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Protein

Breast cancer type 2 susceptibility protein homolog

Gene

Brca2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in double-strand break repair and/or homologous recombination. Binds RAD51 and potentiates recombinational DNA repair by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to displace replication protein-A (RPA) from ssDNA and stabilizing RAD51-ssDNA filaments by blocking ATP hydrolysis. Part of a PALB2-scaffolded HR complex containing RAD51C and which is thought to play a role in DNA repair by HR. May participate in S phase checkpoint activation. Binds selectively to ssDNA, and to ssDNA in tailed duplexes and replication fork structures. 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. In concert with NPM1, regulates centrosome duplication. Interacts with the TREX-2 complex (transcription and export complex 2) subunits PCID2 and DSS1, and is required to prevent R-loop-associated DNA damage and thus transcription-associated genomic instability, independently of its known role in homologous recombination (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

  • brain development Source: MGI
  • cell aging Source: MGI
  • cell proliferation Source: MGI
  • cellular response to DNA damage stimulus Source: UniProtKB
  • centrosome duplication Source: MGI
  • chordate embryonic development Source: MGI
  • chromosome breakage Source: MGI
  • chromosome organization Source: MGI
  • cytokinesis Source: Ensembl
  • DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Source: MGI
  • double-strand break repair Source: MGI
  • double-strand break repair via homologous recombination Source: MGI
  • establishment of protein localization to telomere Source: BHF-UCL
  • female gonad development Source: MGI
  • hemopoiesis Source: MGI
  • histone H3 acetylation Source: MGI
  • histone H4 acetylation Source: MGI
  • inner cell mass cell proliferation Source: MGI
  • intrinsic apoptotic signaling pathway in response to DNA damage Source: MGI
  • intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: MGI
  • male meiosis I Source: MGI
  • mitotic recombination-dependent replication fork processing Source: MGI
  • negative regulation of mammary gland epithelial cell proliferation Source: MGI
  • nucleotide-excision repair Source: MGI
  • oocyte maturation Source: MGI
  • positive regulation of mitotic cell cycle Source: MGI
  • positive regulation of transcription, DNA-templated Source: MGI
  • regulation of cell proliferation Source: GO_Central
  • regulation of cytokinesis Source: MGI
  • regulation of transcription, DNA-templated Source: GO_Central
  • replication fork protection Source: MGI
  • response to gamma radiation Source: MGI
  • response to UV-C Source: MGI
  • response to X-ray Source: MGI
  • spermatogenesis Source: MGI
  • telomere maintenance via recombination Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Cell cycle, DNA damage, DNA recombination, DNA repair

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-5685942. HDR through Homologous Recombination (HRR).
R-MMU-5693554. Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
R-MMU-5693568. Resolution of D-loop Structures through Holliday Junction Intermediates.
R-MMU-5693579. Homologous DNA Pairing and Strand Exchange.
R-MMU-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-MMU-912446. Meiotic recombination.
R-MMU-912497. Meiotic Recombination.

Names & Taxonomyi

Protein namesi
Recommended name:
Breast cancer type 2 susceptibility protein homolog
Alternative name(s):
Fanconi anemia group D1 protein homolog
Gene namesi
Name:Brca2
Synonyms:Fancd1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:109337. Brca2.

Subcellular locationi

GO - Cellular componenti

  • BRCA2-MAGE-D1 complex Source: MGI
  • centrosome Source: UniProtKB
  • cytoplasm Source: MGI
  • lateral element Source: MGI
  • nuclear chromosome, telomeric region Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
  • protein complex Source: MGI
  • secretory granule Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000649851 – 3329Breast cancer type 2 susceptibility protein homologAdd BLAST3329

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei435PhosphoserineBy similarity1
Modified residuei481PhosphoserineBy similarity1
Modified residuei735PhosphoserineBy similarity1
Modified residuei2048PhosphoserineBy similarity1
Modified residuei3214Phosphoserine; by CDK1 and CDK2By similarity1
Modified residuei3241PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylation by CHEK1 and CHEK2 regulates interaction with RAD51. Phosphorylation at Ser-3214 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 (By similarity).By similarity
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 (By similarity).By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP97929.
PaxDbiP97929.
PeptideAtlasiP97929.
PRIDEiP97929.

