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P49959

- MRE11_HUMAN

UniProt

P49959 - MRE11_HUMAN

Protein

Double-strand break repair protein MRE11A

Gene

MRE11A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 3 (26 Sep 2001)
      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.

    Cofactori

    Manganese.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei129 – 1291Proton donorBy similarity

    GO - Molecular functioni

    1. 3'-5' exonuclease activity Source: RefGenome
    2. double-stranded DNA binding Source: ProtInc
    3. endodeoxyribonuclease activity Source: ProtInc
    4. endonuclease activity Source: RefGenome
    5. manganese ion binding Source: InterPro
    6. nuclease activity Source: BHF-UCL
    7. protein binding Source: UniProtKB
    8. protein C-terminus binding Source: UniProtKB
    9. single-stranded DNA endodeoxyribonuclease activity Source: ProtInc

    GO - Biological processi

    1. base-excision repair Source: RefGenome
    2. cell proliferation Source: Ensembl
    3. cellular response to DNA damage stimulus Source: MGI
    4. DNA catabolic process, endonucleolytic Source: GOC
    5. DNA duplex unwinding Source: BHF-UCL
    6. DNA recombination Source: ProtInc
    7. DNA repair Source: Reactome
    8. double-strand break repair Source: RefGenome
    9. double-strand break repair via homologous recombination Source: Reactome
    10. double-strand break repair via nonhomologous end joining Source: ProtInc
    11. innate immune response Source: Reactome
    12. intra-S DNA damage checkpoint Source: RefGenome
    13. mitotic G2 DNA damage checkpoint Source: Ensembl
    14. negative regulation of DNA endoreduplication Source: BHF-UCL
    15. nucleic acid phosphodiester bond hydrolysis Source: GOC
    16. nucleotide-excision repair Source: RefGenome
    17. positive regulation of kinase activity Source: BHF-UCL
    18. positive regulation of protein autophosphorylation Source: BHF-UCL
    19. positive regulation of type I interferon production Source: Reactome
    20. reciprocal meiotic recombination Source: ProtInc
    21. regulation of mitotic recombination Source: ProtInc
    22. sister chromatid cohesion Source: BHF-UCL
    23. synapsis Source: Ensembl
    24. telomere maintenance Source: RefGenome
    25. telomere maintenance via telomerase Source: ProtInc

    Keywords - Molecular functioni

    Endonuclease, Exonuclease, Hydrolase, Nuclease

    Keywords - Biological processi

    DNA damage, DNA repair, Meiosis

    Keywords - Ligandi

    Manganese

    Enzyme and pathway databases

    ReactomeiREACT_163993. IRF3-mediated induction of type I IFN.
    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.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Double-strand break repair protein MRE11A
    Alternative name(s):
    Meiotic recombination 11 homolog 1
    Short name:
    MRE11 homolog 1
    Meiotic recombination 11 homolog A
    Short name:
    MRE11 homolog A
    Gene namesi
    Name:MRE11A
    Synonyms:HNGS1, MRE11
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:7230. MRE11A.

    Subcellular locationi

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

    GO - Cellular componenti

    1. chromatin Source: RefGenome
    2. cytosol Source: Reactome
    3. Mre11 complex Source: BHF-UCL
    4. nucleoplasm Source: Reactome
    5. nucleus Source: HPA
    6. site of double-strand break Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Ataxia-telangiectasia-like disorder (ATLD) [MIM:604391]: A rare disorder characterized by progressive cerebellar ataxia, dysarthria, abnormal eye movements, and absence of telangiectasia. ATLD patients show normal levels of total IgG, IgA and IgM, although there may be reduced levels of specific functional antibodies. At the cellular level, ATLD exhibits hypersensitivity to ionizing radiation and radioresistant DNA synthesis.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti117 – 1171N → S in ATLD. 1 Publication
    VAR_008513
    Defects in MRE11A can be a cause of nephronophthisis-related ciliopathies (NPHP-RC), a group of recessive diseases that affect kidney, retina and brain. A homozygous truncating mutation MRE11A has been found in patients with cerebellar vermis hypoplasia, ataxia and dysarthria.

