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O35923

- BRCA2_RAT

UniProt

O35923 - BRCA2_RAT

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Protein

Breast cancer type 2 susceptibility protein homolog

Gene
Brca2, Fancd1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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 By similarity.

GO - Molecular functioni

  1. gamma-tubulin binding Source: RefGenome
  2. protein binding Source: RGD
  3. single-stranded DNA binding Source: RGD

GO - Biological processi

  1. centrosome duplication Source: RefGenome
  2. chromosome organization Source: RefGenome
  3. DNA recombination Source: RGD
  4. double-strand break repair via homologous recombination Source: UniProtKB
  5. homologous chromosome orientation involved in meiotic metaphase I plate congression Source: RGD
  6. mammary gland development Source: RGD
  7. multicellular organism growth Source: RGD
  8. regulation of cell proliferation Source: RefGenome
  9. regulation of transcription, DNA-templated Source: RefGenome
  10. response to estradiol Source: RGD
  11. response to nutrient Source: RGD
  12. spermatogenesis Source: RGD
Complete GO annotation...

Keywords - Biological processi

Cell cycle, DNA damage, DNA recombination, DNA repair

Keywords - Ligandi

DNA-binding

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi2219. Brca2.

Subcellular locationi

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Nucleus By similarity

GO - Cellular componenti

  1. centrosome Source: UniProtKB
  2. cytoplasm Source: UniProtKB-KW
  3. nucleus Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 33433343Breast cancer type 2 susceptibility protein homologPRO_0000064986Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei736 – 7361Phosphoserine By similarity
Modified residuei3222 – 32221Phosphoserine; by CDK1 and CDK2 By similarity

Post-translational modificationi

Phosphorylation by CHEK1 and CHEK2 regulates interaction with RAD51. Phosphorylation at Ser-3222 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.
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.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiO35923.
PRIDEiO35923.

Expressioni

Tissue specificityi

Highest expression in testis. Also expressed in spleen, skeletal muscle, thymus, mammary gland, heart, ovary, prostate, liver, lung, kidney and brain.

Gene expression databases

GenevestigatoriO35923.

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.

Structurei

Secondary structure

1
3343
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni2407 – 24093
Helixi2410 – 242819
Turni2441 – 24433
Beta strandi2444 – 24463
Helixi2453 – 24575
Beta strandi2467 – 24693
Helixi2470 – 24734
Helixi2479 – 24813
Turni2484 – 24896
Helixi2494 – 24985
Turni2500 – 25023
Beta strandi2503 – 25053
Beta strandi2509 – 25113
Helixi2512 – 25143
Beta strandi2515 – 25173
Helixi2527 – 25359
Helixi2542 – 25443
Helixi2547 – 256721
Turni2569 – 25713
Turni2573 – 25753
Beta strandi2576 – 25783
Helixi2579 – 259315
Helixi2601 – 26066
Beta strandi2615 – 26228
Beta strandi2649 – 26524
Beta strandi2657 – 26604
Helixi2664 – 26718
Beta strandi2680 – 26845
Beta strandi2687 – 26904
Helixi2697 – 26993
Beta strandi2705 – 27073
Turni2710 – 27123
Beta strandi2713 – 27153
Beta strandi2718 – 27203
Beta strandi2722 – 27243
Beta strandi2746 – 27483
Beta strandi2759 – 27635
Beta strandi2765 – 27728
Helixi2774 – 27829
Beta strandi2895 – 29039
Beta strandi2905 – 29095
Beta strandi2913 – 29197
Turni2922 – 29276
Beta strandi2934 – 29385
Beta strandi2962 – 29654
Helixi2970 – 29734
Turni2974 – 29763
Helixi2985 – 29895
Helixi2996 – 29983
Beta strandi2999 – 30057
Beta strandi3008 – 30103
Beta strandi3013 – 30153
Beta strandi3018 – 30225
Beta strandi3028 – 30358
Beta strandi3046 – 30549
Beta strandi3064 – 307613
Helixi3080 – 309718
Helixi3101 – 311010

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IYJX-ray3.40B/D2335-3151[»]
ProteinModelPortaliO35923.
SMRiO35923. Positions 1505-1536, 2403-3112.

