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Protein

Double-strand break repair protein MRE11A

Gene

MRE11A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 (PubMed:9651580, PubMed:9590181, PubMed:9705271, PubMed:11741547). The complex may also be required for DNA damage signaling via activation of the ATM kinase (PubMed:15064416). In telomeres the MRN complex may modulate t-loop formation (PubMed:10888888).5 Publications

Cofactori

Mn2+By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei129Proton donorBy similarity1

GO - Molecular functioni

  • 3'-5' exonuclease activity Source: CACAO
  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • double-stranded DNA binding Source: ProtInc
  • endodeoxyribonuclease activity Source: CACAO
  • manganese ion binding Source: InterPro
  • nuclease activity Source: BHF-UCL
  • protein C-terminus binding Source: UniProtKB
  • single-stranded DNA endodeoxyribonuclease activity Source: CACAO

GO - Biological processi

  • cell proliferation Source: Ensembl
  • cellular response to DNA damage stimulus Source: MGI
  • DNA double-strand break processing Source: Reactome
  • DNA duplex unwinding Source: BHF-UCL
  • DNA recombination Source: ProtInc
  • DNA repair Source: ProtInc
  • DNA replication Source: Reactome
  • DNA synthesis involved in DNA repair Source: Reactome
  • double-strand break repair Source: ProtInc
  • double-strand break repair via homologous recombination Source: Reactome
  • double-strand break repair via nonhomologous end joining Source: CACAO
  • intra-S DNA damage checkpoint Source: GO_Central
  • mitotic G2 DNA damage checkpoint Source: Ensembl
  • negative regulation of apoptotic process Source: BHF-UCL
  • negative regulation of DNA endoreduplication Source: BHF-UCL
  • positive regulation of kinase activity Source: BHF-UCL
  • positive regulation of protein autophosphorylation Source: BHF-UCL
  • positive regulation of telomere maintenance Source: BHF-UCL
  • positive regulation of type I interferon production Source: Reactome
  • reciprocal meiotic recombination Source: ProtInc
  • regulation of mitotic recombination Source: ProtInc
  • regulation of signal transduction by p53 class mediator Source: Reactome
  • sister chromatid cohesion Source: BHF-UCL
  • strand displacement Source: Reactome
  • synapsis Source: Ensembl
  • telomere maintenance via telomerase Source: ProtInc
  • telomeric 3' overhang formation Source: BHF-UCL
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Exonuclease, Hydrolase, Nuclease

Keywords - Biological processi

DNA damage, DNA repair, Host-virus interaction, Meiosis

Keywords - Ligandi

Manganese

Enzyme and pathway databases

BioCyciZFISH:ENSG00000020922-MONOMER.
ReactomeiR-HSA-1834949. Cytosolic sensors of pathogen-associated DNA.
R-HSA-2559586. DNA Damage/Telomere Stress Induced Senescence.
R-HSA-3270619. IRF3-mediated induction of type I IFN.
R-HSA-5685938. HDR through Single Strand Annealing (SSA).
R-HSA-5685939. HDR through MMEJ (alt-NHEJ).
R-HSA-5685942. HDR through Homologous Recombination (HRR).
R-HSA-5693548. Sensing of DNA Double Strand Breaks.
R-HSA-5693554. Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
R-HSA-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-HSA-5693568. Resolution of D-loop Structures through Holliday Junction Intermediates.
R-HSA-5693571. Nonhomologous End-Joining (NHEJ).
R-HSA-5693579. Homologous DNA Pairing and Strand Exchange.
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-69473. G2/M DNA damage checkpoint.
R-HSA-912446. Meiotic recombination.
SIGNORiP49959.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:7230. MRE11A.

