| Tag | Content |
|---|
| CPLM ID | CPLM-004113 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | DNA polymerase alpha catalytic subunit A |
Protein Synonyms/Alias | DNA polymerase I subunit A; DNA polymerase alpha:primase complex p180 subunit; DNA polymerase-primase complex p180 subunit; Pol alpha-primase complex p180 subunit |
Gene Name | POL1 |
Gene Synonyms/Alias | CDC17; YNL102W; N2181 |
Created Date | July 27, 2013 |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID | 559292 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 318 | PGTPIGIKGLTPSKS | acetylation | [1] | | 842 | PVNSKKAKYQGGLVF | acetylation | [1] | | 973 | LAMLVTNKGREILMN | ubiquitination | [2] |
|
Reference | [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C. Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [ PMID: 22865919] [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J. Nat Methods. 2013 Jul;10(7):676-82. [ PMID: 23749301] |
Functional Description | Catalytic component of DNA polymerase alpha, which in complex with DNA primase (DNA polymerase alpha:primase) consitutes a replicative polymerase. POL1 has a role in promoting telomere replication during interaction with CDC13. |
Sequence Annotation | ZN_FING 1287 1317 CysA-type.
REGION 1246 1381 DNA-binding region (Potential).
MOTIF 1348 1372 CysB motif.
METAL 1287 1287 Zinc (By similarity).
METAL 1290 1290 Zinc (By similarity).
METAL 1314 1314 Zinc (By similarity).
METAL 1317 1317 Zinc (By similarity).
METAL 1348 1348 Iron-sulfur (4Fe-4S) (By similarity).
METAL 1353 1353 Iron-sulfur (4Fe-4S) (By similarity).
METAL 1367 1367 Iron-sulfur (4Fe-4S) (By similarity).
METAL 1372 1372 Iron-sulfur (4Fe-4S) (By similarity).
MOD_RES 31 31 Phosphoserine.
MOD_RES 82 82 Phosphoserine.
MOD_RES 83 83 Phosphoserine.
MOD_RES 84 84 Phosphoserine.
MOD_RES 169 169 Phosphoserine.
MOD_RES 170 170 Phosphoserine.
MOD_RES 172 172 Phosphothreonine.
MOD_RES 240 240 Phosphoserine.
MOD_RES 274 274 Phosphoserine.
MOD_RES 309 309 Phosphothreonine.
MOD_RES 313 313 Phosphothreonine. |
Keyword | 3D-structure; 4Fe-4S; Complete proteome; DNA replication; DNA-binding; DNA-directed DNA polymerase; Iron; Iron-sulfur; Metal-binding; Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome; Transferase; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1468 AA |
Protein Sequence | MSSKSEKLEK LRKLQAARNG TSIDDYEGDE SDGDRIYDEI DEKEYRARKR QELLHDDFVV 60
DDDGVGYVDR GVEEDWREVD NSSSDEDTGN LASKDSKRKK NIKREKDHQI TDMLRTQHSK 120
STLLAHAKKS QKKSIPIDNF DDILGEFESG EVEKPNILLP SKLRENLNSS PTSEFKSSIK 180
RVNGNDESSH DAGISKKVKI DPDSSTDKYL EIESSPLKLQ SRKLRYANDV QDLLDDVENS 240
PVVATKRQNV LQDTLLANPP SAQSLADEED DEDSDEDIIL KRRTMRSVTT TRRVNIDSRS 300
NPSTSPFVTA PGTPIGIKGL TPSKSLQSNT DVATLAVNVK KEDVVDPETD TFQMFWLDYC 360
EVNNTLILFG KVKLKDDNCV SAMVQINGLC RELFFLPREG KTPTDIHEEI IPLLMDKYGL 420
DNIRAKPQKM KYSFELPDIP SESDYLKVLL PYQTPKSSRD TIPSDLSSDT FYHVFGGNSN 480
IFESFVIQNR IMGPCWLDIK GADFNSIRNA SHCAVEVSVD KPQNITPTTT KTMPNLRCLS 540
LSIQTLMNPK ENKQEIVSIT LSAYRNISLD SPIPENIKPD DLCTLVRPPQ STSFPLGLAA 600
LAKQKLPGRV RLFNNEKAML SCFCAMLKVE DPDVIIGHRL QNVYLDVLAH RMHDLNIPTF 660
SSIGRRLRRT WPEKFGRGNS NMNHFFISDI CSGRLICDIA NEMGQSLTPK CQSWDLSEMY 720
QVTCEKEHKP LDIDYQNPQY QNDVNSMTMA LQENITNCMI SAEVSYRIQL LTLTKQLTNL 780
AGNAWAQTLG GTRAGRNEYI LLHEFSRNGF IVPDKEGNRS RAQKQRQNEE NADAPVNSKK 840
AKYQGGLVFE PEKGLHKNYV LVMDFNSLYP SIIQEFNICF TTVDRNKEDI DELPSVPPSE 900
VDQGVLPRLL ANLVDRRREV KKVMKTETDP HKRVQCDIRQ QALKLTANSM YGCLGYVNSR 960
FYAKPLAMLV TNKGREILMN TRQLAESMNL LVVYGDTDSV MIDTGCDNYA DAIKIGLGFK 1020
RLVNERYRLL EIDIDNVFKK LLLHAKKKYA ALTVNLDKNG NGTTVLEVKG LDMKRREFCP 1080
LSRDVSIHVL NTILSDKDPE EALQEVYDYL EDIRIKVETN NIRIDKYKIN MKLSKDPKAY 1140
PGGKNMPAVQ VALRMRKAGR VVKAGSVITF VITKQDEIDN AADTPALSVA ERAHALNEVM 1200
IKSNNLIPDP QYYLEKQIFA PVERLLERID SFNVVRLSEA LGLDSKKYFR REGGNNNGED 1260
INNLQPLETT ITDVERFKDT VTLELSCPSC DKRFPFGGIV SSNYYRVSYN GLQCKHCEQL 1320
FTPLQLTSQI EHSIRAHISL YYAGWLQCDD STCGIVTRQV SVFGKRCLND GCTGVMRYKY 1380
SDKQLYNQLL YFDSLFDCEK NKKQELKPIY LPDDLDYPKE QLTESSIKAL TEQNRELMET 1440
GRSVVQKYLN DCGRRYVDMT SIFDFMLN 1468 |
Gene Ontology | GO:0005658; C:alpha DNA polymerase:primase complex; IDA:SGD. GO:0005739; C:mitochondrion; IDA:SGD. GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. GO:0003677; F:DNA binding; IEA:UniProtKB-KW. GO:0003887; F:DNA-directed DNA polymerase activity; IDA:SGD. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0001882; F:nucleoside binding; IEA:InterPro. GO:0000166; F:nucleotide binding; IEA:InterPro. GO:0000076; P:DNA replication checkpoint; IBA:RefGenome. GO:0006270; P:DNA replication initiation; IC:SGD. GO:0006269; P:DNA replication, synthesis of RNA primer; IBA:RefGenome. GO:0000734; P:gene conversion at mating-type locus, DNA repair synthesis; IBA:RefGenome. GO:0006273; P:lagging strand elongation; IC:SGD. GO:0006279; P:premeiotic DNA replication; IMP:SGD. GO:0006278; P:RNA-dependent DNA replication; IDA:SGD. |
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