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UniProtKB - Q9W252 (RAD50_DROME)

Entry version 160 (07 Apr 2021)
Sequence version 4 (18 Apr 2012)
Previous versions | rss
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at transcript leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi689ZincPROSITE-ProRule annotation1
Metal bindingi692ZincPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi36 – 43ATPSequence analysis8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase
Biological processCell cycle, DNA damage, DNA repair, Meiosis
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-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

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
DNA repair protein RAD50 (EC:3.6.-.-)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:rad50
ORF Names:CG6339
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiDrosophila melanogaster (Fruit fly)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri7227 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Holometabola › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000803 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2R

Organism-specific databases

Drosophila genome database

More...FlyBasei		FBgn0034728, rad50

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Chromosome, Nucleus, Telomere

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001386451 – 1318DNA repair protein RAD50Add BLAST1318

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q9W252

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		FBgn0034728, Expressed in female gonad and 50 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q9W252, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q9W252, DM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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

By similarity

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		63180, 17 interactors

Protein interaction database and analysis system

More...IntActi		Q9W252, 5 interactors

STRING: functional protein association networks

More...STRINGi		7227.FBpp0290882

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q9W252

Database of comparative protein structure models

More...ModBasei		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini645 – 741Zinc-hookPROSITE-ProRule annotationAdd BLAST97

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili189 – 256Sequence analysisAdd BLAST68
Coiled coili305 – 333Sequence analysisAdd BLAST29
Coiled coili434 – 641Sequence analysisAdd BLAST208
Coiled coili645 – 685Sequence analysisAdd BLAST41
Coiled coili713 – 741Sequence analysisAdd BLAST29
Coiled coili830 – 1101Sequence analysisAdd BLAST272

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1208 – 1245Ala/Asp-rich (DA-box)Add BLAST38

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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 MRE11 homodimer (By similarity).By similarity

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the SMC family. RAD50 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0962, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00390000018781

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9W252

Identification of Orthologs from Complete Genome Data

More...OMAi		CFGVNCG

Database of Orthologous Groups

More...OrthoDBi		179362at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q9W252

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR027417, P-loop_NTPase
IPR038729, Rad50/SbcC_AAA
IPR004584, Rad50_eukaryotes
IPR013134, Zn_hook_RAD50

Pfam protein domain database

More...Pfami		View protein in Pfam
PF13476, AAA_23, 1 hit
PF04423, Rad50_zn_hook, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52540, SSF52540, 3 hits

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00606, rad50, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51131, ZN_HOOK, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i1C84EB7B3F9E3BB9
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0B4K7L0A0A0B4K7L0_DROME
Rad50, isoform E
rad50 6339, Dmel\CG6339, Dmrad50, RAD50, Rad50
1,318Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAK93530 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAO39559 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti880R → K in AAK93530 (PubMed:12537569).Curated1
Sequence conflicti959H → Q in AAK93530 (PubMed:12537569).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti208E → D in strain: NC335, NC362 and NC390. 1 Publication1
Natural varianti219H → V in strain: NC335, NC362 and NC390. 1 Publication1
Natural varianti220V → E in strain: NC335, NC362 and NC390. 1 Publication1
Natural varianti246A → E in strain: MW25. 1 Publication1
Natural varianti249S → M in strain: MW25. 1 Publication1
Natural varianti281E → Q in strain: NC306. 1 Publication1
Natural varianti349K → T in strain: MW9. 1 Publication1
Natural varianti422V → E in strain: NC361 and NC375. 1 Publication1
Natural varianti450V → I in strain: MW6. 1 Publication1
Natural varianti480D → N in strain: MW6. 1 Publication1
Natural varianti490E → Q in strain: MW25, MW27, MW56, MW9, NC303, NC306, NC335, NC336, NC390 and NC399. 1 Publication1
Natural varianti491V → I in strain: NC303, NC306 and NC335. 1 Publication1
Natural varianti580C → S in strain: MW25. 1 Publication1
Natural varianti586M → I in strain: MW25. 1 Publication1
Natural varianti623S → N in strain: NC336, NC358, NC361, NC362 and NC375. 1 Publication1
Natural varianti646T → S in strain: NC357 and NC397. 1 Publication1
Natural varianti657T → A in strain: MW6, NC357, NC358, NC361, NC362, NC375 and NC397. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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.

NCBI Reference Sequences

More...RefSeqi		NP_726199.3, NM_166533.4

Genome annotation databases

Ensembl metazoan genome annotation project

More...EnsemblMetazoai		FBtr0301668; FBpp0290882; FBgn0034728

Database of genes from NCBI RefSeq genomes

More...GeneIDi		37564

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		dme:Dmel_CG6339

UCSC genome browser

More...UCSCi		CG6339-RB, d. melanogaster

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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

SMRiQ9W252
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi63180, 17 interactors
IntActiQ9W252, 5 interactors
STRINGi7227.FBpp0290882

Proteomic databases

PaxDbiQ9W252

Genome annotation databases

EnsemblMetazoaiFBtr0301668; FBpp0290882; FBgn0034728
GeneIDi37564
KEGGidme:Dmel_CG6339
UCSCiCG6339-RB, d. melanogaster

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		10111
FlyBaseiFBgn0034728, rad50

Phylogenomic databases

eggNOGiKOG0962, Eukaryota
GeneTreeiENSGT00390000018781
InParanoidiQ9W252
OMAiCFGVNCG
OrthoDBi179362at2759
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

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		37564, 1 hit in 1 CRISPR screen

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		37564

Protein Ontology

More...PROi		PR:Q9W252

Gene expression databases

BgeeiFBgn0034728, Expressed in female gonad and 50 other tissues
ExpressionAtlasiQ9W252, baseline and differential
GenevisibleiQ9W252, DM

Family and domain databases

InterProiView protein in InterPro
IPR027417, P-loop_NTPase
IPR038729, Rad50/SbcC_AAA
IPR004584, Rad50_eukaryotes
IPR013134, Zn_hook_RAD50
PfamiView protein in Pfam
PF13476, AAA_23, 1 hit
PF04423, Rad50_zn_hook, 1 hit
SUPFAMiSSF52540, SSF52540, 3 hits
TIGRFAMsiTIGR00606, rad50, 1 hit
PROSITEiView protein in PROSITE
PS51131, ZN_HOOK, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRAD50_DROME
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>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
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: April 18, 2012
Last modified: April 7, 2021
This is version 160 of the entry and version 4 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families
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