| UniProt ID | DPOA2_YEAST | |
|---|---|---|
| UniProt AC | P38121 | |
| Protein Name | DNA polymerase alpha subunit B | |
| Gene Name | POL12 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 705 | |
| Subcellular Localization | Nucleus. | |
| Protein Description | Non-catalytic component of DNA polymerase alpha, which in a complex with DNA primase (DNA polymerase alpha:primase) constitutes a replicative polymerase. POL12 may play an essential role at the early stage of chromosomal DNA replication by coupling DNA polymerase alpha to the cellular replication machinery (By similarity). Interacts with MCM10.. | |
| Protein Sequence | MSGSIDVITHFGPDADKPEIITALENLTKLHALSVEDLYIKWEQFSNQRRQTHTDLTSKNIDEFKQFLQLQMEKRANQISSSSKVNTSTKKPVIKKSLNSSPLFGLSIPKTPTLKKRKLHGPFSLSDSKQTYNVGSEAETNEKGNSSLKLEFTPGMAEDAVGDSAPLSHAKSSDAKTPGSSTFQTPTTNTPTTSRQNVPAGEILDSLNPENIEISSGNPNVGLLSTEEPSYNQVKVEPFYDAKKYKFRTMRQNLQEASDVLDDQIESFTKIIQNHYKLSPNDFADPTIQSQSEIYAVGRIVPDSPTYDKFLNPESLSLETSRMGGVGRRVRLDLSQVNELSFFLGQIVAFKGKNANGDYFTVNSILPLPYPNSPVSTSQELQEFQANLEGSSLKVIVTCGPYFANDNFSLELLQEFIDSINNEVKPHVLIMFGPFIDITHPLIASGKLPNFPQFKTQPKTLDELFLKLFTPILKTISPHIQTVLIPSTKDAISNHAAYPQASLIRKALQLPKRNFKCMANPSSFQINEIYFGCSNVDTFKDLKEVIKGGTTSSRYRLDRVSEHILQQRRYYPIFPGSIRTRIKPKDVSTKKETNDMESKEEKVYEHISGADLDVSYLGLTEFVGGFSPDIMIIPSELQHFARVVQNVVVINPGRFIRATGNRGSYAQITVQCPDLEDGKLTLVEGEEPVYLHNVWKRARVDLIAS | |
| 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 |
|---|---|---|---|---|---|
| 80 | Phosphorylation | EKRANQISSSSKVNT HHHHHHCCCCCCCCC | 17.88 | 23749301 | |
| 81 | Phosphorylation | KRANQISSSSKVNTS HHHHHCCCCCCCCCC | 40.01 | 28889911 | |
| 82 | Phosphorylation | RANQISSSSKVNTST HHHHCCCCCCCCCCC | 27.64 | 23749301 | |
| 83 | Phosphorylation | ANQISSSSKVNTSTK HHHCCCCCCCCCCCC | 42.44 | 21082442 | |
| 84 | Methylation | NQISSSSKVNTSTKK HHCCCCCCCCCCCCC | 41.26 | 20137074 | |
| 87 | Phosphorylation | SSSSKVNTSTKKPVI CCCCCCCCCCCCCCE | 40.54 | 19779198 | |
| 88 | Phosphorylation | SSSKVNTSTKKPVIK CCCCCCCCCCCCCEE | 32.78 | 23749301 | |
| 97 | Phosphorylation | KKPVIKKSLNSSPLF CCCCEECCCCCCCCC | 27.99 | 22890988 | |
| 100 | Phosphorylation | VIKKSLNSSPLFGLS CEECCCCCCCCCCCC | 38.33 | 19823750 | |
| 101 | Phosphorylation | IKKSLNSSPLFGLSI EECCCCCCCCCCCCC | 25.25 | 22369663 | |
| 107 | Phosphorylation | SSPLFGLSIPKTPTL CCCCCCCCCCCCCCC | 36.91 | 22890988 | |
| 111 | Phosphorylation | FGLSIPKTPTLKKRK CCCCCCCCCCCCCCC | 19.02 | 28152593 | |
| 113 | Phosphorylation | LSIPKTPTLKKRKLH CCCCCCCCCCCCCCC | 57.34 | 21440633 | |
