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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

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. 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

  1. gamma-tubulin binding Source: RefGenome
  2. 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 – 7361PhosphoserineBy similarity
Modified residuei3222 – 32221Phosphoserine; by CDK1 and CDK2By 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).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

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. Interacts with the TREX-2 complex subunits PCID2 and DSS1 (By similarity).By similarity1 Publication

Structurei

Secondary structure

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

3D structure databases

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

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 PALB2By similarityAdd
BLAST
Regioni622 – 982361Interaction with NPM1By similarityAdd
BLAST
Regioni2313 – 2475163Interaction with FANCD2By similarityAdd
BLAST

Sequence similaritiesi

Contains 8 BRCA2 repeats.PROSITE-ProRule annotation

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

        10         20         30         40         50
MTVEYKRRPT FWEIFKARCS TADLGPISLN WFEELFSEAP PYNTEHPEES
60 70 80 90 100
EYKPQGHEPQ LFKTPQRNPS YHQFASTPIM FKEQSQTLPL DQSPFKELGN
110 120 130 140 150
VVANSKRKHH SKKKARKDPV VDVASLPLKA CPSESPCTPR CTQVAPQRRK
160 170 180 190 200
PVVSGSLFYT PKLEETPKHI SESLGVEVDP DMSWTSSLAT PPTLSSTVLI
210 220 230 240 250
ARDEEAHRNA FPADSPASLK SYFSNHNESL KKNDRFIPSV SDSENKSQQE
260 270 280 290 300
AFSQGLEKML GDSSSKINRF RDCLRKPIPN VLEDGETAVD TSGEDSFSLC
310 320 330 340 350
FPKRRTRNLQ KTRMGKMKKK IFSETRTDGL SEEARGQADD KNSFALEIEP
360 370 380 390 400
RDSEPLDPSV TNQKPLYSQS GDISSEAGQC SDSIWSQPDP SGLNGTQTRK
410 420 430 440 450
IPLLHISFHK QSILEDFIDM KKEGTGSITF PHISSLPEPE KMFSEETLVD
460 470 480 490 500
KEHEGQHLES LEDSISGKQM VSGTSQTACL SPSIRKSIVK MREPLEETLD
510 520 530 540 550
TVFSDSMTSS AFTEELDASA GGLEIHTACS QREDSLCPSS VDTGSWPTTL
560 570 580 590 600
TDTSATVKNA GLITTLKNKR RKFIYSVSDD ASHQGKKLQT QRQSELTNLS
610 620 630 640 650
APFEASAFEV PFPFTNVDSG IPDSSIKRSN LPNDPEEPSL SLTNSFVTAA
660 670 680 690 700
SKEISYIHAL ISQDLNDKEA ILSEEKPQPY TALEADFLSC LPERSCENDQ
710 720 730 740 750
KSPKVSDRKE KVLVSACRPS GRLAAAVQLS SISFDSQENP LGSHNVTSTL
760 770 780 790 800
KLTPSPKTPL SKPVVVSRGK MCKMPEKLQC KSCKDNIELS KNIPLGVNEM
810 820 830 840 850
CVLSENSETP ELLPPLEYIT EVSSSVKSQF NQNTKIAVVQ KDQKDSTFIS
860 870 880 890 900
EVTVHMNSEE LFPEKENNFA FQVTNESNKP NIGSTVEFQE EDLSHAKGHS
910 920 930 940 950
LKNSPMTVDR DLDDEQAGQV LITEDSDSLA VVHDCTKKSR NTIEQHQKGT
960 970 980 990 1000
ADKDFKSNSS LYLKSDGNND YLDKWSEFLD PLMNHKLGGS FRTASNKEIK
1010 1020 1030 1040 1050
LSEDNVKKSK MFFKDIEEQY PTSLDCIDTV STLQLANKKR LSEPHTFDLK
1060 1070 1080 1090 1100
SGTTVSTQCH SQSSVSHEDT HTAPQMLSSK QDFHSSHNLT PSQKAEITEL
1110 1120 1130 1140 1150
STILEESGSQ FEFTQFKNPS HIAQNNTSAV LGNQMAVVRT ASEEWKDVDL
1160 1170 1180 1190 1200
HLPLNPSSVG QIDHNKKFEC LVGVKQSSSH LLEDTCNQNT SCFLPIKEME
1210 1220 1230 1240 1250
FGGFCSALGT KLSVSNEALR KAMKLFSDIE NISEEPSTKV GPRGFSSCAH
1260 1270 1280 1290 1300
HDSVASVFKI KKQNTDKSFD EKSSKCQVTV QNNKEMTTCI LVDENPENYV
1310 1320 1330 1340 1350
KNIKQDNNYT GSQRNAYKLE NSDVSKSSTS GTVYINKGDS DLPFAAEKGN
1360 1370 1380 1390 1400
KYPESCTQYV REENAQIKES VSDLTCLEVM KAEETCHMKS SDKEQLPSDK
1410 1420 1430 1440 1450
MEQNMKEFNI SFQTASGKNI RVSKESLNKS VNILDQETED LTVTSDSLNS
1460 1470 1480 1490 1500