PTM databases

iPTMnetiP97929.
PhosphoSitePlusiP97929.

Expressioni

Tissue specificityi

Widely expressed. Highest expression in cerebellum, testis, ileum, appendix, epididymis, ovary and mammary gland. No expression in lung.

Developmental stagei

In the mammary gland, expression increases dramatically during pregnancy.

Gene expression databases

BgeeiENSMUSG00000041147.
CleanExiMM_BRCA2.
ExpressionAtlasiP97929. baseline and differential.
GenevisibleiP97929. MM.

Interactioni

Subunit structurei

Monomer and dimer. Interacts with RAD51; regulates RAD51 recruitment and function at sites of DNA repair. Interacts with DSS1, WDR16, USP11, DMC1, ROCK2 and NPM1. Interacts with both nonubiquitinated and monoubiquitinated FANCD2; this complex also includes XRCC3 and phosphorylated FANCG. Part of a BRCA complex containing BRCA1, BRCA2 and PALB2. Interacts directly with PALB2 which may serve as a scaffold for a HR complex containing PALB2, BRCA2, RAD51C, RAD51 and XRCC3. Interacts with BRCA1 only in the presence of PALB2 which serves as the bridging protein. Interacts with POLH; the interaction is direct. Interacts with the TREX-2 complex subunits PCID2 and DSS1 (By similarity).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198384. 6 interactors.
IntActiP97929. 2 interactors.
STRINGi10090.ENSMUSP00000038576.

Structurei

Secondary structure

13329
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2404 – 2420Combined sources17
Helixi2430 – 2435Combined sources6
Helixi2446 – 2448Combined sources3
Beta strandi2456 – 2458Combined sources3
Beta strandi2462 – 2464Combined sources3
Beta strandi2468 – 2472Combined sources5
Turni2475 – 2480Combined sources6
Helixi2486 – 2489Combined sources4
Turni2490 – 2492Combined sources3
Beta strandi2495 – 2497Combined sources3
Beta strandi2503 – 2505Combined sources3
Turni2512 – 2514Combined sources3
Helixi2518 – 2527Combined sources10
Helixi2538 – 2554Combined sources17
Turni2560 – 2562Combined sources3
Beta strandi2564 – 2569Combined sources6
Helixi2570 – 2584Combined sources15
Turni2585 – 2587Combined sources3
Helixi2592 – 2597Combined sources6
Beta strandi2606 – 2608Combined sources3
Beta strandi2640 – 2643Combined sources4
Beta strandi2648 – 2653Combined sources6
Helixi2655 – 2662Combined sources8
Beta strandi2671 – 2674Combined sources4
Beta strandi2675 – 2677Combined sources3
Beta strandi2679 – 2681Combined sources3
Beta strandi2696 – 2699Combined sources4
Helixi2701 – 2703Combined sources3
Beta strandi2704 – 2707Combined sources4
Beta strandi2713 – 2715Combined sources3
Helixi2726 – 2728Combined sources3
Beta strandi2731 – 2733Combined sources3
Beta strandi2736 – 2746Combined sources11
Beta strandi2751 – 2754Combined sources4
Beta strandi2756 – 2758Combined sources3
Beta strandi2760 – 2763Combined sources4
Helixi2767 – 2778Combined sources12
Helixi2782 – 2791Combined sources10
Helixi2813 – 2817Combined sources5
Helixi2822 – 2830Combined sources9
Beta strandi2833 – 2835Combined sources3
Turni2836 – 2840Combined sources5
Beta strandi2848 – 2850Combined sources3
Turni2851 – 2853Combined sources3
Helixi2855 – 2858Combined sources4
Helixi2861 – 2871Combined sources11
Helixi2873 – 2876Combined sources4
Turni2877 – 2881Combined sources5
Beta strandi2889 – 2900Combined sources12
Beta strandi2904 – 2910Combined sources7
Helixi2913 – 2918Combined sources6
Beta strandi2924 – 2930Combined sources7
Beta strandi2938 – 2940Combined sources3
Beta strandi2945 – 2957Combined sources13
Helixi2961 – 2964Combined sources4
Turni2965 – 2967Combined sources3
Helixi2977 – 2980Combined sources4
Beta strandi2981 – 2983Combined sources3
Turni2986 – 2989Combined sources4
Beta strandi2990 – 3001Combined sources12
Beta strandi3004 – 3006Combined sources3
Beta strandi3009 – 3013Combined sources5
Beta strandi3015 – 3017Combined sources3
Beta strandi3019 – 3026Combined sources8
Beta strandi3037 – 3044Combined sources8
Beta strandi3050 – 3052Combined sources3
Beta strandi3056 – 3058Combined sources3
Beta strandi3063 – 3067Combined sources5
Turni3071 – 3073Combined sources3
Helixi3074 – 3080Combined sources7
Helixi3082 – 3085Combined sources4
Helixi3090 – 3102Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MIUX-ray3.10A2378-3115[»]
1MJEX-ray3.50A2378-3113[»]
ProteinModelPortaliP97929.
SMRiP97929.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP97929.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati981 – 1015BRCA2 1Add BLAST35
Repeati1192 – 1226BRCA2 2Add BLAST35
Repeati1394 – 1428BRCA2 3Add BLAST35
Repeati1491 – 1525BRCA2 4Add BLAST35
Repeati1623 – 1657BRCA2 5Add BLAST35
Repeati1924 – 1958BRCA2 6Add BLAST35
Repeati2004 – 2038BRCA2 7Add BLAST35