    Keywords - Diseasei

    Ciliopathy, Disease mutation

    Organism-specific databases

    MIMi604391. phenotype.
    Orphaneti251347. Ataxia-telangiectasia-like disorder.
    145. Hereditary breast and ovarian cancer syndrome.
    PharmGKBiPA30934.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 708707Double-strand break repair protein MRE11APRO_0000138672Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Modified residuei2 – 21PhosphoserineBy similarity
    Modified residuei649 – 6491Phosphoserine2 Publications
    Modified residuei688 – 6881Phosphoserine4 Publications
    Modified residuei689 – 6891Phosphoserine4 Publications
    Modified residuei701 – 7011Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP49959.
    PaxDbiP49959.
    PRIDEiP49959.

    PTM databases

    PhosphoSiteiP49959.

    Miscellaneous databases

    PMAP-CutDBP49959.

    Expressioni

    Gene expression databases

    ArrayExpressiP49959.
    BgeeiP49959.
    CleanExiHS_MRE11A.
    GenevestigatoriP49959.

    Organism-specific databases

    HPAiCAB004081.
    HPA002691.

    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 By similarity. Interacts with DCLRE1C/Artemis and DCLRE1B/Apollo. Interacts with ATF2.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FANCD2Q9BXW96EBI-396513,EBI-359343
    H2AFXP161044EBI-396513,EBI-494830
    HTTP428585EBI-396513,EBI-466029
    NBNO609342EBI-396513,EBI-494844

    Protein-protein interaction databases

    BioGridi110501. 72 interactions.
    DIPiDIP-33238N.
    IntActiP49959. 19 interactions.
    MINTiMINT-131851.
    STRINGi9606.ENSP00000325863.

    Structurei

    Secondary structure

    1
    708
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 113
    Beta strandi12 – 187
    Turni24 – 263
    Turni30 – 345
    Helixi35 – 4915
    Beta strandi53 – 575
    Beta strandi62 – 665
    Helixi69 – 8315
    Beta strandi122 – 1243
    Beta strandi128 – 1303
    Turni134 – 1374
    Helixi140 – 1478
    Beta strandi149 – 1524
    Beta strandi162 – 1643
    Beta strandi167 – 1715
    Beta strandi174 – 1818
    Helixi186 – 1949
    Beta strandi198 – 2003
    Helixi207 – 2093
    Beta strandi210 – 2167
    Beta strandi223 – 2286
    Helixi231 – 2333
    Beta strandi240 – 2434
    Beta strandi250 – 2556
    Turni257 – 2593
    Beta strandi262 – 2654
    Helixi276 – 2794
    Beta strandi283 – 2908
    Beta strandi293 – 3008
    Beta strandi302 – 3043
    Beta strandi307 – 3137
    Helixi314 – 3163
    Turni318 – 3203
    Helixi328 – 35023
    Turni351 – 3533
    Beta strandi355 – 3573
    Beta strandi362 – 3687
    Turni370 – 3723
    Helixi379 – 3857
    Turni386 – 3883
    Beta strandi392 – 3998

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3T1IX-ray3.00A/B/C/D1-411[»]
    ProteinModelPortaliP49959.
    SMRiP49959. Positions 8-400.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the MRE11/RAD32 family.Curated

    Phylogenomic databases

    eggNOGiCOG0420.
    HOGENOMiHOG000216581.
    HOVERGENiHBG052508.
    InParanoidiP49959.
    KOiK10865.
    OrthoDBiEOG7VB2F1.
    PhylomeDBiP49959.
    TreeFamiTF101105.

    Family and domain databases

    Gene3Di3.60.21.10. 2 hits.
    InterProiIPR004843. Calcineurin-like_PHP_apaH.
    IPR003701. DNA_repair_Mre11.
    IPR029052. Metallo-depent_PP-like.
    IPR007281. Mre11_DNA-bd.
    [Graphical view]
    PANTHERiPTHR10139. PTHR10139. 1 hit.
    PfamiPF00149. Metallophos. 1 hit.
    PF04152. Mre11_DNA_bind. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000882. DSB_repair_MRE11. 1 hit.
    SUPFAMiSSF56300. SSF56300. 2 hits.
    TIGRFAMsiTIGR00583. mre11. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P49959-1) [UniParc]FASTAAdd to Basket

