UniProt ID | DBF4_YEAST | |
---|---|---|
UniProt AC | P32325 | |
Protein Name | DDK kinase regulatory subunit DBF4 | |
Gene Name | DBF4 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 704 | |
Subcellular Localization | ||
Protein Description | Regulatory subunit of the CDC7-DBF4 kinase, also called DBF4-dependent kinase (DDK), which is involved in cell cycle regulation of premitotic and premeiotic chromosome replication and in chromosome segregation. DDK plays an essential role in initiating DNA replication at replication origins by phosphorylating the MCM2 and MCM4 subunits of the MCM2-7 helicase complex. DBF4 recruits the catalytic subunit CDC7 to MCM2 and to origins of replication. DDK has also postreplicative functions in meiosis. DDK phosphorylates the meiosis-specific double-strand break protein MER2 for initiation of meiotic recombination. Interacts with CDC5 during meiosis to promote double-strand breaks and monopolar spindle orientation. Inhibits CDC5 activity during mitosis through direct binding to its PBD.. | |
Protein Sequence | MVSPTKMIIRSPLKETDTNLKHNNGIAASTTAAGHLNVFSNDNNCNNNNTTESFPKKRSLERLELQQQQHLHEKKRARIERARSIEGAVQVSKGTGLKNVEPRVTPKELLEWQTNWKKIMKRDSRIYFDITDDVEMNTYNKSKMDKRRDLLKRGFLTLGAQITQFFDTTVTIVITRRSVENIYLLKDTDILSRAKKNYMKVWSYEKAARFLKNLDVDLDHLSKTKSASLAAPTLSNLLHNEKLYGPTDRDPRTKRDDIHYFKYPHVYLYDLWQTWAPIITLEWKPQELTNLDELPYPILKIGSFGRCPFIGDRNYDESSYKRVVKRYSRDKANKKYALQLRALFQYHADTLLNTSSVNDQTKNLIFIPHTCNDSTKSFKKWMQEKAKNFEKTELKKTDDSAVQDVRNEHADQTDEKNSILLNETETKEPPLKEEKENKQSIAEESNKYPQRKELAATPKLNHPVLATFARQETEEVPDDLCTLKTKSRQAFEIKASGAHQSNDVATSFGNGLGPTRASVMSKNMKSLSRLMVDRKLGVKQTNGNNKNYTATIATTAETSKENRHRLDFNALKKDEAPSKETGKDSAVHLETNRKPQNFPKVATKSVSADSKVHNDIKITTTESPTASKKSTSTNVTLHFNAQTAQTAQPVKKETVKNSGYCENCRVKYESLEQHIVSEKHLSFAENDLNFEAIDSLIENLRFQI | |
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 |
---|---|---|---|---|---|
5 | Phosphorylation | ---MVSPTKMIIRSP ---CCCCCCEEEECC | 26.24 | 20865002 | |
11 | Phosphorylation | PTKMIIRSPLKETDT CCCEEEECCCCCCCC | 24.95 | 25752575 | |
16 | Phosphorylation | IRSPLKETDTNLKHN EECCCCCCCCCCCCC | 46.68 | 20865002 | |
18 | Phosphorylation | SPLKETDTNLKHNNG CCCCCCCCCCCCCCC | 50.28 | 20865002 | |
29 | Phosphorylation | HNNGIAASTTAAGHL CCCCCCCCCCCCCCC | 19.78 | 20865002 | |
30 | Phosphorylation | NNGIAASTTAAGHLN CCCCCCCCCCCCCCE | 18.74 | 20865002 | |
31 | Phosphorylation | NGIAASTTAAGHLNV CCCCCCCCCCCCCEE | 16.41 | 20865002 | |
40 | Phosphorylation | AGHLNVFSNDNNCNN CCCCEECCCCCCCCC | 38.70 | 20865002 | |
