UniProtKB - P28340 (DPOD1_HUMAN)
DNA polymerase delta catalytic subunit
POLD1
Functioni
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. Exhibits both DNA polymerase and 3'- to 5'-exonuclease activities (PubMed:16510448, PubMed:19074196, PubMed:20334433, PubMed:24035200, PubMed:24022480).
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).
8 PublicationsCatalytic activityi
- EC:2.7.7.72 Publications
Cofactori
Activity regulationi
Kineticsi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 1012 | ZincBy similarity | 1 | |
Metal bindingi | 1015 | ZincBy similarity | 1 | |
Metal bindingi | 1026 | ZincBy similarity | 1 | |
Metal bindingi | 1029 | ZincBy similarity | 1 | |
Metal bindingi | 1058 | Iron-sulfur (4Fe-4S)By similarity | 1 | |
Metal bindingi | 1061 | Iron-sulfur (4Fe-4S)By similarity | 1 | |
Metal bindingi | 1071 | Iron-sulfur (4Fe-4S)By similarity | 1 | |
Metal bindingi | 1076 | Iron-sulfur (4Fe-4S)By similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 1012 – 1029 | CysA-typeAdd BLAST | 18 |
GO - Molecular functioni
- 3'-5'-exodeoxyribonuclease activity Source: GO_Central
- 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
- chromatin binding Source: UniProtKB
- damaged DNA binding Source: UniProtKB
- DNA binding Source: UniProtKB
- DNA-directed DNA polymerase activity Source: UniProtKB
- enzyme binding Source: Ensembl
- metal ion binding Source: UniProtKB-KW
- nucleotide binding Source: InterPro
GO - Biological processi
- base-excision repair, gap-filling Source: UniProtKB
- cellular response to UV Source: UniProtKB
- DNA biosynthetic process Source: UniProtKB
- DNA-dependent DNA replication Source: ComplexPortal
- DNA repair Source: ProtInc
- DNA replication Source: UniProtKB
- DNA replication proofreading Source: GO_Central
- DNA synthesis involved in DNA repair Source: UniProtKB
- error-free translesion synthesis Source: UniProtKB
- fatty acid homeostasis Source: UniProtKB
- nucleotide-excision repair, DNA gap filling Source: UniProtKB
- response to UV Source: ProtInc
Keywordsi
Molecular function | DNA-binding, DNA-directed DNA polymerase, Exonuclease, Hydrolase, Nuclease, Nucleotidyltransferase, Transferase |
Biological process | DNA damage, DNA excision, DNA repair, DNA replication |
Ligand | 4Fe-4S, Iron, Iron-sulfur, Metal-binding, Zinc |
Enzyme and pathway databases
BRENDAi | 2.7.7.7, 2681 |
PathwayCommonsi | P28340 |
Reactomei | R-HSA-110314, Recognition of DNA damage by PCNA-containing replication complex R-HSA-174411, Polymerase switching on the C-strand of the telomere R-HSA-174414, Processive synthesis on the C-strand of the telomere R-HSA-174417, Telomere C-strand (Lagging Strand) Synthesis R-HSA-174437, Removal of the Flap Intermediate from the C-strand R-HSA-2564830, Cytosolic iron-sulfur cluster assembly R-HSA-5358565, Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) R-HSA-5358606, Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta) R-HSA-5651801, PCNA-Dependent Long Patch Base Excision Repair R-HSA-5656169, Termination of translesion DNA synthesis R-HSA-5685942, HDR through Homologous Recombination (HRR) R-HSA-5696397, Gap-filling DNA repair synthesis and ligation in GG-NER R-HSA-5696400, Dual Incision in GG-NER R-HSA-6782135, Dual incision in TC-NER R-HSA-6782210, Gap-filling DNA repair synthesis and ligation in TC-NER R-HSA-69091, Polymerase switching R-HSA-69166, Removal of the Flap Intermediate R-HSA-69183, Processive synthesis on the lagging strand |
SignaLinki | P28340 |
SIGNORi | P28340 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:9175, POLD1 |
MIMi | 174761, gene |
neXtProti | NX_P28340 |
VEuPathDBi | HostDB:ENSG00000062822 |
Subcellular locationi
Nucleus
- Nucleus 3 Publications
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 on the cell cycle phase, nor on PCNA ubiquitination. This recruitment requires POLD3, PCNA and RFC1-replication factor C complex (PubMed:20227374, PubMed:22801543).3 Publications
Cytosol
- cytosol Source: HPA
Nucleus
- delta DNA polymerase complex Source: UniProtKB
- nucleoplasm Source: HPA
- nucleotide-excision repair complex Source: UniProtKB
- nucleus Source: UniProtKB
Other locations
Keywords - Cellular componenti
NucleusPathology & Biotechi
Involvement in diseasei
