| UniProt ID | DUN1_YEAST | |
|---|---|---|
| UniProt AC | P39009 | |
| Protein Name | DNA damage response protein kinase DUN1 | |
| Gene Name | DUN1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 513 | |
| Subcellular Localization | Nucleus. | |
| Protein Description | Transducer of the DNA damage signal. Phosphorylates SML1 on serine residues. Cooperates with the PAN deadenylation complex in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress.. | |
| Protein Sequence | MSLSTKREHSGDVTDSSFKRQQRSNKPSSEYTCLGHLVNLIPGKEQKVEITNRNVTTIGRSRSCDVILSEPDISTFHAEFHLLQMDVDNFQRNLINVIDKSRNGTFINGNRLVKKDYILKNGDRIVFGKSCSFLFKYASSSSTDIENDDEKVSSESRSYKNDDEVFKKPQISATSSQNATTSAAIRKLNKTRPVSFFDKYLLGKELGAGHYALVKEAKNKKTGQQVAVKIFHAQQNDDQKKNKQFREETNILMRVQHPNIVNLLDSFVEPISKSQIQKYLVLEKIDDGELFERIVRKTCLRQDESKALFKQLLTGLKYLHEQNIIHRDIKPENILLNITRRENPSQVQLGPWDEDEIDIQVKIADFGLAKFTGEMQFTNTLCGTPSYVAPEVLTKKGYTSKVDLWSAGVILYVCLCGFPPFSDQLGPPSLKEQILQAKYAFYSPYWDKIDDSVLHLISNLLVLNPDERYNIDEALNHPWFNDIQQQSSVSLELQRLQITDNKIPKTYSELSCL | |
| 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 |
|---|---|---|---|---|---|
| 10 | Phosphorylation | LSTKREHSGDVTDSS CCCCCCCCCCCCHHH | 31.75 | 19823750 | |
| 14 | Phosphorylation | REHSGDVTDSSFKRQ CCCCCCCCHHHHHHH | 34.60 | 29136822 | |
| 16 | Phosphorylation | HSGDVTDSSFKRQQR CCCCCCHHHHHHHHH | 28.45 | 17287358 | |
| 17 | Phosphorylation | SGDVTDSSFKRQQRS CCCCCHHHHHHHHHC | 37.28 | 17287358 | |
| 19 | Acetylation | DVTDSSFKRQQRSNK CCCHHHHHHHHHCCC | 51.77 | 25381059 | |
| 24 | Phosphorylation | SFKRQQRSNKPSSEY HHHHHHHCCCCCCHH | 44.88 | 17114794 | |
| 28 | Phosphorylation | QQRSNKPSSEYTCLG HHHCCCCCCHHHHHH | 37.09 | 30377154 | |
| 29 | Phosphorylation | QRSNKPSSEYTCLGH HHCCCCCCHHHHHHH | 43.05 | 28889911 | |
| 32 | Phosphorylation | NKPSSEYTCLGHLVN CCCCCHHHHHHHHHH | 9.37 | 30377154 | |
| 101 | Phosphorylation | LINVIDKSRNGTFIN HHHHHHHHCCCCEEC | 27.51 | 30377154 | |
| 105 | Phosphorylation | IDKSRNGTFINGNRL HHHHCCCCEECCCEE | 25.54 | 28889911 | |
| 130 | Phosphorylation | DRIVFGKSCSFLFKY CEEEECCCHHHHHHH | 18.51 | 28889911 | |
| 132 | Phosphorylation | IVFGKSCSFLFKYAS EEECCCHHHHHHHCC | 31.88 | 17114794 | |
| 137 | Phosphorylation | SCSFLFKYASSSSTD CHHHHHHHCCCCCCC | 12.37 | 23749301 | |
| 139 | Phosphorylation | SFLFKYASSSSTDIE HHHHHHCCCCCCCCC | 27.88 | 22369663 | |
| 140 | Phosphorylation | FLFKYASSSSTDIEN HHHHHCCCCCCCCCC | 21.82 | 25521595 | |
| 141 | Phosphorylation | LFKYASSSSTDIEND HHHHCCCCCCCCCCC | 34.46 | 22369663 | |
| 142 | Phosphorylation | FKYASSSSTDIENDD HHHCCCCCCCCCCCC | 31.85 | 22369663 | |
| 143 | Phosphorylation | KYASSSSTDIENDDE HHCCCCCCCCCCCCC | 42.83 | 22369663 | |
| 151 | Ubiquitination | DIENDDEKVSSESRS CCCCCCCCCCHHHHH | 55.18 | 23749301 | |
| 151 | Acetylation | DIENDDEKVSSESRS CCCCCCCCCCHHHHH | 55.18 | 24489116 | |
