RPA1
entrez
6117
canonical
uniprot
P27694
canonical
ensembl
ENSG00000132383
resolver
ensp
ENSP00000254719
resolver
ensp
ENSP00000522120
resolver
enst
ENST00000254719
resolver
genesymbol
RPA1
resolver
genesymbol_syn
REPA1
resolver
genesymbol_syn
RPA70
resolver
hgnc
HGNC:10289
resolver
uniprot
A8K0Y9
resolver
uniprot
Q59ES9
resolver
uniprot_entry
RFA1_HUMAN
resolver
uniprot_sec
A8K0Y9
resolver
uniprot_sec
Q59ES9
resolver
amino_acid_sequence
MVGQLSEGAIAAIMQKGDTNIKPILQVINIRPITTGNSPPRYRLLMSDGLNTLSSFMLATQLNPLVEEEQLSSNCVCQIHRFIVNTLKDGRRVVILMELEVLKSAEAVGVKIGNPVPYNEGLGQPQVAPPAPAASPAASSRPQPQNGSSGMGSTVSKAYGASKTFGKAAGPSLSHTSGGTQSKVVPIASLTPYQSKWTICARVTNKSQIRTWSNSRGEGKLFSLELVDESGEIRATAFNEQVDKFFPLIEVNKVYYFSKGTLKIANKQFTAVKNDYEMTFNNETSVMPCEDDHHLPTVQFDFTGIDDLENKSKDSLVDIIGICKSYEDATKITVRSNNREVAKRNIYLMDTSGKVVTATLWGEDADKFDGSRQPVLAIKGARVSDFGGRSLSVLSSSTIIANPDIPEAYKLRGWFDAEGQALDGVSISDLKSGGVGGSNTNWKTLYEVKSENLGQGDKPDYFSSVATVVYLRKENCMYQACPTQDCNKKVIDQQNGLYRCEKCDTEFPNFKYRMILSVNIADFQENQWVTCFQESAEAILGQNAAYLGELKDKNEQAFEEVFQNANFRSFIFRVRVKVETYNDESRIKATVMDVKPVDYREYGRRLVMSIRRSALM
uniprot
proteins
disease_involvement
DISEASE: Pulmonary fibrosis, and/or bone marrow failure syndrome, telomere-related, 6 (PFBMFT6) [MIM:619767]: An autosomal dominant disease associated with shortened telomeres. Pulmonary fibrosis is the most common manifestation. Other manifestations include aplastic anemia due to bone marrow failure, hepatic fibrosis, and increased cancer risk, particularly myelodysplastic syndrome and acute myeloid leukemia. Phenotype, age at onset, and severity are determined by telomere length. {ECO:0000269|PubMed:34767620}. Note=The disease is caused by variants affecting the gene represented in this entry.
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 (PubMed:17596542, PubMed:27723717, PubMed:27723720). Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage (PubMed:9430682). 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 (PubMed:24332808). It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage (PubMed:17765923). 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 (PubMed:7697716). Also plays a role in base excision repair (BER) probably through interaction with UNG (PubMed:9765279). Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. Plays a role in telomere maintenance (PubMed:17959650, PubMed:34767620). As part of the alternative replication protein A complex, aRPA, binds single-stranded DNA and probably plays a role in DNA repair. Compared to the RPA2-containing, canonical RPA complex, may not support chromosomal DNA replication and cell cycle progression through S-phase. The aRPA may not promote efficient priming by DNA polymerase alpha but could support DNA synthesis by polymerase delta in presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange (PubMed:19996105). RPA stimulates 5'-3' helicase activity of the BRIP1/FANCJ (PubMed:17596542). {ECO:0000269|PubMed:12791985, ECO:0000269|PubMed:17596542, ECO:0000269|PubMed:17765923, ECO:0000269|PubMed:17959650, ECO:0000269|PubMed:19116208, ECO:0000269|PubMed:19996105, ECO:0000269|PubMed:24332808, ECO:0000269|PubMed:27723717, ECO:0000269|PubMed:27723720, ECO:0000269|PubMed:34767620, ECO:0000269|PubMed:7697716, ECO:0000269|PubMed:7700386, ECO:0000269|PubMed:9430682, ECO:0000269|PubMed:9765279}.
uniprot
proteins
mass_dalton
68138
uniprot
proteins
mutagenesis
MUTAGEN 41; /note="R->E: Loss of HELB-binding; when associated with E-43."; /evidence="ECO:0000269|PubMed:22194613"; MUTAGEN 43; /note="R->E: Loss of HELB-binding; when associated with E-41."; /evidence="ECO:0000269|PubMed:22194613"; MUTAGEN 449; /note="K->R: Significant reduction of sumoylation. Loss of sumoylation; when associated with R-577."; /evidence="ECO:0000269|PubMed:20705237"; MUTAGEN 500; /note="C->S: Loss of function in DNA replication and mismatch repair without effect on DNA-binding activity; when associated with S-503."; /evidence="ECO:0000269|PubMed:9430682"; MUTAGEN 503; /note="C->S: Loss of function in DNA replication and mismatch repair without effect on DNA-binding activity; when associated with S-500."; /evidence="ECO:0000269|PubMed:9430682"; MUTAGEN 577; /note="K->R: Slight sumoylation decrease. Loss of sumoylation; when associated with R-449."; /evidence="ECO:0000269|PubMed:20705237
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 (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}.; PTM: Sumoylated on lysine residues Lys-449 and Lys-577, with Lys-449 being the major site. Sumoylation promotes recruitment of RAD51 to the DNA damage foci to initiate DNA repair through homologous recombination. Desumoylated by SENP6. {ECO:0000269|PubMed:20705237}.; PTM: Poly-ADP-ribosylated by PARP1; promoting recruitment of HTATSF1. {ECO:0000269|PubMed:24906880, ECO:0000269|PubMed:35597237}.
uniprot
proteins
protein_family
Replication factor A protein 1 family
uniprot
proteins
pubmed
10563794
uniprot
proteins
pubmed
12791985
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16135809
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
17596542
uniprot
proteins
pubmed
17765923
uniprot
proteins
pubmed
17959650
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19010961
uniprot
proteins
pubmed
19116208
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19996105
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
2050703
uniprot
proteins
pubmed
20705237
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22194613
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24126761
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24332808
uniprot
proteins
pubmed
24906880
uniprot
proteins
pubmed
25550423
uniprot
proteins
pubmed
26474068
uniprot
proteins
pubmed
26774285
uniprot
proteins
pubmed
27601467
uniprot
proteins
pubmed
27723717
uniprot
proteins
pubmed
27723720
uniprot
proteins
pubmed
28534480
uniprot
proteins
pubmed
34767620
uniprot
proteins
pubmed
35597237
uniprot
proteins
pubmed
7697716
uniprot
proteins
pubmed
7700386
uniprot
proteins
pubmed
7760808
uniprot
proteins
pubmed
8420996
uniprot
proteins
pubmed
8990123
uniprot
proteins
pubmed
9214288
uniprot
proteins
pubmed
9430682
uniprot
proteins
pubmed
9699634
uniprot
proteins
pubmed
9765279
uniprot
proteins
sequence_length
616
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17596542, ECO:0000269|PubMed:17959650}. Nucleus, PML body {ECO:0000269|PubMed:17959650}. Note=Enriched in PML bodies in cells displaying alternative lengthening of their telomeres. {ECO:0000269|PubMed:17959650}.
uniprot
proteins