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Q92878

- RAD50_HUMAN

UniProt

Q92878 - RAD50_HUMAN

Protein

DNA repair protein RAD50

Gene

RAD50

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      Previous versions | rss
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    Functioni

    Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis. The complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11A. RAD50 may be required to bind DNA ends and hold them in close proximity. This could facilitate searches for short or long regions of sequence homology in the recombining DNA templates, and may also stimulate the activity of DNA ligases and/or restrict the nuclease activity of MRE11A to prevent nucleolytic degradation past a given point. The complex may also be required for DNA damage signaling via activation of the ATM kinase. In telomeres the MRN complex may modulate t-loop formation.6 Publications

    Cofactori

    Binds 1 zinc ion per homodimer.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi681 – 6811ZincPROSITE-ProRule annotation
    Metal bindingi684 – 6841ZincPROSITE-ProRule annotation

    Regions

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

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. DNA binding Source: BHF-UCL
    3. nuclease activity Source: InterPro
    4. protein binding Source: UniProtKB
    5. protein binding, bridging Source: UniProtKB
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: MGI
    2. DNA catabolic process, endonucleolytic Source: GOC
    3. DNA duplex unwinding Source: BHF-UCL
    4. DNA recombination Source: UniProtKB
    5. DNA repair Source: UniProtKB
    6. double-strand break repair Source: UniProtKB
    7. double-strand break repair via homologous recombination Source: Reactome
    8. nucleic acid phosphodiester bond hydrolysis Source: GOC
    9. positive regulation of kinase activity Source: BHF-UCL
    10. positive regulation of protein autophosphorylation Source: BHF-UCL
    11. reciprocal meiotic recombination Source: ProtInc
    12. regulation of mitotic recombination Source: UniProtKB
    13. telomere maintenance Source: BHF-UCL
    14. telomere maintenance via telomerase Source: UniProtKB

    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

    ReactomeiREACT_169185. DNA Damage/Telomere Stress Induced Senescence.
    REACT_27271. Meiotic recombination.
    REACT_486. Assembly of the RAD50-MRE11-NBS1 complex at DNA double-strand breaks.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA repair protein RAD50 (EC:3.6.-.-)
    Short name:
    hRAD50
    Gene namesi
    Name:RAD50
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:9816. RAD50.

    Subcellular locationi

    Nucleus. Chromosometelomere
    Note: Localizes to discrete nuclear foci after treatment with genotoxic agents.

    GO - Cellular componenti

    1. membrane Source: UniProtKB
    2. Mre11 complex Source: UniProtKB
    3. nuclear chromosome, telomeric region Source: BHF-UCL
    4. nucleoplasm Source: Reactome
    5. nucleus Source: HPA
    6. pronucleus Source: Ensembl
    7. site of double-strand break Source: UniProtKB

    Keywords - Cellular componenti

    Chromosome, Nucleus, Telomere

    Pathology & Biotechi

    Involvement in diseasei

    Nijmegen breakage syndrome-like disorder (NBSLD) [MIM:613078]: A disorder similar to Nijmegen breakage syndrome and characterized by chromosomal instability, radiation sensitivity, microcephaly, growth retardation, short stature and bird-like face. Immunodeficiency is absent.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi42 – 421K → N: Abolishes ability to degrade ATP. 1 Publication
    Mutagenesisi1231 – 12311D → A: Abolishes ability to degrade ATP. 1 Publication

    Organism-specific databases

    MIMi613078. phenotype.
    Orphaneti145. Hereditary breast and ovarian cancer syndrome.
    240760. Nijmegen breakage syndrome-like disorder.
    PharmGKBiPA34175.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13121312DNA repair protein RAD50PRO_0000138641Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei635 – 6351Phosphoserine3 Publications
    Modified residuei690 – 6901Phosphothreonine3 Publications
    Modified residuei959 – 9591N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ92878.
    PaxDbiQ92878.
    PRIDEiQ92878.

    PTM databases

    PhosphoSiteiQ92878.