Subcellular locationi

  • Nucleus 1 Publication
  • Chromosometelomere 1 Publication

  • Note: Localizes to discrete nuclear foci after treatment with genotoxic agents.1 Publication

GO - Cellular componenti

  • cell-cell adherens junction Source: BHF-UCL
  • cytoplasm Source: BHF-UCL
  • cytosol Source: Reactome
  • Mre11 complex Source: BHF-UCL
  • nuclear chromosome, telomeric region Source: BHF-UCL
  • nucleoplasm Source: HPA
  • nucleus Source: ProtInc
  • PML body Source: BHF-UCL
  • site of double-strand break Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus, Telomere

Pathology & Biotechi

Involvement in diseasei

Ataxia-telangiectasia-like disorder 1 (ATLD1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:604391
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_008513117N → S in ATLD1. 1 PublicationCorresponds to variant rs137852760dbSNPEnsembl.1

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

DisGeNETi4361.
MalaCardsiMRE11A.
MIMi604391. phenotype.
OpenTargetsiENSG00000020922.
Orphaneti251347. Ataxia-telangiectasia-like disorder.
145. Hereditary breast and ovarian cancer syndrome.
PharmGKBiPA30934.

Chemistry databases

ChEMBLiCHEMBL3308929.

Polymorphism and mutation databases

BioMutaiMRE11A.
DMDMi17380137.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001386722 – 708Double-strand break repair protein MRE11AAdd BLAST707

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei2PhosphoserineBy similarity1
Modified residuei275PhosphoserineCombined sources1
Modified residuei619PhosphoserineCombined sources1
Modified residuei641PhosphoserineBy similarity1
Modified residuei649PhosphoserineCombined sources1
Modified residuei678PhosphoserineCombined sources1
Modified residuei688PhosphoserineCombined sources1
Modified residuei689PhosphoserineCombined sources1
Modified residuei701PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP49959.
MaxQBiP49959.
PaxDbiP49959.
PeptideAtlasiP49959.
PRIDEiP49959.

PTM databases

iPTMnetiP49959.
PhosphoSitePlusiP49959.

Miscellaneous databases

PMAP-CutDBP49959.

Expressioni

Gene expression databases

BgeeiENSG00000020922.
CleanExiHS_MRE11A.
ExpressionAtlasiP49959. baseline and differential.
GenevisibleiP49959. HS.

Organism-specific databases

HPAiCAB004081.
HPA002691.

Interactioni

Subunit structurei

Component of the MRN complex composed of two heterodimers RAD50/MRE11A associated with a single NBN (PubMed:9651580, PubMed:9590181, PubMed:9705271, PubMed:10839544). Component of the BASC complex, at least composed of BRCA1, MSH2, MSH6, MLH1, ATM, BLM, RAD50, MRE11A and NBN (PubMed:10783165). Found in a complex with TERF2 (PubMed:10888888). Interacts with DCLRE1C/Artemis and DCLRE1B/Apollo (PubMed:15456891, PubMed:15723659). Interacts with ATF2 (PubMed:15916964). Interacts with EXD2 (PubMed:26807646).7 Publications
(Microbial infection) Interacts with herpes simplex virus 1 protein UL12 (PubMed:20943970).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
FANCD2Q9BXW96EBI-396513,EBI-359343
H2AFXP161046EBI-396513,EBI-494830
HTTP428585EBI-396513,EBI-466029
NBNO609343EBI-396513,EBI-494844
RAD17O759432EBI-396513,EBI-968231

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • protein C-terminus binding Source: UniProtKB

Protein-protein interaction databases

BioGridi110501. 116 interactors.
DIPiDIP-33238N.
IntActiP49959. 30 interactors.
MINTiMINT-131851.
STRINGi9606.ENSP00000325863.

Chemistry databases

BindingDBiP49959.