50 | Phosphorylation | NNCNNNNTTESFPKK CCCCCCCCCCCCCCH | 33.78 | 20865002 | |
51 | Phosphorylation | NCNNNNTTESFPKKR CCCCCCCCCCCCCHH | 31.58 | 20865002 | |
53 | Phosphorylation | NNNNTTESFPKKRSL CCCCCCCCCCCHHHH | 44.77 | 20865002 | |
59 | Phosphorylation | ESFPKKRSLERLELQ CCCCCHHHHHHHHHH | 43.38 | 17287358 | |
84 | Phosphorylation | ARIERARSIEGAVQV HHHHHHHHHCCCEEE | 24.81 | 17287358 | |
92 | Phosphorylation | IEGAVQVSKGTGLKN HCCCEEECCCCCCCC | 14.31 | 20865002 | |
95 | Phosphorylation | AVQVSKGTGLKNVEP CEEECCCCCCCCCCC | 42.98 | 20865002 | |
105 | Phosphorylation | KNVEPRVTPKELLEW CCCCCCCCHHHHHHH | 29.89 | 20865002 | |
114 | Phosphorylation | KELLEWQTNWKKIMK HHHHHHHHCHHHHHC | 44.08 | 20865002 | |
124 | Phosphorylation | KKIMKRDSRIYFDIT HHHHCCCCCEEEECC | 25.31 | 20865002 | |
131 | Phosphorylation | SRIYFDITDDVEMNT CCEEEECCCCCCHHC | 28.17 | 20865002 | |
139 | Phosphorylation | DDVEMNTYNKSKMDK CCCCHHCCCHHHHHH | 18.65 | 20865002 | |
171 | Phosphorylation | QFFDTTVTIVITRRS HCCCEEEEEEEECCC | 13.87 | 20865002 | |
175 | Phosphorylation | TTVTIVITRRSVENI EEEEEEEECCCEECE | 14.77 | 20865002 | |
188 | Phosphorylation | NIYLLKDTDILSRAK CEEEECCHHHHHHHH | 24.29 | 20835227 | |
192 | Phosphorylation | LKDTDILSRAKKNYM ECCHHHHHHHHHHHH | 30.44 | 28889911 | |
203 | Phosphorylation | KNYMKVWSYEKAARF HHHHHHCCHHHHHHH | 26.80 | 20835227 | |
222 | Phosphorylation | DVDLDHLSKTKSASL CCCHHHHCCCCCHHH | 34.55 | 20835227 | |
224 | Phosphorylation | DLDHLSKTKSASLAA CHHHHCCCCCHHHHH | 27.19 | 20835227 | |
226 | Phosphorylation | DHLSKTKSASLAAPT HHHCCCCCHHHHHCC | 28.46 | 21440633 | |
228 | Phosphorylation | LSKTKSASLAAPTLS HCCCCCHHHHHCCHH | 26.15 | 20835227 | |
233 | Phosphorylation | SASLAAPTLSNLLHN CHHHHHCCHHHHHCC | 37.78 | 21440633 | |
235 | Phosphorylation | SLAAPTLSNLLHNEK HHHHCCHHHHHCCCC | 28.10 | 20865002 | |
318 | Phosphorylation | GDRNYDESSYKRVVK CCCCCCHHHHHHHHH | 35.75 | 20835227 | |
319 | Phosphorylation | DRNYDESSYKRVVKR CCCCCHHHHHHHHHH | 32.40 | 20835227 | |
328 | Phosphorylation | KRVVKRYSRDKANKK HHHHHHHCCCCCCHH | 37.73 | 20835227 | |
356 | Phosphorylation | DTLLNTSSVNDQTKN HHHCCCCCCCCCCCC | 23.93 | 20865002 | |
374 | Phosphorylation | IPHTCNDSTKSFKKW EEECCCCCHHHHHHH | 24.60 | 20835227 | |
375 | Phosphorylation | PHTCNDSTKSFKKWM EECCCCCHHHHHHHH | 33.30 | 20835227 | |
377 | Phosphorylation | TCNDSTKSFKKWMQE CCCCCHHHHHHHHHH | 42.24 | 20835227 | |
400 | Phosphorylation | ELKKTDDSAVQDVRN CCCCCCCHHHHHHHH | 32.90 | 27214570 | |