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 40Interaction with PALB2By similarityAdd BLAST40
Regioni628 – 979Interaction with NPM1By similarityAdd BLAST352
Regioni2298 – 2466Interaction with FANCD2By similarityAdd BLAST169
Regioni2402 – 2753Interaction with SHFM1/DSS1By similarityAdd BLAST352

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi2603 – 2619Nuclear export signal; masked by interaction with SHFM1/DSS1By similarityAdd BLAST17

Sequence similaritiesi

Contains 7 BRCA2 repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG4751. Eukaryota.
ENOG410Y06W. LUCA.
GeneTreeiENSGT00390000003602.
HOGENOMiHOG000139693.
HOVERGENiHBG050731.
InParanoidiP97929.
KOiK08775.
OMAiHRQMLND.
OrthoDBiEOG091G0C79.
TreeFamiTF105041.

Family and domain databases

InterProiIPR015525. BRCA2.
IPR015252. BRCA2_hlx.
IPR015187. BRCA2_OB_1.
IPR015188. BRCA2_OB_3.
IPR002093. BRCA2_repeat.
IPR012340. NA-bd_OB-fold.
IPR015205. Tower_dom.
[Graphical view]
PANTHERiPTHR11289. PTHR11289. 2 hits.
PfamiPF09169. BRCA-2_helical. 1 hit.
PF09103. BRCA-2_OB1. 1 hit.
PF09104. BRCA-2_OB3. 1 hit.
PF00634. BRCA2. 7 hits.
PF09121. Tower. 1 hit.
[Graphical view]
PIRSFiPIRSF002397. BRCA2. 1 hit.
SMARTiSM01341. Tower. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 4 hits.
SSF81872. SSF81872. 1 hit.
PROSITEiPS50138. BRCA2_REPEAT. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P97929-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPVEYKRRPT FWEIFKARCS TADLGPISLN WFEELSSEAP PYNSEPPEES
60 70 80 90 100
EYKPHGYEPQ LFKTPQRNPP YHQFASTPIM FKERSQTLPL DQSPFRELGK
110 120 130 140 150
VVASSKHKTH SKKKTKVDPV VDVASPPLKS CLSESPLTLR CTQAVLQREK
160 170 180 190 200
PVVSGSLFYT PKLKEGQTPK PISESLGVEV DPDMSWTSSL ATPPTLSSTV
210 220 230 240 250
LIARDEEARS SVTPADSPAT LKSCFSNHNE SPQKNDRSVP SVIDSENKNQ
260 270 280 290 300
QEAFSQGLGK MLGDSSGKRN SFKDCLRKPI PNILEDGETA VDTSEEDSFS
310 320 330 340 350
LCFPKRRTRN LQKMRMGKTR KKIFSETRTD ELSEEARRQT DDKNSFVFEM
360 370 380 390 400
ELRESDPLDP GVTSQKPFYS QNEEICNEAV QCSDSRWSQS NLSGLNETQT
410 420 430 440 450
GKITLPHISS HSQNISEDFI DMKKEGTGSI TSEKSLPHIS SLPEPEKMFS
460 470 480 490 500
EETVVDKEHE GQHFESLEDS IAGKQMVSRT SQAACLSPSI RKSIFKMREP
510 520 530 540 550
LDETLGTVFS DSMTNSTFTE EHEASACGLG ILTACSQRED SICPSSVDTG
560 570 580 590 600
