Brca2
entrez
12190
canonical
uniprot
P97929
canonical
ensembl
ENSMUSG00000041147
resolver
ensp
ENSMUSP00000038576
resolver
ensp
ENSMUSP00000144150
resolver
ensp
ENSMUSP00000346437
resolver
ensp
ENSMUSP00000346438
resolver
ensp
ENSMUSP00000346439
resolver
enst
ENSMUST00000044620
resolver
enst
ENSMUST00000202313
resolver
genesymbol
Brca2
resolver
genesymbol_syn
Fancd1
resolver
uniprot
F8VPU5
resolver
uniprot
O35922
resolver
uniprot
P97383
resolver
uniprot_entry
BRCA2_MOUSE
resolver
uniprot_sec
F8VPU5
resolver
uniprot_sec
O35922
resolver
uniprot_sec
P97383
resolver
amino_acid_sequence
MPVEYKRRPTFWEIFKARCSTADLGPISLNWFEELSSEAPPYNSEPPEESEYKPHGYEPQLFKTPQRNPPYHQFASTPIMFKERSQTLPLDQSPFRELGKVVASSKHKTHSKKKTKVDPVVDVASPPLKSCLSESPLTLRCTQAVLQREKPVVSGSLFYTPKLKEGQTPKPISESLGVEVDPDMSWTSSLATPPTLSSTVLIARDEEARSSVTPADSPATLKSCFSNHNESPQKNDRSVPSVIDSENKNQQEAFSQGLGKMLGDSSGKRNSFKDCLRKPIPNILEDGETAVDTSEEDSFSLCFPKRRTRNLQKMRMGKTRKKIFSETRTDELSEEARRQTDDKNSFVFEMELRESDPLDPGVTSQKPFYSQNEEICNEAVQCSDSRWSQSNLSGLNETQTGKITLPHISSHSQNISEDFIDMKKEGTGSITSEKSLPHISSLPEPEKMFSEETVVDKEHEGQHFESLEDSIAGKQMVSRTSQAACLSPSIRKSIFKMREPLDETLGTVFSDSMTNSTFTEEHEASACGLGILTACSQREDSICPSSVDTGSWPTTLTDTSATVKNAGLISTLKNKKRKFIYSVSDDASLQGKKLQTHRQLELTNLSAQLEASAFEVPLTFTNVNSGIPDSSDKKRCLPNDPEEPSLTNSFGTATSKEISYIHALISQDLNDKEAIVIEEKPQPYTAREADFLLCLPERTCENDQKSPKVSNGKEKVLVSACLPSAVQLSSISFESQENPLGDHNGTSTLKLTPSSKLPLSKADMVSREKMCKMPEKLQCESCKVNIELSKNILEVNEICILSENSKTPGLLPPGENIIEVASSMKSQFNQNAKIVIQKDQKGSPFISEVAVNMNSEELFPDSGNNFAFQVTNKCNKPDLGSSVELQEEDLSHTQGPSLKNSPMAVDEDVDDAHAAQVLITKDSDSLAVVHDYTEKSRNNIEQHQKGTEDKDFKSNSSLNMKSDGNSDCSDKWSEFLDPVLNHNFGGSFRTASNKEIKLSEHNVKKSKMFFKDIEEQYPTRLACIDIVNTLPLANQKKLSEPHIFDLKSVTTVSTQSHNQSSVSHEDTDTAPQMLSSKQDFHSNNLTTSQKAEITELSTILEESGSQFEFTQFRKPSHIAQNTSEVPGNQMVVLSTASKEWKDTDLHLPVDPSVGQTDHSKQFEGSAGVKQSFPHLLEDTCNKNTSCFLPNINEMEFGGFCSALGTKLSVSNEALRKAMKLFSDIENSEEPSAKVGPRGFSSSAHHDSVASVFKIKKQNTEKSFDEKSSKCQVTLQNNIEMTTCIFVGRNPEKYIKNTKHEDSYTSSQRNNLENSDGSMSSTSGPVYIHKGDSDLPADQGSKCPESCTQYAREENTQIKENISDLTCLEIMKAEETCMKSSDKKQLPSDKMEQNIKEFNISFQTASGKNTRVSKESLNKSVNIFNRETDELTVISDSLNSKILHGINKDKMHTSCHKKAISIKKVFEDHFPIVTVSQLPAQQHPEYEIESTKEPTLLSFHTASGKKVKIMQESLDKVKNLFDETQYVRKTASFSQGSKPLKDSKKELTLAYEKIEVTASKCEEMQNFVSKETEMLPQQNYHMYRQTENLKTSNGTSSKVQENIENNVEKNPRICCICQSSYPVTEDSALAYYTEDSRKTCVRESSLSKGRKWLREQGDKLGTRNTIKIECVKEHTEDFAGNASYEHSLVIIRTEIDTNHVSENQVSTLLSDPNVCHSYLSQSSFCHCDDMHNDSGYFLKNKIDSDVPPDMKNAEGNTISPRVSATKERNLHPQTINEYCVQKLETNTSPHANKDVAIDPSLLDSRNCKVGSLVFITAHSQETERTKEIVTDNCYKIVEQNRQSKPDTCQTSCHKVLDDSKDFICPSSSGDVCINSRKDSFCPHNEQILQHNQSMSGLKKAATPPVGLETWDTSKSIREPPQAAHPSRTYGIFSTASGKAIQVSDASLEKARQVFSEMDGDAKQLSSMVSLEGNEKPHHSVKRENSVVHSTQGVLSLPKPLPGNVNSSVFSGFSTAGGKLVTVSESALHKVKGMLEEFDLIRTEHTLQHSPIPEDVSKILPQPCAEIRTPEYPVNSKLQKTYNDKSSLPSNYKESGSSGNTQSIEVSLQLSQMERNQDTQLVLGTKVSHSKANLLGKEQTLPQNIKVKTDEMKTFSDVPVKTNVGEYYSKESENYFETEAVESAKAFMEDDELTDSEQTHAKCSLFTCPQNETLFNSRTRKRGGVTVDAVGQPPIKRSLLNEFDRIIESKGKSLTPSKSTPDGTVKDRSLFTHHMSLEPVTCGPFCSSKERQGAQRPHLTSPAQELLSKGHPWRHSALEKSPSSPIVSILPAHDVSATRTERTRHSGKSTKVFVPPFKMKSQFHGDEHFNSKNVNLEGKNQKSTDGDREDGNDSHVRQFNKDLMSSLQSARDLQDMRIKNKERRHLRLQPGSLYLTKSSTLPRISLQAAVGDRAPSACSPKQLYIYGVSKECINVNSKNAEYFQFDIQDHFGKEDLCAGKGFQLADGGWLIPSNDGKAGKEEFYRALCDTPGVDPKLISSIWVANHYRWIVWKLAAMEFAFPKEFANRCLNPERVLLQLKYRYDVEIDNSRRSALKKILERDDTAAKTLVLCISDIISPSTKVSETSGGKTSGEDANKVDTIELTDGWYAVRAQLDPPLMALVKSGKLTVGQKIITQGAELVGSPDACAPLEAPDSLRLKISANSTRPARWHSRLGFFRDPRPFPLPLSSLFSDGGNVGCVDIIVQRVYPLQWVEKTVSGLYIFRSEREEEKEALRFAEAQQKKLEALFTKVHTEFKDHEEDTTQRCVLSRTLTRQQVHALQDGAELYAAVQYASDPDHLEACFSEEQLRALNNYRQMLNDKKQARIQSEFRKALESAEKEEGLSRDVTTVWKLRVTSYKKKEKSALLSIWRPSSDLSSLLTEGKRYRIYHLAVSKSKSKFERPSIQLTATKRTQYQQLPVSSETLLQVYQPRESLHFSRLSDPAFQPPCSEVDVVGVVVSVVKPIGLAPLVYLSDECLNLLVVKFGIDLNEDIKPRVLIAASNLQCQPESTSGVPTLFAGHFSIFSASPKEAYFQEKVNNLKHAIENIDTFYKEAEKKLIHVLEGDSPKWSTPNKDPTREPHAASTCCASDLLGSGGQFLRISPTGQQSYQSPLSHCTLKGKSMPLAHSAQMAAKSWSGENEIDDPKTCRKRRALDFLSRLPLPSPVSPICTFVSPAAQKAFQPPRSCGTKYATPIKKEPSSPRRRTPFQKTSGVSLPDCDSVADEELALLSTQALTPDSVGGNEQAFPGDSTRNPQPAQRPDQQVGPRSRKESLRDCRGDSSEKLAVES
uniprot
proteins
function
FUNCTION: Tumor suppressor protein that maintains genome stability primarily by repairing damaged DNA through homologous recombination (HR) (PubMed:9126738). Facilitates the repair of double-strand breaks (DSBs) by binding and mediating the loading of the RAD51 protein onto single-stranded DNA (ssDNA), thereby promoting the activity of RAD51, which catalyzes DNA strand exchange (By similarity). BRCA2 nucleates and stabilizes RAD51 on ssDNA directly and delivers RAD51 to ssDNA-double-stranded DNA (dsDNA) junctions by sliding along dsDNA backbone (By similarity). RAD51 targeting to ssDNA promotes removal of replication protein-A (RPA) from ssDNA and stabilization of RAD51-ssDNA filaments by blocking ATP hydrolysis (By similarity). May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with PALB2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity (By similarity). Required to prevent R-loop-associated DNA damage and thus transcription-associated