| UniProt ID | DPOD_YEAST | |
|---|---|---|
| UniProt AC | P15436 | |
| Protein Name | DNA polymerase delta catalytic subunit | |
| Gene Name | POL3 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1097 | |
| 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. POL3 contains the polymerase active site and most likely the active site for the 3'-5' exonuclease activity.. | |
| Protein Sequence | MSEKRSLPMVDVKIDDEDTPQLEKKIKRQSIDHGVGSEPVSTIEIIPSDSFRKYNSQGFKAKDTDLMGTQLESTFEQELSQMEHDMADQEEHDLSSFERKKLPTDFDPSLYDISFQQIDAEQSVLNGIKDENTSTVVRFFGVTSEGHSVLCNVTGFKNYLYVPAPNSSDANDQEQINKFVHYLNETFDHAIDSIEVVSKQSIWGYSGDTKLPFWKIYVTYPHMVNKLRTAFERGHLSFNSWFSNGTTTYDNIAYTLRLMVDCGIVGMSWITLPKGKYSMIEPNNRVSSCQLEVSINYRNLIAHPAEGDWSHTAPLRIMSFDIECAGRIGVFPEPEYDPVIQIANVVSIAGAKKPFIRNVFTLNTCSPITGSMIFSHATEEEMLSNWRNFIIKVDPDVIIGYNTTNFDIPYLLNRAKALKVNDFPYFGRLKTVKQEIKESVFSSKAYGTRETKNVNIDGRLQLDLLQFIQREYKLRSYTLNAVSAHFLGEQKEDVHYSIISDLQNGDSETRRRLAVYCLKDAYLPLRLMEKLMALVNYTEMARVTGVPFSYLLARGQQIKVVSQLFRKCLEIDTVIPNMQSQASDDQYEGATVIEPIRGYYDVPIATLDFNSLYPSIMMAHNLCYTTLCNKATVERLNLKIDEDYVITPNGDYFVTTKRRRGILPIILDELISARKRAKKDLRDEKDPFKRDVLNGRQLALKISANSVYGFTGATVGKLPCLAISSSVTAYGRTMILKTKTAVQEKYCIKNGYKHDAVVVYGDTDSVMVKFGTTDLKEAMDLGTEAAKYVSTLFKHPINLEFEKAYFPYLLINKKRYAGLFWTNPDKFDKLDQKGLASVRRDSCSLVSIVMNKVLKKILIERNVDGALAFVRETINDILHNRVDISKLIISKTLAPNYTNPQPHAVLAERMKRREGVGPNVGDRVDYVIIGGNDKLYNRAEDPLFVLENNIQVDSRYYLTNQLQNPIISIVAPIIGDKQANGMFVVKSIKINTGSQKGGLMSFIKKVEACKSCKGPLRKGEGPLCSNCLARSGELYIKALYDVRDLEEKYSRLWTQCQRCAGNLHSEVLCSNKNCDIFYMRVKVKKELQEKVEQLSKW | |
| 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 |
|---|---|---|---|---|---|
| 19 | Phosphorylation | VKIDDEDTPQLEKKI EECCCCCCHHHHHHH | 15.75 | 21551504 | |
| 24 | Acetylation | EDTPQLEKKIKRQSI CCCHHHHHHHHHHHC | 69.28 | 25381059 | |
| 30 | Phosphorylation | EKKIKRQSIDHGVGS HHHHHHHHCCCCCCC | 33.73 | 22369663 | |
| 37 | Phosphorylation | SIDHGVGSEPVSTIE HCCCCCCCCCCCEEE | 36.00 | 22369663 | |
| 41 | Phosphorylation | GVGSEPVSTIEIIPS CCCCCCCCEEEEECC | 34.09 | 22369663 | |
| 42 | Phosphorylation | VGSEPVSTIEIIPSD CCCCCCCEEEEECCC | 23.90 | 22369663 | |
| 48 | Phosphorylation | STIEIIPSDSFRKYN CEEEEECCCHHHHHC | 35.16 | 27017623 | |
| 50 | Phosphorylation | IEIIPSDSFRKYNSQ EEEECCCHHHHHCCC | 31.15 | 28889911 | |
| 53 | Acetylation | IPSDSFRKYNSQGFK ECCCHHHHHCCCCCC | 46.93 | 25381059 | |
| 56 | Phosphorylation | DSFRKYNSQGFKAKD CHHHHHCCCCCCCCC | 28.70 | 17563356 | |