KILCGINKDK MHISCHKKSI NIKKVFEEHF PIGTVSQLPA LQQYPEYEIE
1510 1520 1530 1540 1550
SIKEPTLLSF HTASGKKVKI MQESLDKVKN LFDETQYVRK TTNFGHQESK
1560 1570 1580 1590 1600
PLKDREDYKE RLTLAYEKIE VTASKCEEMQ NFVSKQTEML PQQNDHMYRQ
1610 1620 1630 1640 1650
TENLTSNGSS PKVHGNIENK IEKNPRICCI CQSSYFVTED SALACYTGDS
1660 1670 1680 1690 1700
RKTCVGESSL SKGKKWLREQ SDKLGTRNTI EIQCVKEHTE DFAGNALYEH
1710 1720 1730 1740 1750
SLVIIRTEID TSHVSENQAS TLFSDPNVCH SYLSHSSFCH HDDMHNDSGY
1760 1770 1780 1790 1800
FLKDKIDSDV QPDMKNTEGN AIFPKISATK EIKLHPQTVN EECVQKLETN
1810 1820 1830 1840 1850
ASPYANKNIA IDSAMLDLRN CKVGSPVFIT THSQETVRMK EIFTDNCSKI
1860 1870 1880 1890 1900
VEQNRESKPD TCQTSCHKAL DNSEDFICPS SSGDVCINSP MAIFYPQSEQ
1910 1920 1930 1940 1950
ILQHNQSVSG LKKAATPPVS LETWDTCKSI RGSPQEVHPS RTYGFFSTAS
1960 1970 1980 1990 2000
GKAVQVSDAS LEKARQVFSE IDGDAKQLAS MVSLEGNEKS HHSVKRESSV
2010 2020 2030 2040 2050
VHNTHGVLSL RKTLPGNVSS FVFSGFSTAG GKLVTVSESA LHKVKGMLEE
2060 2070 2080 2090 2100
FDLIRTEHTL QHSPTPEDVS KIPPQPCLES RTPEYSVSSK LQKTYNDKSR
2110 2120 2130 2140 2150
SPSNYKESGS SGNTQSLEVS PQLSQMERKQ ETQSVLGTKV SQRKTNILEK
2160 2170 2180 2190 2200
KQNLPQNIKI ESNKMETFSD VSMKTNVGEY YSKEPENYFE TEAVEIAKAF
2210 2220 2230 2240 2250
MEDDELTDSE QTHAKCSLFA CPQNEALLNS RTRKRGGMAG VAVGQPPIKR
2260 2270 2280 2290 2300
SLLNEFDRII ESKGKSLTPS KSTPDGTIKD RRLFTHHMSL EPVTCGPFCS
2310 2320 2330 2340 2350
SKERQETQSP HVTSPAQGLQ SKEHPSRHSA VGKSSSNPTV SALRSERTRH
2360 2370 2380 2390 2400
SVSDKSTKVF VPPFKVKSRF HRDEHFDSKN VNLEGKNQKS ADGVSEDGND
2410 2420 2430 2440 2450
SDFPQFNKDL MSSLQNARDL QDIRIKNKER HHLCPQPGSL YLTKSSTLPR
2460 2470 2480 2490 2500
ISLQAAVGDS VPSACSPKQL YMYGVSKACI SVNSKNAEYF QFAIEDHFGK
2510 2520 2530 2540 2550
EALCAGKGFR LADGGWLIPS DDGKAGKEEF YRALCDTPGV DPKLISSVWV
2560 2570 2580 2590 2600
SNHYRWIVWK LAAMEFAFPK EFANRCLNPE RVLLQLKYRY DVEIDNSSRS
2610 2620 2630 2640 2650
ALKKILERDD TAAKTLVLCV SDIISLSTNV SETSGSKASS EDSNKVDTIE
2660 2670 2680 2690 2700
LTDGWYAVKA QLDPPLLALV KSGRLTVGQK IITQGAELVG SPDACAPLEA
2710 2720 2730 2740 2750
PDSLRLKISA NSTRPARWHS KLGFFHDPRP FPLPLSSLFS DGGNVGCVDV
2760 2770 2780 2790 2800
IVQRVYPLQW VEKTVSGSYI FRNEREEEKE ALRFAEAQQK KLEALFTKVH
2810 2820 2830 2840 2850
TELKEHEEDI AQRRVLSRAL TRQQVHALQD GAELYAAVQD ASDPEHLETC
2860 2870 2880 2890 2900
FSEEQLRALN NYRQMLSDKK QARIQSEFRK ALEAAEKEEG LSRDVSTVWK
2910 2920 2930 2940 2950
LRVTSYKKRE KSALLSIWRP SSDLPSLLTE GQRYRIYHLS VSKSKNKFEW
2960 2970 2980 2990 3000
PSIQLTATKR TQYQQLPVSS ETLLQLYQPR ELLPFSKLSD PAFQPPCSEV
3010 3020 3030 3040 3050
DVVGVVVSVV KPIGLAPLVY LSDECLHLLV VKFGIDLNED IKPRVLIAAS
3060 3070 3080 3090 3100
NLQWRPESTS RVPTLFAGNF SVFSASPKEA HFQERVTNMK HAIENIDTFY
3110 3120 3130 3140 3150
KEAEKKLIQV LKGDSPKWST PNKDPTREPY PASTCSASDL ASGGQLPRSS
3160 3170 3180 3190 3200
PTDQQSYRSP LSCCTPTGKS TPLAHSAWMA AKSCSGENEI EDPKTCRKKR
3210 3220 3230 3240 3250
ALDLLSRLPL PPPLSPVCTF VSPAAQKAFQ PPRSCGTKYP TPLKKEGPSS
3260 3270 3280 3290 3300
PWSRAPFQKA SGVSLLDCDS VADEELALLS TQALVPHSVG GSEQVFPSDS
3310 3320 3330 3340
TRTEGPSAST EARPANRSKR ESLRDCRDDS DGKLAAETVP DYS
Length:3,343
Mass (Da):372,216
Last modified:January 1, 1998 - v1
Checksum:i653DB110D2302A8D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U89653 mRNA. Translation: AAB71378.1.
PIRiT42207.
UniGeneiRn.103225.

Genome annotation databases

UCSCiRGD:2219. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U89653 mRNA. Translation: AAB71378.1 .
PIRi T42207.
UniGenei Rn.103225.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 115 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