| Tag | Content |
|---|
| CPLM ID | CPLM-005679 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | DNA polymerase delta catalytic subunit |
Protein Synonyms/Alias | |
Gene Name | POLD1 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Bos taurus (Bovine) |
NCBI Taxa ID | 9913 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 485 | FHFLGEQKEDVQHSI | ubiquitination | [1] | | 795 | PIRLEFEKVYFPYLL | ubiquitination | [1] | | 806 | PYLLISKKRYAGLLF | ubiquitination | [1] | | 826 | AHDRMDCKGLEAVRR | ubiquitination | [1] | | 930 | YVIISAAKGVAAYMK | ubiquitination | [1] | | 991 | RGDHTRCKTVLTGKV | ubiquitination | [1] |
|
Reference | [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments. Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA. Mol Cell Proteomics. 2013 Mar;12(3):825-31. [ PMID: 23266961] |
Functional Description | Possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single stranded DNA in the 3'- to 5'-direction. Required with its accessory proteins (proliferating cell nuclear antigen (PCNA) and replication factor C (RFC) or activator 1) for leading strand synthesis. Also involved in completing Okazaki fragments initiated by the DNA polymerase alpha/primase complex. |
Sequence Annotation | ZN_FING 1011 1028 CysA-type.
MOTIF 4 19 Nuclear localization signal (Potential).
MOTIF 1057 1075 CysB motif.
METAL 1011 1011 Zinc (By similarity).
METAL 1014 1014 Zinc (By similarity).
METAL 1025 1025 Zinc (By similarity).
METAL 1028 1028 Zinc (By similarity).
METAL 1057 1057 Iron-sulfur (4Fe-4S) (By similarity).
METAL 1060 1060 Iron-sulfur (4Fe-4S) (By similarity).
METAL 1070 1070 Iron-sulfur (4Fe-4S) (By similarity).
METAL 1075 1075 Iron-sulfur (4Fe-4S) (By similarity). |
Keyword | 4Fe-4S; Complete proteome; Direct protein sequencing; DNA replication; DNA-binding; DNA-directed DNA polymerase; Exonuclease; Hydrolase; Iron; Iron-sulfur; Metal-binding; Nuclease; Nucleotidyltransferase; Nucleus; Reference proteome; Transferase; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1106 AA |
Protein Sequence | MDGKRRPGPG PGVPPKRARG GLWDEDEAYR PSQFEEELAL MEEMEAERRL QEQEEEELQS 60
ALEAADGQFS PTAIDARWLR PAPPALDPQM EPLIFQQLEI DHYVAPARPL PGAPPPSQDS 120
VPILRAFGVT NEGVSVCCHI HGFAPYFYTP APPGFGPEHL SELQRELSAA ISRDQRGGKE 180
LTGPAVLAVE LCSRESMFGY HGHGPSPFLR ITLALPRLMA PARRLLEQGI RLAGLGTPSF 240
APYEANVDFE IRFMVDTDIV GCNWLELPAG KYILRPEGKA TLCQLEADVL WSDVISHPPE 300
GEWQRIAPLR VLSFDIECAG RKGIFPEPER DPVIQICSLG LRWGEPEPFL RLALTLRPCA 360
PILGAKVQSY EREEDLLQAW STFIRIMDPD VITGYNIQNF DLPYLISRAQ TLKVPGFPLL 420
GRVIGLRSNI RESSFQSRQT GRRDSKVVSM VGRVQMDMLQ VLLREYKLRS YTLNAVSFHF 480
LGEQKEDVQH SIITDLQNGN DQTRRRLAVY CLKDAFLPLR LLERLMVLVN AMEMARVTGV 540
PLGYLLSRGQ QVKVVSQLLR QAMRQGLLMP VVKTEGGEDY TGATVIEPLK GYYDVPIATL 600
DFSSLYPSIM MAHNLCYTTL LRPGAAQKLG LTEDQFIKTP TGDEFVKASV RKGLLPQILE 660
NLLSARKRAK AELAKETDPL RRQVLDGRQL ALKVSANSVY GFTGAQVGRL PCLEISQSVT 720
GFGRQMIEKT KQLVETKYTV ENGYSTSAKV VYGDTDSVMC RFGVSSVAEA MALGREAADW 780
VSGHFPSPIR LEFEKVYFPY LLISKKRYAG LLFSSRPDAH DRMDCKGLEA VRRDNCPLVA 840
NLVTASLRRL LIDRDPSGAV AHAQDVISDL LCNRIDISQL VITKELTRAA ADYAGKQAHV 900
ELAERMRKRD PGSAPSLGDR VPYVIISAAK GVAAYMKSED PLFVLEHSLP IDTQYYLEQQ 960
LAKPLLRIFE PILGEGRAEA VLLRGDHTRC KTVLTGKVGG LLAFAKRRNC CIGCRTVLSH 1020
QGAVCKFCQP RESELYQKEV SHLSALEERF SRLWTQCQRC QGSLHEDVIC TSRDCPIFYM 1080
RKKVRKDLED QERLLRRFGP PGPEAW 1106 |
Gene Ontology | GO:0005634; C:nucleus; IC:UniProtKB. 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; TAS:UniProtKB. GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0000166; F:nucleotide binding; IEA:InterPro. GO:0006260; P:DNA replication; TAS:UniProtKB. GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |