| UniProt ID | TKT_RAT | |
|---|---|---|
| UniProt AC | P50137 | |
| Protein Name | Transketolase | |
| Gene Name | Tkt | |
| Organism | Rattus norvegicus (Rat). | |
| Sequence Length | 623 | |
| Subcellular Localization | ||
| Protein Description | Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.. | |
| Protein Sequence | MEGYHKPDQQKLQALKDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKALDPRNPHNDRFVLSKGHAAPILYAVWAEAGFLPEAELLNLRKISSDLDGHPVPKQAFTDVATGSLGQGLGAACGMAYTGKYFDKASYRVYCMLGDGEVSEGSVWEAMAFAGIYKLDNLVAIFDINRLGQSDPAPLQHQVDVYQKRCEAFGWHAIIVDGHSVEELCKAFGQAKHQPTAIIAKTFKGRGITGIEDKEAWHGKPLPKNMAEQIIQEIYSQVQSKKKILATPPQEDAPSVDIANIRMPTPPNYKVGDKIATRKAYGLALAKLGHASDRIIALDGDTKNSTFSELFKKEHPDRFIECYIAEQNMVSIAVGCATRDRTVPFCSTFAAFFTRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPMSTVFYPSDGVATEKAVELAANTKGICFIRTSRPENAIIYSNNEDFQVGQAKVVLKSKDDQVTVIGAGVTLHEALAAAEMLKKEKIGVRVLDPFTIKPLDKKLILDCARATKGRILTVEDHYYEGGIGEAVSAVVVGEPGVTVTRLAVSQVPRSGKPAELLKMFGIDKDAIVQAVKGLVTKG | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 1 | Acetylation | -------MEGYHKPD -------CCCCCCCC | 8.99 | - | |
| 6 | Acetylation | --MEGYHKPDQQKLQ --CCCCCCCCHHHHH | 41.63 | 14878451 | |
| 11 | Acetylation | YHKPDQQKLQALKDT CCCCCHHHHHHHHHH | 36.61 | 22902405 | |
| 16 | Acetylation | QQKLQALKDTANRLR HHHHHHHHHHHHHHH | 56.92 | 22902405 | |
| 59 | Acetylation | FFHTMRYKALDPRNP HHHHHHCCCCCCCCC | 31.91 | 22902405 | |
| 104 | Phosphorylation | LLNLRKISSDLDGHP HHCHHHCCCCCCCCC | 22.34 | 23984901 | |
| 105 | Phosphorylation | LNLRKISSDLDGHPV HCHHHCCCCCCCCCC | 45.74 | 28432305 | |
| 144 | Acetylation | YTGKYFDKASYRVYC HCCCCCCCCCEEEEE | 29.36 | 22633187 | |
| 150 | Phosphorylation | DKASYRVYCMLGDGE CCCCEEEEEEECCCC | 2.31 | 26022182 | |
| 173 | Phosphorylation | AMAFAGIYKLDNLVA HHHHHCEEECCCEEE | 12.46 | 26022182 | |
| 204 | Acetylation | HQVDVYQKRCEAFGW HHHHHHHHHHHHHCC | 41.13 | 22902405 | |
| 232 | Acetylation | CKAFGQAKHQPTAII HHHHCCCCCCCCEEE | 34.58 | 22902405 | |
| 241 | Acetylation | QPTAIIAKTFKGRGI CCCEEEEEECCCCCC | 44.05 | 22902405 | |
| 254 | Ubiquitination | GITGIEDKEAWHGKP CCCCCCCHHHHCCCC | 36.22 | - | |
| 254 | Acetylation | GITGIEDKEAWHGKP CCCCCCCHHHHCCCC | 36.22 | 22902405 | |
| 260 | Succinylation | DKEAWHGKPLPKNMA CHHHHCCCCCCHHHH | 30.41 | 26843850 | |
| 260 | Acetylation | DKEAWHGKPLPKNMA CHHHHCCCCCCHHHH | 30.41 | 22902405 | |
| 275 | Phosphorylation | EQIIQEIYSQVQSKK HHHHHHHHHHHHCCC | 7.72 | 27097102 | |
| 276 | Phosphorylation | QIIQEIYSQVQSKKK HHHHHHHHHHHCCCC | 29.54 | 27097102 | |
| 280 | Phosphorylation | EIYSQVQSKKKILAT HHHHHHHCCCCCCCC | 47.81 | 28689409 | |