| 60 | Acetylation | KYNSQGFKAKDTDLM HHCCCCCCCCCCCCC | 62.44 | 25381059 | |
| 157 | Ubiquitination | LCNVTGFKNYLYVPA EEECCCCCCEEEEEC | 46.13 | 17644757 | |
| 217 | Phosphorylation | KLPFWKIYVTYPHMV CCCEEEEEECCHHHH | 5.30 | 28889911 | |
| 219 | Phosphorylation | PFWKIYVTYPHMVNK CEEEEEECCHHHHHH | 17.86 | 28889911 | |
| 220 | Phosphorylation | FWKIYVTYPHMVNKL EEEEEECCHHHHHHH | 4.90 | 28889911 | |
| 226 | Acetylation | TYPHMVNKLRTAFER CCHHHHHHHHHHHHH | 28.12 | 24489116 | |
| 657 | Ubiquitination | GDYFVTTKRRRGILP CCEEEECCCCCCCHH | 34.24 | 17644757 | |
| 672 | Phosphorylation | IILDELISARKRAKK HHHHHHHHHHHHHHH | 34.35 | 22369663 | |
| 675 | Ubiquitination | DELISARKRAKKDLR HHHHHHHHHHHHHHC | 57.32 | 17644757 | |
| 724 | Phosphorylation | KLPCLAISSSVTAYG CCCEEEEECCEEECC | 15.79 | 19823750 | |
| 725 | Phosphorylation | LPCLAISSSVTAYGR CCEEEEECCEEECCC | 23.78 | 19823750 | |
| 726 | Phosphorylation | PCLAISSSVTAYGRT CEEEEECCEEECCCE | 19.39 | 19823750 | |
| 728 | Phosphorylation | LAISSSVTAYGRTMI EEEECCEEECCCEEE | 18.99 | 19823750 | |
| 730 | Phosphorylation | ISSSVTAYGRTMILK EECCEEECCCEEEEE | 9.58 | 19823750 | |
| 733 | Phosphorylation | SVTAYGRTMILKTKT CEEECCCEEEEEECC | 12.28 | 19823750 | |
| 794 | Acetylation | KYVSTLFKHPINLEF HHHHHHHCCCCCCCC | 52.13 | 24489116 | |
| 842 | Phosphorylation | LASVRRDSCSLVSIV CHHHCCCCCHHHHHH | 12.09 | 27017623 | |
| 891 | Ubiquitination | ISKLIISKTLAPNYT HHHHHHHCCCCCCCC | 36.83 | 17644757 | |
| 989 | Acetylation | MFVVKSIKINTGSQK EEEEEEEEECCCCCC | 36.67 | 25381059 | |
| 994 | Phosphorylation | SIKINTGSQKGGLMS EEEECCCCCCCCHHH | 27.04 | 30377154 | |
| 1001 | Phosphorylation | SQKGGLMSFIKKVEA CCCCCHHHHHHHHHH | 28.94 | 21440633 | |
| 1018 | Ubiquitination | SCKGPLRKGEGPLCS HCCCCCCCCCCCCCH | 69.83 | 23749301 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 56 | S | Phosphorylation | Kinase | ATM/ATR | - | GPS |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DPOD_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 DPOD_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-30; SER-37 AND SER-50,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-30 AND SER-56, AND MASSSPECTROMETRY. | |
| "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-30, AND MASSSPECTROMETRY. | |
| "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-30, AND MASSSPECTROMETRY. | |
