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Protein

DNA polymerase delta subunit 4

Gene

Pold4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

As a component of the tetrameric DNA polymerase delta complex (Pol-delta4), plays a role in high fidelity genome replication and repair. Within this complex, increases the rate of DNA synthesis and decreases fidelity by regulating POLD1 polymerase and proofreading 3' to 5' exonuclease activity. Pol-delta4 participates in Okazaki fragment processing, through both the short flap pathway, as well as a nick translation system. Under conditions of DNA replication stress, required for the repair of broken replication forks through break-induced replication (BIR), a mechanism that may induce segmental genomic duplications of up to 200 kb. Involved in Pol-delta4 translesion synthesis (TLS) of templates carrying O6-methylguanine or abasic sites. Its degradation in response to DNA damage is required for the inhibition of fork progression and cell survival.By similarity

GO - Molecular functioni

GO - Biological processi

  • DNA-dependent DNA replication Source: GO_Central
  • DNA synthesis involved in DNA repair Source: GO_Central
  • positive regulation of endothelial cell proliferation Source: MGI
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA excision, DNA repair, DNA replication

Enzyme and pathway databases

ReactomeiR-MMU-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-MMU-174411. Polymerase switching on the C-strand of the telomere.
R-MMU-174414. Processive synthesis on the C-strand of the telomere.
R-MMU-174417. Telomere C-strand (Lagging Strand) Synthesis.
R-MMU-174437. Removal of the Flap Intermediate from the C-strand.
R-MMU-5358565. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
R-MMU-5358606. Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
R-MMU-5651801. PCNA-Dependent Long Patch Base Excision Repair.
R-MMU-5656169. Termination of translesion DNA synthesis.
R-MMU-5685942. HDR through Homologous Recombination (HRR).
R-MMU-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-MMU-5696400. Dual Incision in GG-NER.
R-MMU-6782135. Dual incision in TC-NER.
R-MMU-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-MMU-69091. Polymerase switching.
R-MMU-69166. Removal of the Flap Intermediate.
R-MMU-69183. Processive synthesis on the lagging strand.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase delta subunit 4
Alternative name(s):
DNA polymerase delta subunit p12
Gene namesi
Name:Pold4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1916995. Pold4.

Subcellular locationi

  • Nucleus By similarity

  • Note: Partially recruited to DNA damage sites within 2 hours following UV irradiation, before degradation.By similarity

GO - Cellular componenti

  • delta DNA polymerase complex Source: GO_Central
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001860521 – 107DNA polymerase delta subunit 4Add BLAST107

Post-translational modificationi

Ubiquitinated; undergoes 'Lys-48'-linked polyubiquitination in response to UV irradiation or treatment with an alkylating agent, leading to proteasomal degradation. This modification is mediated, at least in part, by RNF8.1 Publication
Ubiquitinated; undergoes 'Lys-48'-linked ubiquitination in response to UV irradiation, leading to proteasomal degradation. This modification is partly mediated by RNF8 and by the DCX(DTL) E3 ubiquitin ligase complex (also called CRL4(CDT2)). Efficient degradation requires the presence of PCNA and is required for the inhibition of fork progression after DNA damage.By similarity

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiQ9CWP8.
PaxDbiQ9CWP8.
PRIDEiQ9CWP8.

PTM databases

PhosphoSitePlusiQ9CWP8.

Expressioni

Inductioni

In response to DNA damage or genotoxic stress, such as UV irradiation or treatment with an alkylating agent, protein expression drastically drops.1 Publication

Gene expression databases

BgeeiENSMUSG00000024854.
CleanExiMM_POLD4.
ExpressionAtlasiQ9CWP8. baseline and differential.
GenevisibleiQ9CWP8. MM.

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 DNA polymerase and 3' to 5' proofreading exonuclease activities. Within this complex, directly interacts with POLD1 and POLD2. Directly interacts with PCNA, as do POLD1 and POLD3; this interaction stimulates Pol-delta4 polymerase activity. As POLD1 and POLD2, directly interacts with WRNIP1; this interaction stimulates DNA polymerase delta-mediated DNA synthesis, independently of the presence of PCNA, possibly by increasing initiation frequency. Upon genotoxic stress induced by DNA damaging agents or by replication stress, POLD4 is proteolytically degraded and Pol-delta4 is converted into a trimeric form of the complex (Pol-delta3) that has a increased proofreading activity. The DNA polymerase delta complex interacts with POLDIP2; this interaction is probably mediated through direct binding to POLD2.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000025773.

