Rpa1
entrez
68275
canonical
uniprot
Q8VEE4
canonical
ensembl
ENSMUSG00000000751
resolver
ensp
ENSMUSP00000000767
resolver
ensp
ENSMUSP00000090585
resolver
ensp
ENSMUSP00000302756
resolver
enst
ENSMUST00000000767
resolver
enst
ENSMUST00000092907
resolver
genesymbol
Rpa1
resolver
uniprot
Q3TEJ8
resolver
uniprot
Q3U8B3
resolver
uniprot
Q5SWN2
resolver
uniprot_entry
Q3U8B3_MOUSE
resolver
uniprot_entry
Q5SWN2_MOUSE
resolver
uniprot_entry
RFA1_MOUSE
resolver
uniprot_sec
Q3TEJ8
resolver
amino_acid_sequence
MVGHLSEGAIEVMIQQENTSIKPILQVINIRPISTGNRSPRYRLLMSDGLNTLSSFMLATQLNTLVEGGQLASNCVCQVHKFIVNTLKDGRKVVVLMDLEVMKSAEDVGLKIGNPVPYNEGYGQQQQQQQQQQQQAVPSPASAATPPASKPQPQNGSLGMGSTAAKAYGASKPFGKPAGTGLLQPSGGTQSKVVPIASLTPYQSKWTICARVTNKSQIRTWSNSRGEGKLFSLELVDESGEIRATAFNEQVDKFFPLIEVNKVYYFSKGALKIANKQFSAVKNDYEMTFNNETSVLPCEDGHHLPTVQFDFTGIGDLESKAKDALVDIIGICKSYEDSIKITVKSNNREVAKRNIYLMDMSGKVVTTTLWGEDADKFDGSRQPVMAIKGARVSDFGGRSLSVLSSSTVIVNPDIPEAYKLRGWFDSEGQALDGVSISDHRSGGAGGGNTNWKTLHEAKSENLGQGDKADYFSTVAAVVFLRKENCMYQACPTQDCNKKVIDQQNGLYRCEKCDREFPNFKYRMILSANIADFQENQWVTCFQESAEAILGQNTMYLGELKEKNEQAFEEVFQNANFRSFTFRIRVKLETYNDESRIKATVMDVKPVDFRDYGRRLIANIRKNM
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:P27694}.
uniprot
proteins
mass_dalton
69037
uniprot
proteins
post_translational_modification
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:P27694}.; PTM: Sumoylated on lysine residues Lys-458 and Lys-586, with Lys-458 being the major site. Sumoylation promotes recruitment of RAD51 to the DNA damage foci to initiate DNA repair through homologous recombination. Desumoylated by SENP6 (By similarity). {ECO:0000250|UniProtKB:P27694}.; PTM: Poly-ADP-ribosylated by PARP1; promoting recruitment of HTATSF1. {ECO:0000250|UniProtKB:P27694}.
uniprot
proteins
protein_family
Replication factor A protein 1 family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
31467087
uniprot
proteins
sequence_length
623
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P27694}. Nucleus, PML body {ECO:0000250|UniProtKB:P27694}.
uniprot
proteins