Overview
| Uniprot ID | P15927 |
| Protein Name | Replication protein A 32 kDa subunit |
| Gene Name | RPA2 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 235 |
QDLKNQLKHMSVSSI |
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. 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. 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. Also plays a role in base excision repair (BER) probably through interaction with UNG. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance. RPA stimulates 5'-3' helicase activity of BRIP1/FANCJ (PubMed:17596542)
Protein Sequence
10
MWNSGFESYG
20
SSSYGGAGGY
30
TQSPGGFGSP
40
APSQAEKKSR
50
ARAQHIVPCT
60
ISQLLSATLV
70
DEVFRIGNVE
80
ISQVTIVGII
90
RHAEKAPTNI
100
VYKIDDMTAA
110
PMDVRQWVDT
120
DDTSSENTVV
130
PPETYVKVAG
140
HLRSFQNKKS
150
LVAFKIMPLE
160
DMNEFTTHIL
170
EVINAHMVLS
180
KANSQPSAGR
190
APISNPGMSE
200
AGNFGGNSFM
210
PANGLTVAQN
220
QVLNLIKACP
230
RPEGLNFQDL
240
KNQLKHMSVS
250
SIKQAVDFLS
260
NEGHIYSTVD
270
DDHFKSTDAE
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0000785 |
chromatin |
| 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:0031571 |
mitotic G1 DNA damage checkpoint signaling |
| Biological Process |
GO:0006289 |
nucleotide-excision repair |
| Biological Process |
GO:0034502 |
protein localization to chromosome |
| Biological Process |
GO:2000001 |
regulation of DNA damage checkpoint |
| Biological Process |
GO:0010569 |
regulation of double-strand break repair via homologous recombination |
| Biological Process |
GO:0000723 |
telomere maintenance |
| Cellular Component |
GO:0000781 |
chromosome, telomeric region |
| Cellular Component |
GO:0005662 |
DNA replication factor A complex |
| Cellular Component |
GO:0016604 |
nuclear body |
| Cellular Component |
GO:0005654 |
nucleoplasm |
| Cellular Component |
GO:0005634 |
nucleus |
| Cellular Component |
GO:0016605 |
PML body |
| Molecular Function |
GO:0003684 |
damaged DNA binding |
| Molecular Function |
GO:0019899 |
enzyme binding |
| Molecular Function |
GO:0098505 |
G-rich strand telomeric DNA binding |
| Molecular Function |
GO:0019903 |
protein phosphatase binding |
| Molecular Function |
GO:0003697 |
single-stranded DNA binding |
| Molecular Function |
GO:0042162 |
telomeric DNA binding |
| Molecular Function |
GO:0031625 |
ubiquitin protein ligase binding |
| Biological Process |
GO:0006284 |
base-excision repair |
Reference
PMID: N/A