Search results for POLH

Showing 19 results out of 24

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Species

Types

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Protein (3 results from a total of 3)

Identifier: R-HSA-110287
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: POLH: Q9Y253
Identifier: R-HSA-5655163
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: POLH: Q9Y253
Identifier: R-HSA-5687494
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: POLQ: O75417

Reaction (5 results from a total of 10)

Identifier: R-HSA-110319
Species: Homo sapiens
Compartment: nucleoplasm
After incorporating two dAMPs opposite the thymine-thymine cyclobutane pyrimidine dimer (TT-CPD), DNA polymerase eta (POLH) can continue translesion DNA synthesis (TLS). POLH preferentially incorporates dAMPs and dGMPs, and may introduce one error per every 18-380 nucleotides (dNMPs) added. POLH stalls after incorporation of a mispaired dNMP, which limits POLH- mediated mutagenesis, in addition to the subsequent polymerase switch (Matsuda et al. 2000, Masutani et al. 2000).
Identifier: R-HSA-5655170
Species: Homo sapiens
Compartment: nucleoplasm
RCHY1 (Pirh2) acts as an E3 ubiquitin ligase to monoubiquitinate POLH (DNA polymerase eta) on lysine residues K682, K686, K694 and K709 located in the NLS (nuclear localization signal) of POLH (Jung et al. 2011). The NLS sequence of POLH is located between UBZ domain and PIP box, involved in POLH binding to monoubiquitinated PCNA (MonoUb:K164-PCNA). POLH monoubiquitination masks the PCNA-interaction region, thus disabling POLH binding to MonoUb:K164-PCNA and preventing POLH-mediated translesion DNA synthesis (TLS) (Bienko et al. 2010).
Identifier: R-HSA-5655142
Species: Homo sapiens
Compartment: nucleoplasm
RCHY1 (Pirh2) is an E3 ubiquitin ligase that binds DNA polymerase eta (POLH). This interaction involves the polymerase-associated domain of POLH and the RING finger of RCHY1 (Jung et al. 2010).
Identifier: R-HSA-5654989
Species: Homo sapiens
Compartment: nucleoplasm
The ATP-ase activity of VCP facilitates release of POLH (DNA polymerase eta) from monoubiquitinated PCNA (MonoUb:K164-PCNA) at DNA damage sites, thus ending POLH-mediated translesion DNA synthesis (TLS) (Davis et al. 2012, Mosbech et al. 2012). Although conjugation of the ubiquitin-like protein ISG15 to PCNA has been found to terminate POLH-dependent TLS, the SPRTN:VCP complex has been implicated in serving as an alternative termination pathway (Park et al. 2014). Since VCP has been found to undergo ISGylation (Giannakopoulos et al. 2005), it remains to be determined whether SPRTN, VCP and the ISG15-conjugating system function in the same TLS-regulatory pathway or two separate pathways.
Identifier: R-HSA-5654986
Species: Homo sapiens
Compartment: nucleoplasm
SPRTN (Spartan, C1orf124, DVC1) contains a PIP box and a UBZ domain that both participate in binding to monoubiquitinated PCNA (MonoUb:K164-PCNA), thus regulating POLH-mediated translesion DNA synthesis (TLS). The SPRTN UBZ domain may also interact with other monoubiquitinated proteins at the site of DNA damage. SPRTN can also bind RAD18 and function in a positive feedback loop to increase (or maintain) PCNA monoubiquitination (Centore et al. 2012, Ghosal et al. 2012).


Endogenous SPRTN is predominantly expressed during S and G2 phases of the cell cycle, and is rapidly degraded by the APC:CDH1 complex at mitotic exit (Mosbech et al. 2012).

Pathway (3 results from a total of 3)

Identifier: R-HSA-110320
Species: Homo sapiens
Compartment: nucleoplasm
DNA polymerase eta (POLH) consists of 713 amino acids and can bypass thymidine-thymidine dimers, correctly adding two dAMPs opposite to the lesion. Mutations in the POLH gene result in the loss of this bypass activity and account for the XP variant phenotype (XPV) in human xeroderma pigmentosum disorder patients. POLH can carry out TLS past various UV and chemically induced lesions via two steps: (a) preferential incorporation of correct bases opposite to the lesion (b) conditional elongation only at the sites where such correct bases are inserted (Masutani et al. 1999, Masutani et al. 2000).
Identifier: R-HSA-73893
Species: Homo sapiens
Compartment: nucleoplasm
In addition to various processes for removing lesions from the DNA, cells have developed specific mechanisms for tolerating unrepaired damage during the replication of the genome. These mechanisms are collectively called DNA damage bypass pathways. The Y family of DNA polymerases plays a key role in DNA damage bypass.

Y family DNA polymerases, REV1, POLH (DNA polymerase eta), POLK (DNA polymerase kappa) and POLI (DNA polymerase iota), as well as the DNA polymerase zeta (POLZ) complex composed of REV3L and MAD2L2, are able to carry out translesion DNA synthesis (TLS) or replicative bypass of damaged bases opposite to template lesions that arrest high fidelity, highly processive replicative DNA polymerase complexes delta (POLD) and epsilon (POLE). REV1, POLH, POLK, POLI and POLZ lack 3'->5' exonuclease activity and exhibit low fidelity and weak processivity. The best established TLS mechanisms are annotated here. TLS details that require substantial experimental clarification have been omitted. For recent and past reviews of this topic, please refer to Lehmann 2000, Friedberg et al. 2001, Zhu and Zhang 2003, Takata and Wood 2009, Ulrich 2011, Saugar et al. 2014.

Identifier: R-HSA-110314
Species: Homo sapiens
Compartment: nucleoplasm
Damaged double strand DNA (dsDNA) cannot be successfully used as a template by replicative DNA polymerase delta (POLD) and epsilon (POLE) complexes (Hoege et al. 2002). When the replication complex composed of PCNA, RPA, RFC and POLD or POLE stalls at a DNA damage site, PCNA becomes monoubiquitinated by RAD18 bound to UBE2B (RAD6). POLD or POLE dissociate from monoubiquitinated PCNA, while Y family DNA polymerases - REV1, POLH (DNA polymerase eta), POLK (DNA polymerase kappa) and POLI (DNA polymerase iota) - bind monoubiquitinated PCNA through their ubiquitin binding and PCNA binding motifs, resulting in a polymerase switch and initiation of translesion synthesis (TLS) (Hoege et al. 2002, Friedberg et al. 2005).

Interactor (1 results from a total of 1)

Identifier: O75417-1
Species: Homo sapiens
Primary external reference: UniProt: O75417-1

Set (2 results from a total of 2)

Identifier: R-HSA-5686093
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-5686084
Species: Homo sapiens
Compartment: nucleoplasm

Complex (5 results from a total of 5)

Identifier: R-HSA-5655156
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-5655139
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-110290
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-110288
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-5654981
Species: Homo sapiens
Compartment: nucleoplasm
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