | PGVAADLSHIETRAN CCHHHCCHHCHHHCC | 23.98 | 27213235 | |
78 | Succinylation | IETRANVKGYLGPEQ CHHHCCCCCCCCHHH | 41.46 | 26843850 | |
78 | Acetylation | IETRANVKGYLGPEQ CHHHCCCCCCCCHHH | 41.46 | 22902405 | |
78 | Succinylation | IETRANVKGYLGPEQ CHHHCCCCCCCCHHH | 41.46 | - | |
80 | Phosphorylation | TRANVKGYLGPEQLP HHCCCCCCCCHHHCC | 11.63 | - | |
91 | Succinylation | EQLPDCLKGCDVVVI HHCCHHHCCCCEEEE | 64.92 | - | |
91 | Acetylation | EQLPDCLKGCDVVVI HHCCHHHCCCCEEEE | 64.92 | 22902405 | |
91 | Succinylation | EQLPDCLKGCDVVVI HHCCHHHCCCCEEEE | 64.92 | - | |
105 | Acetylation | IPAGVPRKPGMTRDD ECCCCCCCCCCCHHH | 39.59 | 22902405 | |
157 | Acetylation | ITAEVFKKHGVYNPN EEHHHHHHCCCCCCC | 33.84 | 22902405 | |
157 | Succinylation | ITAEVFKKHGVYNPN EEHHHHHHCCCCCCC | 33.84 | 26843850 | |
165 | Acetylation | HGVYNPNKIFGVTTL CCCCCCCCEEEEEHH | 40.44 | 22902405 | |
170 | O-linked_Glycosylation | PNKIFGVTTLDIVRA CCCEEEEEHHHHHHH | 23.24 | 27213235 | |
170 | Phosphorylation | PNKIFGVTTLDIVRA CCCEEEEEHHHHHHH | 23.24 | 23984901 | |
171 | Phosphorylation | NKIFGVTTLDIVRAN CCEEEEEHHHHHHHC | 21.74 | 23984901 | |
185 | Acetylation | NTFVAELKGLDPARV CCHHHHHCCCCHHHE | 49.27 | 25786129 | |
185 | Succinylation | NTFVAELKGLDPARV CCHHHHHCCCCHHHE | 49.27 | - | |
185 | Succinylation | NTFVAELKGLDPARV CCHHHHHCCCCHHHE | 49.27 | 26843850 | |
203 | Succinylation | VIGGHAGKTIIPLIS EECCCCCCCHHHHHH | 37.02 | - | |
203 | Acetylation | VIGGHAGKTIIPLIS EECCCCCCCHHHHHH | 37.02 | 22902405 | |
203 | Succinylation | VIGGHAGKTIIPLIS EECCCCCCCHHHHHH | 37.02 | - | |
213 | Phosphorylation | IPLISQCTPKVDFPQ HHHHHHCCCCCCCCH | 20.64 | 23991683 | |
215 | Acetylation | LISQCTPKVDFPQDQ HHHHCCCCCCCCHHH | 35.96 | 22902405 | |
215 | Succinylation | LISQCTPKVDFPQDQ HHHHCCCCCCCCHHH | 35.96 | - | |
215 | Succinylation | LISQCTPKVDFPQDQ HHHHCCCCCCCCHHH | 35.96 | - | |
225 | Phosphorylation | FPQDQLATLTGRIQE CCHHHHHHHHHHHHH | 33.18 | 30181290 | |
227 | Phosphorylation | QDQLATLTGRIQEAG HHHHHHHHHHHHHHC | 21.76 | 30181290 | |
227 | O-linked_Glycosylation | QDQLATLTGRIQEAG HHHHHHHHHHHHHHC | 21.76 | 27213235 | |
235 | Phosphorylation | GRIQEAGTEVVKAKA HHHHHHCCEEEHHCC | 32.43 | 23991683 | |
239 | Acetylation | EAGTEVVKAKAGAGS HHCCEEEHHCCCCCC | 49.71 | 25786129 | |
239 | Malonylation | EAGTEVVKAKAGAGS HHCCEEEHHCCCCCC | 49.71 | - | |
239 | N6-malonyllysine | EAGTEVVKAKAGAGS HHCCEEEHHCCCCCC | 49.71 | - | |
239 | Succinylation | EAGTEVVKAKAGAGS HHCCEEEHHCCCCCC | 49.71 | - | |
246 | Phosphorylation | KAKAGAGSATLSMAY HHCCCCCCHHHHHHH | 19.97 | 23991683 | |
248 | Phosphorylation | KAGAGSATLSMAYAG CCCCCCHHHHHHHHH | 22.51 | 23991683 | |
250 | O-linked_Glycosylation | GAGSATLSMAYAGAR CCCCHHHHHHHHHHH | 9.30 | 27213235 | |
250 | Phosphorylation | GAGSATLSMAYAGAR CCCCHHHHHHHHHHH | 9.30 | 23991683 | |
253 | Phosphorylation | SATLSMAYAGARFVF CHHHHHHHHHHHHHH | 9.27 | 23991683 | |
269 | Succinylation | LVDAMNGKEGVIECS HHHHHCCCCCEEEEE | 46.41 | - | |
269 | Succinylation | LVDAMNGKEGVIECS HHHHHCCCCCEEEEE | 46.41 | - | |
