| UniProt ID | DPOE_YEAST | |
|---|---|---|
| UniProt AC | P21951 | |
| Protein Name | DNA polymerase epsilon catalytic subunit A | |
| Gene Name | POL2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 2222 | |
| 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 | MMFGKKKNNGGSSTARYSAGNKYNTLSNNYALSAQQLLNASKIDDIDSMMGFERYVPPQYNGRFDAKDIDQIPGRVGWLTNMHATLVSQETLSSGSNGGGNSNDGERVTTNQGISGVDFYFLDEEGGSFKSTVVYDPYFFIACNDESRVNDVEELVKKYLESCLKSLQIIRKEDLTMDNHLLGLQKTLIKLSFVNSNQLFEARKLLRPILQDNANNNVQRNIYNVAANGSEKVDAKHLIEDIREYDVPYHVRVSIDKDIRVGKWYKVTQQGFIEDTRKIAFADPVVMAFDIETTKPPLKFPDSAVDQIMMISYMIDGEGFLITNREIISEDIEDFEYTPKPEYPGFFTIFNENDEVALLQRFFEHIRDVRPTVISTFNGDFFDWPFIHNRSKIHGLDMFDEIGFAPDAEGEYKSSYCSHMDCFRWVKRDSYLPQGSQGLKAVTQSKLGYNPIELDPELMTPYAFEKPQHLSEYSVSDAVATYYLYMKYVHPFIFSLCTIIPLNPDETLRKGTGTLCEMLLMVQAYQHNILLPNKHTDPIERFYDGHLLESETYVGGHVESLEAGVFRSDLKNEFKIDPSAIDELLQELPEALKFSVEVENKSSVDKVTNFEEIKNQITQKLLELKENNIRNELPLIYHVDVASMYPNIMTTNRLQPDSIKAERDCASCDFNRPGKTCARKLKWAWRGEFFPSKMDEYNMIKRALQNETFPNKNKFSKKKVLTFDELSYADQVIHIKKRLTEYSRKVYHRVKVSEIVEREAIVCQRENPFYVDTVKSFRDRRYEFKGLAKTWKGNLSKIDPSDKHARDEAKKMIVLYDSLQLAHKVILNSFYGYVMRKGSRWYSMEMAGITCLTGATIIQMARALVERVGRPLELDTDGIWCILPKSFPETYFFTLENGKKLYLSYPCSMLNYRVHQKFTNHQYQELKDPLNYIYETHSENTIFFEVDGPYKAMILPSSKEEGKGIKKRYAVFNEDGSLAELKGFELKRRGELQLIKNFQSDIFKVFLEGDTLEGCYSAVASVCNRWLDVLDSHGLMLEDEDLVSLICENRSMSKTLKEYEGQKSTSITTARRLGDFLGEDMVKDKGLQCKYIISSKPFNAPVTERAIPVAIFSADIPIKRSFLRRWTLDPSLEDLDIRTIIDWGYYRERLGSAIQKIITIPAALQGVSNPVPRVEHPDWLKRKIATKEDKFKQTSLTKFFSKTKNVPTMGKIKDIEDLFEPTVEEDNAKIKIARTTKKKAVSKRKRNQLTNEEDPLVLPSEIPSMDEDYVGWLNYQKIKWKIQARDRKRRDQLFGNTNSSRERSALGSMIRKQAESYANSTWEVLQYKDSGEPGVLEVFVTINGKVQNITFHIPKTIYMKFKSQTMPLQKIKNCLIEKSSASLPNNPKTSNPAGGQLFKITLPESVFLEEKENCTSIFNDENVLGVFEGTITPHQRAIMDLGASVTFRSKAMGALGKGIQQGFEMKDLSMAENERYLSGFSMDIGYLLHFPTSIGYEFFSLFKSWGDTITILVLKPSNQAQEINASSLGQIYKQMFEKKKGKIETYSYLVDIKEDINFEFVYFTDISKLYRRLSQETTKLKEERGLQFLLLLQSPFITKLLGTIRLLNQMPIVKLSLNEVLLPQLNWQPTLLKKLVNHVLSSGSWISHLIKLSQYSNIPICNLRLDSMDYIIDVLYARKLKKENIVLWWNEKAPLPDHGGIQNDFDLNTSWIMNDSEFPKINNSGVYDNVVLDVGVDNLTVNTILTSALINDAEGSDLVNNNMGIDDKDAVINSPSEFVHDAFSNDALNVLRGMLKEWWDEALKENSTADLLVNSLASWVQNPNAKLFDGLLRYHVHNLTKKALLQLVNEFSALGSTIVYADRNQILIKTNKYSPENCYAYSQYMMKAVRTNPMFSYLDLNIKRYWDLLIWMDKFNFSGLACIEIEEKENQDYTAVSQWQLKKFLSPIYQPEFEDWMMIILDSMLKTKQSYLKLNSGTQRPTQIVNVKKQDKEDSVENSLNGFSHLFSKPLMKRVKKLFKNQQEFILDPQYEADYVIPVLPGSHLNVKNPLLELVKSLCHVMLLSKSTILEIRTLRKELLKIFELREFAKVAEFKDPSLSLVVPDFLCEYCFFISDIDFCKAAPESIFSCVRCHKAFNQVLLQEHLIQKLRSDIESYLIQDLRCSRCHKVKRDYMSAHCPCAGAWEGTLPRESIVQKLNVFKQVAKYYGFDILLSCIADLTI | |
| 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 |
|---|---|---|---|---|---|
| 12 | Phosphorylation | KKKNNGGSSTARYSA CCCCCCCCCCCCCCC | 26.39 | 17563356 | |
| 22 | Acetylation | ARYSAGNKYNTLSNN CCCCCCCCCCCCCCC | 38.67 | 24489116 | |
| 23 | Phosphorylation | RYSAGNKYNTLSNNY CCCCCCCCCCCCCCC | 19.85 | 29136822 | |