genomic instability (By similarity). Silencing of BRCA2 promotes R-loop accumulation at actively transcribed genes in replicating and non-replicating cells, suggesting that BRCA2 mediates the control of R-loop associated genomic instability, independently of its known role in homologous recombination (By similarity). Also promotes RAD51 loading to telomeric regions, facilitating telomere replication and capping (By similarity). Also required for homologous recombination during meiosis by promoting the recruitment of RAD51 and DMC1 recombinases to meiotic DSB sites, enabling proper chromosome pairing and crossing over (By similarity). Also promotes homologous recombination by inactivating the FIGNL1-FIRRM complex to protect RAD51 filament from premature disassembly (By similarity). Together with NPM1, may also regulate centrosome duplication (By similarity). {ECO:0000250|UniProtKB:P51587, ECO:0000269|PubMed:9126738}.
uniprot
proteins
mass_dalton
370664
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by ATM upon irradiation-induced DNA damage. Phosphorylation by CHEK1 and CHEK2 regulates interaction with RAD51. Phosphorylation at Ser-3291 by CDK1 and CDK2 is low in S phase when recombination is active, but increases as cells progress towards mitosis; this phosphorylation prevents homologous recombination-dependent repair during S phase and G2 by inhibiting RAD51 binding. {ECO:0000250|UniProtKB:P51587}.; PTM: Ubiquitinated in the absence of DNA damage; this does not lead to proteasomal degradation. In contrast, ubiquitination in response to DNA damage leads to proteasomal degradation. {ECO:0000250|UniProtKB:P51587}.
uniprot
proteins
pubmed
12228710
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
30760716
uniprot
proteins
pubmed
31242413
uniprot
proteins
pubmed
32345962
uniprot
proteins
pubmed
32460033
uniprot
proteins
pubmed
32845237
uniprot
proteins
pubmed
8917547
uniprot
proteins
pubmed
9063750
uniprot
proteins
pubmed
9119389
uniprot
proteins
pubmed
9126738
uniprot
proteins
pubmed
9196008
uniprot
proteins
pubmed
9242436
uniprot
proteins
sequence_length
3329
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:30760716}. Chromosome, telomere {ECO:0000250|UniProtKB:P51587}. Nucleus {ECO:0000250|UniProtKB:P51587}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P51587}. Note=Colocalizes with ERCC5/XPG to nuclear foci following DNA replication stress. {ECO:0000250|UniProtKB:P51587}.
uniprot
proteins