Colorectal cancer 10 (CRCS10)2 Publications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_071966 | 474 | L → P in CRCS10. 1 PublicationCorresponds to variant dbSNP:rs587777627EnsemblClinVar. | 1 | |
Natural variantiVAR_069335 | 478 | S → N in CRCS10; associated with disease susceptibility. 1 PublicationCorresponds to variant dbSNP:rs397514632EnsemblClinVar. | 1 |
Mandibular hypoplasia, deafness, progeroid features, and lipodystrophy syndrome (MDPL)1 Publication
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_070231 | 605 | Missing in MDPL; the mutant enzyme lacks DNA polymerase ability; has decreased exonuclease activity; can bind DNA but is unable to interact with and incorporate dNTPs. 1 Publication | 1 |
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 402 | D → A: Loss of exonuclease activity. No effect on DNA polymerase activity. 2 Publications | 1 |
Keywords - Diseasei
Disease variantOrganism-specific databases
DisGeNETi | 5424 |
MalaCardsi | POLD1 |
MIMi | 612591, phenotype 615381, phenotype |
OpenTargetsi | ENSG00000062822 |
Orphaneti | 363649, Mandibular hypoplasia-deafness-progeroid features-lipodystrophy syndrome 447877, Polymerase proofreading-related adenomatous polyposis |
PharmGKBi | PA33496 |
Miscellaneous databases
Pharosi | P28340, Tclin |
Chemistry databases
ChEMBLi | CHEMBL2735 |
DrugCentrali | P28340 |
Genetic variation databases
BioMutai | POLD1 |
DMDMi | 50403732 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000046442 | 1 – 1107 | DNA polymerase delta catalytic subunitAdd BLAST | 1107 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 19 | Omega-N-methylarginineCombined sources | 1 | |
Cross-linki | 574 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources |
Keywords - PTMi
Isopeptide bond, Methylation, Ubl conjugationProteomic databases
EPDi | P28340 |
jPOSTi | P28340 |
MassIVEi | P28340 |
MaxQBi | P28340 |
PaxDbi | P28340 |
PeptideAtlasi | P28340 |
PRIDEi | P28340 |
ProteomicsDBi | 54478 |
PTM databases
iPTMneti | P28340 |
PhosphoSitePlusi | P28340 |
Expressioni
Tissue specificityi
Developmental stagei
Inductioni
Gene expression databases
Bgeei | ENSG00000062822, Expressed in stomach and 193 other tissues |
ExpressionAtlasi | P28340, baseline and differential |
Genevisiblei | P28340, HS |
Organism-specific databases
HPAi | ENSG00000062822, Low tissue specificity |
Interactioni
Subunit structurei
Component of the tetrameric DNA polymerase delta complex (Pol-delta4), which consists of POLD1/p125, POLD2/p50, POLD3/p66/p68 and POLD4/p12, with POLD1 bearing both DNA polymerase and 3' to 5' proofreading exonuclease activities (PubMed:11595739, PubMed:12522211, PubMed:17317665, PubMed:22801543). Within Pol-delta4, directly interacts with POLD2 and POLD4 (PubMed:11328591, PubMed:12403614, PubMed:16510448). Following genotoxic stress by DNA-damaging agents, such as ultraviolet light and methyl methanesulfonate, or by replication stress induced by treatment with hydroxyurea or aphidicolin, Pol-delta4 is converted into a trimeric form of the complex (Pol-delta3) by POLD4 degradation. Pol-delta3 is the major form at S phase replication sites and DNA damage sites (PubMed:22801543, PubMed:17317665). POLD1 displays different catalytic properties depending upon the complex it is found in (PubMed:17317665). It exhibits higher proofreading activity and fidelity than Pol-delta4, making it particularly well suited to respond to DNA damage (PubMed:19074196, PubMed:20334433). Directly interacts with PCNA, as do POLD3 and POLD4; this interaction stimulates Pol-delta4 polymerase activity (PubMed:11328591, PubMed:12403614, PubMed:12522211, PubMed:16510448, PubMed:24022480, PubMed:24939902). As POLD2 and POLD4, directly interacts with WRNIP1; this interaction stimulates DNA polymerase delta-mediated DNA synthesis, independently of the presence of PCNA. This stimulation may be due predominantly to an increase of initiation frequency and also to increased processivity (PubMed:15670210). Also observed as a dimeric complex with POLD2 (Pol-delta2 complex). Pol-delta2 is relatively insensitive to the PCNA stimulation (2-5-fold) compared to Pol-delta4 that is stimulated by over 50-fold (PubMed:12403614). The DNA polymerase delta complex interacts with POLDIP2; this interaction is probably mediated through direct binding to POLD2 (PubMed:12522211).