    Expressioni

    Tissue specificityi

    Expressed at very low level in most tissues, except in testis where it is expressed at higher level. Expressed in fibroblasts.1 Publication

    Gene expression databases

    ArrayExpressiQ92878.
    BgeeiQ92878.
    CleanExiHS_RAD50.
    GenevestigatoriQ92878.

    Organism-specific databases

    HPAiCAB022103.
    CAB024979.
    HPA052291.

    Interactioni

    Subunit structurei

    Component of the MRN complex composed of two heterodimers RAD50/MRE11A associated with a single NBN. Component of the BASC complex, at least composed of BRCA1, MSH2, MSH6, MLH1, ATM, BLM, RAD50, MRE11A and NBN. Found in a complex with TERF2. Interacts with RINT1. Interacts with BRCA1 via its N-terminal domain. Interacts with DCLRE1C/Artemis.10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ATRXP461005EBI-495494,EBI-396461

    Protein-protein interaction databases

    BioGridi115417. 60 interactions.
    DIPiDIP-33606N.
    IntActiQ92878. 26 interactions.
    MINTiMINT-100363.
    STRINGi9606.ENSP00000265335.

    Structurei

    3D structure databases

    ProteinModelPortaliQ92878.
    SMRiQ92878. Positions 28-67, 1201-1291.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini635 – 734100Zinc-hookPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili228 – 359132Sequence AnalysisAdd
    BLAST
    Coiled coili401 – 598198Sequence AnalysisAdd
    BLAST
    Coiled coili635 – 67339Sequence AnalysisAdd
    BLAST
    Coiled coili706 – 73429Sequence AnalysisAdd
    BLAST
    Coiled coili789 – 1079291Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1201 – 123838Ala/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

    eggNOGiCOG0419.
    HOGENOMiHOG000090195.
    HOVERGENiHBG058033.
    InParanoidiQ92878.
    KOiK10866.
    OMAiSLGSYVH.
    OrthoDBiEOG725DGM.
    PhylomeDBiQ92878.
    TreeFamiTF101217.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR027417. P-loop_NTPase.
    IPR004584. Rad50_eukaryotes.
    IPR007517. Rad50_Zn_hook.
    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]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q92878-1) [UniParc]FASTAAdd to Basket