Miscellaneous databases

EvolutionaryTraceiO35923.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati984 – 101835BRCA2 1Add
BLAST
Repeati1197 – 123135BRCA2 2Add
BLAST
Repeati1405 – 143935BRCA2 3Add
BLAST
Repeati1503 – 153735BRCA2 4Add
BLAST
Repeati1645 – 166925BRCA2 5Add
BLAST
Repeati1828 – 184518BRCA2 6Add
BLAST
Repeati1939 – 197335BRCA2 7Add
BLAST
Repeati2019 – 205335BRCA2 8Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 4040Interaction with PALB2 By similarityAdd
BLAST
Regioni622 – 982361Interaction with NPM1 By similarityAdd
BLAST
Regioni2313 – 2475163Interaction with FANCD2 By similarityAdd
BLAST

Sequence similaritiesi

Contains 8 BRCA2 repeats.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG331296.
HOGENOMiHOG000139693.
HOVERGENiHBG050731.
InParanoidiO35923.
PhylomeDBiO35923.

Family and domain databases

Gene3Di2.40.50.140. 4 hits.
InterProiIPR015525. BRCA2.
IPR015252. BRCA2_hlx.
IPR015187. BRCA2_OB_1.
IPR015188. BRCA2_OB_3.
IPR002093. BRCA2_repeat.
IPR012340. NA-bd_OB-fold.
IPR015205. Tower.
[Graphical view]
PANTHERiPTHR11289. PTHR11289. 1 hit.
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.
SUPFAMiSSF50249. SSF50249. 4 hits.
SSF81872. SSF81872. 1 hit.
PROSITEiPS50138. BRCA2_REPEAT. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O35923-1 [UniParc]FASTAAdd to Basket