Interacts with CIAO1 (PubMed:23891004).
Interacts with POLDIP2 (PubMed:24191025).
14 PublicationsBinary interactionsi
P28340
GO - Molecular functioni
- enzyme binding Source: Ensembl
Protein-protein interaction databases
BioGRIDi | 111420, 185 interactors |
ComplexPortali | CPX-2097, DNA polymerase delta complex |
CORUMi | P28340 |
IntActi | P28340, 53 interactors |
MINTi | P28340 |
STRINGi | 9606.ENSP00000406046 |
Chemistry databases
BindingDBi | P28340 |
Miscellaneous databases
RNActi | P28340, protein |
Structurei
Secondary structure
3D structure databases
SMRi | P28340 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 34 | DisorderedSequence analysisAdd BLAST | 34 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 4 – 19 | Nuclear localization signalSequence analysisAdd BLAST | 16 | |
Motifi | 1058 – 1076 | CysB motifAdd BLAST | 19 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 19 – 34 | Basic and acidic residuesSequence analysisAdd BLAST | 16 |
Domaini
Sequence similaritiesi
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 1012 – 1029 | CysA-typeAdd BLAST | 18 |
Keywords - Domaini
Zinc-fingerPhylogenomic databases
eggNOGi | KOG0969, Eukaryota |
GeneTreei | ENSGT00560000077365 |
HOGENOMi | CLU_000203_2_0_1 |
InParanoidi | P28340 |
PhylomeDBi | P28340 |
TreeFami | TF352785 |
Family and domain databases
Gene3Di | 1.10.132.60, 1 hit 3.30.420.10, 1 hit 3.90.1600.10, 1 hit |
InterProi | View protein in InterPro 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 IPR012337, RNaseH-like_sf IPR036397, RNaseH_sf IPR025687, Znf-C4pol |
Pfami | View protein in Pfam PF00136, DNA_pol_B, 1 hit PF03104, DNA_pol_B_exo1, 1 hit PF14260, zf-C4pol, 1 hit |
PRINTSi | PR00106, DNAPOLB |
SMARTi | View protein in SMART SM00486, POLBc, 1 hit |
SUPFAMi | SSF53098, SSF53098, 1 hit SSF56672, SSF56672, 1 hit |
PROSITEi | View protein in PROSITE PS00116, DNA_POLYMERASE_B, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
This entry has 1 described isoform and 8 potential isoforms that are computationally mapped.Show allAlign All
10 20 30 40 50
MDGKRRPGPG PGVPPKRARG GLWDDDDAPR PSQFEEDLAL MEEMEAEHRL
60 70 80 90 100
QEQEEEELQS VLEGVADGQV PPSAIDPRWL RPTPPALDPQ TEPLIFQQLE
110 120 130 140 150
IDHYVGPAQP VPGGPPPSRG SVPVLRAFGV TDEGFSVCCH IHGFAPYFYT
160 170 180 190 200
PAPPGFGPEH MGDLQRELNL AISRDSRGGR ELTGPAVLAV ELCSRESMFG
210 220 230 240 250
YHGHGPSPFL RITVALPRLV APARRLLEQG IRVAGLGTPS FAPYEANVDF
260 270 280 290 300
EIRFMVDTDI VGCNWLELPA GKYALRLKEK ATQCQLEADV LWSDVVSHPP
310 320 330 340 350
EGPWQRIAPL RVLSFDIECA GRKGIFPEPE RDPVIQICSL GLRWGEPEPF
360 370 380 390 400
LRLALTLRPC APILGAKVQS YEKEEDLLQA WSTFIRIMDP DVITGYNIQN
410 420 430 440 450
FDLPYLISRA QTLKVQTFPF LGRVAGLCSN IRDSSFQSKQ TGRRDTKVVS
460 470 480 490 500
MVGRVQMDML QVLLREYKLR SYTLNAVSFH FLGEQKEDVQ HSIITDLQNG
510 520 530 540 550
NDQTRRRLAV YCLKDAYLPL RLLERLMVLV NAVEMARVTG VPLSYLLSRG
560 570 580 590 600
QQVKVVSQLL RQAMHEGLLM PVVKSEGGED YTGATVIEPL KGYYDVPIAT
610 620 630 640 650
LDFSSLYPSI MMAHNLCYTT LLRPGTAQKL GLTEDQFIRT PTGDEFVKTS
660 670 680 690 700
VRKGLLPQIL ENLLSARKRA KAELAKETDP LRRQVLDGRQ LALKVSANSV
710 720 730 740 750
YGFTGAQVGK LPCLEISQSV TGFGRQMIEK TKQLVESKYT VENGYSTSAK
760 770 780 790 800
VVYGDTDSVM CRFGVSSVAE AMALGREAAD WVSGHFPSPI RLEFEKVYFP
810 820 830 840 850