    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

    MSTADALDDE NTFKILVATD IHLGFMEKDA VRGNDTFVTL DEILRLAQEN    50
    EVDFILLGGD LFHENKPSRK TLHTCLELLR KYCMGDRPVQ FEILSDQSVN 100
    FGFSKFPWVN YQDGNLNISI PVFSIHGNHD DPTGADALCA LDILSCAGFV 150
    NHFGRSMSVE KIDISPVLLQ KGSTKIALYG LGSIPDERLY RMFVNKKVTM 200
    LRPKEDENSW FNLFVIHQNR SKHGSTNFIP EQFLDDFIDL VIWGHEHECK 250
    IAPTKNEQQL FYISQPGSSV VTSLSPGEAV KKHVGLLRIK GRKMNMHKIP 300
    LHTVRQFFME DIVLANHPDI FNPDNPKVTQ AIQSFCLEKI EEMLENAERE 350
    RLGNSHQPEK PLVRLRVDYS GGFEPFSVLR FSQKFVDRVA NPKDIIHFFR 400
    HREQKEKTGE EINFGKLITK PSEGTTLRVE DLVKQYFQTA EKNVQLSLLT 450
    ERGMGEAVQE FVDKEEKDAI EELVKYQLEK TQRFLKERHI DALEDKIDEE 500
    VRRFRETRQK NTNEEDDEVR EAMTRARALR SQSEESASAF SADDLMSIDL 550
    AEQMANDSDD SISAATNKGR GRGRGRRGGR GQNSASRGGS QRGRADTGLE 600
    TSTRSRNSKT AVSASRNMSI IDAFKSTRQQ PSRNVTTKNY SEVIEVDESD 650
    VEEDIFPTTS KTDQRWSSTS SSKIMSQSQV SKGVDFESSE DDDDDPFMNT 700
    SSLRRNRR 708
    Length:708
    Mass (Da):80,593
    Last modified:September 26, 2001 - v3
    Checksum:iD94ABFBDDF6106AD
    GO
    Isoform 2 (identifier: P49959-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         595-622: Missing.

    Show »
    Length:680
    Mass (Da):77,642
    Checksum:iB36BA7EC8CE79BEE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti31 – 311V → A in AAC78721. (PubMed:8530104)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti104 – 1041S → C in cancer. 1 Publication
    VAR_011625
    Natural varianti117 – 1171N → S in ATLD. 1 Publication
    VAR_008513
    Natural varianti157 – 1571M → V.
    Corresponds to variant rs147771140 [ dbSNP | Ensembl ].
    VAR_011626
    Natural varianti237 – 2371F → C in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036416
    Natural varianti302 – 3021H → Y in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036417
    Natural varianti305 – 3051R → W in ovarian cancer. 1 Publication
    VAR_025528
    Natural varianti468 – 4681D → G.1 Publication
    Corresponds to variant rs1805367 [ dbSNP | Ensembl ].
    VAR_019288
    Natural varianti503 – 5031R → H in cancer. 1 Publication
    VAR_011627
    Natural varianti572 – 5721R → Q in cancer. 1 Publication
    Corresponds to variant rs200085146 [ dbSNP | Ensembl ].
    VAR_011628
    Natural varianti698 – 6981M → V.1 Publication
    Corresponds to variant rs1805362 [ dbSNP | Ensembl ].
    VAR_019289

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei595 – 62228Missing in isoform 2. 1 PublicationVSP_003262Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U37359 mRNA. Translation: AAC78721.1.
    AF022778 mRNA. Translation: AAD10197.1.
    AF073362 mRNA. Translation: AAC36249.1.
    AF303395
    , AF303379, AF303380, AF303381, AF303382, AF303383, AF303384, AF303385, AF303386, AF303387, AF303388, AF303389, AF303390, AF303391, AF303392, AF303393, AF303394 Genomic DNA. Translation: AAK18790.1.
    AY584241 Genomic DNA. Translation: AAS79320.1.
    BC063458 mRNA. Translation: AAH63458.1.
    CCDSiCCDS8298.1. [P49959-2]
    CCDS8299.1. [P49959-1]
    RefSeqiNP_005581.2. NM_005590.3. [P49959-2]
    NP_005582.1. NM_005591.3. [P49959-1]
    XP_005274064.1. XM_005274007.1. [P49959-1]
    UniGeneiHs.192649.