    Also known as: RAD50-1, RAD50-2

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSRIEKMSIL GVRSFGIEDK DKQIITFFSP LTILVGPNGA GKTTIIECLK     50
    YICTGDFPPG TKGNTFVHDP KVAQETDVRA QIRLQFRDVN GELIAVQRSM 100
    VCTQKSKKTE FKTLEGVITR TKHGEKVSLS SKCAEIDREM ISSLGVSKAV 150
    LNNVIFCHQE DSNWPLSEGK ALKQKFDEIF SATRYIKALE TLRQVRQTQG 200
    QKVKEYQMEL KYLKQYKEKA CEIRDQITSK EAQLTSSKEI VKSYENELDP 250
    LKNRLKEIEH NLSKIMKLDN EIKALDSRKK QMEKDNSELE EKMEKVFQGT 300
    DEQLNDLYHN HQRTVREKER KLVDCHRELE KLNKESRLLN QEKSELLVEQ 350
    GRLQLQADRH QEHIRARDSL IQSLATQLEL DGFERGPFSE RQIKNFHKLV 400
    RERQEGEAKT ANQLMNDFAE KETLKQKQID EIRDKKTGLG RIIELKSEIL 450
    SKKQNELKNV KYELQQLEGS SDRILELDQE LIKAERELSK AEKNSNVETL 500
    KMEVISLQNE KADLDRTLRK LDQEMEQLNH HTTTRTQMEM LTKDKADKDE 550
    QIRKIKSRHS DELTSLLGYF PNKKQLEDWL HSKSKEINQT RDRLAKLNKE 600
    LASSEQNKNH INNELKRKEE QLSSYEDKLF DVCGSQDFES DLDRLKEEIE 650
    KSSKQRAMLA GATAVYSQFI TQLTDENQSC CPVCQRVFQT EAELQEVISD 700
    LQSKLRLAPD KLKSTESELK KKEKRRDEML GLVPMRQSII DLKEKEIPEL 750
    RNKLQNVNRD IQRLKNDIEE QETLLGTIMP EEESAKVCLT DVTIMERFQM 800
    ELKDVERKIA QQAAKLQGID LDRTVQQVNQ EKQEKQHKLD TVSSKIELNR 850
    KLIQDQQEQI QHLKSTTNEL KSEKLQISTN LQRRQQLEEQ TVELSTEVQS 900
    LYREIKDAKE QVSPLETTLE KFQQEKEELI NKKNTSNKIA QDKLNDIKEK 950
    VKNIHGYMKD IENYIQDGKD DYKKQKETEL NKVIAQLSEC EKHKEKINED 1000
    MRLMRQDIDT QKIQERWLQD NLTLRKRNEE LKEVEEERKQ HLKEMGQMQV 1050
    LQMKSEHQKL EENIDNIKRN HNLALGRQKG YEEEIIHFKK ELREPQFRDA 1100
    EEKYREMMIV MRTTELVNKD LDIYYKTLDQ AIMKFHSMKM EEINKIIRDL 1150
    WRSTYRGQDI EYIEIRSDAD ENVSASDKRR NYNYRVVMLK GDTALDMRGR 1200
    CSAGQKVLAS LIIRLALAET FCLNCGIIAL DEPTTNLDRE NIESLAHALV 1250
    EIIKSRSQQR NFQLLVITHD EDFVELLGRS EYVEKFYRIK KNIDQCSEIV 1300
    KCSVSSLGFN VH 1312
    Length:1,312
    Mass (Da):153,892
    Last modified:February 1, 1997 - v1
    Checksum:i1F208C3817FC41FC
    GO
    Isoform 2 (identifier: Q92878-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-5: MSRIE → MLIFSVRDMFA

    Show »
    Length:1,318
    Mass (Da):154,587
    Checksum:i54B578956FC29852
    GO
    Isoform 3 (identifier: Q92878-3) [UniParc]FASTAAdd to Basket

    Also known as: RAD50-3

    The sequence of this isoform differs from the canonical sequence as follows:
         1-139: Missing.

    Show »
    Length:1,173
    Mass (Da):138,432
    Checksum:iD6734A4E4D898AAE
    GO

    Sequence cautioni

    The sequence AAH62603.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti204 – 2041K → E in CAA99729. 1 PublicationCurated
    Sequence conflicti723 – 7231E → K in AAH62603. (PubMed:15489334)Curated
    Sequence conflicti723 – 7231E → K in AAH73850. (PubMed:15489334)Curated
    Sequence conflicti733 – 7331V → A in CAA99729. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti94 – 941I → L.1 Publication
    Corresponds to variant rs28903085 [ dbSNP | Ensembl ].
    VAR_025526
    Natural varianti127 – 1271V → I.
    Corresponds to variant rs28903086 [ dbSNP | Ensembl ].
    VAR_029168
    Natural varianti191 – 1911T → I.
    Corresponds to variant rs2230017 [ dbSNP | Ensembl ].
    VAR_022085
    Natural varianti193 – 1931R → W.
    Corresponds to variant rs28903087 [ dbSNP | Ensembl ].
    VAR_029169
    Natural varianti224 – 2241R → H.1 Publication
    Corresponds to variant rs28903088 [ dbSNP | Ensembl ].
    VAR_025527
    Natural varianti315 – 3151V → L.
    Corresponds to variant rs28903090 [ dbSNP | Ensembl ].
    VAR_034436
    Natural varianti469 – 4691G → A.
    Corresponds to variant rs55653181 [ dbSNP | Ensembl ].
    VAR_061779
    Natural varianti616 – 6161K → E.1 Publication
    Corresponds to variant rs1047380 [ dbSNP | Ensembl ].
    VAR_020958
    Natural varianti697 – 6971V → A.1 Publication
    Corresponds to variant rs1047382 [ dbSNP | Ensembl ].
    VAR_020959
    Natural varianti842 – 8421V → A.
    Corresponds to variant rs28903093 [ dbSNP | Ensembl ].
    VAR_029170
    Natural varianti964 – 9641Y → H.1 Publication
    Corresponds to variant rs1047386 [ dbSNP | Ensembl ].
    VAR_020960
    Natural varianti973 – 9731K → M.1 Publication
    Corresponds to variant rs1129482 [ dbSNP | Ensembl ].
    VAR_020961
    Natural varianti1038 – 10381R → G.
    Corresponds to variant rs1047387 [ dbSNP | Ensembl ].
    VAR_020962

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 139139Missing in isoform 3. 1 PublicationVSP_012590Add
    BLAST
    Alternative sequencei1 – 55MSRIE → MLIFSVRDMFA in isoform 2. 1 PublicationVSP_012591

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U63139 mRNA. Translation: AAB07119.1.
    AF057299 mRNA. Translation: AAD50325.1.
    AF057300 mRNA. Translation: AAD50326.1.
    Z75311 mRNA. Translation: CAA99729.1.
    AC116366 Genomic DNA. No translation available.
    AC004042 Genomic DNA. No translation available.
    CH471062 Genomic DNA. Translation: EAW62329.1.
    BC062603 mRNA. Translation: AAH62603.1. Sequence problems.
    BC073850 mRNA. Translation: AAH73850.1.
    BC136436 mRNA. Translation: AAI36437.1.
    CCDSiCCDS34233.1. [Q92878-1]
    RefSeqiNP_005723.2. NM_005732.3. [Q92878-1]
    UniGeneiHs.633509.

    Genome annotation databases

    EnsembliENST00000378823; ENSP00000368100; ENSG00000113522. [Q92878-3]
    GeneIDi10111.
    KEGGihsa:10111.
    UCSCiuc003kxh.3. human. [Q92878-1]

    Polymorphism databases

    DMDMi60392986.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U63139 mRNA. Translation: AAB07119.1 .
    AF057299 mRNA. Translation: AAD50325.1 .
    AF057300 mRNA. Translation: AAD50326.1 .
    Z75311 mRNA. Translation: CAA99729.1 .
    AC116366 Genomic DNA. No translation available.
    AC004042 Genomic DNA. No translation available.
    CH471062 Genomic DNA. Translation: EAW62329.1 .
    BC062603 mRNA. Translation: AAH62603.1 . Sequence problems.
    BC073850 mRNA. Translation: AAH73850.1 .
    BC136436 mRNA. Translation: AAI36437.1 .
    CCDSi CCDS34233.1. [Q92878-1 ]
    RefSeqi NP_005723.2. NM_005732.3. [Q92878-1 ]
    UniGenei Hs.633509.

    3D structure databases

    ProteinModelPortali Q92878.
    SMRi Q92878. Positions 28-67, 1201-1291.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115417. 60 interactions.
    DIPi DIP-33606N.
    IntActi Q92878. 26 interactions.
    MINTi MINT-100363.
    STRINGi 9606.ENSP00000265335.

    PTM databases

    PhosphoSitei Q92878.

    Polymorphism databases

    DMDMi 60392986.

    Proteomic databases

    MaxQBi Q92878.
    PaxDbi Q92878.
    PRIDEi Q92878.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000378823 ; ENSP00000368100 ; ENSG00000113522 . [Q92878-3 ]
    GeneIDi 10111.
    KEGGi hsa:10111.
    UCSCi uc003kxh.3. human. [Q92878-1 ]

    Organism-specific databases

    CTDi 10111.
    GeneCardsi GC05P131920.
    HGNCi HGNC:9816. RAD50.
    HPAi CAB022103.
    CAB024979.
    HPA052291.
    MIMi 604040. gene.
    613078. phenotype.
    neXtProti NX_Q92878.
    Orphaneti 145. Hereditary breast and ovarian cancer syndrome.
    240760. Nijmegen breakage syndrome-like disorder.
    PharmGKBi PA34175.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0419.
    HOGENOMi HOG000090195.
    HOVERGENi HBG058033.
    InParanoidi Q92878.
    KOi K10866.
    OMAi SLGSYVH.
    OrthoDBi EOG725DGM.
    PhylomeDBi Q92878.
    TreeFami TF101217.

    Enzyme and pathway databases

    Reactomei REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
    REACT_27271. Meiotic recombination.
    REACT_486. Assembly of the RAD50-MRE11-NBS1 complex at DNA double-strand breaks.

    Miscellaneous databases

    ChiTaRSi RAD50. human.
    GeneWikii Rad50.
    GenomeRNAii 10111.
    NextBioi 38249.
    PROi Q92878.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92878.
    Bgeei Q92878.
    CleanExi HS_RAD50.
    Genevestigatori Q92878.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR027417. P-loop_NTPase.
    IPR004584. Rad50_eukaryotes.
    IPR007517. Rad50_Zn_hook.
    IPR013134. Zn_hook_Rad50.
    [Graphical view ]
    PANTHERi PTHR18867. PTHR18867. 1 hit.
    Pfami PF04423. Rad50_zn_hook. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 3 hits.
    TIGRFAMsi TIGR00606. rad50. 1 hit.
    PROSITEi PS51131. ZN_HOOK. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human Rad50 is physically associated with human Mre11: identification of a conserved multiprotein complex implicated in recombinational DNA repair."
      Dolganov G.M., Maser R.S., Novikov A., Tosto L., Chong S., Bressan D.A., Petrini J.H.J.
      Mol. Cell. Biol. 16:4832-4841(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH MRE11A, TISSUE SPECIFICITY.
    2. "Molecular cloning and characterization of splice variants of human RAD50 gene."
      Kim K.K., Shin B.A., Seo K.H., Kim P.N., Koh J.T., Kim J.H., Park B.R.
      Gene 235:59-67(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
    3. Offenberg H.H.
      Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS GLU-616; ALA-697; HIS-964 AND MET-973.
      Tissue: Testis.
    4. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Lymph.
    7. "The hMre11/hRad50 protein complex and Nijmegen breakage syndrome: linkage of double-strand break repair to the cellular DNA damage response."
      Carney J.P., Maser R.S., Olivares H., Davis E.M., Le Beau M., Yates J.R. III, Hays L., Morgan W.F., Petrini J.H.J.
      Cell 93:477-486(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DSB REPAIR, IDENTIFICATION IN THE MRN COMPLEX WITH MRE11A AND NBN.
    8. "Nuclease activities in a complex of human recombination and DNA repair factors Rad50, Mre11, and p95."
      Trujillo K.M., Yuan S.-S.F., Lee E.Y.-H.P., Sung P.
      J. Biol. Chem. 273:21447-21450(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DSB REPAIR, IDENTIFICATION IN THE MRN COMPLEX WITH MRE11A AND NBN.
    9. "The 3' to 5' exonuclease activity of Mre 11 facilitates repair of DNA double-strand breaks."
      Paull T.T., Gellert M.
      Mol. Cell 1:969-979(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ATP-BINDING, MUTAGENESIS OF LYS-42 AND ASP-1231.
    10. "Association of BRCA1 with the hRad50-hMre11-p95 complex and the DNA damage response."
      Zhong Q., Chen C.-F., Li S., Chen Y., Wang C.-C., Xiao J., Chen P.-L., Sharp Z.D., Lee W.-H.
      Science 285:747-750(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH BRCA1.
    11. "BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures."
      Wang Y., Cortez D., Yazdi P., Neff N., Elledge S.J., Qin J.
      Genes Dev. 14:927-939(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN THE BASC COMPLEX WITH BRCA1; MSH2; MSH6; MLH1; ATM; BLM; MRE11A AND NBN.
    12. "Functional link between ataxia-telangiectasia and Nijmegen breakage syndrome gene products."
      Zhao S., Weng Y.-C., Yuan S.-S.F., Lin Y.-T., Hsu H.-C., Lin S.-C., Gerbino E., Song M.-H., Zdzienicka M.Z., Gatti R.A., Shay J.W., Ziv Y., Shiloh Y., Lee E.Y.-H.P.
      Nature 405:473-477(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE MRN COMPLEX WITH MRE11A AND NBN.
    13. "Cell-cycle-regulated association of RAD50/MRE11/NBS1 with TRF2 and human telomeres."