281 | Acetylation | ECSFVQSKETECTYF EEEEEECCCCCCEEE | 52.11 | 26302492 | |
283 | Phosphorylation | SFVQSKETECTYFST EEEECCCCCCEEEEC | 39.85 | 22673903 | |
286 | Phosphorylation | QSKETECTYFSTPLL ECCCCCCEEEECCHH | 22.75 | 22673903 | |
287 | Phosphorylation | SKETECTYFSTPLLL CCCCCCEEEECCHHC | 13.75 | 22673903 | |
289 | Phosphorylation | ETECTYFSTPLLLGK CCCCEEEECCHHCCC | 20.78 | 22673903 | |
290 | Phosphorylation | TECTYFSTPLLLGKK CCCEEEECCHHCCCC | 14.20 | 22673903 | |
296 | Acetylation | STPLLLGKKGLEKNL ECCHHCCCCCHHHCC | 43.57 | 25786129 | |
296 | Succinylation | STPLLLGKKGLEKNL ECCHHCCCCCHHHCC | 43.57 | - | |
296 | Succinylation | STPLLLGKKGLEKNL ECCHHCCCCCHHHCC | 43.57 | - | |
297 | Acetylation | TPLLLGKKGLEKNLG CCHHCCCCCHHHCCC | 67.91 | 22902405 | |
301 | Succinylation | LGKKGLEKNLGIGKI CCCCCHHHCCCCCCC | 63.62 | 26843850 | |
301 | Acetylation | LGKKGLEKNLGIGKI CCCCCHHHCCCCCCC | 63.62 | 25786129 | |
301 | Succinylation | LGKKGLEKNLGIGKI CCCCCHHHCCCCCCC | 63.62 | - | |
307 | Malonylation | EKNLGIGKITPFEEK HHCCCCCCCCHHHHH | 41.30 | - | |
307 | Succinylation | EKNLGIGKITPFEEK HHCCCCCCCCHHHHH | 41.30 | 26843850 | |
307 | Acetylation | EKNLGIGKITPFEEK HHCCCCCCCCHHHHH | 41.30 | 22902405 | |
307 | N6-malonyllysine | EKNLGIGKITPFEEK HHCCCCCCCCHHHHH | 41.30 | - | |
309 | Phosphorylation | NLGIGKITPFEEKMI CCCCCCCCHHHHHHH | 25.97 | 23984901 | |
314 | Acetylation | KITPFEEKMIAEAIP CCCHHHHHHHHHHHH | 28.54 | 22902405 | |
314 | Succinylation | KITPFEEKMIAEAIP CCCHHHHHHHHHHHH | 28.54 | 26843850 | |
314 | Succinylation | KITPFEEKMIAEAIP CCCHHHHHHHHHHHH | 28.54 | - | |
324 | Succinylation | AEAIPELKASIKKGE HHHHHHHHHHHHCCH | 38.12 | 26843850 | |
324 | Acetylation | AEAIPELKASIKKGE HHHHHHHHHHHHCCH | 38.12 | 22902405 | |
324 | Succinylation | AEAIPELKASIKKGE HHHHHHHHHHHHCCH | 38.12 | - | |
326 | Phosphorylation | AIPELKASIKKGEDF HHHHHHHHHHCCHHH | 33.10 | 25575281 | |
328 | Acetylation | PELKASIKKGEDFVK HHHHHHHHCCHHHHH | 52.83 | 22902405 | |
328 | Succinylation | PELKASIKKGEDFVK HHHHHHHHCCHHHHH | 52.83 | - | |
328 | Succinylation | PELKASIKKGEDFVK HHHHHHHHCCHHHHH | 52.83 | - | |
329 | Malonylation | ELKASIKKGEDFVKN HHHHHHHCCHHHHHH | 66.90 | - | |
329 | Acetylation | ELKASIKKGEDFVKN HHHHHHHCCHHHHHH | 66.90 | 22902405 | |
329 | N6-malonyllysine | ELKASIKKGEDFVKN HHHHHHHCCHHHHHH | 66.90 | - | |
329 | Succinylation | ELKASIKKGEDFVKN HHHHHHHCCHHHHHH | 66.90 | 26843850 | |
335 | Succinylation | KKGEDFVKNMK---- HCCHHHHHHCC---- | 51.85 | - | |
335 | Succinylation | KKGEDFVKNMK---- HCCHHHHHHCC---- | 51.85 | - | |
335 | Acetylation | KKGEDFVKNMK---- HCCHHHHHHCC---- | 51.85 | 25786129 | |
338 | Acetylation | EDFVKNMK------- HHHHHHCC------- | 67.59 | 26302492 |
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 MDHM_RAT !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MDHM_RAT !! |
* 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 MDHM_RAT !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of MDHM_RAT !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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