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Protein

DNA repair protein RAD50

Gene

rad50

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Essential component of the MRN complex, a complex that possesses single-stranded DNA endonuclease and 3' to 5' exonuclease activities, and plays a central role in double-strand break (DSB) repair. The complex participates in processes such as DNA recombination, DNA repair, genome stability, telomere integrity and meiosis. The MRN complex may protect telomeres by facilitating recruitment of HOAP and HP1 at chromosome ends. In the complex, it mediates the ATP-binding and is probably required to bind DNA ends and hold them in close proximity.2 Publications

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per homodimer.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi689 – 6891ZincPROSITE-ProRule annotation
Metal bindingi692 – 6921ZincPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi36 – 438ATPSequence analysis

GO - Molecular functioni

  • ATPase activity Source: InterPro
  • ATP binding Source: UniProtKB-KW
  • double-stranded DNA binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • cellular response to DNA damage stimulus Source: FlyBase
  • chromosome organization Source: FlyBase
  • double-strand break repair Source: UniProtKB
  • instar larval development Source: FlyBase
  • meiotic cell cycle Source: UniProtKB-KW
  • protein localization Source: UniProtKB
  • telomere capping Source: FlyBase
  • telomere maintenance Source: CACAO
  • telomere maintenance via recombination Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Cell cycle, DNA damage, DNA repair, Meiosis

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiR-DME-2559586. DNA Damage/Telomere Stress Induced Senescence.
R-DME-5685939. HDR through MMEJ (alt-NHEJ).
R-DME-5693548. Sensing of DNA Double Strand Breaks.
R-DME-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-DME-5693607. Processing of DNA double-strand break ends.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA repair protein RAD50 (EC:3.6.-.-)
Gene namesi
Name:rad50
ORF Names:CG6339
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0034728. rad50.

Subcellular locationi

GO - Cellular componenti

  • chromosome, telomeric region Source: UniProtKB-SubCell
  • condensed chromosome Source: UniProtKB
  • Mre11 complex Source: UniProtKB
  • nucleus Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus, Telomere

Pathology & Biotechi

Disruption phenotypei

Death during pupal stage, possibly due to the accumulation of DNA DSBs and the induction of apoptosis in third instar larvae.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13181318DNA repair protein RAD50PRO_0000138645Add
BLAST

Proteomic databases

PaxDbiQ9W252.
PRIDEiQ9W252.

Expressioni

Gene expression databases

BgeeiQ9W252.
ExpressionAtlasiQ9W252. differential.
GenevisibleiQ9W252. DM.

Interactioni

Subunit structurei

Homodimer. Probable component of the MRN complex with mre11 (By similarity).By similarity

Protein-protein interaction databases

BioGridi63180. 6 interactions.
IntActiQ9W252. 5 interactions.
MINTiMINT-832947.
STRINGi7227.FBpp0290882.

Structurei

3D structure databases

ProteinModelPortaliQ9W252.
SMRiQ9W252. Positions 1-68, 1207-1285.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini645 – 74197Zinc-hookPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili189 – 25668Sequence analysisAdd
BLAST
Coiled coili305 – 33329Sequence analysisAdd
BLAST
Coiled coili434 – 641208Sequence analysisAdd
BLAST
Coiled coili645 – 68541Sequence analysisAdd
BLAST
Coiled coili713 – 74129Sequence analysisAdd
BLAST
Coiled coili830 – 1101272Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1208 – 124538Ala/Asp-rich (DA-box)Add
BLAST

Domaini

The zinc-hook, which separates the large intramolecular coiled coil regions, contains 2 Cys residues that coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another RAD50 molecule, thereby forming a V-shaped homodimer. The two heads of the homodimer, which constitute the ATP-binding domain, interact with the MRE11A homodimer (By similarity).By similarity

