RPA2
entrez
6118
canonical
uniprot
P15927
canonical
ensembl
ENSG00000117748
resolver
ensp
ENSP00000363017
resolver
ensp
ENSP00000363021
resolver
ensp
ENSP00000552563
resolver
ensp
ENSP00000605545
resolver
genesymbol
RPA2
resolver
genesymbol_syn
REPA2
resolver
genesymbol_syn
RPA32
resolver
genesymbol_syn
RPA34
resolver
hgnc
HGNC:10290
resolver
uniprot
B4DUL2
resolver
uniprot
Q52II0
resolver
uniprot
Q5TEI9
resolver
uniprot
Q5TEJ5
resolver
uniprot_entry
B4DUL2_HUMAN
resolver
uniprot_entry
RFA2_HUMAN
resolver
uniprot_sec
Q52II0
resolver
uniprot_sec
Q5TEI9
resolver
uniprot_sec
Q5TEJ5
resolver
amino_acid_sequence
MWNSGFESYGSSSYGGAGGYTQSPGGFGSPAPSQAEKKSRARAQHIVPCTISQLLSATLVDEVFRIGNVEISQVTIVGIIRHAEKAPTNIVYKIDDMTAAPMDVRQWVDTDDTSSENTVVPPETYVKVAGHLRSFQNKKSLVAFKIMPLEDMNEFTTHILEVINAHMVLSKANSQPSAGRAPISNPGMSEAGNFGGNSFMPANGLTVAQNQVLNLIKACPRPEGLNFQDLKNQLKHMSVSSIKQAVDFLSNEGHIYSTVDDDHFKSTDAE
uniprot
proteins
function
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). {ECO:0000269|PubMed:15205463, ECO:0000269|PubMed:17596542, ECO:0000269|PubMed:17765923, ECO:0000269|PubMed:17959650, ECO:0000269|PubMed:19116208, ECO:0000269|PubMed:20154705, ECO:0000269|PubMed:21504906, ECO:0000269|PubMed:2406247, ECO:0000269|PubMed:24332808, ECO:0000269|PubMed:7697716, ECO:0000269|PubMed:7700386, ECO:0000269|PubMed:8702565, ECO:0000269|PubMed:9430682, ECO:0000269|PubMed:9765279}.
uniprot
proteins
mass_dalton
29247
uniprot
proteins
mutagenesis
MUTAGEN 4; /note="S->A: Increased RAD51 foci formation and homologous recombination efficiency at DNA double-strand breaks; when associated with A-8."; /evidence="ECO:0000269|PubMed:21731742"; MUTAGEN 8; /note="S->A: Increased RAD51 foci formation and homologous recombination efficiency at DNA double-strand breaks; when associated with A-4."; /evidence="ECO:0000269|PubMed:20154705, ECO:0000269|PubMed:21731742"; MUTAGEN 8; /note="S->D: Lower homologous recombination efficiency following DNA double strand break. Impaired DNA synthesis following DNA damage; when associated with D-33. No effect on cell-cycle progression, nor DNA synthesis in undamaged cells; when associated with D-23; D-29 and D-33. Impaired DNA double strand breaks repair; when associated with D-23; D-29 and D-33. Extended DNA damage-induced G2-M checkpoint; when associated with D-23; D-29 and D-33. Preferentially interacts with RAD51; when associated with D-23; D-29 and D-33."; /evidence="ECO:0000269|PubMed:20154705, ECO:0000269|PubMed:21731742"; MUTAGEN 23; /note="S->D: No effect on DNA synthesis following DNA damage; when associated with D-29. No effect on cell-cycle progression, nor DNA synthesis in undamaged cells; when associated with D-8; D-29 and D-33. Impaired DNA double strand breaks repair; when associated with D-8; D-29 and D-33. Extended DNA damage-induced G2-M checkpoint; when associated with D-8; D-29 and D-33. Preferentially interacts with RAD51; when associated with D-8; D-29 and D-33."; /evidence="ECO:0000269|PubMed:20154705"; MUTAGEN 29; /note="S->A: Reduces phosphorylation by CDK1."; /evidence="ECO:0000269|PubMed:20154705, ECO:0000269|PubMed:9139719"; MUTAGEN 29; /note="S->D: No effect on DNA synthesis following DNA damage; when associated with D-23. No effect on cell-cycle progression, nor DNA synthesis in undamaged cells; when associated with D-8; D-23 and D-33. Impaired DNA double strand breaks repair; when associated with D-8; D-23 and D-33. Extended DNA damage-induced G2-M checkpoint; when associated with D-8; D-23 and D-33. Preferentially interacts with RAD51; when associated with D-8; D-23 and D-33."; /evidence="ECO:0000269|PubMed:20154705, ECO:0000269|PubMed:9139719"; MUTAGEN 33; /note="S->D: Lower homologous recombination efficiency following DNA double strand break. Impaired DNA synthesis following DNA damage; when associated with D-8. No effect on cell-cycle progression, nor DNA synthesis in undamaged cells; when associated with D-8; D-23 and D-29. Impaired DNA double strand breaks repair; when associated with D-8; D-23 and D-29. Extended DNA damage-induced G2-M checkpoint; when associated with D-8; D-23 and D-29. Preferentially interacts with RAD51; when associated with D-8; D-23 and D-29."; /evidence="ECO:0000269|PubMed:20154705"; MUTAGEN 37..38; /note="KK->RR: Impaired ubiquitination without affecting homologous recombination."; /evidence="ECO:0000269|PubMed:26474068"; MUTAGEN 248; /note="F->A: Abolishes interaction with RFWD3, leading to impair DNA interstrand cross-links (ICL) repair."; /evidence="ECO:0000269|PubMed:28575657"; MUTAGEN 252; /note="E->A: Abolishes interaction with RFWD3, leading to impair DNA interstrand cross-links (ICL) repair."; /evidence="ECO:0000269|PubMed:28575657"; MUTAGEN 253; /note="G->A: Does not affect interaction with RFWD3."; /evidence="ECO:0000269|PubMed:28575657"; MUTAGEN 254; /note="H->A: Abolishes interaction with RFWD3, leading to impair DNA interstrand cross-links (ICL) repair."; /evidence="ECO:0000269|PubMed:28575657
uniprot
proteins
post_translational_modification
PTM: Differentially phosphorylated throughout the cell cycle, becoming phosphorylated at the G1-S transition and dephosphorylated in late mitosis. Mainly phosphorylated at Ser-23 and Ser-29, by cyclin A-CDK2 and cyclin B-CDK1, respectively during DNA replication and mitosis. Dephosphorylation may require the serine/threonine-protein phosphatase 4. Phosphorylation at Ser-23 and Ser-29 is a prerequisite for further phosphorylation. Becomes hyperphosphorylated on additional residues including Ser-4, Ser-8, Thr-21 and Ser-33 in response to DNA damage. Hyperphosphorylation is mediated by ATM, ATR and PRKDC. Primarily recruited to DNA repair nuclear foci as a hypophosphorylated form it undergoes subsequent hyperphosphorylation, catalyzed by ATR. Hyperphosphorylation is required for RAD51 recruitment to chromatin and efficient DNA repair. Phosphorylation at Thr-21 depends upon RFWD3 presence. {ECO:0000269|PubMed:12814551, ECO:0000269|PubMed:1318195, ECO:0000269|PubMed:20154705, ECO:0000269|PubMed:21558276, ECO:0000269|PubMed:21731742, ECO:0000269|PubMed:26474068, ECO:0000269|PubMed:8246944, ECO:0000269|PubMed:9139719, ECO:0000269|PubMed:9295339}.; PTM: DNA damage-induced 'Lys-63'-linked polyubiquitination by PRPF19 mediates ATRIP recruitment to the RPA complex at sites of DNA damage and activation of ATR (PubMed:24332808). 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). {ECO:0000269|PubMed:24332808, ECO:0000269|PubMed:26474068}.
uniprot
proteins
protein_family
Replication factor A protein 2 family
uniprot
proteins
pubmed
10449415
uniprot
proteins
pubmed
10982866
uniprot
proteins
pubmed
11081631
uniprot
proteins
pubmed
11927569
uniprot
proteins
pubmed
12814551
uniprot
proteins
pubmed
1318195
uniprot
proteins
pubmed
15205463
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17141802
uniprot
proteins
pubmed
17296725
uniprot
proteins
pubmed
17596542
uniprot
proteins
pubmed
17765923
uniprot
proteins
pubmed
17959650
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19116208
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19793861
uniprot
proteins
pubmed
19793862
uniprot
proteins
pubmed
19793863
uniprot
proteins
pubmed
19996105
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20154705
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21504906
uniprot
proteins
pubmed
21558276
uniprot
proteins
pubmed
21731742
uniprot
proteins
pubmed
2200738
uniprot
proteins
pubmed
22521144
uniprot
proteins
pubmed
22684010
uniprot
proteins
pubmed
23319600
uniprot
proteins
pubmed
23393223
uniprot
proteins
pubmed
2406247
uniprot
proteins
pubmed
24332808
uniprot
proteins
pubmed
24910198
uniprot
proteins
pubmed
26474068
uniprot
proteins
pubmed
27601467
uniprot
proteins
pubmed
27723717
uniprot
proteins
pubmed
27723720
uniprot
proteins
pubmed
28575657
uniprot
proteins
pubmed
29290612
uniprot
proteins
pubmed
7697716
uniprot
proteins
pubmed
7700386
uniprot
proteins
pubmed
8246944
uniprot
proteins
pubmed
8702565
uniprot
proteins
pubmed
9139719
uniprot
proteins
pubmed
9295339
uniprot
proteins
pubmed
9430682
uniprot
proteins
pubmed
9765279
uniprot
proteins
sequence_length
270
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10982866, ECO:0000269|PubMed:12814551, ECO:0000269|PubMed:17596542, ECO:0000269|PubMed:20154705, ECO:0000269|PubMed:21504906}. Nucleus, PML body {ECO:0000269|PubMed:12814551}. Note=Redistributes to discrete nuclear foci upon DNA damage in an ATR-dependent manner. {ECO:0000269|PubMed:12814551}.
uniprot
proteins