Structurei

3D structure databases

ProteinModelPortaliQ9CWP8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1 – 16PCNA-interaction protein motif (PIP box)By similarityAdd BLAST16

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410J65P. Eukaryota.
ENOG410XUCX. LUCA.
GeneTreeiENSGT00390000005096.
HOGENOMiHOG000031022.
HOVERGENiHBG057838.
InParanoidiQ9CWP8.
KOiK03505.
OMAiWERAKLH.
OrthoDBiEOG091G10DR.
PhylomeDBiQ9CWP8.
TreeFamiTF103004.

Family and domain databases

InterProiIPR007218. DNA_pol_delta_4.
[Graphical view]
PfamiPF04081. DNA_pol_delta_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9CWP8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRKRFITDS YPVVKKREGP PGHSKGELAP ELGEDTQSLS QEETELELLR
60 70 80 90 100
QFDLAWQYGP CTGITRLQRW SRAEQMGLKP PLEVYQVLKA HPEDPHFQCS

LWHLYPL
Length:107
Mass (Da):12,403
Last modified:June 1, 2001 - v1
Checksum:i14A27054D4E7511E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK010477 mRNA. Translation: BAB26970.1.
BC028520 mRNA. Translation: AAH28520.1.
CCDSiCCDS29424.1.
RefSeqiNP_081472.1. NM_027196.4.
UniGeneiMm.32518.

Genome annotation databases

EnsembliENSMUST00000025773; ENSMUSP00000025773; ENSMUSG00000024854.
ENSMUST00000180621; ENSMUSP00000137813; ENSMUSG00000097508.
GeneIDi69745.
KEGGimmu:69745.
UCSCiuc008fzm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK010477 mRNA. Translation: BAB26970.1.
BC028520 mRNA. Translation: AAH28520.1.
CCDSiCCDS29424.1.
RefSeqiNP_081472.1. NM_027196.4.
UniGeneiMm.32518.

3D structure databases

ProteinModelPortaliQ9CWP8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000025773.

PTM databases

PhosphoSitePlusiQ9CWP8.

Proteomic databases

MaxQBiQ9CWP8.
PaxDbiQ9CWP8.
PRIDEiQ9CWP8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025773; ENSMUSP00000025773; ENSMUSG00000024854.
ENSMUST00000180621; ENSMUSP00000137813; ENSMUSG00000097508.
GeneIDi69745.
KEGGimmu:69745.
UCSCiuc008fzm.2. mouse.

Organism-specific databases

CTDi57804.
MGIiMGI:1916995. Pold4.

Phylogenomic databases

eggNOGiENOG410J65P. Eukaryota.
ENOG410XUCX. LUCA.
GeneTreeiENSGT00390000005096.
HOGENOMiHOG000031022.
HOVERGENiHBG057838.
InParanoidiQ9CWP8.
KOiK03505.
OMAiWERAKLH.
OrthoDBiEOG091G10DR.
PhylomeDBiQ9CWP8.
TreeFamiTF103004.

Enzyme and pathway databases

ReactomeiR-MMU-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-MMU-174411. Polymerase switching on the C-strand of the telomere.
R-MMU-174414. Processive synthesis on the C-strand of the telomere.
R-MMU-174417. Telomere C-strand (Lagging Strand) Synthesis.
R-MMU-174437. Removal of the Flap Intermediate from the C-strand.
R-MMU-5358565. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
R-MMU-5358606. Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
R-MMU-5651801. PCNA-Dependent Long Patch Base Excision Repair.
R-MMU-5656169. Termination of translesion DNA synthesis.
R-MMU-5685942. HDR through Homologous Recombination (HRR).
R-MMU-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-MMU-5696400. Dual Incision in GG-NER.
R-MMU-6782135. Dual incision in TC-NER.
R-MMU-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-MMU-69091. Polymerase switching.
R-MMU-69166. Removal of the Flap Intermediate.
R-MMU-69183. Processive synthesis on the lagging strand.

Miscellaneous databases

PROiQ9CWP8.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000024854.
CleanExiMM_POLD4.
ExpressionAtlasiQ9CWP8. baseline and differential.
GenevisibleiQ9CWP8. MM.

Family and domain databases

InterProiIPR007218. DNA_pol_delta_4.
[Graphical view]
PfamiPF04081. DNA_pol_delta_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDPOD4_MOUSE
AccessioniPrimary (citable) accession number: Q9CWP8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: June 1, 2001
Last modified: November 30, 2016
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.