| UniProt ID | DPOD3_YEAST | |
|---|---|---|
| UniProt AC | P47110 | |
| Protein Name | DNA polymerase delta subunit 3 | |
| Gene Name | POL32 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 350 | |
| Subcellular Localization | Nucleus. | |
| Protein Description | DNA polymerase delta (DNA polymerase III) 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.. | |
| Protein Sequence | MDQKASYFINEKLFTEVKPVLFTDLIHHLKIGPSMAKKLMFDYYKQTTNAKYNCVVICCYKDQTIKIIHDLSNIPQQDSIIDCFIYAFNPMDSFIPYYDIIDQKDCLTIKNSYELKVSESSKIIERTKTLEEKSKPLVRPTARSKTTPEETTGRKSKSKDMGLRSTALLAKMKKDRDDKETSRQNELRKRKEENLQKINKQNPEREAQMKELNNLFVEDDLDTEEVNGGSKPNSPKETDSNDKDKNNDDLEDLLETTAEDSLMDVPKIQQTKPSETEHSKEPKSEEEPSSFIDEDGYIVTKRPATSTPPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK | |
| 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 |
|---|---|---|---|---|---|
| 112 | Phosphorylation | DCLTIKNSYELKVSE HCEEECCCEEEEECC | 18.25 | 27017623 | |
| 113 | Phosphorylation | CLTIKNSYELKVSES CEEECCCEEEEECCH | 34.37 | 27017623 | |
| 127 | Phosphorylation | SSKIIERTKTLEEKS HHHHHHHHCCHHHHC | 18.65 | 21440633 | |
| 129 | Phosphorylation | KIIERTKTLEEKSKP HHHHHHCCHHHHCCC | 38.50 | 21440633 | |
| 146 | Phosphorylation | RPTARSKTTPEETTG CCCCCCCCCCCHHCC | 49.15 | 27214570 | |
| 197 | Acetylation | RKEENLQKINKQNPE HHHHHHHHHHHCCHH | 51.95 | 25381059 | |
| 223 | Phosphorylation | FVEDDLDTEEVNGGS CCCCCCCCCCCCCCC | 41.14 | 19823750 | |
| 230 | Phosphorylation | TEEVNGGSKPNSPKE CCCCCCCCCCCCCCC | 46.46 | 22369663 | |
| 234 | Phosphorylation | NGGSKPNSPKETDSN CCCCCCCCCCCCCCC | 45.97 | 22369663 | |
| 238 | Phosphorylation | KPNSPKETDSNDKDK CCCCCCCCCCCCCCC | 51.35 | 21440633 | |
| 240 | Phosphorylation | NSPKETDSNDKDKNN CCCCCCCCCCCCCCC | 55.11 | 21551504 | |
| 256 | Phosphorylation | DLEDLLETTAEDSLM CHHHHHHHHHHHHHC | 31.13 | 21551504 | |
| 257 | Phosphorylation | LEDLLETTAEDSLMD HHHHHHHHHHHHHCC | 20.76 | 21440633 | |
| 261 | Phosphorylation | LETTAEDSLMDVPKI HHHHHHHHHCCCCCH | 19.66 | 21551504 | |
| 279 | Phosphorylation | KPSETEHSKEPKSEE CCCCCCCCCCCCCCC | 32.27 | 28889911 | |
| 284 | Phosphorylation | EHSKEPKSEEEPSSF CCCCCCCCCCCCCCC | 62.04 | 25521595 | |
| 289 | Phosphorylation | PKSEEEPSSFIDEDG CCCCCCCCCCCCCCC | 40.95 | 22369663 | |
| 290 | Phosphorylation | KSEEEPSSFIDEDGY CCCCCCCCCCCCCCC | 36.62 | 22369663 | |
| 297 | Phosphorylation | SFIDEDGYIVTKRPA CCCCCCCCEEEECCC | 12.44 | 19823750 | |
| 300 | Phosphorylation | DEDGYIVTKRPATST CCCCCEEEECCCCCC | 16.27 | 19823750 | |
| 305 | Phosphorylation | IVTKRPATSTPPRKP EEEECCCCCCCCCCC | 35.50 | 19823750 | |
| 306 | Phosphorylation | VTKRPATSTPPRKPS EEECCCCCCCCCCCC | 40.81 | 29136822 | |
| 307 | Phosphorylation | TKRPATSTPPRKPSP EECCCCCCCCCCCCH | 32.72 | 19823750 | |
| 313 | Phosphorylation | STPPRKPSPVVKRAL CCCCCCCCHHHHHHH | 33.10 | 19823750 | |
| 325 | Acetylation | RALSSSKKQETPSSN HHHCCCCCCCCCCCC | 56.14 | 25381059 | |
| 333 | Acetylation | QETPSSNKRLKKQGT CCCCCCCHHHHHHCC | 62.14 | 25381059 | |
| 340 | Phosphorylation | KRLKKQGTLESFFKR HHHHHHCCHHHHHHH | 25.51 | 20377248 |
| 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 DPOD3_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DPOD3_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 DPOD3_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-234 AND SER-313, ANDMASS 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 THR-307 AND SER-313, ANDMASS SPECTROMETRY. | |