YLLISKKRYA GLLFSSRPDA HDRMDCKGLE AVRRDNCPLV ANLVTASLRR
860 870 880 890 900
LLIDRDPEGA VAHAQDVISD LLCNRIDISQ LVITKELTRA ASDYAGKQAH
910 920 930 940 950
VELAERMRKR DPGSAPSLGD RVPYVIISAA KGVAAYMKSE DPLFVLEHSL
960 970 980 990 1000
PIDTQYYLEQ QLAKPLLRIF EPILGEGRAE AVLLRGDHTR CKTVLTGKVG
1010 1020 1030 1040 1050
GLLAFAKRRN CCIGCRTVLS HQGAVCEFCQ PRESELYQKE VSHLNALEER
1060 1070 1080 1090 1100
FSRLWTQCQR CQGSLHEDVI CTSRDCPIFY MRKKVRKDLE DQEQLLRRFG
PPGPEAW
Computationally mapped potential isoform sequencesi
There are 8 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketM0R2B7 | M0R2B7_HUMAN | DNA polymerase | POLD1 | 1,133 | Annotation score: | ||
A0A087WYJ2 | A0A087WYJ2_HUMAN | DNA polymerase | POLD1 | 1,083 | Annotation score: | ||
M0QZR8 | M0QZR8_HUMAN | DNA polymerase | POLD1 | 1,009 | Annotation score: | ||
A0A2R8Y705 | A0A2R8Y705_HUMAN | DNA polymerase | POLD1 | 447 | Annotation score: | ||
A0A2R8Y7K6 | A0A2R8Y7K6_HUMAN | DNA-directed DNA polymerase | POLD1 | 762 | Annotation score: | ||
M0QXQ2 | M0QXQ2_HUMAN | DNA-directed DNA polymerase | POLD1 | 291 | Annotation score: | ||
M0QXE6 | M0QXE6_HUMAN | DNA-directed DNA polymerase | POLD1 | 289 | Annotation score: | ||
M0R2J2 | M0R2J2_HUMAN | DNA polymerase delta catalytic subu... | POLD1 | 105 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 472 | Y → H in AAA58439 (PubMed:1722322).Curated | 1 | |
Sequence conflicti | 776 | R → G in AAA35768 (PubMed:1542570).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_048878 | 5 | R → W. Corresponds to variant dbSNP:rs9282830EnsemblClinVar. | 1 | |
Natural variantiVAR_019340 | 19 | R → H1 PublicationCorresponds to variant dbSNP:rs3218773EnsemblClinVar. | 1 | |
Natural variantiVAR_048879 | 21 | G → C. Corresponds to variant dbSNP:rs9282831EnsemblClinVar. | 1 | |
Natural variantiVAR_016146 | 30 | R → W2 PublicationsCorresponds to variant dbSNP:rs3218772EnsemblClinVar. | 1 | |
Natural variantiVAR_019341 | 119 | R → H3 PublicationsCorresponds to variant dbSNP:rs1726801EnsemblClinVar. | 1 | |
Natural variantiVAR_069333 | 145 | A → D Found in a colorectal sample; somatic mutation. 1 Publication | 1 | |
Natural variantiVAR_019342 | 173 | S → N2 PublicationsCorresponds to variant dbSNP:rs1726803EnsemblClinVar. | 1 | |
Natural variantiVAR_019343 | 177 | R → H1 PublicationCorresponds to variant dbSNP:rs3218750EnsemblClinVar. | 1 | |
Natural variantiVAR_048880 | 347 | P → L. Corresponds to variant dbSNP:rs2230243EnsemblClinVar. | 1 | |
Natural variantiVAR_069334 | 461 | Q → H Found in a colorectal sample; somatic mutation. 1 Publication | 1 | |
Natural variantiVAR_071966 | 474 | L → P in CRCS10. 1 PublicationCorresponds to variant dbSNP:rs587777627EnsemblClinVar. | 1 | |
Natural variantiVAR_069335 | 478 | S → N in CRCS10; associated with disease susceptibility. 1 PublicationCorresponds to variant dbSNP:rs397514632EnsemblClinVar. | 1 | |
Natural variantiVAR_070231 | 605 | Missing in MDPL; the mutant enzyme lacks DNA polymerase ability; has decreased exonuclease activity; can bind DNA but is unable to interact with and incorporate dNTPs. 1 Publication | 1 | |
Natural variantiVAR_069336 | 787 | P → L Found in a colorectal sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs199783227EnsemblClinVar. | 1 | |
Natural variantiVAR_069337 | 808 | R → H Found in a colorectal sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs771700024EnsemblClinVar. | 1 | |
Natural variantiVAR_019344 | 849 | R → H1 PublicationCorresponds to variant dbSNP:rs3218775EnsemblClinVar. | 1 | |
Natural variantiVAR_069338 | 864 | A → T Found in a colorectal sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs765437818EnsemblClinVar. | 1 | |
Natural variantiVAR_019345 | 1086 | R → Q1 PublicationCorresponds to variant dbSNP:rs3219457EnsemblClinVar. | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M80397 mRNA Translation: AAA58439.1 M81735 mRNA Translation: AAA35768.1 AY129569 Genomic DNA Translation: AAM76971.1 BC008800 mRNA Translation: AAH08800.1 |
CCDSi | CCDS12795.1 |
PIRi | A41618 |
RefSeqi | NP_001243778.1, NM_001256849.1 NP_002682.2, NM_002691.3 XP_011525340.1, XM_011527038.1 XP_016882370.1, XM_017026881.1 |
Genome annotation databases
Ensembli | ENST00000440232; ENSP00000406046; ENSG00000062822 ENST00000599857; ENSP00000473052; ENSG00000062822 ENST00000601098; ENSP00000472600; ENSG00000062822 |
GeneIDi | 5424 |
KEGGi | hsa:5424 |
MANE-Selecti | ENST00000440232.7; ENSP00000406046.1; NM_002691.4; NP_002682.2 |
UCSCi | uc002psb.6, human |
Similar proteinsi
Cross-referencesi
Web resourcesi
NIEHS-SNPs |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M80397 mRNA Translation: AAA58439.1 M81735 mRNA Translation: AAA35768.1 AY129569 Genomic DNA Translation: AAM76971.1 BC008800 mRNA Translation: AAH08800.1 |
CCDSi | CCDS12795.1 |
PIRi | A41618 |
RefSeqi | NP_001243778.1, NM_001256849.1 NP_002682.2, NM_002691.3 XP_011525340.1, XM_011527038.1 XP_016882370.1, XM_017026881.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
6S1M | electron microscopy | 4.27 | A | 1-1107 | [»] | |
6S1N | electron microscopy | 4.86 | A | 1-1107 | [»] | |
6S1O | electron microscopy | 8.10 | A | 1-1107 | [»] | |
6TNY | electron microscopy | 3.08 | A | 1-1107 | [»] | |
6TNZ | electron microscopy | 4.05 | A | 1-1107 | [»] | |
SMRi | P28340 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 111420, 185 interactors |
ComplexPortali | CPX-2097, DNA polymerase delta complex |
CORUMi | P28340 |
IntActi | P28340, 53 interactors |
MINTi | P28340 |
STRINGi | 9606.ENSP00000406046 |
Chemistry databases
BindingDBi | P28340 |
ChEMBLi | CHEMBL2735 |
DrugCentrali | P28340 |
PTM databases
iPTMneti | P28340 |
PhosphoSitePlusi | P28340 |
Genetic variation databases
BioMutai | POLD1 |
DMDMi | 50403732 |
Proteomic databases
EPDi | P28340 |
jPOSTi | P28340 |
MassIVEi | P28340 |
MaxQBi | P28340 |
PaxDbi | P28340 |
PeptideAtlasi | P28340 |
PRIDEi | P28340 |
ProteomicsDBi | 54478 |
Protocols and materials databases
Antibodypediai | 3821, 358 antibodies from 36 providers |
CPTCi | P28340, 1 antibody |
DNASUi | 5424 |
Genome annotation databases
Ensembli | ENST00000440232; ENSP00000406046; ENSG00000062822 ENST00000599857; ENSP00000473052; ENSG00000062822 ENST00000601098; ENSP00000472600; ENSG00000062822 |
GeneIDi | 5424 |
KEGGi | hsa:5424 |
MANE-Selecti | ENST00000440232.7; ENSP00000406046.1; NM_002691.4; NP_002682.2 |
UCSCi | uc002psb.6, human |
Organism-specific databases
CTDi | 5424 |
DisGeNETi | 5424 |
GeneCardsi | POLD1 |
HGNCi | HGNC:9175, POLD1 |
HPAi | ENSG00000062822, Low tissue specificity |
