| UniProt ID | DAK1_YEAST | |
|---|---|---|
| UniProt AC | P54838 | |
| Protein Name | Dihydroxyacetone kinase 1 | |
| Gene Name | DAK1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 584 | |
| Subcellular Localization | ||
| Protein Description | Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde.. | |
| Protein Sequence | MSAKSFEVTDPVNSSLKGFALANPSITLVPEEKILFRKTDSDKIALISGGGSGHEPTHAGFIGKGMLSGAVVGEIFASPSTKQILNAIRLVNENASGVLLIVKNYTGDVLHFGLSAERARALGINCRVAVIGDDVAVGREKGGMVGRRALAGTVLVHKIVGAFAEEYSSKYGLDGTAKVAKIINDNLVTIGSSLDHCKVPGRKFESELNEKQMELGMGIHNEPGVKVLDPIPSTEDLISKYMLPKLLDPNDKDRAFVKFDEDDEVVLLVNNLGGVSNFVISSITSKTTDFLKENYNITPVQTIAGTLMTSFNGNGFSITLLNATKATKALQSDFEEIKSVLDLLNAFTNAPGWPIADFEKTSAPSVNDDLLHNEVTAKAVGTYDFDKFAEWMKSGAEQVIKSEPHITELDNQVGDGDCGYTLVAGVKGITENLDKLSKDSLSQAVAQISDFIEGSMGGTSGGLYSILLSGFSHGLIQVCKSKDEPVTKEIVAKSLGIALDTLYKYTKARKGSSTMIDALEPFVKEFTASKDFNKAVKAAEEGAKSTATFEAKFGRASYVGDSSQVEDPGAVGLCEFLKGVQSAL | |
| 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 |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MSAKSFEVT ------CCCCCEEEC | 44.39 | 15665377 | |
| 2 | Acetylation | ------MSAKSFEVT ------CCCCCEEEC | 44.39 | 15665377 | |
| 5 | Phosphorylation | ---MSAKSFEVTDPV ---CCCCCEEECCCC | 26.76 | 22369663 | |
| 9 | Phosphorylation | SAKSFEVTDPVNSSL CCCCEEECCCCCCCC | 27.64 | 28889911 | |
| 14 | Phosphorylation | EVTDPVNSSLKGFAL EECCCCCCCCCCEEE | 36.96 | 30377154 | |
| 15 | Phosphorylation | VTDPVNSSLKGFALA ECCCCCCCCCCEEEC | 28.97 | 29136822 | |
| 25 | Phosphorylation | GFALANPSITLVPEE CEEECCCCEEEEEHH | 28.19 | 28889911 | |
| 27 | Phosphorylation | ALANPSITLVPEEKI EECCCCEEEEEHHHE | 26.49 | 21551504 | |
| 33 | Ubiquitination | ITLVPEEKILFRKTD EEEEEHHHEEEECCC | 42.94 | 24961812 | |
| 105 | Phosphorylation | VLLIVKNYTGDVLHF EEEEEEECCCCCEEE | 13.34 | 22369663 | |
| 106 | Phosphorylation | LLIVKNYTGDVLHFG EEEEEECCCCCEEEE | 35.98 | 22369663 | |
| 178 | Ubiquitination | YGLDGTAKVAKIIND HCCCCHHHHHHHHCC | 42.43 | 23749301 | |
| 189 | Phosphorylation | IINDNLVTIGSSLDH HHCCCEEEECCCCCC | 23.84 | 22369663 | |
| 192 | Phosphorylation | DNLVTIGSSLDHCKV CCEEEECCCCCCCCC | 24.71 | 22369663 | |
| 193 | Phosphorylation | NLVTIGSSLDHCKVP CEEEECCCCCCCCCC | 32.38 | 22369663 | |
| 203 | Ubiquitination | HCKVPGRKFESELNE CCCCCCCHHHHHHHH | 60.44 | 23749301 | |
| 203 | Acetylation | HCKVPGRKFESELNE CCCCCCCHHHHHHHH | 60.44 | 22865919 | |
| 211 | Acetylation | FESELNEKQMELGMG HHHHHHHHHHHHCCC | 54.60 | 24489116 | |
| 226 | Acetylation | IHNEPGVKVLDPIPS CCCCCCCEECCCCCC | 42.89 | 24489116 | |
