| UniProt ID | DPOA_YEAST | |
|---|---|---|
| UniProt AC | P13382 | |
| Protein Name | DNA polymerase alpha catalytic subunit A | |
| Gene Name | POL1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1468 | |
| Subcellular Localization | Nucleus. | |
| Protein Description | Catalytic component of DNA polymerase alpha, which in complex with DNA primase (DNA polymerase alpha:primase) constitutes a replicative polymerase. POL1 has a role in promoting telomere replication during interaction with CDC13.. | |
| Protein Sequence | MSSKSEKLEKLRKLQAARNGTSIDDYEGDESDGDRIYDEIDEKEYRARKRQELLHDDFVVDDDGVGYVDRGVEEDWREVDNSSSDEDTGNLASKDSKRKKNIKREKDHQITDMLRTQHSKSTLLAHAKKSQKKSIPIDNFDDILGEFESGEVEKPNILLPSKLRENLNSSPTSEFKSSIKRVNGNDESSHDAGISKKVKIDPDSSTDKYLEIESSPLKLQSRKLRYANDVQDLLDDVENSPVVATKRQNVLQDTLLANPPSAQSLADEEDDEDSDEDIILKRRTMRSVTTTRRVNIDSRSNPSTSPFVTAPGTPIGIKGLTPSKSLQSNTDVATLAVNVKKEDVVDPETDTFQMFWLDYCEVNNTLILFGKVKLKDDNCVSAMVQINGLCRELFFLPREGKTPTDIHEEIIPLLMDKYGLDNIRAKPQKMKYSFELPDIPSESDYLKVLLPYQTPKSSRDTIPSDLSSDTFYHVFGGNSNIFESFVIQNRIMGPCWLDIKGADFNSIRNASHCAVEVSVDKPQNITPTTTKTMPNLRCLSLSIQTLMNPKENKQEIVSITLSAYRNISLDSPIPENIKPDDLCTLVRPPQSTSFPLGLAALAKQKLPGRVRLFNNEKAMLSCFCAMLKVEDPDVIIGHRLQNVYLDVLAHRMHDLNIPTFSSIGRRLRRTWPEKFGRGNSNMNHFFISDICSGRLICDIANEMGQSLTPKCQSWDLSEMYQVTCEKEHKPLDIDYQNPQYQNDVNSMTMALQENITNCMISAEVSYRIQLLTLTKQLTNLAGNAWAQTLGGTRAGRNEYILLHEFSRNGFIVPDKEGNRSRAQKQRQNEENADAPVNSKKAKYQGGLVFEPEKGLHKNYVLVMDFNSLYPSIIQEFNICFTTVDRNKEDIDELPSVPPSEVDQGVLPRLLANLVDRRREVKKVMKTETDPHKRVQCDIRQQALKLTANSMYGCLGYVNSRFYAKPLAMLVTNKGREILMNTRQLAESMNLLVVYGDTDSVMIDTGCDNYADAIKIGLGFKRLVNERYRLLEIDIDNVFKKLLLHAKKKYAALTVNLDKNGNGTTVLEVKGLDMKRREFCPLSRDVSIHVLNTILSDKDPEEALQEVYDYLEDIRIKVETNNIRIDKYKINMKLSKDPKAYPGGKNMPAVQVALRMRKAGRVVKAGSVITFVITKQDEIDNAADTPALSVAERAHALNEVMIKSNNLIPDPQYYLEKQIFAPVERLLERIDSFNVVRLSEALGLDSKKYFRREGGNNNGEDINNLQPLETTITDVERFKDTVTLELSCPSCDKRFPFGGIVSSNYYRVSYNGLQCKHCEQLFTPLQLTSQIEHSIRAHISLYYAGWLQCDDSTCGIVTRQVSVFGKRCLNDGCTGVMRYKYSDKQLYNQLLYFDSLFDCEKNKKQELKPIYLPDDLDYPKEQLTESSIKALTEQNRELMETGRSVVQKYLNDCGRRYVDMTSIFDFMLN | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
|
|
||
* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MSSKSEKLE ------CCHHHHHHH | 58.75 | 22814378 | |
| 21 | Phosphorylation | LQAARNGTSIDDYEG HHHHHCCCCCCCCCC | 26.51 | 22369663 | |
| 22 | Phosphorylation | QAARNGTSIDDYEGD HHHHCCCCCCCCCCC | 25.97 | 22369663 | |
| 26 | Phosphorylation | NGTSIDDYEGDESDG CCCCCCCCCCCCCCC | 20.33 | 22369663 | |
| 31 | Phosphorylation | DDYEGDESDGDRIYD CCCCCCCCCCCCCHH | 52.19 | 22369663 | |
