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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: DNA polymerase delta catalytic subunit

UniprotKB/SwissProt ID: P28340 (P28340)

Gene Name: POLD1

Organism: Homo sapiens (Human)

Function: As the catalytic component of the trimeric (Pol-delta3 complex) and tetrameric DNA polymerase delta complexes (Pol-delta4 complex), plays a crucial role in high fidelity genome replication, including in lagging strand synthesis, and repair (PubMed:16510448, PubMed:19074196, PubMed:20334433, PubMed:24022480, PubMed:24035200, PubMed:31449058). Exhibits both DNA polymerase and 3'- to 5'-exonuclease activities (PubMed:16510448, PubMed:19074196, PubMed:20334433, PubMed:24022480, PubMed:24035200). Requires the presence of accessory proteins POLD2, POLD3 and POLD4 for full activity. Depending upon the absence (Pol-delta3) or the presence of POLD4 (Pol-delta4), displays differences in catalytic activity. Most notably, expresses higher proofreading activity in the context of Pol-delta3 compared with that of Pol-delta4 (PubMed:19074196, PubMed:20334433). Although both Pol-delta3 and Pol-delta4 process Okazaki fragments in vitro, Pol-delta3 may be better suited to fulfill this task, exhibiting near-absence of strand displacement activity compared to Pol-delta4 and stalling on encounter with the 5'-blocking oligonucleotides. Pol-delta3 idling process may avoid the formation of a gap, while maintaining a nick that can be readily ligated (PubMed:24035200). Along with DNA polymerase kappa, DNA polymerase delta carries out approximately half of nucleotide excision repair (NER) synthesis following UV irradiation (PubMed:20227374). Under conditions of DNA replication stress, in the presence of POLD3 and POLD4, may catalyze the repair of broken replication forks through break-induced replication (BIR) (PubMed:24310611). Involved in the translesion synthesis (TLS) of templates carrying O6-methylguanine, 8oxoG or abasic sites (PubMed:19074196, PubMed:24191025)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Nucleus

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR006172 DNA-dir_DNA_pol_B
IPR017964 DNA-dir_DNA_pol_B_CS
IPR006133 DNA-dir_DNA_pol_B_exonuc
IPR006134 DNA-dir_DNA_pol_B_multi_dom
IPR043502 DNA/RNA_pol_sf
IPR042087 DNA_pol_B_thumb
IPR023211 DNA_pol_palm_dom_sf
IPR050240 DNA_pol_type-B
IPR056435 DPOD/Z_N
IPR012337 RNaseH-like_sf
IPR036397 RNaseH_sf
IPR025687 Znf-C4pol

The S-nitrosylation sites of P28340

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 1076 HEDVICTSRD C PIFYMRKKVR   
2 319 PLRVLSFDIE C AGRKGIFPEP   
3 338 EPERDPVIQI C SLGLRWGEPE   
4 428 FPFLGRVAGL C SNIRDSSFQS   
5 713 FTGAQVGKLP C LEISQSVTGF   
6 761 VVYGDTDSVM C RFGVSSVAEA   
7 837 KGLEAVRRDN C PLVANLVTAS