SWPTTLTDTS ATVKNAGLIS TLKNKKRKFI YSVSDDASLQ GKKLQTHRQL
610 620 630 640 650
ELTNLSAQLE ASAFEVPLTF TNVNSGIPDS SDKKRCLPND PEEPSLTNSF
660 670 680 690 700
GTATSKEISY IHALISQDLN DKEAIVIEEK PQPYTAREAD FLLCLPERTC
710 720 730 740 750
ENDQKSPKVS NGKEKVLVSA CLPSAVQLSS ISFESQENPL GDHNGTSTLK
760 770 780 790 800
LTPSSKLPLS KADMVSREKM CKMPEKLQCE SCKVNIELSK NILEVNEICI
810 820 830 840 850
LSENSKTPGL LPPGENIIEV ASSMKSQFNQ NAKIVIQKDQ KGSPFISEVA
860 870 880 890 900
VNMNSEELFP DSGNNFAFQV TNKCNKPDLG SSVELQEEDL SHTQGPSLKN
910 920 930 940 950
SPMAVDEDVD DAHAAQVLIT KDSDSLAVVH DYTEKSRNNI EQHQKGTEDK
960 970 980 990 1000
DFKSNSSLNM KSDGNSDCSD KWSEFLDPVL NHNFGGSFRT ASNKEIKLSE
1010 1020 1030 1040 1050
HNVKKSKMFF KDIEEQYPTR LACIDIVNTL PLANQKKLSE PHIFDLKSVT
1060 1070 1080 1090 1100
TVSTQSHNQS SVSHEDTDTA PQMLSSKQDF HSNNLTTSQK AEITELSTIL
1110 1120 1130 1140 1150
EESGSQFEFT QFRKPSHIAQ NTSEVPGNQM VVLSTASKEW KDTDLHLPVD
1160 1170 1180 1190 1200
PSVGQTDHSK QFEGSAGVKQ SFPHLLEDTC NKNTSCFLPN INEMEFGGFC
1210 1220 1230 1240 1250
SALGTKLSVS NEALRKAMKL FSDIENSEEP SAKVGPRGFS SSAHHDSVAS
1260 1270 1280 1290 1300
VFKIKKQNTE KSFDEKSSKC QVTLQNNIEM TTCIFVGRNP EKYIKNTKHE
1310 1320 1330 1340 1350
DSYTSSQRNN LENSDGSMSS TSGPVYIHKG DSDLPADQGS KCPESCTQYA
1360 1370 1380 1390 1400
REENTQIKEN ISDLTCLEIM KAEETCMKSS DKKQLPSDKM EQNIKEFNIS
1410 1420 1430 1440 1450
FQTASGKNTR VSKESLNKSV NIFNRETDEL TVISDSLNSK ILHGINKDKM
1460 1470 1480 1490 1500
HTSCHKKAIS IKKVFEDHFP IVTVSQLPAQ QHPEYEIEST KEPTLLSFHT
1510 1520 1530 1540 1550
ASGKKVKIMQ ESLDKVKNLF DETQYVRKTA SFSQGSKPLK DSKKELTLAY
1560 1570 1580 1590 1600
EKIEVTASKC EEMQNFVSKE TEMLPQQNYH MYRQTENLKT SNGTSSKVQE
1610 1620 1630 1640 1650
NIENNVEKNP RICCICQSSY PVTEDSALAY YTEDSRKTCV RESSLSKGRK
1660 1670 1680 1690 1700
WLREQGDKLG TRNTIKIECV KEHTEDFAGN ASYEHSLVII RTEIDTNHVS
1710 1720 1730 1740 1750
ENQVSTLLSD PNVCHSYLSQ SSFCHCDDMH NDSGYFLKNK IDSDVPPDMK
1760 1770 1780 1790 1800
NAEGNTISPR VSATKERNLH PQTINEYCVQ KLETNTSPHA NKDVAIDPSL
1810 1820 1830 1840 1850
LDSRNCKVGS LVFITAHSQE TERTKEIVTD NCYKIVEQNR QSKPDTCQTS
1860 1870 1880 1890 1900
CHKVLDDSKD FICPSSSGDV CINSRKDSFC PHNEQILQHN QSMSGLKKAA
1910 1920 1930 1940 1950
TPPVGLETWD TSKSIREPPQ AAHPSRTYGI FSTASGKAIQ VSDASLEKAR
1960 1970 1980 1990 2000
QVFSEMDGDA KQLSSMVSLE GNEKPHHSVK RENSVVHSTQ GVLSLPKPLP