« Hide

MTVEYKRRPT FWEIFKARCS TADLGPISLN WFEELFSEAP PYNTEHPEES     50
EYKPQGHEPQ LFKTPQRNPS YHQFASTPIM FKEQSQTLPL DQSPFKELGN 100
VVANSKRKHH SKKKARKDPV VDVASLPLKA CPSESPCTPR CTQVAPQRRK 150
PVVSGSLFYT PKLEETPKHI SESLGVEVDP DMSWTSSLAT PPTLSSTVLI 200
ARDEEAHRNA FPADSPASLK SYFSNHNESL KKNDRFIPSV SDSENKSQQE 250
AFSQGLEKML GDSSSKINRF RDCLRKPIPN VLEDGETAVD TSGEDSFSLC 300
FPKRRTRNLQ KTRMGKMKKK IFSETRTDGL SEEARGQADD KNSFALEIEP 350
RDSEPLDPSV TNQKPLYSQS GDISSEAGQC SDSIWSQPDP SGLNGTQTRK 400
IPLLHISFHK QSILEDFIDM KKEGTGSITF PHISSLPEPE KMFSEETLVD 450
KEHEGQHLES LEDSISGKQM VSGTSQTACL SPSIRKSIVK MREPLEETLD 500
TVFSDSMTSS AFTEELDASA GGLEIHTACS QREDSLCPSS VDTGSWPTTL 550
TDTSATVKNA GLITTLKNKR RKFIYSVSDD ASHQGKKLQT QRQSELTNLS 600
APFEASAFEV PFPFTNVDSG IPDSSIKRSN LPNDPEEPSL SLTNSFVTAA 650
SKEISYIHAL ISQDLNDKEA ILSEEKPQPY TALEADFLSC LPERSCENDQ 700
KSPKVSDRKE KVLVSACRPS GRLAAAVQLS SISFDSQENP LGSHNVTSTL 750
KLTPSPKTPL SKPVVVSRGK MCKMPEKLQC KSCKDNIELS KNIPLGVNEM 800
CVLSENSETP ELLPPLEYIT EVSSSVKSQF NQNTKIAVVQ KDQKDSTFIS 850
EVTVHMNSEE LFPEKENNFA FQVTNESNKP NIGSTVEFQE EDLSHAKGHS 900
LKNSPMTVDR DLDDEQAGQV LITEDSDSLA VVHDCTKKSR NTIEQHQKGT 950
ADKDFKSNSS LYLKSDGNND YLDKWSEFLD PLMNHKLGGS FRTASNKEIK 1000
LSEDNVKKSK MFFKDIEEQY PTSLDCIDTV STLQLANKKR LSEPHTFDLK 1050
SGTTVSTQCH SQSSVSHEDT HTAPQMLSSK QDFHSSHNLT PSQKAEITEL 1100
STILEESGSQ FEFTQFKNPS HIAQNNTSAV LGNQMAVVRT ASEEWKDVDL 1150
HLPLNPSSVG QIDHNKKFEC LVGVKQSSSH LLEDTCNQNT SCFLPIKEME 1200
FGGFCSALGT KLSVSNEALR KAMKLFSDIE NISEEPSTKV GPRGFSSCAH 1250
HDSVASVFKI KKQNTDKSFD EKSSKCQVTV QNNKEMTTCI LVDENPENYV 1300
KNIKQDNNYT GSQRNAYKLE NSDVSKSSTS GTVYINKGDS DLPFAAEKGN 1350
KYPESCTQYV REENAQIKES VSDLTCLEVM KAEETCHMKS SDKEQLPSDK 1400
MEQNMKEFNI SFQTASGKNI RVSKESLNKS VNILDQETED LTVTSDSLNS 1450
KILCGINKDK MHISCHKKSI NIKKVFEEHF PIGTVSQLPA LQQYPEYEIE 1500
SIKEPTLLSF HTASGKKVKI MQESLDKVKN LFDETQYVRK TTNFGHQESK 1550
PLKDREDYKE RLTLAYEKIE VTASKCEEMQ NFVSKQTEML PQQNDHMYRQ 1600
TENLTSNGSS PKVHGNIENK IEKNPRICCI CQSSYFVTED SALACYTGDS 1650
RKTCVGESSL SKGKKWLREQ SDKLGTRNTI EIQCVKEHTE DFAGNALYEH 1700
SLVIIRTEID TSHVSENQAS TLFSDPNVCH SYLSHSSFCH HDDMHNDSGY 1750
FLKDKIDSDV QPDMKNTEGN AIFPKISATK EIKLHPQTVN EECVQKLETN 1800
ASPYANKNIA IDSAMLDLRN CKVGSPVFIT THSQETVRMK EIFTDNCSKI 1850
VEQNRESKPD TCQTSCHKAL DNSEDFICPS SSGDVCINSP MAIFYPQSEQ 1900
ILQHNQSVSG LKKAATPPVS LETWDTCKSI RGSPQEVHPS RTYGFFSTAS 1950
GKAVQVSDAS LEKARQVFSE IDGDAKQLAS MVSLEGNEKS HHSVKRESSV 2000
VHNTHGVLSL RKTLPGNVSS FVFSGFSTAG GKLVTVSESA LHKVKGMLEE 2050
FDLIRTEHTL QHSPTPEDVS KIPPQPCLES RTPEYSVSSK LQKTYNDKSR 2100
SPSNYKESGS SGNTQSLEVS PQLSQMERKQ ETQSVLGTKV SQRKTNILEK 2150
KQNLPQNIKI ESNKMETFSD VSMKTNVGEY YSKEPENYFE TEAVEIAKAF 2200
MEDDELTDSE QTHAKCSLFA CPQNEALLNS RTRKRGGMAG VAVGQPPIKR 2250
SLLNEFDRII ESKGKSLTPS KSTPDGTIKD RRLFTHHMSL EPVTCGPFCS 2300
SKERQETQSP HVTSPAQGLQ SKEHPSRHSA VGKSSSNPTV SALRSERTRH 2350
SVSDKSTKVF VPPFKVKSRF HRDEHFDSKN VNLEGKNQKS ADGVSEDGND 2400
SDFPQFNKDL MSSLQNARDL QDIRIKNKER HHLCPQPGSL YLTKSSTLPR 2450
ISLQAAVGDS VPSACSPKQL YMYGVSKACI SVNSKNAEYF QFAIEDHFGK 2500
EALCAGKGFR LADGGWLIPS DDGKAGKEEF YRALCDTPGV DPKLISSVWV 2550
SNHYRWIVWK LAAMEFAFPK EFANRCLNPE RVLLQLKYRY DVEIDNSSRS 2600
ALKKILERDD TAAKTLVLCV SDIISLSTNV SETSGSKASS EDSNKVDTIE 2650
LTDGWYAVKA QLDPPLLALV KSGRLTVGQK IITQGAELVG SPDACAPLEA 2700
PDSLRLKISA NSTRPARWHS KLGFFHDPRP FPLPLSSLFS DGGNVGCVDV 2750
IVQRVYPLQW VEKTVSGSYI FRNEREEEKE ALRFAEAQQK KLEALFTKVH 2800
TELKEHEEDI AQRRVLSRAL TRQQVHALQD GAELYAAVQD ASDPEHLETC 2850
FSEEQLRALN NYRQMLSDKK QARIQSEFRK ALEAAEKEEG LSRDVSTVWK 2900
LRVTSYKKRE KSALLSIWRP SSDLPSLLTE GQRYRIYHLS VSKSKNKFEW 2950
PSIQLTATKR TQYQQLPVSS ETLLQLYQPR ELLPFSKLSD PAFQPPCSEV 3000
DVVGVVVSVV KPIGLAPLVY LSDECLHLLV VKFGIDLNED IKPRVLIAAS 3050
NLQWRPESTS RVPTLFAGNF SVFSASPKEA HFQERVTNMK HAIENIDTFY 3100
KEAEKKLIQV LKGDSPKWST PNKDPTREPY PASTCSASDL ASGGQLPRSS 3150
PTDQQSYRSP LSCCTPTGKS TPLAHSAWMA AKSCSGENEI EDPKTCRKKR 3200
ALDLLSRLPL PPPLSPVCTF VSPAAQKAFQ PPRSCGTKYP TPLKKEGPSS 3250
PWSRAPFQKA SGVSLLDCDS VADEELALLS TQALVPHSVG GSEQVFPSDS 3300
TRTEGPSAST EARPANRSKR ESLRDCRDDS DGKLAAETVP DYS 3343
Length:3,343
Mass (Da):372,216
Last modified:January 1, 1998 - v1
Checksum:i653DB110D2302A8D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U89653 mRNA. Translation: AAB71378.1.
PIRiT42207.
UniGeneiRn.103225.

