UniProt ID | DPB3_YEAST | |
---|---|---|
UniProt AC | P27344 | |
Protein Name | DNA polymerase epsilon subunit C | |
Gene Name | DPB3 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 201 | |
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.. | |
Protein Sequence | MSNLVKEKAPVFPISKVKKIAKCDPEYVITSNVAISATAFAAELFVQNLVEESLVLAQLNSKGKTSLRLSLNSIEECVEKRDNFRFLEDAIKQLKKNSALDKKRELNMQPGRSDQEVVIEEPELHEDDGVEEEEEEDEVSEEEEPVHNEELLDDSKDQQNDKSTRSVASLLSRFQYKSALDVGEHSDSSDIEVDHTKSTDP | |
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 |
---|---|---|---|---|---|
163 | Phosphorylation | KDQQNDKSTRSVASL CHHHCCHHHHHHHHH | 31.73 | 24961812 | |
164 | Phosphorylation | DQQNDKSTRSVASLL HHHCCHHHHHHHHHH | 32.48 | 24961812 | |
166 | Phosphorylation | QNDKSTRSVASLLSR HCCHHHHHHHHHHHH | 23.32 | 22369663 | |
169 | Phosphorylation | KSTRSVASLLSRFQY HHHHHHHHHHHHHHH | 27.90 | 22369663 | |
178 | Phosphorylation | LSRFQYKSALDVGEH HHHHHHCCCCCCCCC | 29.18 | 22890988 | |
186 | Phosphorylation | ALDVGEHSDSSDIEV CCCCCCCCCCCCCCC | 34.58 | 22369663 | |
188 | Phosphorylation | DVGEHSDSSDIEVDH CCCCCCCCCCCCCCC | 32.69 | 22369663 | |
189 | Phosphorylation | VGEHSDSSDIEVDHT CCCCCCCCCCCCCCC | 47.82 | 22369663 | |
196 | Phosphorylation | SDIEVDHTKSTDP-- CCCCCCCCCCCCC-- | 23.40 | 22890988 | |
198 | Phosphorylation | IEVDHTKSTDP---- CCCCCCCCCCC---- | 38.92 | 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 DPB3_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DPB3_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 DPB3_YEAST !! |
Kegg Drug | ||||||
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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-166; SER-169; SER-186;SER-188 AND SER-189, 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-186; SER-188 ANDSER-189, 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-186 AND SER-189, ANDMASS SPECTROMETRY. | |
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND MASSSPECTROMETRY. |