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P49959 (MRE11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 155. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:MRE11A
Synonyms:HNGS1, MRE11
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length708 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Cofactor

Manganese By similarity.

Subunit structure

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. Ref.8 Ref.9 Ref.10 Ref.13

Subcellular location

Nucleus By similarity. Note: Localizes to discrete nuclear foci after treatment with genotoxic agents By similarity. Ref.10

Involvement in disease

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. Ref.22

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. Ref.20

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.

Sequence similarities

Belongs to the MRE11/RAD32 family.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Meiosis
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCiliopathy
Disease mutation
   LigandManganese
   Molecular functionEndonuclease
Exonuclease
Hydrolase
Nuclease
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA catabolic process, endonucleolytic

Traceable author statement Ref.4PubMed 9705271. Source: GOC

DNA duplex unwinding

Inferred from mutant phenotype PubMed 15790808. Source: BHF-UCL

DNA recombination

Traceable author statement PubMed 9705271. Source: ProtInc

DNA repair

Traceable author statement. Source: Reactome

cell proliferation

Inferred from electronic annotation. Source: Ensembl

cellular response to DNA damage stimulus

Inferred from direct assay PubMed 17500065. Source: MGI

double-strand break repair

Traceable author statement. Source: Reactome

double-strand break repair via homologous recombination

Traceable author statement. Source: Reactome

double-strand break repair via nonhomologous end joining

Traceable author statement Ref.4. Source: ProtInc

innate immune response

Traceable author statement. Source: Reactome

intra-S DNA damage checkpoint

Inferred from electronic annotation. Source: Ensembl

mitotic G2 DNA damage checkpoint

Inferred from electronic annotation. Source: Ensembl

negative regulation of DNA endoreduplication

Inferred from mutant phenotype PubMed 15917200. Source: BHF-UCL

nucleic acid phosphodiester bond hydrolysis

Traceable author statement. Source: GOC

positive regulation of kinase activity

Inferred from direct assay PubMed 15790808. Source: BHF-UCL

positive regulation of protein autophosphorylation

Inferred from direct assay PubMed 15790808. Source: BHF-UCL

positive regulation of type I interferon production

Traceable author statement. Source: Reactome

reciprocal meiotic recombination

Traceable author statement Ref.1PubMed 9931460. Source: ProtInc

regulation of mitotic recombination

Traceable author statement Ref.1. Source: ProtInc

sister chromatid cohesion

Inferred from mutant phenotype PubMed 15917200. Source: BHF-UCL

synapsis

Inferred from electronic annotation. Source: Ensembl

telomere maintenance via telomerase

Traceable author statement PubMed 9705271PubMed 9931460. Source: ProtInc

   Cellular_componentMre11 complex

Non-traceable author statement PubMed 15790808. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

site of double-strand break

Inferred from direct assay Ref.10. Source: UniProtKB

   Molecular_function3'-5' exonuclease activity

Traceable author statement. Source: ProtInc

double-stranded DNA binding

Traceable author statement PubMed 10802669. Source: ProtInc

endodeoxyribonuclease activity

Traceable author statement Ref.4. Source: ProtInc

manganese ion binding

Inferred from electronic annotation. Source: InterPro

nuclease activity

Traceable author statement PubMed 15790808. Source: BHF-UCL

protein C-terminus binding

Inferred from physical interaction PubMed 9590181. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.10PubMed 18716619PubMed 24651726. Source: UniProtKB

single-stranded DNA endodeoxyribonuclease activity

Traceable author statement PubMed 9705271. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P49959-1)

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.
Isoform 2 (identifier: P49959-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.15
Chain2 – 708707Double-strand break repair protein MRE11A
PRO_0000138672

Sites

Active site1291Proton donor By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.15 Ref.21
Modified residue21Phosphoserine By similarity
Modified residue6491Phosphoserine Ref.14 Ref.16
Modified residue6881Phosphoserine Ref.14 Ref.16 Ref.17 Ref.19
Modified residue6891Phosphoserine Ref.14 Ref.16 Ref.17 Ref.19
Modified residue7011Phosphoserine Ref.14

Natural variations

Alternative sequence595 – 62228Missing in isoform 2.
VSP_003262
Natural variant1041S → C in cancer. Ref.23
VAR_011625
Natural variant1171N → S in ATLD. Ref.22
VAR_008513
Natural variant1571M → V.
Corresponds to variant rs147771140 [ dbSNP | Ensembl ].
VAR_011626
Natural variant2371F → C in a breast cancer sample; somatic mutation. Ref.25
VAR_036416
Natural variant3021H → Y in a breast cancer sample; somatic mutation. Ref.25
VAR_036417
Natural variant3051R → W in ovarian cancer. Ref.24
VAR_025528
Natural variant4681D → G. Ref.6
Corresponds to variant rs1805367 [ dbSNP | Ensembl ].
VAR_019288
Natural variant5031R → H in cancer. Ref.23
VAR_011627
Natural variant5721R → Q in cancer. Ref.23
Corresponds to variant rs200085146 [ dbSNP | Ensembl ].
VAR_011628
Natural variant6981M → V. Ref.6
Corresponds to variant rs1805362 [ dbSNP | Ensembl ].
VAR_019289

Experimental info

Sequence conflict311V → A in AAC78721. Ref.1

Secondary structure

............................................................................. 708
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 26, 2001. Version 3.
Checksum: D94ABFBDDF6106AD

FASTA70880,593
        10         20         30         40         50         60 
MSTADALDDE NTFKILVATD IHLGFMEKDA VRGNDTFVTL DEILRLAQEN EVDFILLGGD 