2010 2020 2030 2040 2050
GNVNSSVFSG FSTAGGKLVT VSESALHKVK GMLEEFDLIR TEHTLQHSPI
2060 2070 2080 2090 2100
PEDVSKILPQ PCAEIRTPEY PVNSKLQKTY NDKSSLPSNY KESGSSGNTQ
2110 2120 2130 2140 2150
SIEVSLQLSQ MERNQDTQLV LGTKVSHSKA NLLGKEQTLP QNIKVKTDEM
2160 2170 2180 2190 2200
KTFSDVPVKT NVGEYYSKES ENYFETEAVE SAKAFMEDDE LTDSEQTHAK
2210 2220 2230 2240 2250
CSLFTCPQNE TLFNSRTRKR GGVTVDAVGQ PPIKRSLLNE FDRIIESKGK
2260 2270 2280 2290 2300
SLTPSKSTPD GTVKDRSLFT HHMSLEPVTC GPFCSSKERQ GAQRPHLTSP
2310 2320 2330 2340 2350
AQELLSKGHP WRHSALEKSP SSPIVSILPA HDVSATRTER TRHSGKSTKV
2360 2370 2380 2390 2400
FVPPFKMKSQ FHGDEHFNSK NVNLEGKNQK STDGDREDGN DSHVRQFNKD
2410 2420 2430 2440 2450
LMSSLQSARD LQDMRIKNKE RRHLRLQPGS LYLTKSSTLP RISLQAAVGD
2460 2470 2480 2490 2500
RAPSACSPKQ LYIYGVSKEC INVNSKNAEY FQFDIQDHFG KEDLCAGKGF
2510 2520 2530 2540 2550
QLADGGWLIP SNDGKAGKEE FYRALCDTPG VDPKLISSIW VANHYRWIVW
2560 2570 2580 2590 2600
KLAAMEFAFP KEFANRCLNP ERVLLQLKYR YDVEIDNSRR SALKKILERD
2610 2620 2630 2640 2650
DTAAKTLVLC ISDIISPSTK VSETSGGKTS GEDANKVDTI ELTDGWYAVR
2660 2670 2680 2690 2700
AQLDPPLMAL VKSGKLTVGQ KIITQGAELV GSPDACAPLE APDSLRLKIS
2710 2720 2730 2740 2750
ANSTRPARWH SRLGFFRDPR PFPLPLSSLF SDGGNVGCVD IIVQRVYPLQ
2760 2770 2780 2790 2800
WVEKTVSGLY IFRSEREEEK EALRFAEAQQ KKLEALFTKV HTEFKDHEED
2810 2820 2830 2840 2850
TTQRCVLSRT LTRQQVHALQ DGAELYAAVQ YASDPDHLEA CFSEEQLRAL
2860 2870 2880 2890 2900
NNYRQMLNDK KQARIQSEFR KALESAEKEE GLSRDVTTVW KLRVTSYKKK
2910 2920 2930 2940 2950
EKSALLSIWR PSSDLSSLLT EGKRYRIYHL AVSKSKSKFE RPSIQLTATK
2960 2970 2980 2990 3000
RTQYQQLPVS SETLLQVYQP RESLHFSRLS DPAFQPPCSE VDVVGVVVSV
3010 3020 3030 3040 3050
VKPIGLAPLV YLSDECLNLL VVKFGIDLNE DIKPRVLIAA SNLQCQPEST
3060 3070 3080 3090 3100
SGVPTLFAGH FSIFSASPKE AYFQEKVNNL KHAIENIDTF YKEAEKKLIH
3110 3120 3130 3140 3150
VLEGDSPKWS TPNKDPTREP HAASTCCASD LLGSGGQFLR ISPTGQQSYQ
3160 3170 3180 3190 3200
SPLSHCTLKG KSMPLAHSAQ MAAKSWSGEN EIDDPKTCRK RRALDFLSRL
3210 3220 3230 3240 3250
PLPSPVSPIC TFVSPAAQKA FQPPRSCGTK YATPIKKEPS SPRRRTPFQK
3260 3270 3280 3290 3300
TSGVSLPDCD SVADEELALL STQALTPDSV GGNEQAFPGD STRNPQPAQR
3310 3320
PDQQVGPRSR KESLRDCRGD SSEKLAVES
Length:3,329
Mass (Da):370,664
Last modified:October 3, 2012 - v2
