Search Results

Overview

Uniprot IDP51587
Protein NameBreast cancer type 2 susceptibility protein
Gene NameBRCA2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1795 SKVISNVKDANAYPQ
1944 SGLEKVSKISPCDVS
1964 ICKCSIGKLHKSVSS
2104 TSRQNVSKILPRVDK

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)

Protein Sequence

10 MPIGSKERPT 20 FFEIFKTRCN 30 KADLGPISLN 40 WFEELSSEAP 50 PYNSEPAEES 60 EHKNNNYEPN 70 LFKTPQRKPS 80 YNQLASTPII 90 FKEQGLTLPL 100 YQSPVKELDK 110 FKLDLGRNVP 120 NSRHKSLRTV 130 KTKMDQADDV 140 SCPLLNSCLS 150 ESPVVLQCTH 160 VTPQRDKSVV 170 CGSLFHTPKF 180 VKGRQTPKHI 190 SESLGAEVDP 200 DMSWSSSLAT 210 PPTLSSTVLI 220 VRNEEASETV 230 FPHDTTANVK 240 SYFSNHDESL 250 KKNDRFIASV 260 TDSENTNQRE 270 AASHGFGKTS 280 GNSFKVNSCK 290 DHIGKSMPNV 300 LEDEVYETVV 310 DTSEEDSFSL 320 CFSKCRTKNL 330 QKVRTSKTRK 340 KIFHEANADE 350 CEKSKNQVKE 360 KYSFVSEVEP 370 NDTDPLDSNV 380 ANQKPFESGS 390 DKISKEVVPS 400 LACEWSQLTL 410 SGLNGAQMEK 420 IPLLHISSCD 430 QNISEKDLLD 440 TENKRKKDFL 450 TSENSLPRIS 460 SLPKSEKPLN 470 EETVVNKRDE 480 EQHLESHTDC 490 ILAVKQAISG 500 TSPVASSFQG 510 IKKSIFRIRE 520 SPKETFNASF 530 SGHMTDPNFK 540 KETEASESGL 550 EIHTVCSQKE 560 DSLCPNLIDN 570 GSWPATTTQN 580 SVALKNAGLI 590 STLKKKTNKF 600 IYAIHDETSY 610 KGKKIPKDQK 620 SELINCSAQF 630 EANAFEAPLT 640 FANADSGLLH 650 SSVKRSCSQN 660 DSEEPTLSLT 670 SSFGTILRKC 680 SRNETCSNNT 690 VISQDLDYKE 700 AKCNKEKLQL 710 FITPEADSLS 720 CLQEGQCEND 730 PKSKKVSDIK 740 EEVLAAACHP 750 VQHSKVEYSD 760 TDFQSQKSLL 770 YDHENASTLI 780 LTPTSKDVLS 790 NLVMISRGKE 800 SYKMSDKLKG 810 NNYESDVELT 820 KNIPMEKNQD 830 VCALNENYKN 840 VELLPPEKYM 850 RVASPSRKVQ 860 FNQNTNLRVI 870 QKNQEETTSI 880 SKITVNPDSE 890 ELFSDNENNF 900 VFQVANERNN 910 LALGNTKELH 920 ETDLTCVNEP 930 IFKNSTMVLY 940 GDTGDKQATQ 950 VSIKKDLVYV 960 LAEENKNSVK 970 QHIKMTLGQD 980 LKSDISLNID 990 KIPEKNNDYM 1000 NKWAGLLGPI 1010 SNHSFGGSFR 1020 TASNKEIKLS 1030 EHNIKKSKMF 1040 FKDIEEQYPT 1050 SLACVEIVNT 1060 LALDNQKKLS 1070 KPQSINTVSA 1080 HLQSSVVVSD 1090 CKNSHITPQM 1100 LFSKQDFNSN 1110 HNLTPSQKAE 1120 ITELSTILEE 1130 SGSQFEFTQF 1140 RKPSYILQKS 1150 TFEVPENQMT 1160 ILKTTSEECR 1170 DADLHVIMNA 1180 PSIGQVDSSK 1190 QFEGTVEIKR 1200 KFAGLLKNDC 1210 NKSASGYLTD 1220 ENEVGFRGFY 1230 SAHGTKLNVS 1240 TEALQKAVKL 1250 FSDIENISEE 1260 TSAEVHPISL 1270 SSSKCHDSVV 1280 SMFKIENHND 1290 KTVSEKNNKC 1300 QLILQNNIEM 1310 TTGTFVEEIT 1320 ENYKRNTENE 1330 DNKYTAASRN 1340 SHNLEFDGSD 1350 SSKNDTVCIH 1360 KDETDLLFTD 1370 QHNICLKLSG 1380 QFMKEGNTQI 1390 KEDLSDLTFL 1400 EVAKAQEACH 1410 GNTSNKEQLT 1420 ATKTEQNIKD 1430 FETSDTFFQT 1440 ASGKNISVAK 1450 ESFNKIVNFF 1460 DQKPEELHNF 1470 SLNSELHSDI 1480 RKNKMDILSY 1490 EETDIVKHKI 1500 LKESVPVGTG 1510 NQLVTFQGQP 1520 ERDEKIKEPT 1530 LLGFHTASGK 1540 KVKIAKESLD 1550 KVKNLFDEKE 1560 QGTSEITSFS 1570 HQWAKTLKYR 1580 EACKDLELAC 1590 ETIEITAAPK 1600 CKEMQNSLNN 1610 DKNLVSIETV 1620 VPPKLLSDNL 1630 CRQTENLKTS 1640 KSIFLKVKVH 