      Zhu X.-D., Kuester B., Mann M., Petrini J.H.J., de Lange T.
      Nat. Genet. 25:347-352(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TELOMERES, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE A COMPLEX WITH TERF2.
    14. "RINT-1, a novel Rad50-interacting protein, participates in radiation-induced G2/M checkpoint control."
      Xiao J., Liu C.-C., Chen P.-L., Lee W.-H.
      J. Biol. Chem. 276:6105-6111(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RINT1.
    15. "Human Rad50/Mre11 is a flexible complex that can tether DNA ends."
      de Jager M., van Noort J., van Gent D.C., Dekker C., Kanaar R., Wyman C.
      Mol. Cell 8:1129-1135(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTRAMOLECULAR COILED-COIL DOMAINS.
    16. "Adenovirus oncoproteins inactivate the Mre11-Rad50-NBS1 DNA repair complex."
      Stracker T.H., Carson C.T., Weitzman M.D.
      Nature 418:348-352(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INACTIVATION BY ADENOVIRUS ONCOPROTEINS.
    17. "DNA end-binding specificity of human Rad50/Mre11 is influenced by ATP."
      de Jager M., Wyman C., van Gent D.C., Kanaar R.
      Nucleic Acids Res. 30:4425-4431(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: ATP-BINDING.
    18. "Artemis is a phosphorylation target of ATM and ATR and is involved in the G2/M DNA damage checkpoint response."
      Zhang X., Succi J., Feng Z., Prithivirajsingh S., Story M.D., Legerski R.J.
      Mol. Cell. Biol. 24:9207-9220(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DCLRE1C.
    19. "Direct activation of the ATM protein kinase by the Mre11/Rad50/Nbs1 complex."
      Lee J.-H., Paull T.T.
      Science 304:93-96(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ATM ACTIVATION.
    20. "Ataxia-telangiectasia-mutated dependent phosphorylation of Artemis in response to DNA damage."
      Chen L., Morio T., Minegishi Y., Nakada S., Nagasawa M., Komatsu K., Chessa L., Villa A., Lecis D., Delia D., Mizutani S.
      Cancer Sci. 96:134-141(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DCLRE1C.
    21. "ATM-dependent phosphorylation of ATF2 is required for the DNA damage response."
      Bhoumik A., Takahashi S., Breitweiser W., Shiloh Y., Jones N., Ronai Z.
      Mol. Cell 18:577-587(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    22. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635 AND THR-690, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. Cited for: INVOLVEMENT IN NBSLD.
    25. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-690, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    26. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-959, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635 AND THR-690, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "Mutation screening of Mre11 complex genes: indication of RAD50 involvement in breast and ovarian cancer susceptibility."
      Heikkinen K., Karppinen S.-M., Soini Y., Maekinen M., Winqvist R.
      J. Med. Genet. 40:E131-E131(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS LEU-94 AND HIS-224.

    Entry informationi

    Entry nameiRAD50_HUMAN
    AccessioniPrimary (citable) accession number: Q92878
    Secondary accession number(s): B9EGF5
    , O43254, Q6GMT7, Q6P5X3, Q9UP86
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 2005
    Last sequence update: February 1, 1997
    Last modified: October 1, 2014
    This is version 133 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    In case of infection by adenovirus E4, the MRN complex is inactivated and degraded by viral oncoproteins, thereby preventing concatenation of viral genomes in infected cells.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3