RPA3

RPA3 (Replication Protein A3) is a Protein Coding gene. Diseases associated with RPA3 include Epidemic Typhus and Retinitis Pigmentosa 12. Among its related pathways are Mismatch repair and Telomere C-strand (Lagging Strand) Synthesis. Gene Ontology (GO) annotations related to this gene include single-stranded DNA binding and damaged DNA binding.

replication protein A3, 14kDa

As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage (PubMed:9430682).
In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response (PubMed:24332808).
It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin, in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair (PubMed:7697716).
Also plays a role in base excision repair (BER), probably through interaction with UNG (PubMed:9765279).
Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance. RPA3 has its own single-stranded DNA-binding activity and may be responsible for polarity of the binding of the complex to DNA (PubMed:19010961).
As part of the alternative replication protein A complex, aRPA, binds single-stranded DNA and probably plays a role in DNA repair. Compared to the RPA2-containing, canonical RPA complex, may not support chromosomal DNA replication and cell cycle progression through S-phase. The aRPA may not promote efficient priming by DNA polymerase alpha but could support DNA synthesis by polymerase delta in presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange (PubMed:19996105).

Biological Process base-excision repairManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process DNA repairManual Assertion Based On ExperimentIDA:ComplexPortal
Biological Process DNA replicationManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process double-strand break repair via homologous recombinationManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process mismatch repairManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process nucleotide-excision repairManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process regulation of cell population proliferationIEA:Ensembl
Biological Process regulation of mitotic cell cycleIEA:Ensembl
Biological Process telomere maintenanceManual Assertion Based On ExperimentTAS:BHF-UCL

Nucleus

Ubiquitinated by RFWD3 at stalled replication forks in response to DNA damage: ubiquitination by RFWD3 does not lead to degradation by the proteasome and promotes removal of the RPA complex from stalled replication forks, promoting homologous recombination (PubMed:26474068).