Details for: RAD50

Gene ID: 10111

Symbol: RAD50

Ensembl ID: ENSG00000113522

Description: RAD50 double strand break repair protein

Associated with

Other Information

Genular Protein ID: 231470592

Symbol: RAD50_HUMAN

Name: DNA repair protein RAD50

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 8756642

Title: Human Rad50 is physically associated with human Mre11: identification of a conserved multiprotein complex implicated in recombinational DNA repair.

PubMed ID: 8756642

DOI: 10.1128/mcb.16.9.4832

PubMed ID: 10415333

Title: Molecular cloning and characterization of splice variants of human RAD50 gene.

PubMed ID: 10415333

DOI: 10.1016/s0378-1119(99)00215-2

PubMed ID: 15372022

Title: The DNA sequence and comparative analysis of human chromosome 5.

PubMed ID: 15372022

DOI: 10.1038/nature02919

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 9590181

Title: The hMre11/hRad50 protein complex and Nijmegen breakage syndrome: linkage of double-strand break repair to the cellular DNA damage response.

PubMed ID: 9590181

DOI: 10.1016/s0092-8674(00)81175-7

PubMed ID: 9705271

Title: Nuclease activities in a complex of human recombination and DNA repair factors Rad50, Mre11, and p95.

PubMed ID: 9705271

DOI: 10.1074/jbc.273.34.21447

PubMed ID: 9651580

Title: The 3' to 5' exonuclease activity of Mre 11 facilitates repair of DNA double-strand breaks.

PubMed ID: 9651580

DOI: 10.1016/s1097-2765(00)80097-0

PubMed ID: 10426999

Title: Association of BRCA1 with the hRad50-hMre11-p95 complex and the DNA damage response.

PubMed ID: 10426999

DOI: 10.1126/science.285.5428.747

PubMed ID: 10783165

Title: BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures.

PubMed ID: 10783165

PubMed ID: 10839544

Title: Functional link between ataxia-telangiectasia and Nijmegen breakage syndrome gene products.

PubMed ID: 10839544

DOI: 10.1038/35013083

PubMed ID: 10888888

Title: Cell-cycle-regulated association of RAD50/MRE11/NBS1 with TRF2 and human telomeres.

PubMed ID: 10888888

DOI: 10.1038/77139

PubMed ID: 11096100

Title: RINT-1, a novel Rad50-interacting protein, participates in radiation-induced G2/M checkpoint control.

PubMed ID: 11096100

DOI: 10.1074/jbc.m008893200

PubMed ID: 11741547

Title: Human Rad50/Mre11 is a flexible complex that can tether DNA ends.

PubMed ID: 11741547

DOI: 10.1016/s1097-2765(01)00381-1

PubMed ID: 12124628

Title: Adenovirus oncoproteins inactivate the Mre11-Rad50-NBS1 DNA repair complex.

PubMed ID: 12124628

DOI: 10.1038/nature00863

PubMed ID: 12384589

Title: DNA end-binding specificity of human Rad50/Mre11 is influenced by ATP.

PubMed ID: 12384589

DOI: 10.1093/nar/gkf574

PubMed ID: 15456891

Title: Artemis is a phosphorylation target of ATM and ATR and is involved in the G2/M DNA damage checkpoint response.

PubMed ID: 15456891

DOI: 10.1128/mcb.24.20.9207-9220.2004

PubMed ID: 15064416

Title: Direct activation of the ATM protein kinase by the Mre11/Rad50/Nbs1 complex.

PubMed ID: 15064416

DOI: 10.1126/science.1091496

PubMed ID: 15723659

Title: Ataxia-telangiectasia-mutated dependent phosphorylation of Artemis in response to DNA damage.

PubMed ID: 15723659

DOI: 10.1111/j.1349-7006.2005.00019.x

PubMed ID: 15916964

Title: ATM-dependent phosphorylation of ATF2 is required for the DNA damage response.

PubMed ID: 15916964

DOI: 10.1016/j.molcel.2005.04.015

PubMed ID: 17525332

Title: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.

PubMed ID: 17525332

DOI: 10.1126/science.1140321

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19409520

Title: Human RAD50 deficiency in a Nijmegen breakage syndrome-like disorder.

PubMed ID: 19409520

DOI: 10.1016/j.ajhg.2009.04.010

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20943970

Title: Physical interaction between the herpes simplex virus type 1 exonuclease, UL12, and the DNA double-strand break-sensing MRN complex.