    Genome annotation databases

    EnsembliENST00000323929; ENSP00000325863; ENSG00000020922. [P49959-1]
    ENST00000323977; ENSP00000326094; ENSG00000020922. [P49959-2]
    GeneIDi4361.
    KEGGihsa:4361.
    UCSCiuc001peu.2. human. [P49959-1]
    uc001pev.2. human. [P49959-2]

    Polymorphism databases

    DMDMi17380137.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    MRE11base

    MRE11A mutation db

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U37359 mRNA. Translation: AAC78721.1 .
    AF022778 mRNA. Translation: AAD10197.1 .
    AF073362 mRNA. Translation: AAC36249.1 .
    AF303395
    , AF303379 , AF303380 , AF303381 , AF303382 , AF303383 , AF303384 , AF303385 , AF303386 , AF303387 , AF303388 , AF303389 , AF303390 , AF303391 , AF303392 , AF303393 , AF303394 Genomic DNA. Translation: AAK18790.1 .
    AY584241 Genomic DNA. Translation: AAS79320.1 .
    BC063458 mRNA. Translation: AAH63458.1 .
    CCDSi CCDS8298.1. [P49959-2 ]
    CCDS8299.1. [P49959-1 ]
    RefSeqi NP_005581.2. NM_005590.3. [P49959-2 ]
    NP_005582.1. NM_005591.3. [P49959-1 ]
    XP_005274064.1. XM_005274007.1. [P49959-1 ]
    UniGenei Hs.192649.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3T1I X-ray 3.00 A/B/C/D 1-411 [» ]
    ProteinModelPortali P49959.
    SMRi P49959. Positions 8-400.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110501. 72 interactions.
    DIPi DIP-33238N.
    IntActi P49959. 19 interactions.
    MINTi MINT-131851.
    STRINGi 9606.ENSP00000325863.

    PTM databases

    PhosphoSitei P49959.

    Polymorphism databases

    DMDMi 17380137.

    Proteomic databases

    MaxQBi P49959.
    PaxDbi P49959.
    PRIDEi P49959.

    Protocols and materials databases

    DNASUi 4361.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000323929 ; ENSP00000325863 ; ENSG00000020922 . [P49959-1 ]
    ENST00000323977 ; ENSP00000326094 ; ENSG00000020922 . [P49959-2 ]
    GeneIDi 4361.
    KEGGi hsa:4361.
    UCSCi uc001peu.2. human. [P49959-1 ]
    uc001pev.2. human. [P49959-2 ]

    Organism-specific databases

    CTDi 4361.
    GeneCardsi GC11M094150.
    HGNCi HGNC:7230. MRE11A.
    HPAi CAB004081.
    HPA002691.
    MIMi 600814. gene.
    604391. phenotype.
    neXtProti NX_P49959.
    Orphaneti 251347. Ataxia-telangiectasia-like disorder.
    145. Hereditary breast and ovarian cancer syndrome.
    PharmGKBi PA30934.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0420.
    HOGENOMi HOG000216581.
    HOVERGENi HBG052508.
    InParanoidi P49959.
    KOi K10865.
    OrthoDBi EOG7VB2F1.
    PhylomeDBi P49959.
    TreeFami TF101105.

    Enzyme and pathway databases

    Reactomei REACT_163993. IRF3-mediated induction of type I IFN.
    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 MRE11A. human.
    GeneWikii MRE11A.
    GenomeRNAii 4361.
    NextBioi 17163.
    PMAP-CutDB P49959.
    PROi P49959.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49959.
    Bgeei P49959.
    CleanExi HS_MRE11A.
    Genevestigatori P49959.

