Rpa2
entrez
19891
canonical
uniprot
Q62193
canonical
ensembl
ENSMUSG00000028884
resolver
ensp
ENSMUSP00000099621
resolver
enst
ENSMUST00000102561
resolver
genesymbol
Rpa2
resolver
genesymbol_syn
Rpa34
resolver
uniprot
Q3TE40
resolver
uniprot_entry
RFA2_MOUSE
resolver
uniprot_sec
Q3TE40
resolver
amino_acid_sequence
MWNSGFESFSSSTYGGAGGYTQSPGGFGSPTPSQAEKKSRVRAQHIVPCTISQLLSATLTDEVFRIGDVEISQVTIVGIIRHAEKAPTNIVYKIDDMTAPPMDVRQWVDTDDASGENAVVPPETYVKVAGHLRSFQNKKSLVAFKIIPLEDMNEFTAHILEVVNSHMMLSKPNSQASAGRPSMSNPGMSEPGNFSGNNFMPANGLTVVQNQVLNLIKACPRPEGLNFQDLRSQLQHMPVPSIKQAVDFLCNEGHIYSTVDDDHFKSTDAE
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. {ECO:0000250|UniProtKB:P15927}.
uniprot
proteins
mass_dalton
29440
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:0000250|UniProtKB:P15927}.; 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. 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. {ECO:0000250|UniProtKB:P15927}.
uniprot
proteins
protein_family
Replication factor A protein 2 family
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17141802
uniprot
proteins
pubmed
1908076
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
sequence_length
270
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P15927}. Nucleus, PML body {ECO:0000250|UniProtKB:P15927}. Note=Redistributes to discrete nuclear foci upon DNA damage in an ATR-dependent manner. {ECO:0000250|UniProtKB:P15927, ECO:0000269|PubMed:17141802}.
uniprot
proteins