| 153 | Phosphorylation | ENDDEKVSSESRSYK CCCCCCCCHHHHHCC | 39.18 | 23749301 | |
| 154 | Phosphorylation | NDDEKVSSESRSYKN CCCCCCCHHHHHCCC | 42.45 | 30377154 | |
| 158 | Phosphorylation | KVSSESRSYKNDDEV CCCHHHHHCCCCHHH | 50.14 | 17287358 | |
| 159 | Phosphorylation | VSSESRSYKNDDEVF CCHHHHHCCCCHHHH | 16.83 | 21440633 | |
| 172 | Phosphorylation | VFKKPQISATSSQNA HHCCCCCEECCCCCC | 21.90 | 17114794 | |
| 174 | Phosphorylation | KKPQISATSSQNATT CCCCCEECCCCCCCH | 23.32 | 30377154 | |
| 175 | Phosphorylation | KPQISATSSQNATTS CCCCEECCCCCCCHH | 29.64 | 17114794 | |
| 176 | Phosphorylation | PQISATSSQNATTSA CCCEECCCCCCCHHH | 24.09 | 17114794 | |
| 180 | Phosphorylation | ATSSQNATTSAAIRK ECCCCCCCHHHHHHH | 28.91 | 30377154 | |
| 181 | Phosphorylation | TSSQNATTSAAIRKL CCCCCCCHHHHHHHH | 17.60 | 30377154 | |
| 195 | Phosphorylation | LNKTRPVSFFDKYLL HHCCCCCCHHHHHHH | 23.91 | 17114794 | |
| 199 | Acetylation | RPVSFFDKYLLGKEL CCCCHHHHHHHCCCC | 32.42 | 24489116 | |
| 266 | Phosphorylation | NIVNLLDSFVEPISK CHHHHHHHHCCCCCH | 31.03 | 17114794 | |
| 272 | Phosphorylation | DSFVEPISKSQIQKY HHHCCCCCHHHHHHH | 36.65 | 30377154 | |
| 274 | Phosphorylation | FVEPISKSQIQKYLV HCCCCCHHHHHHHEE | 26.23 | 17114794 | |
| 310 | Acetylation | DESKALFKQLLTGLK HHHHHHHHHHHHHHH | 40.67 | 24489116 | |
| 345 | Phosphorylation | ITRRENPSQVQLGPW EEECCCCCCCCCCCC | 55.34 | 17114794 | |
| 372 | Phosphorylation | DFGLAKFTGEMQFTN CCCCCEECCEEEEEC | 31.37 | 28889911 | |
| 378 | Phosphorylation | FTGEMQFTNTLCGTP ECCEEEEECCCCCCC | 15.48 | 17114794 | |
| 380 | Phosphorylation | GEMQFTNTLCGTPSY CEEEEECCCCCCCCC | 21.99 | 17114794 | |
| 487 | Phosphorylation | FNDIQQQSSVSLELQ HHCHHHHHCCEEEEE | 28.50 | 30377154 | |
| 488 | Phosphorylation | NDIQQQSSVSLELQR HCHHHHHCCEEEEEE | 16.04 | 17114794 | |
| 490 | Phosphorylation | IQQQSSVSLELQRLQ HHHHHCCEEEEEEHH | 20.34 | 17114794 | |
| 506 | Phosphorylation | TDNKIPKTYSELSCL CCCCCCCCHHHHCCC | 27.25 | 21440633 | |
| 507 | Phosphorylation | DNKIPKTYSELSCL- CCCCCCCHHHHCCC- | 13.28 | 30377154 | |
| 508 | Phosphorylation | NKIPKTYSELSCL-- CCCCCCHHHHCCC-- | 36.97 | 21440633 | |
| 511 | Phosphorylation | PKTYSELSCL----- CCCHHHHCCC----- | 14.88 | 21440633 |
| 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 DUN1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DUN1_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 DUN1_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-10; SER-17; SER-130;SER-132; SER-139; SER-141; SER-142; SER-158; SER-176; THR-372; THR-378AND THR-380, 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-10; SER-17; SER-139;SER-140 AND SER-141, 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-10; SER-16; SER-17 ANDSER-158, AND MASS SPECTROMETRY. | |