Sequence similaritiesi

Belongs to the SMC family. RAD50 subfamily.Curated
Contains 1 zinc-hook domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0962. Eukaryota.
COG0419. LUCA.
GeneTreeiENSGT00390000018781.
InParanoidiQ9W252.
OMAiRSMVCTQ.
OrthoDBiEOG725DGM.
PhylomeDBiQ9W252.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR027417. P-loop_NTPase.
IPR004584. Rad50_eukaryotes.
IPR013134. Zn_hook_RAD50.
[Graphical view]
PANTHERiPTHR18867. PTHR18867. 1 hit.
PfamiPF04423. Rad50_zn_hook. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
TIGRFAMsiTIGR00606. rad50. 1 hit.
PROSITEiPS51131. ZN_HOOK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9W252-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSIESLSIQ GIRSFGTYAD DLQSIKFSSP VTLILGENGC GKTTVVECLK
60 70 80 90 100
YALTGECPPG SDRGKSFVHD PKIFGLNEVL AQIKMQVRDR RGAQVSICRT
110 120 130 140 150
MKVSKKRNKM SFETMDSTIN FLTGAGQSKR EKQDSLSGRS VDIDVAISDF
160 170 180 190 200
MGVSKAIINN VLFCHQEDSS WPLDESKKLK EKFDAIFGIT EYNKALDKII
210 220 230 240 250
KLRKEAMEEL KIKEANIKHV AYLKQEMEVK TLNLQKAQRK CDAIKAQCSE
260 270 280 290 300
CEEEMKPIEA RLVEIRNVEF EIGKYQAQKV EMDTKHKNCK DQISTLTLKI
310 320 330 340 350
KKPFRGTLDE LDQEISNFDQ RMLEMRQKRT EVEGDLSQIK RSSVAEQEKL
360 370 380 390 400
GTQDRKHCLA KQRHQSELAC RAQLLKRVKE FCRELHIPID CDLVEQPEKM
410 420 430 440 450
GEVLRDIEAM IITKHCEITE IVEQNEKADR SRQVKIDELR IELTKSEQSV
460 470 480 490 500
TAQEKQRESS KRESETLGVE IKKIETSMQD LKKLEKEINE VNELYESATK
510 520 530 540 550
NIDQQAIKDA IARKKASIAE NQIQFKKLDE QLTFLGSMAK LVAECSLKQK
560 570 580 590 600
ELDKKNQEVH RVRSRHSDHF GKLFKEPITC NYRRSMQVVY EKLRREIQEL
610 620 630 640 650
NEKANTQKLK EQSYEIKRKN LISDISRMEK ELKDSEELIY QKCRSTPYDD
660 670 680 690 700
LLERSKTTIS KLQFDHGALK SSEALYKKYI QKMDEEPSCP LCHHNMTSDE
710 720 730 740 750
ACDLTSELTD EIQKLPDNIT RAEKALKAEQ IKYENLLQLK PTILKVKELK
760 770 780 790 800
DSLPQKKEEL KKVEELLGDS VSEYETLIAL IGEPTHNMEL ANSMMGDMSL
810 820 830 840 850
LDEALKDSAR LTKDLDLQKG QLPASYDSSV SMDDLQAEKS KVSKELETER
860 870 880 890 900
KELESAQNAV QQQMDALNRL REKKNSLKDR QIHLREGLQS LPQLKERLEK
910 920 930 940 950
LNSFLTTVAS EISELKAKIQ PLKLNLRAAI EEKERLKKSE SEKLAQLNSK
960 970 980 990 1000
YNSYKSTDHD IQRLNKEAED YAKLDLRNEI KKLDEIIMAS KDKLRKLEAE
1010 1020 1030 1040 1050
ISLKTDELET IKTECSNQQT VERDLKDNRE LKQLEDKEAK LRESCQVLDK
1060 1070 1080 1090 1100
QLGNLDFHSV SKEKVNLTKQ RDKATVRKGE LLGQLGEIHS QVNKLQREID
1110 1120 1130 1140 1150
EPRFKESLKN FRKANYEIEV TRLCIEDLGQ YRLALEWALI QFHSEKMEMI
1160 1170 1180 1190 1200
NRLIREYWRK IYRGNDIDYI QVKTDEVSSD ASADRRKTYN YRVVQSKNYS
1210 1220 1230 1240 1250
EIEMRGRCSA GQRVLASLII RLALAETFSS NCGVLALDEP TTNLDRANIN
1260 1270 1280 1290 1300
SLCEALNCIV EERQSQSNFM LIIITHDENF VSSLGKITSY HRVFRNEECK
1310
SVIRRVEAGP SKKALIDQ
Length:1,318
Mass (Da):152,160
Last modified:April 18, 2012 - v4
Checksum:i1C84EB7B3F9E3BB9
GO