    Family and domain databases

    Gene3Di 3.60.21.10. 2 hits.
    InterProi IPR004843. Calcineurin-like_PHP_apaH.
    IPR003701. DNA_repair_Mre11.
    IPR029052. Metallo-depent_PP-like.
    IPR007281. Mre11_DNA-bd.
    [Graphical view ]
    PANTHERi PTHR10139. PTHR10139. 1 hit.
    Pfami PF00149. Metallophos. 1 hit.
    PF04152. Mre11_DNA_bind. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000882. DSB_repair_MRE11. 1 hit.
    SUPFAMi SSF56300. SSF56300. 2 hits.
    TIGRFAMsi TIGR00583. mre11. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of the human MRE11 homologue."
      Petrini J.H.J., Walsh M.E., Dimare C., Chen X.-N., Korenberg J.R., Weaver D.T.
      Genomics 29:80-86(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    2. Petrini J.H.J., Walsh M.E., Dimare C., Chen X.-N., Korenberg J.R., Weaver D.T.
      Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO C-TERMINUS.
    3. "Molecular cloning and functional characterization of hNGS1, a yeast and human MRE11 homolog."
      Chamankhah M., Wei Y., Xiao W.
      Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    5. "hMRE11: genomic structure and a null mutation identified in a transcript protected from nonsense-mediated mRNA decay."
      Pitts S.A., Kullar H.S., Stankovic T., Stewart G.S., Last J.I.K., Bedenham T., Armstrong S.J., Piane M., Chessa L., Taylor A.M.R., Byrd P.J.
      Hum. Mol. Genet. 10:1155-1162(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    6. NIEHS SNPs program
      Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLY-468 AND VAL-698.
    7. "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: Brain.
    8. "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.
    9. "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.
    10. "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: INTERACTION WITH ATF2, SUBCELLULAR LOCATION.
    11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Snm1B/Apollo mediates replication fork collapse and S Phase checkpoint activation in response to DNA interstrand cross-links."
      Bae J.B., Mukhopadhyay S.S., Liu L., Zhang N., Tan J., Akhter S., Liu X., Shen X., Li L., Legerski R.J.
      Oncogene 27:5045-5056(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DCLRE1B.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649; SER-688; SER-689 AND SER-701, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    16. "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 SER-649; SER-688 AND SER-689, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    17. "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-688 AND SER-689, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-688 AND SER-689, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Exome capture reveals ZNF423 and CEP164 mutations, linking renal ciliopathies to DNA damage response signaling."
      Chaki M., Airik R., Ghosh A.K., Giles R.H., Chen R., Slaats G.G., Wang H., Hurd T.W., Zhou W., Cluckey A., Gee H.Y., Ramaswami G., Hong C.J., Hamilton B.A., Cervenka I., Ganji R.S., Bryja V., Arts H.H.
      , van Reeuwijk J., Oud M.M., Letteboer S.J., Roepman R., Husson H., Ibraghimov-Beskrovnaya O., Yasunaga T., Walz G., Eley L., Sayer J.A., Schermer B., Liebau M.C., Benzing T., Le Corre S., Drummond I., Janssen S., Allen S.J., Natarajan S., O'Toole J.F., Attanasio M., Saunier S., Antignac C., Koenekoop R.K., Ren H., Lopez I., Nayir A., Stoetzel C., Dollfus H., Massoudi R., Gleeson J.G., Andreoli S.P., Doherty D.G., Lindstrad A., Golzio C., Katsanis N., Pape L., Abboud E.B., Al-Rajhi A.A., Lewis R.A., Omran H., Lee E.Y., Wang S., Sekiguchi J.M., Saunders R., Johnson C.A., Garner E., Vanselow K., Andersen J.S., Shlomai J., Nurnberg G., Nurnberg P., Levy S., Smogorzewska A., Otto E.A., Hildebrandt F.
      Cell 150:533-548(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN NPHP-RC.
    21. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "The DNA double-strand break repair gene hMRE11 is mutated in individuals with an ataxia-telangiectasia-like disorder."
      Stewart G.S., Maser R.S., Stankovic T., Bressan D.A., Kaplan M.I., Jaspers N.G.J., Raams A., Byrd P.J., Petrini J.H.J., Taylor A.M.R.
      Cell 99:577-587(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ATLD SER-117.
    23. "Alterations of the double-strand break repair gene MRE11 in cancer."
      Fukuda T., Sumiyoshi T., Takahashi M., Kataoka T., Asahara T., Inui H., Watatani M., Yasutomi M., Kamada N., Miyagawa K.
      Cancer Res. 61:23-26(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CANCER CYS-104; HIS-503 AND GLN-572.
    24. "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: VARIANT OVARIAN CANCER TRP-305.
    25. Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-237 AND TYR-302.

    Entry informationi

    Entry nameiMRE11_HUMAN
    AccessioniPrimary (citable) accession number: P49959
    Secondary accession number(s): O43475
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: September 26, 2001
    Last modified: October 1, 2014
    This is version 157 of the entry and version 3 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3