Structurei

Secondary structure

1708
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 11Combined sources3
Beta strandi12 – 18Combined sources7
Turni24 – 26Combined sources3
Turni30 – 34Combined sources5
Helixi35 – 49Combined sources15
Beta strandi53 – 57Combined sources5
Beta strandi62 – 66Combined sources5
Helixi69 – 83Combined sources15
Beta strandi122 – 124Combined sources3
Beta strandi128 – 130Combined sources3
Turni134 – 137Combined sources4
Helixi140 – 147Combined sources8
Beta strandi149 – 152Combined sources4
Beta strandi162 – 164Combined sources3
Beta strandi167 – 171Combined sources5
Beta strandi174 – 181Combined sources8
Helixi186 – 194Combined sources9
Beta strandi198 – 200Combined sources3
Helixi207 – 209Combined sources3
Beta strandi210 – 216Combined sources7
Beta strandi223 – 228Combined sources6
Helixi231 – 233Combined sources3
Beta strandi240 – 243Combined sources4
Beta strandi250 – 255Combined sources6
Turni257 – 259Combined sources3
Beta strandi262 – 265Combined sources4
Helixi276 – 279Combined sources4
Beta strandi283 – 290Combined sources8
Beta strandi293 – 300Combined sources8
Beta strandi302 – 304Combined sources3
Beta strandi307 – 313Combined sources7
Helixi314 – 316Combined sources3
Turni318 – 320Combined sources3
Helixi328 – 350Combined sources23
Turni351 – 353Combined sources3
Beta strandi355 – 357Combined sources3
Beta strandi362 – 368Combined sources7
Turni370 – 372Combined sources3
Helixi379 – 385Combined sources7
Turni386 – 388Combined sources3
Beta strandi392 – 399Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3T1IX-ray3.00A/B/C/D1-411[»]
ProteinModelPortaliP49959.
SMRiP49959.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the MRE11/RAD32 family.Curated

Phylogenomic databases

eggNOGiKOG2310. Eukaryota.
COG0420. LUCA.
GeneTreeiENSGT00390000017288.
HOGENOMiHOG000216581.
HOVERGENiHBG052508.
InParanoidiP49959.
KOiK10865.
OMAiNSRQPEK.
OrthoDBiEOG091G06P4.
PhylomeDBiP49959.
TreeFamiTF101105.

Family and domain databases

Gene3Di3.60.21.10. 2 hits.
InterProiIPR004843. Calcineurin-like_PHP_ApaH.
IPR029052. Metallo-depent_PP-like.
IPR003701. Mre11.
IPR007281. Mre11_DNA-bd.
[Graphical view]
PANTHERiPTHR10139:SF1. PTHR10139:SF1. 1 hit.
PfamiPF00149. Metallophos. 1 hit.
PF04152. Mre11_DNA_bind. 1 hit.
[Graphical view]
PIRSFiPIRSF000882. DSB_repair_MRE11. 1 hit.
SMARTiSM01347. Mre11_DNA_bind. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 2 hits.
TIGRFAMsiTIGR00583. mre11. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

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

        10         20         30         40         50
MSTADALDDE NTFKILVATD IHLGFMEKDA VRGNDTFVTL DEILRLAQEN
60 70 80 90 100
EVDFILLGGD LFHENKPSRK TLHTCLELLR KYCMGDRPVQ FEILSDQSVN
110 120 130 140 150
FGFSKFPWVN YQDGNLNISI PVFSIHGNHD DPTGADALCA LDILSCAGFV
160 170 180 190 200
NHFGRSMSVE KIDISPVLLQ KGSTKIALYG LGSIPDERLY RMFVNKKVTM
210 220 230 240 250
LRPKEDENSW FNLFVIHQNR SKHGSTNFIP EQFLDDFIDL VIWGHEHECK
260 270 280 290 300
IAPTKNEQQL FYISQPGSSV VTSLSPGEAV KKHVGLLRIK GRKMNMHKIP
310 320 330 340 350
LHTVRQFFME DIVLANHPDI FNPDNPKVTQ AIQSFCLEKI EEMLENAERE
360 370 380 390 400
RLGNSHQPEK PLVRLRVDYS GGFEPFSVLR FSQKFVDRVA NPKDIIHFFR
410 420 430 440 450
HREQKEKTGE EINFGKLITK PSEGTTLRVE DLVKQYFQTA EKNVQLSLLT
460 470 480 490 500
ERGMGEAVQE FVDKEEKDAI EELVKYQLEK TQRFLKERHI DALEDKIDEE
510 520 530 540 550
VRRFRETRQK NTNEEDDEVR EAMTRARALR SQSEESASAF SADDLMSIDL
560 570 580 590 600
AEQMANDSDD SISAATNKGR GRGRGRRGGR GQNSASRGGS QRGRADTGLE
610 620 630 640 650
TSTRSRNSKT AVSASRNMSI IDAFKSTRQQ PSRNVTTKNY SEVIEVDESD
660 670 680 690 700
VEEDIFPTTS KTDQRWSSTS SSKIMSQSQV SKGVDFESSE DDDDDPFMNT