MalaCardsi | POLD1 |
MIMi | 174761, gene 612591, phenotype 615381, phenotype |
neXtProti | NX_P28340 |
OpenTargetsi | ENSG00000062822 |
Orphaneti | 363649, Mandibular hypoplasia-deafness-progeroid features-lipodystrophy syndrome 447877, Polymerase proofreading-related adenomatous polyposis |
PharmGKBi | PA33496 |
VEuPathDBi | HostDB:ENSG00000062822 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG0969, Eukaryota |
GeneTreei | ENSGT00560000077365 |
HOGENOMi | CLU_000203_2_0_1 |
InParanoidi | P28340 |
PhylomeDBi | P28340 |
TreeFami | TF352785 |
Enzyme and pathway databases
BRENDAi | 2.7.7.7, 2681 |
PathwayCommonsi | P28340 |
Reactomei | R-HSA-110314, Recognition of DNA damage by PCNA-containing replication complex R-HSA-174411, Polymerase switching on the C-strand of the telomere R-HSA-174414, Processive synthesis on the C-strand of the telomere R-HSA-174417, Telomere C-strand (Lagging Strand) Synthesis R-HSA-174437, Removal of the Flap Intermediate from the C-strand R-HSA-2564830, Cytosolic iron-sulfur cluster assembly R-HSA-5358565, Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) R-HSA-5358606, Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta) R-HSA-5651801, PCNA-Dependent Long Patch Base Excision Repair R-HSA-5656169, Termination of translesion DNA synthesis R-HSA-5685942, HDR through Homologous Recombination (HRR) R-HSA-5696397, Gap-filling DNA repair synthesis and ligation in GG-NER R-HSA-5696400, Dual Incision in GG-NER R-HSA-6782135, Dual incision in TC-NER R-HSA-6782210, Gap-filling DNA repair synthesis and ligation in TC-NER R-HSA-69091, Polymerase switching R-HSA-69166, Removal of the Flap Intermediate R-HSA-69183, Processive synthesis on the lagging strand |
SignaLinki | P28340 |
SIGNORi | P28340 |
Miscellaneous databases
BioGRID-ORCSi | 5424, 772 hits in 1051 CRISPR screens |
ChiTaRSi | POLD1, human |
GeneWikii | POLD1 |
GenomeRNAii | 5424 |
Pharosi | P28340, Tclin |
PROi | PR:P28340 |
RNActi | P28340, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000062822, Expressed in stomach and 193 other tissues |
ExpressionAtlasi | P28340, baseline and differential |
Genevisiblei | P28340, HS |
Family and domain databases
Gene3Di | 1.10.132.60, 1 hit 3.30.420.10, 1 hit 3.90.1600.10, 1 hit |
InterProi | View protein in InterPro 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 IPR012337, RNaseH-like_sf IPR036397, RNaseH_sf IPR025687, Znf-C4pol |
Pfami | View protein in Pfam PF00136, DNA_pol_B, 1 hit PF03104, DNA_pol_B_exo1, 1 hit PF14260, zf-C4pol, 1 hit |
PRINTSi | PR00106, DNAPOLB |
SMARTi | View protein in SMART SM00486, POLBc, 1 hit |
SUPFAMi | SSF53098, SSF53098, 1 hit SSF56672, SSF56672, 1 hit |
PROSITEi | View protein in PROSITE PS00116, DNA_POLYMERASE_B, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | DPOD1_HUMAN | |
Accessioni | P28340Primary (citable) accession number: P28340 Secondary accession number(s): Q8NER3, Q96H98 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | December 1, 1992 |
Last sequence update: | July 19, 2004 | |
Last modified: | February 23, 2022 | |
This is version 213 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Human chromosome 19
Human chromosome 19: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families