POLD1
entrez
5424
canonical
uniprot
P28340
canonical
ensembl
ENSG00000062822
resolver
ensp
ENSP00000406046
resolver
ensp
ENSP00000472445
resolver
ensp
ENSP00000472600
resolver
ensp
ENSP00000472607
resolver
ensp
ENSP00000473052
resolver
ensp
ENSP00000481858
resolver
ensp
ENSP00000510052
resolver
ensp
ENSP00000539835
resolver
ensp
ENSP00000539839
resolver
ensp
ENSP00000539841
resolver
ensp
ENSP00000539842
resolver
ensp
ENSP00000605902
resolver
ensp
ENSP00000605903
resolver
ensp
ENSP00000605906
resolver
ensp
ENSP00000605907
resolver
ensp
ENSP00000605908
resolver
ensp
ENSP00000605913
resolver
ensp
ENSP00000605914
resolver
ensp
ENSP00000605915
resolver
ensp
ENSP00000605917
resolver
ensp
ENSP00000605918
resolver
ensp
ENSP00000639707
resolver
ensp
ENSP00000639708
resolver
ensp
ENSP00000639709
resolver
enst
ENST00000440232
resolver
enst
ENST00000593887
resolver
enst
ENST00000595904
resolver
enst
ENST00000599857
resolver
enst
ENST00000601098
resolver
enst
ENST00000613923
resolver
enst
ENST00000687454
resolver
enst
ENST00000869776
resolver
enst
ENST00000869780
resolver
enst
ENST00000869782
resolver
enst
ENST00000869783
resolver
enst
ENST00000935843
resolver
enst
ENST00000935844
resolver
enst
ENST00000935847
resolver
enst
ENST00000935848
resolver
enst
ENST00000935849
resolver
enst
ENST00000935854
resolver
enst
ENST00000935855
resolver
enst
ENST00000935856
resolver
enst
ENST00000935858
resolver
enst
ENST00000935859
resolver
enst
ENST00000969648
resolver
enst
ENST00000969649
resolver
enst
ENST00000969650
resolver
genesymbol
POLD1
resolver
genesymbol_syn
POLD
resolver
hgnc
HGNC:9175
resolver
uniprot
A0A087WYJ2
resolver
uniprot
M0R2B7
resolver
uniprot
Q308M6
resolver
uniprot
Q59FA0
resolver
uniprot
Q8NER3
resolver
uniprot
Q96H98
resolver
uniprot_entry
A0A087WYJ2_HUMAN
resolver
uniprot_entry
DPOD1_HUMAN
resolver
uniprot_entry
M0R2B7_HUMAN
resolver
uniprot_entry
Q308M6_HUMAN
resolver
uniprot_entry
Q59FA0_HUMAN
resolver
uniprot_sec
Q8NER3
resolver
uniprot_sec
Q96H98
resolver
activity_regulation
ACTIVITY REGULATION: Regulated by alteration of quaternary structure. Exhibits burst rates of DNA synthesis are about 5 times faster in the presence of POLD4 (Pol-delta4 complex) than in its absence (Pol-delta3 complex), while the affinity of the enzyme for its DNA and dNTP substrates appears unchanged. The Pol-delta3 complex is more likely to proofread DNA synthesis because it cleaves single-stranded DNA twice as fast and transfers mismatched DNA from the polymerase to the exonuclease sites 9 times faster compared to the Pol-delta3 complex. Pol-delta3 also extends mismatched primers 3 times more slowly in the absence of POLD4. The conversion of Pol-delta4 into Pol-delta3 is induced by genotoxic stress or by replication stress leading POLD4 degradation (PubMed:19074196, PubMed:20334433). Stimulated in the presence of PCNA (PubMed:11328591, PubMed:12403614, PubMed:12522211, PubMed:16510448, PubMed:24022480, PubMed:24939902). This stimulation is further increased in the presence of KCTD13/PDIP1, most probably via direct interaction between KCTD13 and POLD2 (By similarity). {ECO:0000250|UniProtKB:P28339, ECO:0000269|PubMed:11328591, ECO:0000269|PubMed:12403614, ECO:0000269|PubMed:12522211, ECO:0000269|PubMed:16510448, ECO:0000269|PubMed:19074196, ECO:0000269|PubMed:20334433, ECO:0000269|PubMed:24022480, ECO:0000269|PubMed:24939902}.