Checksum:i50A32E8BADE2CF7E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1038L → I in AAB48306 (PubMed:9063750).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti44S → F in strain: C57BL/6 and 129/Sv. 1
Natural varianti340T → P in strain: 129/Sv. 1
Natural varianti377N → H in strain: C57BL/6. 1
Natural varianti407H → P in strain: C57BL/6. 1
Natural varianti661I → V in strain: C57BL/6. 1
Natural varianti739P → H in strain: C57BL/6. 1
Natural varianti1198 – 1199GF → RI in strain: C57BL/6. 2
Natural varianti1257Q → P in strain: C57BL/6. 1
Natural varianti1392Q → R in strain: C57BL/6. 1
Natural varianti1520 – 1521FD → CG in strain: C57BL/6. 2
Natural varianti1583R → W in strain: C57BL/6. 1
Natural varianti1613C → W in strain: C57BL/6. 1
Natural varianti1686S → R in strain: C57BL/6. 1
Natural varianti1799S → F in strain: 129/Sv. 1
Natural varianti1881P → L in strain: C57BL/6. 1
Natural varianti1894S → F in strain: 129/Sv. 1
Natural varianti2141Q → K in strain: C57BL/6. 1
Natural varianti2392S → R in strain: C57BL/6. 1
Natural varianti2605K → Q in strain: C57BL/6. 1
Natural varianti2648A → P in strain: C57BL/6. 1
Natural varianti2717R → C in strain: 129/Sv. 1
Natural varianti2729L → M in strain: 129/Sv. 1
Natural varianti2814Q → H in strain: C57BL/6. 1
Natural varianti2827A → P in strain: C57BL/6. 1
Natural varianti2907S → I in strain: 129/Sv. 1
Natural varianti2929H → L in strain: 129/Sv. 1
Natural varianti3058A → G in strain: C57BL/6. 1
Natural varianti3071A → G in strain: C57BL/6. 1
Natural varianti3081K → E in strain: C57BL/6. 1
Natural varianti3089T → S in strain: C57BL/6. 1
Natural varianti3105 – 3109DSPKW → SQSQV in strain: C57BL/6. 5
Natural varianti3220A → G in strain: 129/Sv. 1
Natural varianti3238E → K in strain: 129/Sv. 1
Natural varianti3243Missing in strain: C57BL/6. 1
Natural varianti3245R → K in strain: 129/Sv. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U82270 mRNA. Translation: AAB48306.1.
U65594 mRNA. Translation: AAC23702.1.
U89652 mRNA. Translation: AAB71377.1.
AC154885 Genomic DNA. No translation available.
U72947 mRNA. Translation: AAB40720.1.
U89503 Genomic DNA. Translation: AAC53276.1.
CCDSiCCDS39411.1.
PIRiT30835.
T30904.
T42205.
RefSeqiNP_001074470.1. NM_001081001.2.
NP_033895.2. NM_009765.3.
XP_017176117.1. XM_017320628.1.
UniGeneiMm.236256.