1650 ENVEKETAKS 1660 PATCYTNQSP 1670 YSVIENSALA 1680 FYTSCSRKTS 1690 VSQTSLLEAK 1700 KWLREGIFDG 1710 QPERINTADY 1720 VGNYLYENNS 1730 NSTIAENDKN 1740 HLSEKQDTYL 1750 SNSSMSNSYS 1760 YHSDEVYNDS 1770 GYLSKNKLDS 1780 GIEPVLKNVE 1790 DQKNTSFSKV 1800 ISNVKDANAY 1810 PQTVNEDICV 1820 EELVTSSSPC 1830 KNKNAAIKLS 1840 ISNSNNFEVG 1850 PPAFRIASGK 1860 IVCVSHETIK 1870 KVKDIFTDSF 1880 SKVIKENNEN 1890 KSKICQTKIM 1900 AGCYEALDDS 1910 EDILHNSLDN 1920 DECSTHSHKV 1930 FADIQSEEIL 1940 QHNQNMSGLE 1950 KVSKISPCDV 1960 SLETSDICKC 1970 SIGKLHKSVS 1980 SANTCGIFST 1990 ASGKSVQVSD 2000 ASLQNARQVF 2010 SEIEDSTKQV 2020 FSKVLFKSNE 2030 HSDQLTREEN 2040 TAIRTPEHLI 2050 SQKGFSYNVV 2060 NSSAFSGFST 2070 ASGKQVSILE 2080 SSLHKVKGVL 2090 EEFDLIRTEH 2100 SLHYSPTSRQ 2110 NVSKILPRVD 2120 KRNPEHCVNS 2130 EMEKTCSKEF 2140 KLSNNLNVEG 2150 GSSENNHSIK 2160 VSPYLSQFQQ 2170 DKQQLVLGTK 2180 VSLVENIHVL 2190 GKEQASPKNV 2200 KMEIGKTETF 2210 SDVPVKTNIE 2220 VCSTYSKDSE 2230 NYFETEAVEI 2240 AKAFMEDDEL 2250 TDSKLPSHAT 2260 HSLFTCPENE 2270 EMVLSNSRIG 2280 KRRGEPLILV 2290 GEPSIKRNLL 2300 NEFDRIIENQ 2310 EKSLKASKST 2320 PDGTIKDRRL 2330 FMHHVSLEPI 2340 TCVPFRTTKE 2350 RQEIQNPNFT 2360 APGQEFLSKS 2370 HLYEHLTLEK 2380 SSSNLAVSGH 2390 PFYQVSATRN 2400 EKMRHLITTG 2410 RPTKVFVPPF 2420 KTKSHFHRVE 2430 QCVRNINLEE 2440 NRQKQNIDGH 2450 GSDDSKNKIN 2460 DNEIHQFNKN 2470 NSNQAVAVTF 2480 TKCEEEPLDL 2490 ITSLQNARDI 2500 QDMRIKKKQR 2510 QRVFPQPGSL 2520 YLAKTSTLPR 2530 ISLKAAVGGQ 2540 VPSACSHKQL 2550 YTYGVSKHCI 2560 KINSKNAESF 2570 QFHTEDYFGK 2580 ESLWTGKGIQ 2590 LADGGWLIPS 2600 NDGKAGKEEF 2610 YRALCDTPGV 2620 DPKLISRIWV 2630 YNHYRWIIWK 2640 LAAMECAFPK 2650 EFANRCLSPE 2660 RVLLQLKYRY 2670 DTEIDRSRRS 2680 AIKKIMERDD 2690 TAAKTLVLCV 2700 SDIISLSANI 2710 SETSSNKTSS 2720 ADTQKVAIIE 2730 LTDGWYAVKA 2740 QLDPPLLAVL 2750 KNGRLTVGQK 2760 IILHGAELVG 2770 SPDACTPLEA 2780 PESLMLKISA 2790 NSTRPARWYT 2800 KLGFFPDPRP 2810 FPLPLSSLFS 2820 DGGNVGCVDV 2830 IIQRAYPIQW 2840 MEKTSSGLYI 2850 FRNEREEEKE 2860 AAKYVEAQQK 2870 RLEALFTKIQ 2880 EEFEEHEENT 2890 TKPYLPSRAL 2900 TRQQVRALQD 2910 GAELYEAVKN 2920 AADPAYLEGY 2930 FSEEQLRALN 2940 NHRQMLNDKK 2950 QAQIQLEIRK 2960 AMESAEQKEQ 2970 GLSRDVTTVW 2980 KLRIVSYSKK 2990 EKDSVILSIW 3000 RPSSDLYSLL 3010 TEGKRYRIYH 3020 LATSKSKSKS 3030 ERANIQLAAT 3040 KKTQYQQLPV 3050 SDEILFQIYQ 3060 PREPLHFSKF 3070 LDPDFQPSCS 3080 EVDLIGFVVS 3090 VVKKTGLAPF 3100 VYLSDECYNL 3110 LAIKFWIDLN 3120 EDIIKPHMLI 3130 AASNLQWRPE 3140 SKSGLLTLFA 3150 GDFSVFSASP 3160 KEGHFQETFN 3170 KMKNTVENID 3180 ILCNEAENKL 3190 MHILHANDPK 3200 WSTPTKDCTS 3210 GPYTAQIIPG 3220 TGNKLLMSSP 3230 NCEIYYQSPL 3240 SLCMAKRKSV 3250 STPVSAQMTS 3260 KSCKGEKEID 3270 DQKNCKKRRA 3280 LDFLSRLPLP 3290 PPVSPICTFV 3300 SPAAQKAFQP 3310 PRSCGTKYET 3320 PIKKKELNSP 3330 QMTPFKKFNE 3340 ISLLESNSIA 3350 DEELALINTQ 3360 ALLSGSTGEK 3370 QFISVSESTR 3380 TAPTSSEDYL 3390 RLKRRCTTSL 3400 IKEQESSQAS 3410 TEECEKNKQD TITTKKYI