Sequence cautioni

The sequence AAK93530.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAO39559.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti880 – 8801R → K in AAK93530 (PubMed:12537569).Curated
Sequence conflicti959 – 9591H → Q in AAK93530 (PubMed:12537569).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti208 – 2081E → D in strain: NC335, NC362 and NC390. 1 Publication
Natural varianti219 – 2191H → V in strain: NC335, NC362 and NC390. 1 Publication
Natural varianti220 – 2201V → E in strain: NC335, NC362 and NC390. 1 Publication
Natural varianti246 – 2461A → E in strain: MW25. 1 Publication
Natural varianti249 – 2491S → M in strain: MW25. 1 Publication
Natural varianti281 – 2811E → Q in strain: NC306. 1 Publication
Natural varianti349 – 3491K → T in strain: MW9. 1 Publication
Natural varianti422 – 4221V → E in strain: NC361 and NC375. 1 Publication
Natural varianti450 – 4501V → I in strain: MW6. 1 Publication
Natural varianti480 – 4801D → N in strain: MW6. 1 Publication
Natural varianti490 – 4901E → Q in strain: MW25, MW27, MW56, MW9, NC303, NC306, NC335, NC336, NC390 and NC399. 1 Publication
Natural varianti491 – 4911V → I in strain: NC303, NC306 and NC335. 1 Publication
Natural varianti580 – 5801C → S in strain: MW25. 1 Publication
Natural varianti586 – 5861M → I in strain: MW25. 1 Publication
Natural varianti623 – 6231S → N in strain: NC336, NC358, NC361, NC362 and NC375. 1 Publication
Natural varianti646 – 6461T → S in strain: NC357 and NC397. 1 Publication
Natural varianti657 – 6571T → A in strain: MW6, NC357, NC358, NC361, NC362, NC375 and NC397. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF46847.3.
BT003555 mRNA. Translation: AAO39559.1. Different initiation.
FJ219324 Genomic DNA. Translation: ACI97309.1.
FJ219329 Genomic DNA. Translation: ACI97314.1.
FJ219330 Genomic DNA. Translation: ACI97315.1.
FJ219331 Genomic DNA. Translation: ACI97316.1.
FJ219332 Genomic DNA. Translation: ACI97317.1.
FJ219333 Genomic DNA. Translation: ACI97318.1.
FJ219334 Genomic DNA. Translation: ACI97319.1.
FJ219335 Genomic DNA. Translation: ACI97320.1.
FJ219336 Genomic DNA. Translation: ACI97321.1.
FJ219337 Genomic DNA. Translation: ACI97322.1.
FJ219338 Genomic DNA. Translation: ACI97323.1.
FJ219339 Genomic DNA. Translation: ACI97324.1.
FJ219340 Genomic DNA. Translation: ACI97325.1.
FJ219341 Genomic DNA. Translation: ACI97326.1.
FJ219342 Genomic DNA. Translation: ACI97327.1.
FJ219343 Genomic DNA. Translation: ACI97328.1.
FJ219344 Genomic DNA. Translation: ACI97329.1.
FJ219345 Genomic DNA. Translation: ACI97330.1.
FJ219346 Genomic DNA. Translation: ACI97331.1.
FJ219347 Genomic DNA. Translation: ACI97332.1.
FJ219348 Genomic DNA. Translation: ACI97333.1.
FJ219349 Genomic DNA. Translation: ACI97334.1.
FJ219350 Genomic DNA. Translation: ACI97335.1.
AY052106 mRNA. Translation: AAK93530.1. Different initiation.
RefSeqiNP_726199.3. NM_166533.4.

Genome annotation databases

EnsemblMetazoaiFBtr0301668; FBpp0290882; FBgn0034728.
GeneIDi37564.
UCSCiCG6339-RB. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF46847.3.
BT003555 mRNA. Translation: AAO39559.1. Different initiation.
FJ219324 Genomic DNA. Translation: ACI97309.1.
FJ219329 Genomic DNA. Translation: ACI97314.1.
FJ219330 Genomic DNA. Translation: ACI97315.1.
FJ219331 Genomic DNA. Translation: ACI97316.1.
FJ219332 Genomic DNA. Translation: ACI97317.1.
FJ219333 Genomic DNA. Translation: ACI97318.1.
FJ219334 Genomic DNA. Translation: ACI97319.1.
FJ219335 Genomic DNA. Translation: ACI97320.1.
FJ219336 Genomic DNA. Translation: ACI97321.1.
FJ219337 Genomic DNA. Translation: ACI97322.1.
FJ219338 Genomic DNA. Translation: ACI97323.1.
FJ219339 Genomic DNA. Translation: ACI97324.1.
FJ219340 Genomic DNA. Translation: ACI97325.1.
FJ219341 Genomic DNA. Translation: ACI97326.1.
FJ219342 Genomic DNA. Translation: ACI97327.1.
FJ219343 Genomic DNA. Translation: ACI97328.1.
FJ219344 Genomic DNA. Translation: ACI97329.1.
FJ219345 Genomic DNA. Translation: ACI97330.1.
FJ219346 Genomic DNA. Translation: ACI97331.1.
FJ219347 Genomic DNA. Translation: ACI97332.1.
FJ219348 Genomic DNA. Translation: ACI97333.1.
FJ219349 Genomic DNA. Translation: ACI97334.1.
FJ219350 Genomic DNA. Translation: ACI97335.1.
AY052106 mRNA. Translation: AAK93530.1. Different initiation.
RefSeqiNP_726199.3. NM_166533.4.