Genome annotation databases

EnsembliENSMUST00000044620; ENSMUSP00000038576; ENSMUSG00000041147.
ENSMUST00000202313; ENSMUSP00000144150; ENSMUSG00000041147.
GeneIDi12190.
KEGGimmu:12190.
UCSCiuc009aty.2. mouse.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U82270 mRNA. Translation: AAB48306.1.
U65594 mRNA. Translation: AAC23702.1.
U89652 mRNA. Translation: AAB71377.1.
AC154885 Genomic DNA. No translation available.
U72947 mRNA. Translation: AAB40720.1.
U89503 Genomic DNA. Translation: AAC53276.1.
CCDSiCCDS39411.1.
PIRiT30835.
T30904.
T42205.
RefSeqiNP_001074470.1. NM_001081001.2.
NP_033895.2. NM_009765.3.
XP_017176117.1. XM_017320628.1.
UniGeneiMm.236256.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MIUX-ray3.10A2378-3115[»]
1MJEX-ray3.50A2378-3113[»]
ProteinModelPortaliP97929.
SMRiP97929.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198384. 6 interactors.
IntActiP97929. 2 interactors.
STRINGi10090.ENSMUSP00000038576.

PTM databases

iPTMnetiP97929.
PhosphoSitePlusiP97929.

Proteomic databases

EPDiP97929.
PaxDbiP97929.
PeptideAtlasiP97929.
PRIDEiP97929.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000044620; ENSMUSP00000038576; ENSMUSG00000041147.
ENSMUST00000202313; ENSMUSP00000144150; ENSMUSG00000041147.
GeneIDi12190.
KEGGimmu:12190.
UCSCiuc009aty.2. mouse.

Organism-specific databases

CTDi675.
MGIiMGI:109337. Brca2.

Phylogenomic databases

eggNOGiKOG4751. Eukaryota.
ENOG410Y06W. LUCA.
GeneTreeiENSGT00390000003602.
HOGENOMiHOG000139693.
HOVERGENiHBG050731.
InParanoidiP97929.
KOiK08775.
OMAiHRQMLND.
OrthoDBiEOG091G0C79.
TreeFamiTF105041.

Enzyme and pathway databases

ReactomeiR-MMU-5685942. HDR through Homologous Recombination (HRR).
R-MMU-5693554. Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
R-MMU-5693568. Resolution of D-loop Structures through Holliday Junction Intermediates.
R-MMU-5693579. Homologous DNA Pairing and Strand Exchange.
R-MMU-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-MMU-912446. Meiotic recombination.
R-MMU-912497. Meiotic Recombination.

Miscellaneous databases

EvolutionaryTraceiP97929.
PROiP97929.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000041147.
CleanExiMM_BRCA2.
ExpressionAtlasiP97929. baseline and differential.
GenevisibleiP97929. MM.

Family and domain databases

InterProiIPR015525. BRCA2.
IPR015252. BRCA2_hlx.
IPR015187. BRCA2_OB_1.
IPR015188. BRCA2_OB_3.
IPR002093. BRCA2_repeat.
IPR012340. NA-bd_OB-fold.
IPR015205. Tower_dom.
[Graphical view]
PANTHERiPTHR11289. PTHR11289. 2 hits.
PfamiPF09169. BRCA-2_helical. 1 hit.
PF09103. BRCA-2_OB1. 1 hit.
PF09104. BRCA-2_OB3. 1 hit.
PF00634. BRCA2. 7 hits.
PF09121. Tower. 1 hit.
[Graphical view]
PIRSFiPIRSF002397. BRCA2. 1 hit.
SMARTiSM01341. Tower. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 4 hits.
SSF81872. SSF81872. 1 hit.
PROSITEiPS50138. BRCA2_REPEAT. 6 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBRCA2_MOUSE
AccessioniPrimary (citable) accession number: P97929
Secondary accession number(s): F8VPU5, O35922, P97383
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: October 3, 2012
Last modified: November 2, 2016
This is version 155 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.