UniProt ID | DPB2_YEAST | |
---|---|---|
UniProt AC | P24482 | |
Protein Name | DNA polymerase epsilon subunit B | |
Gene Name | DPB2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 689 | |
Subcellular Localization | Cytoplasm . 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 | MFGSGNVLPVKIQPPLLRPLAYRVLSRKYGLSIKSDGLSALAEFVGTNIGANWRQGPATIKFLEQFAAVWKQQERGLFIDQSGVKEVIQEMKEREKVEWSHEHPIQHEENILGRTDDDENNSDDEMPIAADSSLQNVSLSSPMRQPTERDEYKQPFKPESSKALDWRDYFKVINASQQQRFSYNPHKMQFIFVPNKKQNGLGGIAGFLPDIEDKVQMFLTRYYLTNDRVMRNENFQNSDMFNPLSSMVSLQNELSNTNRQQQSSSMSITPIKNLLGRDAQNFLLLGLLNKNFKGNWSLEDPSGSVEIDISQTIPTQGHYYVPGCMVLVEGIYYSVGNKFHVTSMTLPPGERREITLETIGNLDLLGIHGISNNNFIARLDKDLKIRLHLLEKELTDHKFVILGANLFLDDLKIMTALSKILQKLNDDPPTLLIWQGSFTSVPVFASMSSRNISSSTQFKNNFDALATLLSRFDNLTENTTMIFIPGPNDLWGSMVSLGASGTLPQDPIPSAFTKKINKVCKNVVWSSNPTRIAYLSQEIVIFRDDLSGRFKRHRLEFPFNESEDVYTENDNMMSKDTDIVPIDELVKEPDQLPQKVQETRKLVKTILDQGHLSPFLDSLRPISWDLDHTLTLCPIPSTMVLCDTTSAQFDLTYNGCKVINPGSFIHNRRARYMEYVPSSKKTIQEEIYI | |
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 |
---|---|---|---|---|---|
4 | Phosphorylation | ----MFGSGNVLPVK ----CCCCCCEECCC | 18.87 | 30377154 | |
115 | Phosphorylation | EENILGRTDDDENNS CHHCCCCCCCCCCCC | 41.82 | 28132839 | |
122 | Phosphorylation | TDDDENNSDDEMPIA CCCCCCCCCCCCCCC | 59.00 | 23749301 | |
138 | Phosphorylation | DSSLQNVSLSSPMRQ CCCCCCCCCCCCCCC | 30.04 | 27017623 | |
141 | Phosphorylation | LQNVSLSSPMRQPTE CCCCCCCCCCCCCCC | 28.19 | 14747467 | |
238 | Phosphorylation | RNENFQNSDMFNPLS CCCCCCCCCCCCHHH | 21.48 | 27017623 | |
246 | Phosphorylation | DMFNPLSSMVSLQNE CCCCHHHHHHHHHHH | 30.77 | 27017623 | |
255 | Phosphorylation | VSLQNELSNTNRQQQ HHHHHHHHCCCHHHH | 35.11 | 27017623 | |
392 | Acetylation | IRLHLLEKELTDHKF HHHHHHHHHCCCCCE | 58.98 | 24489116 | |
415 | Phosphorylation | LDDLKIMTALSKILQ HHHHHHHHHHHHHHH | 28.11 | 26447709 | |
419 | Ubiquitination | KIMTALSKILQKLND HHHHHHHHHHHHHCC | 48.57 | 24961812 | |
613 | Phosphorylation | ILDQGHLSPFLDSLR HHHCCCCHHHHHHCC | 14.13 | 14747467 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
141 | S | Phosphorylation | Kinase | CDC28 | P00546 | Uniprot |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
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Oops, there are no SNP-PTM records of DPB2_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Cell cycle-dependent phosphorylation of the DNA polymerase epsilonsubunit, Dpb2, by the Cdc28 cyclin-dependent protein kinase."; Kesti T., McDonald W.H., Yates J.R. III, Wittenberg C.; J. Biol. Chem. 279:14245-14255(2004). Cited for: PROTEIN SEQUENCE OF 132-144 AND 606-622, PHOSPHORYLATION AT SER-141AND SER-613, AND MASS SPECTROMETRY. |