uniprot
proteins
amino_acid_sequence
MDGKRRPGPGPGVPPKRARGGLWDDDDAPRPSQFEEDLALMEEMEAEHRLQEQEEEELQSVLEGVADGQVPPSAIDPRWLRPTPPALDPQTEPLIFQQLEIDHYVGPAQPVPGGPPPSRGSVPVLRAFGVTDEGFSVCCHIHGFAPYFYTPAPPGFGPEHMGDLQRELNLAISRDSRGGRELTGPAVLAVELCSRESMFGYHGHGPSPFLRITVALPRLVAPARRLLEQGIRVAGLGTPSFAPYEANVDFEIRFMVDTDIVGCNWLELPAGKYALRLKEKATQCQLEADVLWSDVVSHPPEGPWQRIAPLRVLSFDIECAGRKGIFPEPERDPVIQICSLGLRWGEPEPFLRLALTLRPCAPILGAKVQSYEKEEDLLQAWSTFIRIMDPDVITGYNIQNFDLPYLISRAQTLKVQTFPFLGRVAGLCSNIRDSSFQSKQTGRRDTKVVSMVGRVQMDMLQVLLREYKLRSYTLNAVSFHFLGEQKEDVQHSIITDLQNGNDQTRRRLAVYCLKDAYLPLRLLERLMVLVNAVEMARVTGVPLSYLLSRGQQVKVVSQLLRQAMHEGLLMPVVKSEGGEDYTGATVIEPLKGYYDVPIATLDFSSLYPSIMMAHNLCYTTLLRPGTAQKLGLTEDQFIRTPTGDEFVKTSVRKGLLPQILENLLSARKRAKAELAKETDPLRRQVLDGRQLALKVSANSVYGFTGAQVGKLPCLEISQSVTGFGRQMIEKTKQLVESKYTVENGYSTSAKVVYGDTDSVMCRFGVSSVAEAMALGREAADWVSGHFPSPIRLEFEKVYFPYLLISKKRYAGLLFSSRPDAHDRMDCKGLEAVRRDNCPLVANLVTASLRRLLIDRDPEGAVAHAQDVISDLLCNRIDISQLVITKELTRAASDYAGKQAHVELAERMRKRDPGSAPSLGDRVPYVIISAAKGVAAYMKSEDPLFVLEHSLPIDTQYYLEQQLAKPLLRIFEPILGEGRAEAVLLRGDHTRCKTVLTGKVGGLLAFAKRRNCCIGCRTVLSHQGAVCEFCQPRESELYQKEVSHLNALEERFSRLWTQCQRCQGSLHEDVICTSRDCPIFYMRKKVRKDLEDQEQLLRRFGPPGPEAW
uniprot
proteins
disease_involvement
DISEASE: Colorectal cancer 10 (CRCS10) [MIM:612591]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history. {ECO:0000269|PubMed:23263490, ECO:0000269|PubMed:24501277}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Mandibular hypoplasia, deafness, progeroid features, and lipodystrophy syndrome (MDPL) [MIM:615381]: An autosomal dominant systemic disorder characterized by prominent loss of subcutaneous fat, metabolic abnormalities including insulin resistance and diabetes mellitus, sclerodermatous skin, and a facial appearance characterized by mandibular hypoplasia. Sensorineural deafness occurs late in the first or second decades of life. {ECO:0000269|PubMed:23770608}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Immunodeficiency 120 (IMD120) [MIM:620836]: An autosomal recessive immunologic disorder manifesting in early childhood with recurrent upper and lower respiratory tract infections, lymphopenia, and hypogammaglobulinemia. Affected individuals may also develop persistent viral infections, particularly of the herpes family. Additional variable features include hearing loss, speech delay, short stature, and mildly impaired intellectual development. {ECO:0000269|PubMed:31449058, ECO:0000269|PubMed:31629014}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.7.7.7
uniprot
proteins
ec_number
3.1.11.-
uniprot
proteins
function
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). {ECO:0000269|PubMed:16510448, ECO:0000269|PubMed:19074196, ECO:0000269|PubMed:20227374, ECO:0000269|PubMed:20334433, ECO:0000269|PubMed:24022480, ECO:0000269|PubMed:24035200, ECO:0000269|PubMed:24191025, ECO:0000269|PubMed:24310611, ECO:0000269|PubMed:31449058}.
uniprot
proteins
mass_dalton
123631
uniprot
proteins
mutagenesis
MUTAGEN 402; /note="D->A: Loss of exonuclease activity. No effect on DNA polymerase activity."; /evidence="ECO:0000269|PubMed:19074196, ECO:0000269|PubMed:20334433"; MUTAGEN 602; /note="D->A: Loss of polymerase activity; when associated with A-757."; /evidence="ECO:0000269|PubMed:31449058"; MUTAGEN 757; /note="D->A: Loss of polymerase activity; when associated with A-602."; /evidence="ECO:0000269|PubMed:31449058
uniprot
proteins
protein_family
DNA polymerase type-B family
uniprot
proteins
pubmed
11328591
uniprot
proteins
pubmed
11595739
uniprot
proteins
pubmed
12403614
uniprot
proteins
pubmed
12522211
uniprot
proteins
pubmed
1542570
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15670210
uniprot
proteins
pubmed
16510448
uniprot
proteins
pubmed
1722322
uniprot
proteins
pubmed
17317665
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19074196
uniprot
proteins
pubmed
20227374
uniprot
proteins
pubmed
20334433
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22801543
uniprot
proteins
pubmed
23263490
uniprot
proteins
pubmed
23770608
uniprot
proteins
pubmed
23891004
uniprot
proteins
pubmed
23913683
uniprot
proteins
pubmed
24022480
uniprot
proteins
pubmed
24035200
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24191025
uniprot
proteins
pubmed
24310611
uniprot
proteins
pubmed
24501277
uniprot
proteins
pubmed
24939902
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
29320706
uniprot
proteins
pubmed
31449058
uniprot
proteins
pubmed
31629014
uniprot
proteins
sequence_length
1107
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11595739, ECO:0000269|PubMed:20227374, ECO:0000269|PubMed:22801543}. Note=Colocalizes with PCNA and POLD3 at S phase replication sites (PubMed:11595739). After UV irradiation, recruited to DNA damage sites within 2 hours, independently of the cell cycle phase, nor on PCNA ubiquitination. This recruitment requires POLD3, PCNA and RFC1-replication factor C complex (PubMed:20227374, PubMed:22801543). {ECO:0000269|PubMed:11595739, ECO:0000269|PubMed:20227374, ECO:0000269|PubMed:22801543}.
uniprot
proteins