413 | Phosphorylation | RNEHADQTDEKNSIL HHHCCCCCCHHCCCC | 46.82 | 21551504 | |
440 | Phosphorylation | EEKENKQSIAEESNK HHHHHHHHHHHHHHC | 25.94 | 28889911 | |
473 | Phosphorylation | ATFARQETEEVPDDL HHHHCCCCCCCCCCC | 29.16 | 20865002 | |
496 | Phosphorylation | QAFEIKASGAHQSND CCEEEECCCCCCCCC | 31.35 | 30377154 | |
501 | Phosphorylation | KASGAHQSNDVATSF ECCCCCCCCCCCHHC | 25.73 | 28889911 | |
506 | Phosphorylation | HQSNDVATSFGNGLG CCCCCCCHHCCCCCC | 25.16 | 30377154 | |
507 | Phosphorylation | QSNDVATSFGNGLGP CCCCCCHHCCCCCCH | 22.78 | 23749301 | |
515 | Phosphorylation | FGNGLGPTRASVMSK CCCCCCHHHHHHHCC | 36.75 | 30377154 | |
518 | Phosphorylation | GLGPTRASVMSKNMK CCCHHHHHHHCCCHH | 18.30 | 20835227 | |
521 | Phosphorylation | PTRASVMSKNMKSLS HHHHHHHCCCHHHHH | 20.79 | 20835227 | |
526 | Phosphorylation | VMSKNMKSLSRLMVD HHCCCHHHHHHHHHH | 22.32 | 20835227 | |
528 | Phosphorylation | SKNMKSLSRLMVDRK CCCHHHHHHHHHHHH | 30.38 | 21440633 | |
548 | Phosphorylation | TNGNNKNYTATIATT CCCCCCEEEEEEEEE | 10.20 | 30377154 | |
549 | Phosphorylation | NGNNKNYTATIATTA CCCCCEEEEEEEEEC | 27.07 | 30377154 | |
551 | Phosphorylation | NNKNYTATIATTAET CCCEEEEEEEEECCC | 11.89 | 30377154 | |
554 | Phosphorylation | NYTATIATTAETSKE EEEEEEEEECCCCCH | 23.76 | 30377154 | |
555 | Phosphorylation | YTATIATTAETSKEN EEEEEEEECCCCCHH | 17.30 | 30377154 | |
558 | Phosphorylation | TIATTAETSKENRHR EEEEECCCCCHHHHC | 42.51 | 30377154 | |
559 | Phosphorylation | IATTAETSKENRHRL EEEECCCCCHHHHCC | 29.49 | 30377154 | |
604 | Acetylation | NFPKVATKSVSADSK CCCCCCCCEECCCCC | 38.84 | 25381059 | |
605 | Phosphorylation | FPKVATKSVSADSKV CCCCCCCEECCCCCC | 19.56 | 23749301 | |
607 | Phosphorylation | KVATKSVSADSKVHN CCCCCEECCCCCCCC | 33.19 | 30377154 | |
620 | Phosphorylation | HNDIKITTTESPTAS CCCEEEEECCCCCCC | 31.85 | 30377154 | |
621 | Phosphorylation | NDIKITTTESPTASK CCEEEEECCCCCCCC | 26.30 | 23749301 | |
623 | Phosphorylation | IKITTTESPTASKKS EEEEECCCCCCCCCC | 26.01 | 21036905 | |
625 | Phosphorylation | ITTTESPTASKKSTS EEECCCCCCCCCCCC | 53.49 | 23749301 | |
627 | Phosphorylation | TTESPTASKKSTSTN ECCCCCCCCCCCCCC | 42.99 | 23749301 |
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 DBF4_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DBF4_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 DBF4_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-11; SER-235 AND SER-623,AND MASS SPECTROMETRY. | |
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59 AND SER-84, AND MASSSPECTROMETRY. |