        70         80         90        100        110        120 
LFHENKPSRK TLHTCLELLR KYCMGDRPVQ FEILSDQSVN FGFSKFPWVN YQDGNLNISI 

       130        140        150        160        170        180 
PVFSIHGNHD DPTGADALCA LDILSCAGFV NHFGRSMSVE KIDISPVLLQ KGSTKIALYG 

       190        200        210        220        230        240 
LGSIPDERLY RMFVNKKVTM LRPKEDENSW FNLFVIHQNR SKHGSTNFIP EQFLDDFIDL 

       250        260        270        280        290        300 
VIWGHEHECK IAPTKNEQQL FYISQPGSSV VTSLSPGEAV KKHVGLLRIK GRKMNMHKIP 

       310        320        330        340        350        360 
LHTVRQFFME DIVLANHPDI FNPDNPKVTQ AIQSFCLEKI EEMLENAERE RLGNSHQPEK 

       370        380        390        400        410        420 
PLVRLRVDYS GGFEPFSVLR FSQKFVDRVA NPKDIIHFFR HREQKEKTGE EINFGKLITK 

       430        440        450        460        470        480 
PSEGTTLRVE DLVKQYFQTA EKNVQLSLLT ERGMGEAVQE FVDKEEKDAI EELVKYQLEK 

       490        500        510        520        530        540 
TQRFLKERHI DALEDKIDEE VRRFRETRQK NTNEEDDEVR EAMTRARALR SQSEESASAF 

       550        560        570        580        590        600 
SADDLMSIDL AEQMANDSDD SISAATNKGR GRGRGRRGGR GQNSASRGGS QRGRADTGLE 

       610        620        630        640        650        660 
TSTRSRNSKT AVSASRNMSI IDAFKSTRQQ PSRNVTTKNY SEVIEVDESD VEEDIFPTTS 

       670        680        690        700 
KTDQRWSSTS SSKIMSQSQV SKGVDFESSE DDDDDPFMNT SSLRRNRR 

« Hide

Isoform 2 [UniParc].

Checksum: B36BA7EC8CE79BEE
Show »

FASTA68077,642

References

« Hide 'large scale' references
[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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-237 AND TYR-302.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U37359 mRNA. Translation: AAC78721.1.
AF022778 mRNA. Translation: AAD10197.1.
AF073362 mRNA. Translation: AAC36249.1.
AF303395 expand/collapse EMBL AC list , 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.
CCDSCCDS8298.1. [P49959-2]
CCDS8299.1. [P49959-1]
RefSeqNP_005581.2. NM_005590.3. [P49959-2]
NP_005582.1. NM_005591.3. [P49959-1]
XP_005274064.1. XM_005274007.1. [P49959-1]
UniGeneHs.192649.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3T1IX-ray3.00A/B/C/D1-411[»]
ProteinModelPortalP49959.
SMRP49959. Positions 8-400.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110501. 73 interactions.
DIPDIP-33238N.
IntActP49959. 17 interactions.
MINTMINT-131851.
STRING9606.ENSP00000325863.

PTM databases

PhosphoSiteP49959.

Polymorphism databases

DMDM17380137.

Proteomic databases

MaxQBP49959.
PaxDbP49959.
PRIDEP49959.

Protocols and materials databases

DNASU4361.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000323929; ENSP00000325863; ENSG00000020922. [P49959-1]
ENST00000323977; ENSP00000326094; ENSG00000020922. [P49959-2]
GeneID4361.
KEGGhsa:4361.
UCSCuc001peu.2. human. [P49959-1]
uc001pev.2. human. [P49959-2]

Organism-specific databases

CTD4361.
GeneCardsGC11M094150.
HGNCHGNC:7230. MRE11A.
HPACAB004081.
HPA002691.
MIM600814. gene.
604391. phenotype.
neXtProtNX_P49959.
Orphanet251347. Ataxia-telangiectasia-like disorder.
145. Hereditary breast and ovarian cancer syndrome.
PharmGKBPA30934.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0420.
HOGENOMHOG000216581.
HOVERGENHBG052508.
InParanoidP49959.
KOK10865.
OrthoDBEOG7VB2F1.
PhylomeDBP49959.
TreeFamTF101105.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_120956. Cellular responses to stress.
REACT_216. DNA Repair.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP49959.
BgeeP49959.
CleanExHS_MRE11A.
GenevestigatorP49959.

Family and domain databases

Gene3D3.60.21.10. 2 hits.
InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR003701. DNA_repair_Mre11.
IPR029052. Metallo-depent_PP-like.
IPR007281. Mre11_DNA-bd.
[Graphical view]
PANTHERPTHR10139. PTHR10139. 1 hit.
PfamPF00149. Metallophos. 1 hit.
PF04152. Mre11_DNA_bind. 1 hit.
[Graphical view]
PIRSFPIRSF000882. DSB_repair_MRE11. 1 hit.
SUPFAMSSF56300. SSF56300. 2 hits.
TIGRFAMsTIGR00583. mre11. 1 hit.
ProtoNetSearch...

Other

ChiTaRSMRE11A. human.
GeneWikiMRE11A.
GenomeRNAi4361.
NextBio17163.
PMAP-CutDBP49959.
PROP49959.
SOURCESearch...

Entry information

Entry nameMRE11_HUMAN
AccessionPrimary (citable) accession number: P49959
Secondary accession number(s): O43475
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 26, 2001
Last modified: July 9, 2014
This is version 155 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM