BRCA2
entrez
675
canonical
uniprot
P51587
canonical
ensembl
ENSG00000139618
resolver
ensp
ENSP00000369497
resolver
ensp
ENSP00000439902
resolver
ensp
ENSP00000505508
resolver
ensp
ENSP00000514856
resolver
enst
ENST00000380152
resolver
enst
ENST00000544455
resolver
enst
ENST00000680887
resolver
enst
ENST00000700202
resolver
genesymbol
BRCA2
resolver
genesymbol_syn
FACD
resolver
genesymbol_syn
FANCD1
resolver
hgnc
HGNC:1101
resolver
uniprot
A0A7P0T9D7
resolver
uniprot
A0A8V8TPZ2
resolver
uniprot
O00183
resolver
uniprot
O15008
resolver
uniprot
Q13879
resolver
uniprot
Q5TBJ7
resolver
uniprot_entry
A0A7P0T9D7_HUMAN
resolver
uniprot_entry
A0A8V8TPZ2_HUMAN
resolver
uniprot_entry
BRCA2_HUMAN
resolver
uniprot_sec
O00183
resolver
uniprot_sec
O15008
resolver
uniprot_sec
Q13879
resolver
uniprot_sec
Q5TBJ7
resolver
amino_acid_sequence
MPIGSKERPTFFEIFKTRCNKADLGPISLNWFEELSSEAPPYNSEPAEESEHKNNNYEPNLFKTPQRKPSYNQLASTPIIFKEQGLTLPLYQSPVKELDKFKLDLGRNVPNSRHKSLRTVKTKMDQADDVSCPLLNSCLSESPVVLQCTHVTPQRDKSVVCGSLFHTPKFVKGRQTPKHISESLGAEVDPDMSWSSSLATPPTLSSTVLIVRNEEASETVFPHDTTANVKSYFSNHDESLKKNDRFIASVTDSENTNQREAASHGFGKTSGNSFKVNSCKDHIGKSMPNVLEDEVYETVVDTSEEDSFSLCFSKCRTKNLQKVRTSKTRKKIFHEANADECEKSKNQVKEKYSFVSEVEPNDTDPLDSNVANQKPFESGSDKISKEVVPSLACEWSQLTLSGLNGAQMEKIPLLHISSCDQNISEKDLLDTENKRKKDFLTSENSLPRISSLPKSEKPLNEETVVNKRDEEQHLESHTDCILAVKQAISGTSPVASSFQGIKKSIFRIRESPKETFNASFSGHMTDPNFKKETEASESGLEIHTVCSQKEDSLCPNLIDNGSWPATTTQNSVALKNAGLISTLKKKTNKFIYAIHDETSYKGKKIPKDQKSELINCSAQFEANAFEAPLTFANADSGLLHSSVKRSCSQNDSEEPTLSLTSSFGTILRKCSRNETCSNNTVISQDLDYKEAKCNKEKLQLFITPEADSLSCLQEGQCENDPKSKKVSDIKEEVLAAACHPVQHSKVEYSDTDFQSQKSLLYDHENASTLILTPTSKDVLSNLVMISRGKESYKMSDKLKGNNYESDVELTKNIPMEKNQDVCALNENYKNVELLPPEKYMRVASPSRKVQFNQNTNLRVIQKNQEETTSISKITVNPDSEELFSDNENNFVFQVANERNNLALGNTKELHETDLTCVNEPIFKNSTMVLYGDTGDKQATQVSIKKDLVYVLAEENKNSVKQHIKMTLGQDLKSDISLNIDKIPEKNNDYMNKWAGLLGPISNHSFGGSFRTASNKEIKLSEHNIKKSKMFFKDIEEQYPTSLACVEIVNTLALDNQKKLSKPQSINTVSAHLQSSVVVSDCKNSHITPQMLFSKQDFNSNHNLTPSQKAEITELSTILEESGSQFEFTQFRKPSYILQKSTFEVPENQMTILKTTSEECRDADLHVIMNAPSIGQVDSSKQFEGTVEIKRKFAGLLKNDCNKSASGYLTDENEVGFRGFYSAHGTKLNVSTEALQKAVKLFSDIENISEETSAEVHPISLSSSKCHDSVVSMFKIENHNDKTVSEKNNKCQLILQNNIEMTTGTFVEEITENYKRNTENEDNKYTAASRNSHNLEFDGSDSSKNDTVCIHKDETDLLFTDQHNICLKLSGQFMKEGNTQIKEDLSDLTFLEVAKAQEACHGNTSNKEQLTATKTEQNIKDFETSDTFFQTASGKNISVAKESFNKIVNFFDQKPEELHNFSLNSELHSDIRKNKMDILSYEETDIVKHKILKESVPVGTGNQLVTFQGQPERDEKIKEPTLLGFHTASGKKVKIAKESLDKVKNLFDEKEQGTSEITSFSHQWAKTLKYREACKDLELACETIEITAAPKCKEMQNSLNNDKNLVSIETVVPPKLLSDNLCRQTENLKTSKSIFLKVKVHENVEKETAKSPATCYTNQSPYSVIENSALAFYTSCSRKTSVSQTSLLEAKKWLREGIFDGQPERINTADYVGNYLYENNSNSTIAENDKNHLSEKQDTYLSNSSMSNSYSYHSDEVYNDSGYLSKNKLDSGIEPVLKNVEDQKNTSFSKVISNVKDANAYPQTVNEDICVEELVTSSSPCKNKNAAIKLSISNSNNFEVGPPAFRIASGKIVCVSHETIKKVKDIFTDSFSKVIKENNENKSKICQTKIMAGCYEALDDSEDILHNSLDNDECSTHSHKVFADIQSEEILQHNQNMSGLEKVSKISPCDVSLETSDICKCSIGKLHKSVSSANTCGIFSTASGKSVQVSDASLQNARQVFSEIEDSTKQVFSKVLFKSNEHSDQLTREENTAIRTPEHLISQKGFSYNVVNSSAFSGFSTASGKQVSILESSLHKVKGVLEEFDLIRTEHSLHYSPTSRQNVSKILPRVDKRNPEHCVNSEMEKTCSKEFKLSNNLNVEGGSSENNHSIKVSPYLSQFQQDKQQLVLGTKVSLVENIHVLGKEQASPKNVKMEIGKTETFSDVPVKTNIEVCSTYSKDSENYFETEAVEIAKAFMEDDELTDSKLPSHATHSLFTCPENEEMVLSNSRIGKRRGEPLILVGEPSIKRNLLNEFDRIIENQEKSLKASKSTPDGTIKDRRLFMHHVSLEPITCVPFRTTKERQEIQNPNFTAPGQEFLSKSHLYEHLTLEKSSSNLAVSGHPFYQVSATRNEKMRHLITTGRPTKVFVPPFKTKSHFHRVEQCVRNINLEENRQKQNIDGHGSDDSKNKINDNEIHQFNKNNSNQAVAVTFTKCEEEPLDLITSLQNARDIQDMRIKKKQRQRVFPQPGSLYLAKTSTLPRISLKAAVGGQVPSACSHKQLYTYGVSKHCIKINSKNAESFQFHTEDYFGKESLWTGKGIQLADGGWLIPSNDGKAGKEEFYRALCDTPGVDPKLISRIWVYNHYRWIIWKLAAMECAFPKEFANRCLSPERVLLQLKYRYDTEIDRSRRSAIKKIMERDDTAAKTLVLCVSDIISLSANISETSSNKTSSADTQKVAIIELTDGWYAVKAQLDPPLLAVLKNGRLTVGQKIILHGAELVGSPDACTPLEAPESLMLKISANSTRPARWYTKLGFFPDPRPFPLPLSSLFSDGGNVGCVDVIIQRAYPIQWMEKTSSGLYIFRNEREEEKEAAKYVEAQQKRLEALFTKIQEEFEEHEENTTKPYLPSRALTRQQVRALQDGAELYEAVKNAADPAYLEGYFSEEQLRALNNHRQMLNDKKQAQIQLEIRKAMESAEQKEQGLSRDVTTVWKLRIVSYSKKEKDSVILSIWRPSSDLYSLLTEGKRYRIYHLATSKSKSKSERANIQLAATKKTQYQQLPVSDEILFQIYQPREPLHFSKFLDPDFQPSCSEVDLIGFVVSVVKKTGLAPFVYLSDECYNLLAIKFWIDLNEDIIKPHMLIAASNLQWRPESKSGLLTLFAGDFSVFSASPKEGHFQETFNKMKNTVENIDILCNEAENKLMHILHANDPKWSTPTKDCTSGPYTAQIIPGTGNKLLMSSPNCEIYYQSPLSLCMAKRKSVSTPVSAQMTSKSCKGEKEIDDQKNCKKRRALDFLSRLPLPPPVSPICTFVSPAAQKAFQPPRSCGTKYETPIKKKELNSPQMTPFKKFNEISLLESNSIADEELALINTQALLSGSTGEKQFISVSESTRTAPTSSEDYLRLKRRCTTSLIKEQESSQASTEECEKNKQDTITTKKYI
uniprot
proteins
disease_involvement
DISEASE: Breast cancer (BC) [MIM:114480]: A common malignancy originating from breast epithelial tissue. Breast neoplasms can be distinguished by their histologic pattern. Invasive ductal carcinoma is by far the most common type. Breast cancer is etiologically and genetically heterogeneous. Important genetic factors have been indicated by familial occurrence and bilateral involvement. Mutations at more than one locus can be involved in different families or even in the same case. {ECO:0000269|PubMed:10399947, ECO:0000269|PubMed:10978364, ECO:0000269|PubMed:11139248, ECO:0000269|PubMed:11149425, ECO:0000269|PubMed:11241844, ECO:0000269|PubMed:11948477, ECO:0000269|PubMed:12145750, ECO:0000269|PubMed:12373604, ECO:0000269|PubMed:12442274, ECO:0000269|PubMed:12442275, ECO:0000269|PubMed:12569143, ECO:0000269|PubMed:12938098, ECO:0000269|PubMed:14722926, ECO:0000269|PubMed:15026808, ECO:0000269|PubMed:15172753, ECO:0000269|PubMed:15365993, ECO:0000269|PubMed:16793542, ECO:0000269|PubMed:17924331, ECO:0000269|PubMed:23108138, ECO:0000269|PubMed:24013206, ECO:0000269|PubMed:29161300, ECO:0000269|PubMed:8640237, ECO:0000269|PubMed:9150152, ECO:0000269|PubMed:9609997, ECO:0000269|PubMed:9654203, ECO:0000269|PubMed:9971877}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Pancreatic cancer 2 (PNCA2) [MIM:613347]: A malignant neoplasm of the pancreas. Tumors can arise from both the exocrine and endocrine portions of the pancreas, but 95% of them develop from the exocrine portion, including the ductal epithelium, acinar cells, connective tissue, and lymphatic tissue. {ECO:0000269|PubMed:9140390}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Breast-ovarian cancer, familial, 2 (BROVCA2) [MIM:612555]: A condition associated with familial predisposition to cancer of the breast and ovaries. Characteristic features in affected families are an early age of onset of breast cancer (often before age 50), increased chance of bilateral cancers (cancer that develop in both breasts, or both ovaries, independently), frequent occurrence of breast cancer among men, increased incidence of tumors of other specific organs, such as the prostate. {ECO:0000269|PubMed:10584720, ECO:0000269|PubMed:11158174, ECO:0000269|PubMed:7658781, ECO:0000269|PubMed:9150155}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Fanconi anemia complementation group D1 (FANCD1) [MIM:605724]: A disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair. {ECO:0000269|PubMed:12065746, ECO:0000269|PubMed:14670928, ECO:0000269|PubMed:16825431, ECO:0000269|PubMed:17924331, ECO:0000269|PubMed:21719596, ECO:0000269|PubMed:23108138}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Glioma 3 (GLM3) [MIM:613029]: Gliomas are benign or malignant central nervous system neoplasms derived from glial cells. They comprise astrocytomas and glioblastoma multiforme that are derived from astrocytes, oligodendrogliomas derived from oligodendrocytes and ependymomas derived from ependymocytes. {ECO:0000269|PubMed:15689453}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Medulloblastoma (MDB) [MIM:155255]: Malignant, invasive embryonal tumor of the cerebellum with a preferential manifestation in children. {ECO:0000269|PubMed:29753700}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Tumor suppressor protein that maintains genome stability primarily by repairing damaged DNA through homologous recombination (HR) (PubMed:11239456, PubMed:12442171, PubMed:15115758, PubMed:15199141, PubMed:15671039, PubMed:15937124, PubMed:17515903, PubMed:17515904, PubMed:18317453, PubMed:19303847, PubMed:20729832, PubMed:20729858, PubMed:20729859, PubMed:21719596, PubMed:27941124, PubMed:37499663, PubMed:37515771). 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 (PubMed:11239456, PubMed:12442171, PubMed:15937124, PubMed:17515903, PubMed:17515904, PubMed:18317453, PubMed:19303847, PubMed:20729832, PubMed:20729858, PubMed:20729859, PubMed:27941124, PubMed:37499663). BRCA2 nucleates and stabilizes RAD51 on ssDNA directly and delivers RAD51 to ssDNA-double-stranded DNA (dsDNA) junctions by sliding along dsDNA backbone (PubMed:12442171, PubMed:19303847, PubMed:37499663). RAD51 targeting to ssDNA promotes removal of replication protein-A (RPA) from ssDNA and stabilization of RAD51-ssDNA filaments by blocking ATP hydrolysis (PubMed:20729859). 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 (PubMed:24485656). Required to prevent R-loop-associated DNA damage and thus transcription-associated genomic instability (PubMed:24896180). 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 (PubMed:24896180). Also promotes RAD51 loading to telomeric regions, facilitating telomere replication and capping (PubMed:21076401). 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 (PubMed:26976601). Also promotes homologous recombination by inactivating the FIGNL1-FIRRM complex to protect RAD51 filament from premature disassembly (PubMed:37515771). Together with NPM1, may also regulate centrosome duplication (PubMed:21084279). {ECO:0000269|PubMed:11239456, ECO:0000269|PubMed:12442171, ECO:0000269|PubMed:15115758, ECO:0000269|PubMed:15199141, ECO:0000269|PubMed:15671039, ECO:0000269|PubMed:15937124, ECO:0000269|PubMed:17515903, ECO:0000269|PubMed:17515904, ECO:0000269|PubMed:18317453, ECO:0000269|PubMed:19303847, ECO:0000269|PubMed:20729832, ECO:0000269|PubMed:20729858, ECO:0000269|PubMed:20729859, ECO:0000269|PubMed:21076401, ECO:0000269|PubMed:21084279, ECO:0000269|PubMed:21719596, ECO:0000269|PubMed:24485656, ECO:0000269|PubMed:24896180, ECO:0000269|PubMed:26976601, ECO:0000269|PubMed:27941124, ECO:0000269|PubMed:37499663, ECO:0000269|PubMed:37515771}.
uniprot
proteins
mass_dalton
384230
uniprot
proteins
mutagenesis
MUTAGEN 2401; /note="R->A: Decreased interaction with DMC1."; /evidence="ECO:0000269|PubMed:38828772"; MUTAGEN 2404; /note="K->A: Decreased interaction with DMC1."; /evidence="ECO:0000269|PubMed:38828772"; MUTAGEN 2406..2409; /note="FVPP->AVPA: Abolished interaction with DMC1."; /evidence="ECO:0000269|PubMed:38828772"; MUTAGEN 2406; /note="F->A: Abolished interaction with DMC1."; /evidence="ECO:0000269|PubMed:39333100"; MUTAGEN 2408; /note="P->A: Abolished interaction with DMC1."; /evidence="ECO:0000269|PubMed:39333100"; MUTAGEN 2409; /note="P->A: Abolished interaction with DMC1."; /evidence="ECO:0000269|PubMed:39333100"; MUTAGEN 2411..2413; /note="KTK->ATA: Abolished interaction with DMC1."; /evidence="ECO:0000269|PubMed:38828772"; MUTAGEN 2411; /note="K->A: Does not affect interaction with DMC1."; /evidence="ECO:0000269|PubMed:38828772"; MUTAGEN 2413; /note="K->A: Does not affect interaction with DMC1."; /evidence="ECO:0000269|PubMed:38828772"; MUTAGEN 2725; /note="W->A: Disrupts interaction with SEM1."; /evidence="ECO:0000269|PubMed:24013206"; MUTAGEN 3291; /note="S->E: Impaired interaction with RAD51."; /evidence="ECO:0000269|PubMed:15800615"; MUTAGEN 3387; /note="T->A: Loss of phosphorylation by CHEK1 and CHEK2 (in vitro)."; /evidence="ECO:0000269|PubMed:18317453
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by ATM upon irradiation-induced DNA damage (PubMed:15199141). Phosphorylation by CHEK1 and CHEK2 regulates interaction with RAD51 (PubMed:18317453). 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 (PubMed:15800615, PubMed:17515903). {ECO:0000269|PubMed:15199141, ECO:0000269|PubMed:15800615, ECO:0000269|PubMed:17515903, ECO:0000269|PubMed:18317453}.; PTM: Ubiquitinated in the absence of DNA damage; this does not lead to proteasomal degradation (PubMed:15314155). In contrast, ubiquitination in response to DNA damage leads to proteasomal degradation (PubMed:15314155). {ECO:0000269|PubMed:15314155}.
uniprot
proteins
pubmed
10323242
uniprot
proteins
pubmed
10373512
uniprot
proteins
pubmed
10399947
uniprot
proteins
pubmed
10486320
uniprot
proteins
pubmed
10584720
uniprot
proteins
pubmed
10978364
uniprot
proteins
pubmed
11062481
uniprot
proteins
pubmed
11139248
uniprot
proteins
pubmed
11149425
uniprot
proteins
pubmed
11158174
uniprot
proteins
pubmed
11239456
uniprot
proteins
pubmed
11241844
uniprot
proteins
pubmed
11948123
uniprot
proteins
pubmed
11948477
uniprot
proteins
pubmed
12065746
uniprot
proteins
pubmed
12097290
uniprot
proteins
pubmed
12145750
uniprot
proteins
pubmed
12215251
uniprot
proteins
pubmed
12373604
uniprot
proteins
pubmed
12442171
uniprot
proteins
pubmed
12442273
uniprot
proteins
pubmed
12442274
uniprot
proteins
pubmed
12442275
uniprot
proteins
pubmed
12552570
uniprot
proteins
pubmed
12569143
uniprot
proteins
pubmed
12624724
uniprot
proteins
pubmed
12938098
uniprot
proteins
pubmed
14670928
uniprot
proteins
pubmed
14722926
uniprot
proteins
pubmed
14746861
uniprot
proteins
pubmed
15026808
uniprot
proteins
pubmed
15057823
uniprot
proteins
pubmed
15115758
uniprot
proteins
pubmed
15172753
uniprot
proteins
pubmed
15199141
uniprot
proteins
pubmed
15300854
uniprot
proteins
pubmed
15314155
uniprot
proteins
pubmed
15365993
uniprot
proteins
pubmed
15635067
uniprot
proteins
pubmed
15671039
uniprot
proteins
pubmed
15689453
uniprot
proteins
pubmed
15800615
uniprot
proteins
pubmed
15937124
uniprot
proteins
pubmed
15967112
uniprot
proteins
pubmed
16205630
uniprot
proteins
pubmed
16793542
uniprot
proteins
pubmed
16825431
uniprot
proteins
pubmed
17515903
uniprot
proteins
pubmed
17515904
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
17924331
uniprot
proteins
pubmed
18212739
uniprot
proteins
pubmed
18317453
uniprot
proteins
pubmed
19303847
uniprot
proteins
pubmed
19369211
uniprot
proteins
pubmed
19609323
uniprot
proteins
pubmed
20513136
uniprot
proteins
pubmed
20729832
uniprot
proteins
pubmed
20729858
uniprot
proteins
pubmed
20729859
uniprot
proteins
pubmed
21076401
uniprot
proteins
pubmed
21084279
uniprot
proteins
pubmed
21276791
uniprot
proteins
pubmed
21719596
uniprot
proteins
pubmed
23108138
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24013206
uniprot
proteins
pubmed
24141787
uniprot
proteins
pubmed
24485656
uniprot
proteins
pubmed
24896180
uniprot
proteins
pubmed
26566883
uniprot
proteins
pubmed
26833090
uniprot
proteins
pubmed
26976601
uniprot
proteins
pubmed
27941124
uniprot
proteins
pubmed
28319063
uniprot
proteins
pubmed
29161300
uniprot
proteins
pubmed
29753700
uniprot
proteins
pubmed
31242413
uniprot
proteins
pubmed
37499663
uniprot
proteins
pubmed
37515771
uniprot
proteins
pubmed
38828772
uniprot
proteins
pubmed
39333100
uniprot
proteins
pubmed
7658781
uniprot
proteins
pubmed
8524414
uniprot
proteins
pubmed
8589730
uniprot
proteins
pubmed
8640235
uniprot
proteins
pubmed
8640236
uniprot
proteins
pubmed
8640237
uniprot
proteins
pubmed
8665505
uniprot
proteins
pubmed
8673091
uniprot
proteins
pubmed
9140390
uniprot
proteins
pubmed
9150152
uniprot
proteins
pubmed
9150155
uniprot
proteins
pubmed
9609997
uniprot
proteins
pubmed
9654203
uniprot
proteins
pubmed
9971877
uniprot
proteins
sequence_length
3418
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:11239456, ECO:0000269|PubMed:19303847, ECO:0000269|PubMed:37499663}. Chromosome, telomere {ECO:0000269|PubMed:21076401}. Nucleus {ECO:0000269|PubMed:24013206, ECO:0000269|PubMed:26833090, ECO:0000305|PubMed:21276791}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:21276791}. Note=Colocalizes with ERCC5/XPG to nuclear foci following DNA replication stress. {ECO:0000269|PubMed:26833090}.
uniprot
proteins