RAD51AP1
entrez
10635
canonical
uniprot
Q96B01
canonical
ensembl
ENSG00000111247
resolver
ensp
ENSP00000228843
resolver
ensp
ENSP00000309479
resolver
ensp
ENSP00000446296
resolver
ensp
ENSP00000542212
resolver
ensp
ENSP00000542213
resolver
ensp
ENSP00000595643
resolver
ensp
ENSP00000595644
resolver
ensp
ENSP00000751385
resolver
ensp
ENSP00000751389
resolver
enst
ENST00000544927
resolver
genesymbol
RAD51AP1
resolver
genesymbol_syn
PIR51
resolver
hgnc
HGNC:16956
resolver
uniprot
A8K7D3
resolver
uniprot
B4DUS5
resolver
uniprot
F5H1Y0
resolver
uniprot
O43403
resolver
uniprot
Q7Z779
resolver
uniprot_entry
B4DUS5_HUMAN
resolver
uniprot_entry
F5H1Y0_HUMAN
resolver
uniprot_entry
R51A1_HUMAN
resolver
uniprot_sec
A8K7D3
resolver
uniprot_sec
O43403
resolver
uniprot_sec
Q7Z779
resolver
amino_acid_sequence
MVRPVRHKKPVNYSQFDHSDSDDDFVSATVPLNKKSRTAPKELKQDKPKPNLNNLRKEEIPVQEKTPKKRLPEGTFSIPASAVPCTKMALDDKLYQRDLEVALALSVKELPTVTTNVQNSQDKSIEKHGSSKIETMNKSPHISNCSVASDYLDLDKITVEDDVGGVQGKRKAASKAAAQQRKILLEGSDGDSANDTEPDFAPGEDSEDDSDFCESEDNDEDFSMRKSKVKEIKKKEVKVKSPVEKKEKKSKSKCNALVTSVDSAPAAVKSESQSLPKKVSLSSDTTRKPLEIRSPSAESKKPKWVPPAASGGSRSSSSPLVVVSVKSPNQSLRLGLSRLARVKPLHPNATST
uniprot
proteins
function
FUNCTION: Structure-specific DNA-binding protein involved in DNA repair by promoting RAD51-mediated homologous recombination (PubMed:17996710, PubMed:17996711, PubMed:20871616, PubMed:25288561, PubMed:26323318). Acts by stimulating D-Loop formation by RAD51: specifically enhances joint molecule formation through its structure-specific DNA interaction and its interaction with RAD51 (PubMed:17996710, PubMed:17996711). Binds single-stranded DNA (ssDNA), double-stranded DNA (dsDNA) and secondary DNA structures, such as D-loop structures: has a strong preference for branched-DNA structures that are obligatory intermediates during joint molecule formation (PubMed:17996710, PubMed:17996711, PubMed:22375013, PubMed:9396801). Cooperates with WDR48/UAF1 to stimulate RAD51-mediated homologous recombination: both WDR48/UAF1 and RAD51AP1 have coordinated role in DNA-binding during homologous recombination and DNA repair (PubMed:27239033, PubMed:27463890, PubMed:32350107). WDR48/UAF1 and RAD51AP1 also have a coordinated role in DNA-binding to promote USP1-mediated deubiquitination of FANCD2 (PubMed:31253762). Also involved in meiosis by promoting DMC1-mediated homologous meiotic recombination (PubMed:21307306). Key mediator of alternative lengthening of telomeres (ALT) pathway, a homology-directed repair mechanism of telomere elongation that controls proliferation in aggressive cancers, by stimulating homologous recombination (PubMed:31400850). May also bind RNA; additional evidence is however required to confirm RNA-binding in vivo (PubMed:9396801). {ECO:0000269|PubMed:17996710, ECO:0000269|PubMed:17996711, ECO:0000269|PubMed:20871616, ECO:0000269|PubMed:21307306, ECO:0000269|PubMed:22375013, ECO:0000269|PubMed:25288561, ECO:0000269|PubMed:26323318, ECO:0000269|PubMed:27239033, ECO:0000269|PubMed:27463890, ECO:0000269|PubMed:31253762, ECO:0000269|PubMed:31400850, ECO:0000269|PubMed:32350107, ECO:0000269|PubMed:9396801}.
uniprot
proteins
mass_dalton
38457
uniprot
proteins
mutagenesis
MUTAGEN 34..47; /note="KKSRTAPKELKQDK->AASATAPAELAQDA: In K6RA; impaired DNA-binding."; /evidence="ECO:0000269|PubMed:22375013"; MUTAGEN 34..37; /note="KKSR->AASA: In K2RA; impaired DNA-binding."; /evidence="ECO:0000269|PubMed:22375013"; MUTAGEN 44; /note="K->R: Does not affect sumoylation."; /evidence="ECO:0000269|PubMed:31400850"; MUTAGEN 150..153; /note="DYLD->AYLA: Abolished interaction with WDR48/UAF1."; /evidence="ECO:0000269|PubMed:27463890"; MUTAGEN 154..159; /note="LDKITV->ADKATA: Reduced sumoylation. Reduced ubiquitination."; /evidence="ECO:0000269|PubMed:31400850"; MUTAGEN 154..157; /note="LDKI->ADKA: Decreased interaction with WDR48/UAF1."; /evidence="ECO:0000269|PubMed:27239033"; MUTAGEN 156; /note="K->R: Does not affect interaction with WDR48/UAF1."; /evidence="ECO:0000269|PubMed:27463890"; MUTAGEN 157..159; /note="ITV->ATA: Decreased interaction with WDR48/UAF1."; /evidence="ECO:0000269|PubMed:27239033"; MUTAGEN 240; /note="K->R: Does not affect sumoylation."; /evidence="ECO:0000269|PubMed:31400850"; MUTAGEN 248..253; /note="KKSKSK->AASASA: In K4A; reduced DNA-binding. In K7WA; strongly decreased DNA-binding; when associated with 300-A--A-304."; /evidence="ECO:0000269|PubMed:22375013"; MUTAGEN 269; /note="K->R: Strongly reduced sumoylation. Strongly reduced ubiquitination."; /evidence="ECO:0000269|PubMed:31400850"; MUTAGEN 300..304; /note="KKPKW->AAPAA: In K3WA; reduced DNA-binding. In K7WA; strongly decreased DNA-binding; when associated with 248-A--A-253."; /evidence="ECO:0000269|PubMed:22375013"; MUTAGEN 304; /note="W->A: Abolished interaction with DMC1 without affecting interaction with RAD51."; /evidence="ECO:0000269|PubMed:21903585"; MUTAGEN 326; /note="K->R: Does not affect sumoylation."; /evidence="ECO:0000269|PubMed:31400850"; MUTAGEN 327..352; /note="Missing: Abolished interaction with RAD51."; /evidence="ECO:0000269|PubMed:17996710"; MUTAGEN 328..352; /note="Missing: In mutant delta25; abolished interaction with RAD51."; /evidence="ECO:0000269|PubMed:17996711"; MUTAGEN 333; /note="R->A: Strongly decreases interaction with RAD51; when associated with Q-336, A-345 and A-346."; /evidence="ECO:0000269|PubMed:16990250"; MUTAGEN 336; /note="L->Q: Strongly decreases interaction with RAD51; when associated with A-333, A-345 and A-346. Decreased interacting with RAD51 and ability to stimulate RAD51-mediated homologous recombination. Does not affect interaction with DMC1."; /evidence="ECO:0000269|PubMed:16990250, ECO:0000269|PubMed:17996711, ECO:0000269|PubMed:21307306"; MUTAGEN 345..346; /note="LH->AA: Strongly decreases interaction with RAD51; when associated with A-333; and Q-336."; /evidence="ECO:0000269|PubMed:16990250"; MUTAGEN 346; /note="H->A: Decreased interacting with RAD51 and ability to stimulate RAD51-mediated homologous recombination. Does not affect interaction with DMC1."; /evidence="ECO:0000269|PubMed:17996711, ECO:0000269|PubMed:21307306
uniprot
proteins
post_translational_modification
PTM: Sumoylation with SUMO2/3 by NSMCE2/MMS21 promotes stabilization, possibly by preventing ubiquitination (PubMed:31400850). Sumoylation is required for alternative lengthening of telomeres (ALT) pathway (PubMed:31400850). {ECO:0000269|PubMed:31400850}.
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16990250
uniprot
proteins
pubmed
17996710
uniprot
proteins
pubmed
17996711
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20871616
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21307306
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21903585
uniprot
proteins
pubmed
22375013
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23754376
uniprot
proteins
pubmed
25288561
uniprot
proteins
pubmed
26323318
uniprot
proteins
pubmed
27239033
uniprot
proteins
pubmed
27463890
uniprot
proteins
pubmed
31253762
uniprot
proteins
pubmed
31400850
uniprot
proteins
pubmed
31585101
uniprot
proteins
pubmed
32350107
uniprot
proteins
pubmed
9396801
uniprot
proteins
sequence_length
352
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:26323318, ECO:0000269|PubMed:31400850}. Nucleus {ECO:0000269|PubMed:26323318}. Chromosome, telomere {ECO:0000269|PubMed:31400850}. Note=Colocalizes with RAD51 to multiple nuclear foci (By similarity). Colocalizes with DMC1 on meiotic chromatin (By similarity). {ECO:0000250|UniProtKB:Q8C551}.
uniprot
proteins