Genome annotation databases

UCSCiRGD:2219. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U89653 mRNA. Translation: AAB71378.1 .
PIRi T42207.
UniGenei Rn.103225.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1IYJ X-ray 3.40 B/D 2335-3151 [» ]
ProteinModelPortali O35923.
SMRi O35923. Positions 1505-1536, 2403-3112.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PaxDbi O35923.
PRIDEi O35923.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

UCSCi RGD:2219. rat.

Organism-specific databases

RGDi 2219. Brca2.

Phylogenomic databases

eggNOGi NOG331296.
HOGENOMi HOG000139693.
HOVERGENi HBG050731.
InParanoidi O35923.
PhylomeDBi O35923.

Miscellaneous databases

EvolutionaryTracei O35923.
NextBioi 21679528.
PROi O35923.

Gene expression databases

Genevestigatori O35923.

Family and domain databases

Gene3Di 2.40.50.140. 4 hits.
InterProi IPR015525. BRCA2.
IPR015252. BRCA2_hlx.
IPR015187. BRCA2_OB_1.
IPR015188. BRCA2_OB_3.
IPR002093. BRCA2_repeat.
IPR012340. NA-bd_OB-fold.
IPR015205. Tower.
[Graphical view ]
PANTHERi PTHR11289. PTHR11289. 1 hit.
Pfami PF09169. 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 ]
PIRSFi PIRSF002397. BRCA2. 1 hit.
SUPFAMi SSF50249. SSF50249. 4 hits.
SSF81872. SSF81872. 1 hit.
PROSITEi PS50138. BRCA2_REPEAT. 6 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Characterization of the rat and mouse homologues of the BRCA2 breast cancer susceptibility gene."
    McAllister K.A., Haugen-Strano A., Hagevik S., Brownlee H.A., Collins N.K., Futreal P.A., Bennett L.M., Wiseman R.W.
    Cancer Res. 57:3121-3125(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Testis.
  2. "BRCA2 function in DNA binding and recombination from a BRCA2-DSS1-ssDNA structure."
    Yang H., Jeffrey P.D., Miller J., Kinnucan E., Sun Y., Thoma N.H., Zheng N., Chen P.L., Lee W.H., Pavletich N.P.
    Science 297:1837-1848(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 2335-3151 IN COMPLEX WITH DSS1.

Entry informationi

Entry nameiBRCA2_RAT
AccessioniPrimary (citable) accession number: O35923
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: January 1, 1998
Last modified: September 3, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi