| UniProt ID | DPB11_YEAST | |
|---|---|---|
| UniProt AC | P47027 | |
| Protein Name | DNA replication regulator DPB11 | |
| Gene Name | DPB11 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 764 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Has a role in the initiation of DNA replication. Required at S-phase checkpoint. Required for the association of PSF1 with origins. Also required for the proper activation of RAD53 in response to DNA damage and replication blocks. Multicopy suppressor of DPB2 mutation. Overexpression restores the growth defect conferred by POL2 mutation.. | |
| Protein Sequence | MKPFQGITFCPTAINNEILAKKISKKIIKLGGIFSKDLTRQVNVLVVGSTTNTNKFKFAVKHRFDIIFIDIQAIDDIYQLWLSGENILPDSNTATMTGSTYEMLKILYRRFSFKYLHNFNIFIGRITDTNITSIDSLVRSIKKLGCSSYNYQNFVIKDTSSHNDDDDQGQNGQISIFVTDTLLGARVNAAIEQNIPIVHFKWILDCQKRSALLPYDPYYLLPNIKDLPYDSIGSNSCDCWDKINTTFPTNIDAQSSLQRQQSSSTLTPSLPKTSSLLNKFKPKGEKIWDKAMSLQQHSKTNFSVLGQSPLSINNKQEDLSDNSTLIFKNCAFIIHHIFPGNHRSILTKIVVQNGGKIETSYLSGIYDHSYYIIPSNKALDSFNDLPEIIDDNDGIVTEFFIERCLYYQKLLHPIDLWSKPFLSTIEFQVSSSSKLLHHEFSSSPFLNVTITGFSGVELLHLTKVLNLLKPMGINYVEYLNKSTDILLINLAALPSIPKTHPLWSNEFSDLFTQFCINNNNDDPGDNNRKDFQNNSILRNSMKRKIEYIKKFHSIPVVTPAFIFKLLSAASGENNEIFLNNIKWCIICPRGHKDDFKCKIKKPYYTSISSEKKYQNNDPKIDKTILLKRNNSSLSEHSMKDTKNELLQKIRETDSGRKKRSVSSSIMDVSSERQMPDTKRIKLESLPKNFVPKQIKRTTSWGTIMSENVPTEQPTAISNPEEIPRTEEVSHTQVTYGSIQDKKRTASLEKPMRRQTRNQTKELDS | |
| 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 |
|---|---|---|---|---|---|
| 249 | Phosphorylation | KINTTFPTNIDAQSS HCCCCCCCCCCHHHH | 40.38 | 21440633 | |
| 255 | Phosphorylation | PTNIDAQSSLQRQQS CCCCCHHHHHHHHHC | 34.43 | 28889911 | |
| 256 | Phosphorylation | TNIDAQSSLQRQQSS CCCCHHHHHHHHHCC | 19.21 | 28889911 | |
| 262 | Phosphorylation | SSLQRQQSSSTLTPS HHHHHHHCCCCCCCC | 20.23 | 23749301 | |
| 263 | Phosphorylation | SLQRQQSSSTLTPSL HHHHHHCCCCCCCCC | 24.01 | 20377248 | |
| 275 | Phosphorylation | PSLPKTSSLLNKFKP CCCCCHHHHHHHCCC | 41.95 | 28889911 | |
| 308 | Phosphorylation | NFSVLGQSPLSINNK CCEECCCCCCCCCCC | 26.47 | 27214570 | |
| 631 | Phosphorylation | ILLKRNNSSLSEHSM HEEECCCCCCCHHHC | 35.88 | 23749301 | |
| 632 | Phosphorylation | LLKRNNSSLSEHSMK EEECCCCCCCHHHCH | 37.73 | 19823750 | |
| 637 | Phosphorylation | NSSLSEHSMKDTKNE CCCCCHHHCHHHHHH | 24.39 | 28889911 | |
| 660 | Phosphorylation | DSGRKKRSVSSSIMD CCCCCCCCCCHHCCC | 34.92 | 23749301 | |
| 662 | Phosphorylation | GRKKRSVSSSIMDVS CCCCCCCCHHCCCCC | 21.44 | 23749301 | |
| 684 | Phosphorylation | TKRIKLESLPKNFVP CCCEEHHHCCCCCCC | 61.48 | 28889911 | |
| 697 | Phosphorylation | VPKQIKRTTSWGTIM CCCCCEEECCHHHCC | 21.85 | 27017623 | |
| 698 | Phosphorylation | PKQIKRTTSWGTIMS CCCCEEECCHHHCCC | 26.90 | 27017623 | |
| 699 | Phosphorylation | KQIKRTTSWGTIMSE CCCEEECCHHHCCCC | 23.93 | 27017623 | |
| 702 | Phosphorylation | KRTTSWGTIMSENVP EEECCHHHCCCCCCC | 13.77 | 27017623 | |
| 737 | Phosphorylation | HTQVTYGSIQDKKRT CEEEEECCCCCHHHC | 13.48 | 30377154 | |
| 746 | Phosphorylation | QDKKRTASLEKPMRR CCHHHCCCCCHHHHH | 36.13 | 25752575 |
| 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 DPB11_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DPB11_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 DPB11_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-255; SER-256; SER-275;SER-662; SER-684 AND SER-746, AND MASS SPECTROMETRY. | |
