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P49959

- MRE11_HUMAN

UniProt

P49959 - MRE11_HUMAN

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Protein
Double-strand break repair protein MRE11A
Gene
MRE11A, HNGS1, MRE11
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 donor By 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 C-terminus binding Source: UniProtKB
  8. protein binding Source: UniProtKB
  9. single-stranded DNA endodeoxyribonuclease activity Source: ProtInc

GO - Biological processi

  1. DNA catabolic process, endonucleolytic Source: GOC
  2. DNA duplex unwinding Source: BHF-UCL
  3. DNA recombination Source: ProtInc
  4. DNA repair Source: Reactome
  5. base-excision repair Source: RefGenome
  6. cell proliferation Source: Ensembl
  7. cellular response to DNA damage stimulus Source: MGI
  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
Complete GO annotation...

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.1 Publication

GO - Cellular componenti

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

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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.1 Publication

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 – 11Removed1 Publication
Chaini2 – 708707Double-strand break repair protein MRE11A
PRO_0000138672Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei2 – 21Phosphoserine By 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 ATF2.4 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

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.

Family & Domainsi

Sequence similaritiesi

Belongs to the MRE11/RAD32 family.

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

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.
VSP_003262Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 311V → A in AAC78721. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 156 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

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