| UniProt ID | DBF2_YEAST | |
|---|---|---|
| UniProt AC | P22204 | |
| Protein Name | Cell cycle protein kinase DBF2 | |
| Gene Name | DBF2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 572 | |
| Subcellular Localization | Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Bud neck. Nucleus. Localizes on spindle ole body (SPB) for much of the cell cycle and migrates from there to the bud neck in late mitosis. SPB localization during anaphase coi | |
| Protein Description | Ser/Thr-protein kinase involved in the mitotic exit network (MEN) and required after the metaphase to anaphase cell cycle transition. Phosphorylates CHS2 to regulate its dynamics and chitin synthesis at the division site during cytokinesis. Coordinates septin and actomyosin ring (AMR) functions during cytokinesis through the phosphorylation of HOF1. In complex with MOB1, phosphorylates CDC14 at sites adjacent to its nuclear localization sequence, thereby retaining CDC14 in the cytoplasm. Binds also to SWI5 and CLB2 mRNAs cotranscriptionally to regulate their decay. In the nucleus, the DBF2-MOB1 complex regulates passenger protein localization during anaphase. Mediates sorbic acid stress tolerance through promoting vacuolar H(+)-ATPase function, probably through phosphorylation of VMA1 and VMA2 subunits.. | |
| Protein Sequence | MLSKSEKNVDLLAGNMSNLSFDGHGTPGGTGLFPNQNITKRRTRPAGINDSPSPVKPSFFPYEDTSNMDIDEVSQPDMDVSNSPKKLPPKFYERATSNKTQRVVSVCKMYFLEHYCDMFDYVISRRQRTKQVLEYLQQQSQLPNSDQIKLNEEWSSYLQREHQVLRKRRLKPKNRDFEMITQVGQGGYGQVYLARKKDTKEVCALKILNKKLLFKLNETKHVLTERDILTTTRSEWLVKLLYAFQDLQSLYLAMEFVPGGDFRTLLINTRCLKSGHARFYISEMFCAVNALHDLGYTHRDLKPENFLIDAKGHIKLTDFGLAAGTISNERIESMKIRLEKIKDLEFPAFTEKSIEDRRKMYNQLREKEINYANSMVGSPDYMALEVLEGKKYDFTVDYWSLGCMLFESLVGYTPFSGSSTNETYDNLRRWKQTLRRPRQSDGRAAFSDRTWDLITRLIADPINRLRSFEHVKRMSYFADINFSTLRSMIPPFTPQLDSETDAGYFDDFTSEADMAKYADVFKRQDKLTAMVDDSAVSSKLVGFTFRHRNGKQGSSGILFNGLEHSDPFSTFY | |
| 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 |
|---|---|---|---|---|---|
| 17 | Phosphorylation | DLLAGNMSNLSFDGH HCCCCCCCCCEECCC | 38.32 | 22369663 | |
| 20 | Phosphorylation | AGNMSNLSFDGHGTP CCCCCCCEECCCCCC | 26.07 | 20377248 | |
| 26 | Phosphorylation | LSFDGHGTPGGTGLF CEECCCCCCCCCCCC | 17.06 | 21440633 | |
| 30 | Phosphorylation | GHGTPGGTGLFPNQN CCCCCCCCCCCCCCC | 36.30 | 22369663 | |
| 39 | Phosphorylation | LFPNQNITKRRTRPA CCCCCCCCCCCCCCC | 26.50 | 22369663 | |
| 43 | Phosphorylation | QNITKRRTRPAGIND CCCCCCCCCCCCCCC | 45.07 | 23749301 | |
| 51 | Phosphorylation | RPAGINDSPSPVKPS CCCCCCCCCCCCCCC | 23.84 | 21440633 | |
| 53 | Phosphorylation | AGINDSPSPVKPSFF CCCCCCCCCCCCCCC | 46.40 | 21440633 | |
| 58 | Phosphorylation | SPSPVKPSFFPYEDT CCCCCCCCCCCCCCC | 33.53 | 23749301 | |
| 62 | Phosphorylation | VKPSFFPYEDTSNMD CCCCCCCCCCCCCCC | 22.68 | 19779198 | |
| 65 | Phosphorylation | SFFPYEDTSNMDIDE CCCCCCCCCCCCHHH | 15.29 | 30377154 | |
| 66 | Phosphorylation | FFPYEDTSNMDIDEV CCCCCCCCCCCHHHC | 42.34 | 19779198 | |
| 74 | Phosphorylation | NMDIDEVSQPDMDVS CCCHHHCCCCCCCCC | 33.67 | 23749301 | |
| 81 | Phosphorylation | SQPDMDVSNSPKKLP CCCCCCCCCCCCCCC | 27.59 | 23749301 | |
| 83 | Phosphorylation | PDMDVSNSPKKLPPK CCCCCCCCCCCCCHH | 30.50 | 28152593 | |
| 130 | Ubiquitination | ISRRQRTKQVLEYLQ HHHHHHHHHHHHHHH | 40.37 | 23749301 | |
| 325 | Phosphorylation | DFGLAAGTISNERIE CCCEEECCCCHHHHH | 19.26 | 24961812 | |
| 327 | Phosphorylation | GLAAGTISNERIESM CEEECCCCHHHHHHH | 32.26 | 24961812 | |
| 333 | Phosphorylation | ISNERIESMKIRLEK CCHHHHHHHCEEHHH | 24.01 | 20377248 | |
| 342 | Acetylation | KIRLEKIKDLEFPAF CEEHHHHHCCCCCCC | 68.29 | 24489116 | |
| 371 | Phosphorylation | LREKEINYANSMVGS HHHHHHHHHHHCCCC | 16.90 | 28889911 | |
| 374 | Phosphorylation | KEINYANSMVGSPDY HHHHHHHHCCCCCCE | 13.48 | 21551504 | |
| 378 | Phosphorylation | YANSMVGSPDYMALE HHHHCCCCCCEEHHH | 11.82 | 29734811 | |
| 440 | Phosphorylation | TLRRPRQSDGRAAFS HHCCCCCCCCCHHCC | 43.22 | 30377154 | |
| 537 | Phosphorylation | MVDDSAVSSKLVGFT EECCHHHHHHHEEEE | 22.82 | 30377154 | |
| 538 | Phosphorylation | VDDSAVSSKLVGFTF ECCHHHHHHHEEEEE | 24.34 | 21551504 | |
| 544 | Phosphorylation | SSKLVGFTFRHRNGK HHHHEEEEEECCCCC | 17.52 | 22890988 | |
| 554 | Phosphorylation | HRNGKQGSSGILFNG CCCCCCCCCCEEECC | 23.93 | 21440633 |
* 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 DBF2_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-374, AND MASSSPECTROMETRY. | |
| "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-374, AND MASSSPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-544, AND MASSSPECTROMETRY. | |