SSLRRNRR
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
Isoform 3 (identifier: P49959-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: MSTADAL → MNRNISHQKG

Note: No experimental confirmation available.
Show »
Length:711
Mass (Da):81,070
Checksum:i10AE0AC05AFB9351
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti31V → A in AAC78721 (PubMed:8530104).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_011625104S → C in cancer. 1 PublicationCorresponds to variant rs748434421dbSNPEnsembl.1
Natural variantiVAR_008513117N → S in ATLD1. 1 PublicationCorresponds to variant rs137852760dbSNPEnsembl.1
Natural variantiVAR_011626157M → V.Corresponds to variant rs147771140dbSNPEnsembl.1
Natural variantiVAR_036416237F → C in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_036417302H → Y in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_025528305R → W in ovarian cancer. 1 PublicationCorresponds to variant rs372000848dbSNPEnsembl.1
Natural variantiVAR_019288468D → G.1 PublicationCorresponds to variant rs1805367dbSNPEnsembl.1
Natural variantiVAR_011627503R → H in cancer. 1 PublicationCorresponds to variant rs774057024dbSNPEnsembl.1
Natural variantiVAR_011628572R → Q in cancer. 1 PublicationCorresponds to variant rs200085146dbSNPEnsembl.1
Natural variantiVAR_019289698M → V.1 PublicationCorresponds to variant rs1805362dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0573501 – 7MSTADAL → MNRNISHQKG in isoform 3. 1 Publication7
Alternative sequenceiVSP_003262595 – 622Missing in isoform 2. 1 PublicationAdd BLAST28

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
AK095388 mRNA. Translation: BAG53039.1.
AY584241 Genomic DNA. Translation: AAS79320.1.
AP000765 Genomic DNA. No translation available.
AP000786 Genomic DNA. No translation available.
KF455448 Genomic DNA. No translation available.
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_011541139.1. XM_011542837.2. [P49959-1]
XP_016873261.1. XM_017017772.1. [P49959-1]
UniGeneiHs.192649.

Genome annotation databases

EnsembliENST00000323929; ENSP00000325863; ENSG00000020922. [P49959-1]
ENST00000323977; ENSP00000326094; ENSG00000020922. [P49959-2]
ENST00000407439; ENSP00000385614; ENSG00000020922. [P49959-3]
GeneIDi4361.
KEGGihsa:4361.
UCSCiuc001peu.4. human. [P49959-1]

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:
EMBLi
GenBanki
DDBJi
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.
AK095388 mRNA. Translation: BAG53039.1.
AY584241 Genomic DNA. Translation: AAS79320.1.
AP000765 Genomic DNA. No translation available.
AP000786 Genomic DNA. No translation available.
KF455448 Genomic DNA. No translation available.
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_011541139.1. XM_011542837.2. [P49959-1]
XP_016873261.1. XM_017017772.1. [P49959-1]
UniGeneiHs.192649.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3T1IX-ray3.00A/B/C/D1-411[»]
ProteinModelPortaliP49959.
SMRiP49959.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110501. 116 interactors.
DIPiDIP-33238N.
IntActiP49959. 30 interactors.
MINTiMINT-131851.
STRINGi9606.ENSP00000325863.