3D structure databases

ProteinModelPortaliQ9W252.
SMRiQ9W252. Positions 1-68, 1207-1285.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi63180. 6 interactions.
IntActiQ9W252. 5 interactions.
MINTiMINT-832947.
STRINGi7227.FBpp0290882.

Proteomic databases

PaxDbiQ9W252.
PRIDEiQ9W252.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0301668; FBpp0290882; FBgn0034728.
GeneIDi37564.
UCSCiCG6339-RB. d. melanogaster.

Organism-specific databases

CTDi10111.
FlyBaseiFBgn0034728. rad50.

Phylogenomic databases

eggNOGiKOG0962. Eukaryota.
COG0419. LUCA.
GeneTreeiENSGT00390000018781.
InParanoidiQ9W252.
OMAiRSMVCTQ.
OrthoDBiEOG725DGM.
PhylomeDBiQ9W252.

Enzyme and pathway databases

ReactomeiR-DME-2559586. DNA Damage/Telomere Stress Induced Senescence.
R-DME-5685939. HDR through MMEJ (alt-NHEJ).
R-DME-5693548. Sensing of DNA Double Strand Breaks.
R-DME-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-DME-5693607. Processing of DNA double-strand break ends.

Miscellaneous databases

GenomeRNAii37564.
NextBioi804309.
PROiQ9W252.

Gene expression databases

BgeeiQ9W252.
ExpressionAtlasiQ9W252. differential.
GenevisibleiQ9W252. DM.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR027417. P-loop_NTPase.
IPR004584. Rad50_eukaryotes.
IPR013134. Zn_hook_RAD50.
[Graphical view]
PANTHERiPTHR18867. PTHR18867. 1 hit.
PfamiPF04423. Rad50_zn_hook. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
TIGRFAMsiTIGR00606. rad50. 1 hit.
PROSITEiPS51131. ZN_HOOK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Larva and Pupae.
  4. "Molecular population genetics and evolution of Drosophila meiosis genes."
    Anderson J.A., Gilliland W.D., Langley C.H.
    Genetics 181:177-185(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-657, VARIANTS ASP-208; VAL-219; GLU-220; GLU-246; MET-249; GLN-281; THR-349; GLU-422; ILE-450; ASN-480; GLN-490; ILE-491; SER-580; ILE-586; ASN-623; SER-646 AND ALA-657.
    Strain: MW11, MW25, MW27, MW56, MW6, MW9, NC301, NC303, NC304, NC306, NC322, NC335, NC336, NC350, NC357, NC358, NC359, NC361, NC362, NC375, NC390, NC397 and NC399.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 500-1318.
    Strain: Berkeley.
    Tissue: Embryo.
  6. "The Drosophila Mre11/Rad50 complex is required to prevent both telomeric fusion and chromosome breakage."
    Ciapponi L., Cenci G., Ducau J., Flores C., Johnson-Schlitz D., Gorski M.M., Engels W.R., Gatti M.
    Curr. Biol. 14:1360-1366(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  7. "Disruption of Drosophila Rad50 causes pupal lethality, the accumulation of DNA double-strand breaks and the induction of apoptosis in third instar larvae."
    Gorski M.M., Romeijn R.J., Eeken J.C.J., de Jong A.W.M., van Veen B.L., Szuhai K., Mullenders L.H., Ferro W., Pastink A.
    DNA Repair 3:603-615(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiRAD50_DROME
AccessioniPrimary (citable) accession number: Q9W252
Secondary accession number(s): B6UXS6
, B6UXT1, B6UXT2, B6UXT3, B6UXT4, B6UXT5, B6UXT6, B6UXT7, B6UXT8, B6UXT9, B6UXU1, B6UXU2, B6UXU3, B6UXU4, B6UXU5, B6UXU6, B6UXU7, B6UXU8, B6UXU9, B6UXV0, B6UXV1, B6UXV2, Q86NZ9, Q960E0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: April 18, 2012
Last modified: May 11, 2016
This is version 124 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. 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.