| 233 | Phosphorylation | KVLDPIPSTEDLISK EECCCCCCHHHHHHH | 45.19 | 22369663 | |
| 234 | Phosphorylation | VLDPIPSTEDLISKY ECCCCCCHHHHHHHH | 28.32 | 29734811 | |
| 240 | Acetylation | STEDLISKYMLPKLL CHHHHHHHHCCHHHC | 27.90 | 24489116 | |
| 245 | Succinylation | ISKYMLPKLLDPNDK HHHHCCHHHCCCCCC | 58.69 | 23954790 | |
| 245 | Acetylation | ISKYMLPKLLDPNDK HHHHCCHHHCCCCCC | 58.69 | 24489116 | |
| 252 | Succinylation | KLLDPNDKDRAFVKF HHCCCCCCCCCEEEC | 56.61 | 23954790 | |
| 360 | Ubiquitination | WPIADFEKTSAPSVN CCHHHCCCCCCCCCC | 48.01 | 17644757 | |
| 361 | Phosphorylation | PIADFEKTSAPSVND CHHHCCCCCCCCCCH | 23.95 | 22369663 | |
| 362 | Phosphorylation | IADFEKTSAPSVNDD HHHCCCCCCCCCCHH | 49.61 | 22369663 | |
| 365 | Phosphorylation | FEKTSAPSVNDDLLH CCCCCCCCCCHHHCC | 33.01 | 22369663 | |
| 376 | Phosphorylation | DLLHNEVTAKAVGTY HHCCCCHHHHHHCCC | 19.09 | 22369663 | |
| 378 | Ubiquitination | LHNEVTAKAVGTYDF CCCCHHHHHHCCCCH | 33.95 | 17644757 | |
| 435 | Acetylation | GITENLDKLSKDSLS HHHHCHHHHCHHHHH | 58.80 | 24489116 | |
| 482 | 2-Hydroxyisobutyrylation | LIQVCKSKDEPVTKE HHHHHCCCCCCCHHH | 52.16 | - | |
| 482 | Acetylation | LIQVCKSKDEPVTKE HHHHHCCCCCCCHHH | 52.16 | 25381059 | |
| 504 | Acetylation | IALDTLYKYTKARKG HHHHHHHHHHHHCCC | 49.94 | 24489116 | |
| 512 | Phosphorylation | YTKARKGSSTMIDAL HHHHCCCCCCHHHHH | 26.18 | 28889911 | |
| 524 | Acetylation | DALEPFVKEFTASKD HHHHHHHHHHHCCCC | 47.71 | 24489116 | |
| 537 | 2-Hydroxyisobutyrylation | KDFNKAVKAAEEGAK CCHHHHHHHHHHHHC | 46.90 | - | |
| 545 | Phosphorylation | AAEEGAKSTATFEAK HHHHHHCCCEEEEEH | 23.81 | 28889911 | |
| 552 | Acetylation | STATFEAKFGRASYV CCEEEEEHHCCCEEC | 40.95 | 24489116 | |
| 557 | Phosphorylation | EAKFGRASYVGDSSQ EEHHCCCEECCCHHH | 20.99 | 21440633 | |
| 558 | Phosphorylation | AKFGRASYVGDSSQV EHHCCCEECCCHHHC | 13.89 | 21440633 | |
| 562 | Phosphorylation | RASYVGDSSQVEDPG CCEECCCHHHCCCCC | 19.42 | 30377154 | |
| 563 | Phosphorylation | ASYVGDSSQVEDPGA CEECCCHHHCCCCCH | 42.88 | 20190278 | |
| 578 | Ubiquitination | VGLCEFLKGVQSAL- HHHHHHHHHHHHHC- | 63.46 | 17644757 |
| 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 DAK1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DAK1_YEAST !! | ||||||
* 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 DAK1_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-25; SER-233;SER-365 AND SER-563, AND MASS SPECTROMETRY. | |
| "Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, AND MASSSPECTROMETRY. | |