| 37 | Phosphorylation | ESDGDRIYDEIDEKE CCCCCCCHHHCCHHH | 14.39 | 21440633 | |
| 82 | Phosphorylation | DWREVDNSSSDEDTG CHHCCCCCCCCCCCC | 27.10 | 23749301 | |
| 83 | Phosphorylation | WREVDNSSSDEDTGN HHCCCCCCCCCCCCC | 48.33 | 23749301 | |
| 84 | Phosphorylation | REVDNSSSDEDTGNL HCCCCCCCCCCCCCC | 44.85 | 23749301 | |
| 88 | Phosphorylation | NSSSDEDTGNLASKD CCCCCCCCCCCCCCH | 26.39 | 19795423 | |
| 111 | Phosphorylation | REKDHQITDMLRTQH HHHHHHHHHHHHHHC | 14.58 | 24961812 | |
| 116 | Phosphorylation | QITDMLRTQHSKSTL HHHHHHHHHCCHHHH | 27.03 | 24961812 | |
| 119 | Phosphorylation | DMLRTQHSKSTLLAH HHHHHHCCHHHHHHH | 20.63 | 19823750 | |
| 121 | Phosphorylation | LRTQHSKSTLLAHAK HHHHCCHHHHHHHHH | 27.57 | 28889911 | |
| 134 | Phosphorylation | AKKSQKKSIPIDNFD HHHHCCCCCCCCCHH | 40.40 | 21440633 | |
| 149 | Phosphorylation | DILGEFESGEVEKPN HHHHCCCCCCCCCCC | 45.64 | 21440633 | |
| 162 | Acetylation | PNILLPSKLRENLNS CCEECCHHHHHHCCC | 50.01 | 24489116 | |
| 169 | Phosphorylation | KLRENLNSSPTSEFK HHHHHCCCCCCHHHH | 40.64 | 22369663 | |
| 170 | Phosphorylation | LRENLNSSPTSEFKS HHHHCCCCCCHHHHH | 30.99 | 22369663 | |
| 172 | Phosphorylation | ENLNSSPTSEFKSSI HHCCCCCCHHHHHHH | 42.72 | 22369663 | |
| 173 | Phosphorylation | NLNSSPTSEFKSSIK HCCCCCCHHHHHHHE | 44.41 | 22369663 | |
| 178 | Phosphorylation | PTSEFKSSIKRVNGN CCHHHHHHHEECCCC | 32.49 | 21440633 | |
| 188 | Phosphorylation | RVNGNDESSHDAGIS ECCCCCCCCCCCCCC | 35.52 | 21440633 | |
| 189 | Phosphorylation | VNGNDESSHDAGISK CCCCCCCCCCCCCCC | 24.28 | 23749301 | |
| 195 | Phosphorylation | SSHDAGISKKVKIDP CCCCCCCCCCEEECC | 26.04 | 19823750 | |
| 204 | Phosphorylation | KVKIDPDSSTDKYLE CEEECCCCCCCCEEE | 40.29 | 25521595 | |
| 205 | Phosphorylation | VKIDPDSSTDKYLEI EEECCCCCCCCEEEE | 48.26 | 25521595 | |
| 206 | Phosphorylation | KIDPDSSTDKYLEIE EECCCCCCCCEEEEC | 40.23 | 20377248 | |
| 209 | Phosphorylation | PDSSTDKYLEIESSP CCCCCCCEEEECCCC | 16.63 | 22890988 | |
| 214 | Phosphorylation | DKYLEIESSPLKLQS CCEEEECCCCHHHHH | 42.81 | 22369663 | |
| 215 | Phosphorylation | KYLEIESSPLKLQSR CEEEECCCCHHHHHC | 22.82 | 22369663 | |
| 226 | Phosphorylation | LQSRKLRYANDVQDL HHHCHHHHCCHHHHH | 21.86 | 22369663 | |
| 240 | Phosphorylation | LLDDVENSPVVATKR HHHHHHCCCCEEECC | 12.93 | 22369663 | |
| 245 | Phosphorylation | ENSPVVATKRQNVLQ HCCCCEEECCCCHHH | 18.36 | 22369663 | |
| 246 | Acetylation | NSPVVATKRQNVLQD CCCCEEECCCCHHHH | 42.10 | 25381059 | |