Gene Ontology

Classification GO ID Description
Cellular Component GO:0033593 BRCA2-MAGE-D1 complex
Molecular Function GO:0003697 single-stranded DNA binding
Biological Process GO:0071479 cellular response to ionizing radiation
Biological Process GO:0051298 centrosome duplication
Biological Process GO:0006302 double-strand break repair
Biological Process GO:0000724 double-strand break repair via homologous recombination
Biological Process GO:0070200 establishment of protein localization to telomere
Biological Process GO:0007141 male meiosis I
Biological Process GO:1990426 mitotic recombination-dependent replication fork processing
Biological Process GO:0033600 negative regulation of mammary gland epithelial cell proliferation
Biological Process GO:0006289 nucleotide-excision repair
Biological Process GO:0045893 positive regulation of DNA-templated transcription
Biological Process GO:2000001 regulation of DNA damage checkpoint
Biological Process GO:0006355 regulation of DNA-templated transcription
Biological Process GO:0000722 telomere maintenance via recombination
Cellular Component GO:0005813 centrosome
Cellular Component GO:0000781 chromosome, telomeric region
Cellular Component GO:0005829 cytosol
Cellular Component GO:0000800 lateral element
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0032991 protein-containing complex
Cellular Component GO:0030141 secretory granule
Molecular Function GO:0043015 gamma-tubulin binding
Molecular Function GO:0010484 histone H3 acetyltransferase activity
Molecular Function GO:0010485 histone H4 acetyltransferase activity
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0002020 protease binding

Reference

[1] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.