Search results for POLD1

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Protein (2 results from a total of 2)

Identifier: R-HSA-2564763
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: POLD1: P28340
Identifier: R-HSA-68449
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: POLD1: P28340

Complex (1 results from a total of 1)

Identifier: R-HSA-2564786
Species: Homo sapiens
Compartment: cytosol

Reaction (3 results from a total of 3)

Identifier: R-HSA-5653838
Species: Homo sapiens
Compartment: nucleoplasm
Once deubiquitinated and deISGylated, PCNA can again associate with the catalytic subunit POLD1 of replicative DNA polymerase delta complex (POLD), or presumably POLE of DNA polymerase epsilon complex (POLE) (Park et al. 2014). Double monoubiquitination of PCNA-associated protein KIAA0101 (PAF15) facilitates the switch from translesion DNA synthesis (TLS) polymerases to replicative DNA polymerases POLD or POLE (Povlsen et al. 2012).
Identifier: R-HSA-5652009
Species: Homo sapiens
Compartment: nucleoplasm
The complex of RAD18, an E3 ubiquitin ligase, and UBE2B (RAD6), an E2 ubiquitin conjugating enzyme, monoubiquitinates PCNA associated with damaged DNA on lysine residue K164, using the ubiquitin residue K63 to create the covalent bond (Hoege et al. 2002). The catalytic subunit of DNA polymerase delta (POLD), POLD1, does not bind monoubiquitinated PCNA (Park et al. 2014), implying that replicative polymerases POLD and POLE (DNA polymerase epsilon complex) dissociate from PCNA monubiquitinated at K164. This is in accordance with the proposed DNA polymerase switch during translesion DNA synthesis (TLS) (Friedberg et al. 2005). DNA damage induced removal of PCNA-associated protein KIAA0101 (PAF15) through proteasome-mediated degradation facilitates switching from replicative DNA polymerases POLD and POLE to TLS polymerases (Povlsen et al. 2012).

The ubiquitin ligase complex RBX1:CUL4:DDB1:DTL can also monoubiquitinate PCNA. RBX1:CUL4:DDB1:DTL is probably responsible for the basal monoubiquitination of PCNA and may contribute to the kinetics of DNA-damage induced PCNA monoubiquitination (Terai et al. 2010).

Identifier: R-HSA-2564828
Species: Homo sapiens
Compartment: cytosol
A complex of four proteins termed CIA targeting complex is involved in the delivery of the NUBP1-NUBP2-bound Fe/S cluster to specific target apoproteins. NARFL (IOP1, Nar1 in yeast) is similar in sequence to iron-only hydrogenases and binds two [4Fe-4S] clusters. These cofactors are essential for biogenesis but their molecular function is unknown. The WD40 domain protein CIAO1 (Cia1 in yeast) forms a propeller-like structure which may serve as a docking site for the other members of the CIA targeting complex. The role of FAM96B (YHR122W, CIA2 in yeast) and MMS19 is still unclear, but they show some specificity for the delivery of Fe/S clusters into certain target apoproteins. They directly interact with numerous Fe/S target proteins including many proteins involved in nuclear DNA integrity and maintenance such as DNA polymerases (POLD1), helicases of the DNA repair pathway (XPD or FANCJ) or of telomere maintenance (RTEL1), and primases. Cells with mutated MMS19 are hypersensitive to DNA damage and have elongated telomeres therefore these target proteins are relevant to various cancer-related diseases and aging.

Pathway (1 results from a total of 1)

Identifier: R-HSA-2564830
Species: Homo sapiens
Compartment: cytosol
Iron-sulfur clusters containing 4 atoms of iron and 4 atoms of sulfur (4Fe-4S clusters) are assembled in the cytosol on a heterotetrameric scaffold composed of NUBP2 and NUBP1 subunits (reviewed in Lill et al. 2012, Rouault et al. 2012, Sharma et al. 2010, Lill and Muhlenhoff 2006). The sources of iron and sulfur are uncertain but the process requires a sulfur-containing compound exported from mitochondria via ABCB7 (ABC7). Newly synthesized 4Fe-4S are transferred to apoproteins such as XPD and POLD1 via the CIA targeting complex, composed of NARFL, CIAO1, FAM96B, and MMS19.
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