| 254 | Phosphorylation | RQNVLQDTLLANPPS CCCHHHHHHHCCCCC | 15.65 | 22369663 | |
| 261 | Phosphorylation | TLLANPPSAQSLADE HHHCCCCCHHHHCCC | 39.95 | 22369663 | |
| 264 | Phosphorylation | ANPPSAQSLADEEDD CCCCCHHHHCCCCCC | 25.82 | 21440633 | |
| 274 | Phosphorylation | DEEDDEDSDEDIILK CCCCCCCCCHHHHHH | 40.63 | 22369663 | |
| 298 | Phosphorylation | TRRVNIDSRSNPSTS EEEEECCCCCCCCCC | 33.54 | 28889911 | |
| 300 | Phosphorylation | RVNIDSRSNPSTSPF EEECCCCCCCCCCCE | 57.98 | 22369663 | |
| 303 | Phosphorylation | IDSRSNPSTSPFVTA CCCCCCCCCCCEECC | 45.85 | 22369663 | |
| 304 | Phosphorylation | DSRSNPSTSPFVTAP CCCCCCCCCCEECCC | 41.50 | 22369663 | |
| 305 | Phosphorylation | SRSNPSTSPFVTAPG CCCCCCCCCEECCCC | 22.22 | 22369663 | |
| 309 | Phosphorylation | PSTSPFVTAPGTPIG CCCCCEECCCCCCCE | 27.75 | 29136822 | |
| 313 | Phosphorylation | PFVTAPGTPIGIKGL CEECCCCCCCEECCC | 15.63 | 22369663 | |
| 318 | Acetylation | PGTPIGIKGLTPSKS CCCCCEECCCCCCCC | 42.53 | 24489116 | |
| 325 | Phosphorylation | KGLTPSKSLQSNTDV CCCCCCCCCCCCCCC | 35.66 | 22369663 | |
| 328 | Phosphorylation | TPSKSLQSNTDVATL CCCCCCCCCCCCEEE | 47.17 | 22369663 | |
| 330 | Phosphorylation | SKSLQSNTDVATLAV CCCCCCCCCCEEEEE | 36.78 | 22369663 | |
| 402 | Phosphorylation | FLPREGKTPTDIHEE CCCCCCCCCCCHHHH | 42.13 | 27017623 | |
| 404 | Phosphorylation | PREGKTPTDIHEEII CCCCCCCCCHHHHHH | 53.47 | 27017623 | |
| 674 | Acetylation | LRRTWPEKFGRGNSN HHHHCCHHHCCCCCC | 49.38 | 25381059 | |
| 842 | Acetylation | PVNSKKAKYQGGLVF CCCCCHHHCCCCEEE | 47.16 | 24489116 | |
| 973 | Ubiquitination | LAMLVTNKGREILMN EEEHHHCHHHHHHHC | 50.40 | 23749301 | |
| 1004 | Phosphorylation | TDSVMIDTGCDNYAD CCCEEEECCCCCHHH | 28.87 | 28132839 | |
| 1166 | Phosphorylation | GRVVKAGSVITFVIT CCEEEECCEEEEEEE | 18.40 | 30377154 | |
| 1231 | Phosphorylation | RLLERIDSFNVVRLS HHHHHHHHCCEEEHH | 19.15 | 27214570 |
| 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 DPOA_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DPOA_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 DPOA_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| 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-31; SER-169; SER-170;THR-172; SER-205; TYR-209; SER-214; SER-215; SER-240; SER-274; SER-300AND SER-1231, 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-31; SER-169; SER-170;SER-204; SER-215 AND SER-240, 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-170, 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-170 AND THR-313, ANDMASS SPECTROMETRY. | |
