Overview
| Uniprot ID | P35244 |
|---|
| Protein Name | Replication protein A 14 kDa subunit |
|---|
| Gene Name | RPA3 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 23 |
MLAQFIDKPVCFVGR |
| 33 |
CFVGRLEKIHPTGKM |
Function
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:17596542, 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). RPA stimulates 5'-3' helicase activity of BRIP1/FANCJ (PubMed:17596542). 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)
Protein Sequence
10
MVDMMDLPRS
20
RINAGMLAQF
30
IDKPVCFVGR
40
LEKIHPTGKM
50
FILSDGEGKN
60
GTIELMEPLD
70
EEISGIVEVV
80
GRVTAKATIL
90
CTSYVQFKED
100
SHPFDLGLYN
110
EAVKIIHDFP
120
QFYPLGIVQH
D
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005662 |
DNA replication factor A complex |
| Cellular Component |
GO:0005654 |
nucleoplasm |
| Cellular Component |
GO:0035861 |
site of double-strand break |
| Molecular Function |
GO:0003684 |
damaged DNA binding |
| Molecular Function |
GO:0003697 |
single-stranded DNA binding |
| Biological Process |
GO:0006284 |
base-excision repair |
| Biological Process |
GO:0006281 |
DNA repair |
| Biological Process |
GO:0006260 |
DNA replication |
| Biological Process |
GO:0000724 |
double-strand break repair via homologous recombination |
| Biological Process |
GO:0006298 |
mismatch repair |
| Biological Process |
GO:0006289 |
nucleotide-excision repair |
| Biological Process |
GO:0000723 |
telomere maintenance |
Reference
[1] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.