| 281 | Acetylation | IYSQVQSKKKILATP HHHHHHCCCCCCCCC | 40.78 | 22902405 | |
| 282 | Ubiquitination | YSQVQSKKKILATPP HHHHHCCCCCCCCCC | 50.74 | - | |
| 283 | Ubiquitination | SQVQSKKKILATPPQ HHHHCCCCCCCCCCC | 46.84 | - | |
| 287 | Phosphorylation | SKKKILATPPQEDAP CCCCCCCCCCCCCCC | 31.86 | 29779826 | |
| 295 | Phosphorylation | PPQEDAPSVDIANIR CCCCCCCCCCCCCCC | 33.86 | 27097102 | |
| 305 | Phosphorylation | IANIRMPTPPNYKVG CCCCCCCCCCCCCCC | 41.87 | 21738781 | |
| 309 | Phosphorylation | RMPTPPNYKVGDKIA CCCCCCCCCCCCCHH | 16.90 | 23984901 | |
| 310 | Acetylation | MPTPPNYKVGDKIAT CCCCCCCCCCCCHHH | 46.51 | 22902405 | |
| 314 | Acetylation | PNYKVGDKIATRKAY CCCCCCCCHHHHHHH | 28.45 | 22902405 | |
| 319 | Acetylation | GDKIATRKAYGLALA CCCHHHHHHHHHHHH | 41.42 | 22902405 | |
| 327 | Acetylation | AYGLALAKLGHASDR HHHHHHHHHCCCCCC | 56.71 | 22902405 | |
| 342 | Phosphorylation | IIALDGDTKNSTFSE EEEECCCCCCCCHHH | 37.34 | 22673903 | |
| 345 | Phosphorylation | LDGDTKNSTFSELFK ECCCCCCCCHHHHHH | 32.17 | 21738781 | |
| 346 | Phosphorylation | DGDTKNSTFSELFKK CCCCCCCCHHHHHHH | 40.34 | 23984901 | |
| 348 | Phosphorylation | DTKNSTFSELFKKEH CCCCCCHHHHHHHHC | 33.22 | 23984901 | |
| 352 | Acetylation | STFSELFKKEHPDRF CCHHHHHHHHCCCCE | 70.63 | 22902405 | |
| 353 | Acetylation | TFSELFKKEHPDRFI CHHHHHHHHCCCCEE | 54.65 | 22902405 | |
| 481 | Phosphorylation | RPENAIIYSNNEDFQ CCCCEEEECCCCCCC | 10.15 | 25575281 | |
| 482 | Phosphorylation | PENAIIYSNNEDFQV CCCEEEECCCCCCCC | 23.83 | 28689409 | |
| 499 | Acetylation | AKVVLKSKDDQVTVI EEEEEECCCCCEEEE | 64.83 | 22902405 | |
| 523 | Acetylation | LAAAEMLKKEKIGVR HHHHHHHHHCCCCCE | 58.54 | 22902405 | |
| 538 | Acetylation | VLDPFTIKPLDKKLI EECCCCCCCCCCHHH | 36.15 | 22902405 | |
| 538 | Succinylation | VLDPFTIKPLDKKLI EECCCCCCCCCCHHH | 36.15 | 26843850 | |
| 542 | Acetylation | FTIKPLDKKLILDCA CCCCCCCCHHHHHHH | 58.10 | 22902405 | |
| 590 | Phosphorylation | TVTRLAVSQVPRSGK EEEEEEEECCCCCCC | 21.61 | 28689409 | |
| 597 | Acetylation | SQVPRSGKPAELLKM ECCCCCCCHHHHHHH | 42.15 | 22902405 | |
| 603 | Acetylation | GKPAELLKMFGIDKD CCHHHHHHHHCCCHH | 44.82 | 22902405 | |
| 609 | Acetylation | LKMFGIDKDAIVQAV HHHHCCCHHHHHHHH | 47.33 | 22902405 | |
| 609 | Succinylation | LKMFGIDKDAIVQAV HHHHCCCHHHHHHHH | 47.33 | 26843850 |
| 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 TKT_RAT !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TKT_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 TKT_RAT !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of TKT_RAT !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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