Chemistry databases

BindingDBiP49959.
ChEMBLiCHEMBL3308929.

PTM databases

iPTMnetiP49959.
PhosphoSitePlusiP49959.

Polymorphism and mutation databases

BioMutaiMRE11A.
DMDMi17380137.

Proteomic databases

EPDiP49959.
MaxQBiP49959.
PaxDbiP49959.
PeptideAtlasiP49959.
PRIDEiP49959.

Protocols and materials databases

DNASUi4361.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000323929; ENSP00000325863; ENSG00000020922. [P49959-1]
ENST00000323977; ENSP00000326094; ENSG00000020922. [P49959-2]
ENST00000407439; ENSP00000385614; ENSG00000020922. [P49959-3]
GeneIDi4361.
KEGGihsa:4361.
UCSCiuc001peu.4. human. [P49959-1]

Organism-specific databases

CTDi4361.
DisGeNETi4361.
GeneCardsiMRE11A.
HGNCiHGNC:7230. MRE11A.
HPAiCAB004081.
HPA002691.
MalaCardsiMRE11A.
MIMi600814. gene.
604391. phenotype.
neXtProtiNX_P49959.
OpenTargetsiENSG00000020922.
Orphaneti251347. Ataxia-telangiectasia-like disorder.
145. Hereditary breast and ovarian cancer syndrome.
PharmGKBiPA30934.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2310. Eukaryota.
COG0420. LUCA.
GeneTreeiENSGT00390000017288.
HOGENOMiHOG000216581.
HOVERGENiHBG052508.
InParanoidiP49959.
KOiK10865.
OMAiNSRQPEK.
OrthoDBiEOG091G06P4.
PhylomeDBiP49959.
TreeFamiTF101105.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000020922-MONOMER.
ReactomeiR-HSA-1834949. Cytosolic sensors of pathogen-associated DNA.
R-HSA-2559586. DNA Damage/Telomere Stress Induced Senescence.
R-HSA-3270619. IRF3-mediated induction of type I IFN.
R-HSA-5685938. HDR through Single Strand Annealing (SSA).
R-HSA-5685939. HDR through MMEJ (alt-NHEJ).
R-HSA-5685942. HDR through Homologous Recombination (HRR).
R-HSA-5693548. Sensing of DNA Double Strand Breaks.
R-HSA-5693554. Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
R-HSA-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-HSA-5693568. Resolution of D-loop Structures through Holliday Junction Intermediates.
R-HSA-5693571. Nonhomologous End-Joining (NHEJ).
R-HSA-5693579. Homologous DNA Pairing and Strand Exchange.
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-69473. G2/M DNA damage checkpoint.
R-HSA-912446. Meiotic recombination.
SIGNORiP49959.

Miscellaneous databases

ChiTaRSiMRE11A. human.
GeneWikiiMRE11A.
GenomeRNAii4361.
PMAP-CutDBP49959.
PROiP49959.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000020922.
CleanExiHS_MRE11A.
ExpressionAtlasiP49959. baseline and differential.
GenevisibleiP49959. HS.

Family and domain databases

Gene3Di3.60.21.10. 2 hits.
InterProiIPR004843. Calcineurin-like_PHP_ApaH.
IPR029052. Metallo-depent_PP-like.
IPR003701. Mre11.
IPR007281. Mre11_DNA-bd.
[Graphical view]
PANTHERiPTHR10139:SF1. PTHR10139:SF1. 1 hit.
PfamiPF00149. Metallophos. 1 hit.
PF04152. Mre11_DNA_bind. 1 hit.
[Graphical view]
PIRSFiPIRSF000882. DSB_repair_MRE11. 1 hit.
SMARTiSM01347. Mre11_DNA_bind. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 2 hits.
TIGRFAMsiTIGR00583. mre11. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMRE11_HUMAN
AccessioniPrimary (citable) accession number: P49959
Secondary accession number(s): B3KTC7, O43475
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 26, 2001
Last modified: November 30, 2016
This is version 182 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.