| 25 | Phosphorylation | SAGNKYNTLSNNYAL CCCCCCCCCCCCCCC | 28.59 | 30377154 | |
| 27 | Phosphorylation | GNKYNTLSNNYALSA CCCCCCCCCCCCCCH | 22.46 | 29136822 | |
| 30 | Phosphorylation | YNTLSNNYALSAQQL CCCCCCCCCCCHHHH | 17.11 | 29136822 | |
| 33 | Phosphorylation | LSNNYALSAQQLLNA CCCCCCCCHHHHHCC | 18.83 | 29136822 | |
| 257 | Ubiquitination | HVRVSIDKDIRVGKW EEEEEECCCCCCCEE | 54.08 | 21427232 | |
| 415 | Phosphorylation | AEGEYKSSYCSHMDC CCCCCCCCCCCHHHH | 26.46 | 19779198 | |
| 416 | Phosphorylation | EGEYKSSYCSHMDCF CCCCCCCCCCHHHHH | 12.69 | 19779198 | |
| 418 | Phosphorylation | EYKSSYCSHMDCFRW CCCCCCCCHHHHHHH | 17.39 | 19779198 | |
| 1063 | Ubiquitination | LKEYEGQKSTSITTA HHHHCCCCCCCHHHH | 67.56 | 23749301 | |
| 1065 | Phosphorylation | EYEGQKSTSITTARR HHCCCCCCCHHHHHH | 31.05 | 19779198 | |
| 1066 | Phosphorylation | YEGQKSTSITTARRL HCCCCCCCHHHHHHH | 25.65 | 19779198 | |
| 1068 | Phosphorylation | GQKSTSITTARRLGD CCCCCCHHHHHHHHH | 17.73 | 19779198 | |
| 1198 | Acetylation | FKQTSLTKFFSKTKN HCHHHHHHHHHCCCC | 50.10 | 22865919 | |
| 1222 | Phosphorylation | IEDLFEPTVEEDNAK HHHHHCCCCCCCCCE | 33.09 | 27017623 | |
| 1297 | Phosphorylation | RDQLFGNTNSSRERS HHHHCCCCCCHHHHH | 36.54 | 28889911 | |
| 1304 | Phosphorylation | TNSSRERSALGSMIR CCCHHHHHHHHHHHH | 24.08 | 21126336 | |
| 1308 | Phosphorylation | RERSALGSMIRKQAE HHHHHHHHHHHHHHH | 16.34 | 30377154 | |
| 1676 | Phosphorylation | DYIIDVLYARKLKKE HHHHHHHHHHHCCCC | 12.28 | 28132839 | |
| 1774 | Phosphorylation | DKDAVINSPSEFVHD CCCCCCCCHHHHHHH | 20.76 | 22369663 | |
| 1776 | Phosphorylation | DAVINSPSEFVHDAF CCCCCCHHHHHHHHC | 43.41 | 22369663 | |
| 1873 | Phosphorylation | ILIKTNKYSPENCYA EEEECCCCCHHHHHH | 31.37 | 30377154 | |
| 1874 | Phosphorylation | LIKTNKYSPENCYAY EEECCCCCHHHHHHH | 27.61 | 30377154 | |
| 1879 | Phosphorylation | KYSPENCYAYSQYMM CCCHHHHHHHHHHHH | 21.84 | 19779198 | |
| 1881 | Phosphorylation | SPENCYAYSQYMMKA CHHHHHHHHHHHHHH | 3.06 | 30377154 | |
| 1882 | Phosphorylation | PENCYAYSQYMMKAV HHHHHHHHHHHHHHH | 13.48 | 30377154 | |
| 1884 | Phosphorylation | NCYAYSQYMMKAVRT HHHHHHHHHHHHHHH | 8.01 | 30377154 | |
| 1976 | Phosphorylation | QSYLKLNSGTQRPTQ HHHHHCCCCCCCCEE | 54.37 | 30377154 | |
| 1995 | Phosphorylation | KKQDKEDSVENSLNG ECCCCHHHHHHHCCH | 32.21 | 29136822 | |
| 1999 | Phosphorylation | KEDSVENSLNGFSHL CHHHHHHHCCHHHHH | 15.09 | 29136822 | |
| 2004 | Phosphorylation | ENSLNGFSHLFSKPL HHHCCHHHHHHCHHH | 22.22 | 29136822 | |
| 2008 | Phosphorylation | NGFSHLFSKPLMKRV CHHHHHHCHHHHHHH | 39.46 | 29136822 |
| 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 DPOE_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DPOE_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 DPOE_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "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-12, AND MASSSPECTROMETRY. | |