| 124 | Phosphorylation | RKLHGPFSLSDSKQT CCCCCCCCCCCCCCE | 30.05 | 20377248 | |
| 126 | Phosphorylation | LHGPFSLSDSKQTYN CCCCCCCCCCCCEEE | 38.34 | 22369663 | |
| 128 | Phosphorylation | GPFSLSDSKQTYNVG CCCCCCCCCCEEECC | 24.24 | 22369663 | |
| 131 | Phosphorylation | SLSDSKQTYNVGSEA CCCCCCCEEECCCCE | 22.31 | 22369663 | |
| 132 | Phosphorylation | LSDSKQTYNVGSEAE CCCCCCEEECCCCEE | 12.83 | 22369663 | |
| 136 | Phosphorylation | KQTYNVGSEAETNEK CCEEECCCCEECCCC | 29.38 | 22369663 | |
| 140 | Phosphorylation | NVGSEAETNEKGNSS ECCCCEECCCCCCCC | 56.58 | 22369663 | |
| 146 | Phosphorylation | ETNEKGNSSLKLEFT ECCCCCCCCEEEEEC | 45.79 | 20377248 | |
| 147 | Phosphorylation | TNEKGNSSLKLEFTP CCCCCCCCEEEEECC | 33.26 | 20377248 | |
| 153 | Phosphorylation | SSLKLEFTPGMAEDA CCEEEEECCCCCCCC | 15.01 | 22369663 | |
| 164 | Phosphorylation | AEDAVGDSAPLSHAK CCCCCCCCCCCCCCC | 26.34 | 21440633 | |
| 168 | Phosphorylation | VGDSAPLSHAKSSDA CCCCCCCCCCCCCCC | 21.97 | 20377248 | |
| 172 | Phosphorylation | APLSHAKSSDAKTPG CCCCCCCCCCCCCCC | 33.94 | 20377248 | |
| 173 | Phosphorylation | PLSHAKSSDAKTPGS CCCCCCCCCCCCCCC | 40.66 | 20377248 | |
| 177 | Phosphorylation | AKSSDAKTPGSSTFQ CCCCCCCCCCCCCCC | 34.30 | 21440633 | |
| 180 | Phosphorylation | SDAKTPGSSTFQTPT CCCCCCCCCCCCCCC | 27.66 | 21440633 | |
| 181 | Phosphorylation | DAKTPGSSTFQTPTT CCCCCCCCCCCCCCC | 38.87 | 23749301 | |
| 182 | Phosphorylation | AKTPGSSTFQTPTTN CCCCCCCCCCCCCCC | 22.81 | 25752575 | |
| 185 | Phosphorylation | PGSSTFQTPTTNTPT CCCCCCCCCCCCCCC | 20.57 | 25752575 | |
| 187 | Phosphorylation | SSTFQTPTTNTPTTS CCCCCCCCCCCCCCC | 35.75 | 23749301 | |
| 188 | Phosphorylation | STFQTPTTNTPTTSR CCCCCCCCCCCCCCC | 37.99 | 21440633 | |
| 190 | Phosphorylation | FQTPTTNTPTTSRQN CCCCCCCCCCCCCCC | 21.66 | 28152593 | |
| 192 | Phosphorylation | TPTTNTPTTSRQNVP CCCCCCCCCCCCCCC | 35.05 | 30377154 | |
| 193 | Phosphorylation | PTTNTPTTSRQNVPA CCCCCCCCCCCCCCC | 24.10 | 29688323 | |
| 194 | Phosphorylation | TTNTPTTSRQNVPAG CCCCCCCCCCCCCCH | 34.05 | 30377154 | |
| 304 | Phosphorylation | VGRIVPDSPTYDKFL EEEECCCCCCCHHHC | 17.05 | 17563356 | |
| 309 | Acetylation | PDSPTYDKFLNPESL CCCCCCHHHCCHHHC | 41.14 | 24489116 |
| 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 DPOA2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DPOA2_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 DPOA2_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-101; SER-180 ANDTHR-190, 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-126 AND SER-304, ANDMASS SPECTROMETRY. | |
