Rpa2
entrez
59102
canonical
uniprot
Q63528
canonical
ensembl
ENSRNOG00000013005
resolver
ensembl
ENSRNOG00065028723
resolver
ensp
ENSRNOP00000017549
resolver
ensp
ENSRNOP00000087831
resolver
ensp
ENSRNOP00065040700
resolver
enst
ENSRNOT00000017549
resolver
enst
ENSRNOT00000105125
resolver
enst
ENSRNOT00065049578
resolver
genesymbol
Rpa2
resolver
uniprot
A0A8I6A4W5
resolver
uniprot
Q6AY60
resolver
uniprot_entry
A0A8I6A4W5_RAT
resolver
uniprot_entry
RFA2_RAT
resolver
uniprot_sec
Q6AY60
resolver
amino_acid_sequence
MWNSGFESFSSSSYGAAGGYTQSPGGFGSPTPSQAEKKSRARAQHIVPCTISQLLSATLTDEVFKIGDVEISQVTIVGIIRHAEKAPTNIVYKIDDMTAAPMDVRQWVDTDDTSGENTVVPPETYVKVAGHLRSFQNKKSLVAFKIIPLEDMNEFTAHILEVVNSHLMLSKANSQASVGRPSMSNPGMGEPGNFSGNNFMPANGLTVVQNQVLNLIKACPRPEGLNFQDLRSQLQHMPVASIKQAVDFLCNEGHIYSTVDDDHFKSTDAE
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
29346
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
15489334
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}.
uniprot
proteins