| UniProt ID | DPB4_YEAST | |
|---|---|---|
| UniProt AC | Q04603 | |
| Protein Name | DNA polymerase epsilon subunit D | |
| Gene Name | DPB4 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 196 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | DNA polymerase epsilon (DNA polymerase II) participates in chromosomal DNA replication. It is required during synthesis of the leading and lagging DNA strands at the replication fork and binds at/or near replication origins and moves along DNA with the replication fork. It has 3'-5' proofreading exonuclease activity that correct errors arising during DNA replication. It is also involved in DNA synthesis during DNA repair. Also functions as component of the ISW2 complex, which acts in remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. The ISW2 complex is involved in coordinating transcriptional repression and in inheritance of telomeric silencing. It is involved in repression of MAT a-specific genes, INO1, and early meiotic genes during mitotic growth dependent upon transcription factor UME6 and in a parallel pathway to the RPD3-SIN3 histone deacetylase complex.. | |
| Protein Sequence | MPPKGWRKDAQGNYPTTSYIKEQENITIQDLLFPKSTIVNLAREVPQQSGKKLLINKDASLALQRGATVFVNHLLLFAREIAKSQDKKSCSVDDVLSALDHIGHSALKGPVRDKLDEYQAAVEQRKKEKLDSGEVDADGDIDMGEDKENVPVEKVKEHDEIEEQGDALQDVEESSEKKQKTESQDVETRVQNLEQT | |
| 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 |
|---|---|---|---|---|---|
| 16 | Phosphorylation | DAQGNYPTTSYIKEQ CCCCCCCCCHHHCHH | 20.29 | 30377154 | |
| 18 | Phosphorylation | QGNYPTTSYIKEQEN CCCCCCCHHHCHHCC | 27.60 | 28889911 | |
| 97 | Phosphorylation | CSVDDVLSALDHIGH CCHHHHHHHHHHHCH | 27.00 | 21440633 | |
| 114 | Ubiquitination | LKGPVRDKLDEYQAA HCCCHHHHHHHHHHH | 47.47 | 23749301 | |
| 114 | Acetylation | LKGPVRDKLDEYQAA HCCCHHHHHHHHHHH | 47.47 | 24489116 | |
| 118 | Phosphorylation | VRDKLDEYQAAVEQR HHHHHHHHHHHHHHH | 11.79 | 27017623 | |
| 174 | Phosphorylation | ALQDVEESSEKKQKT HHHHHHHHHHHHHHH | 30.23 | 24961812 | |
| 175 | Phosphorylation | LQDVEESSEKKQKTE HHHHHHHHHHHHHHH | 57.63 | 24961812 | |
| 177 | Acetylation | DVEESSEKKQKTESQ HHHHHHHHHHHHHHH | 63.55 | 24489116 | |
| 181 | Phosphorylation | SSEKKQKTESQDVET HHHHHHHHHHHHHHH | 38.07 | 19823750 | |
| 183 | Phosphorylation | EKKQKTESQDVETRV HHHHHHHHHHHHHHH | 36.59 | 20190278 | |
| 188 | Phosphorylation | TESQDVETRVQNLEQ HHHHHHHHHHHHHHC | 35.67 | 28889911 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DPB4_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 DPB4_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-18 AND SER-183, 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-183, AND MASSSPECTROMETRY. | |