PubMed ID: 20943970

DOI: 10.1128/jvi.01506-10

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 26215093

Title: MCM8-9 complex promotes resection of double-strand break ends by MRE11-RAD50-NBS1 complex.

PubMed ID: 26215093

DOI: 10.1038/ncomms8744

PubMed ID: 27568553

Title: MRNIP/C5orf45 interacts with the MRN complex and contributes to the DNA damage response.

PubMed ID: 27568553

DOI: 10.1016/j.celrep.2016.07.087

PubMed ID: 14684699

Title: Mutation screening of Mre11 complex genes: indication of RAD50 involvement in breast and ovarian cancer susceptibility.

PubMed ID: 14684699

DOI: 10.1136/jmg.40.12.e131

Sequence Information:

  • Length: 1312
  • Mass: 153892
  • Checksum: 1F208C3817FC41FC
  • Sequence:
  • MSRIEKMSIL GVRSFGIEDK DKQIITFFSP LTILVGPNGA GKTTIIECLK YICTGDFPPG 
    TKGNTFVHDP KVAQETDVRA QIRLQFRDVN GELIAVQRSM VCTQKSKKTE FKTLEGVITR 
    TKHGEKVSLS SKCAEIDREM ISSLGVSKAV LNNVIFCHQE DSNWPLSEGK ALKQKFDEIF 
    SATRYIKALE TLRQVRQTQG QKVKEYQMEL KYLKQYKEKA CEIRDQITSK EAQLTSSKEI 
    VKSYENELDP LKNRLKEIEH NLSKIMKLDN EIKALDSRKK QMEKDNSELE EKMEKVFQGT 
    DEQLNDLYHN HQRTVREKER KLVDCHRELE KLNKESRLLN QEKSELLVEQ GRLQLQADRH 
    QEHIRARDSL IQSLATQLEL DGFERGPFSE RQIKNFHKLV RERQEGEAKT ANQLMNDFAE 
    KETLKQKQID EIRDKKTGLG RIIELKSEIL SKKQNELKNV KYELQQLEGS SDRILELDQE 
    LIKAERELSK AEKNSNVETL KMEVISLQNE KADLDRTLRK LDQEMEQLNH HTTTRTQMEM 
    LTKDKADKDE QIRKIKSRHS DELTSLLGYF PNKKQLEDWL HSKSKEINQT RDRLAKLNKE 
    LASSEQNKNH INNELKRKEE QLSSYEDKLF DVCGSQDFES DLDRLKEEIE KSSKQRAMLA 
    GATAVYSQFI TQLTDENQSC CPVCQRVFQT EAELQEVISD LQSKLRLAPD KLKSTESELK 
    KKEKRRDEML GLVPMRQSII DLKEKEIPEL RNKLQNVNRD IQRLKNDIEE QETLLGTIMP 
    EEESAKVCLT DVTIMERFQM ELKDVERKIA QQAAKLQGID LDRTVQQVNQ EKQEKQHKLD 
    TVSSKIELNR KLIQDQQEQI QHLKSTTNEL KSEKLQISTN LQRRQQLEEQ TVELSTEVQS 
    LYREIKDAKE QVSPLETTLE KFQQEKEELI NKKNTSNKIA QDKLNDIKEK VKNIHGYMKD 
    IENYIQDGKD DYKKQKETEL NKVIAQLSEC EKHKEKINED MRLMRQDIDT QKIQERWLQD 
    NLTLRKRNEE LKEVEEERKQ HLKEMGQMQV LQMKSEHQKL EENIDNIKRN HNLALGRQKG 
    YEEEIIHFKK ELREPQFRDA EEKYREMMIV MRTTELVNKD LDIYYKTLDQ AIMKFHSMKM 
    EEINKIIRDL WRSTYRGQDI EYIEIRSDAD ENVSASDKRR NYNYRVVMLK GDTALDMRGR 
    CSAGQKVLAS LIIRLALAET FCLNCGIIAL DEPTTNLDRE NIESLAHALV EIIKSRSQQR 
    NFQLLVITHD EDFVELLGRS EYVEKFYRIK KNIDQCSEIV KCSVSSLGFN VH

Genular Protein ID: 3902154380

Symbol: A5D6Y3_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

Sequence Information:

  • Length: 110
  • Mass: 12259
  • Checksum: B25CD5B6ED40C592
  • Sequence:
  • MSRIEKMSIL GVRSFGIEDK DKQIITFFSP LTILVGPNGA GKTTIIECLK YICTGDFPPG 
    TKGNTFVHDP KVAQETDVRA QIRLQFRDVN GELIAVQRSM VCTQKSKKKK

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.