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Protein

Double-strand break repair protein MRE11

Gene

MRE11

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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 MRE11. 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 MRE11 to prevent nucleolytic degradation past a given point (PubMed:9651580, PubMed:9590181, PubMed:9705271, PubMed:11741547, PubMed:29670289). 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).6 Publications

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.

Cofactori

Mn2+By similarity

Activity regulationi

Interaction with SAMHD1 stimulates the double-strand-specific 3'-5' exonuclease activity.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei129Proton donorBy similarity1

GO - Molecular functioni

  • 3'-5' exonuclease activity Source: CACAO
  • cadherin binding Source: BHF-UCL
  • double-stranded DNA binding Source: ProtInc
  • endodeoxyribonuclease activity Source: CACAO
  • identical protein binding Source: IntAct
  • 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

Keywordsi

Molecular functionEndonuclease, Exonuclease, Hydrolase, Nuclease
Biological processDNA damage, DNA repair, Host-virus interaction, Meiosis
LigandManganese

Enzyme and pathway databases

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 MRE11 (EC:3.1.-.-1 Publication)
Alternative name(s):
Double-strand break repair protein MRE11A
Meiotic recombination 11 homolog 1
Short name:
MRE11 homolog 1
Meiotic recombination 11 homolog A
Short name:
MRE11 homolog A
Gene namesi
Name:MRE11Imported
Synonyms:HNGS1, MRE11A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

EuPathDBiHostDB:ENSG00000020922.12
HGNCiHGNC:7230 MRE11
MIMi600814 gene
neXtProtiNX_P49959

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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 dbSNP:rs137852760EnsemblClinVar.1
Defects in MRE11 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 MRE11 has been found in patients with cerebellar vermis hypoplasia, ataxia and dysarthria.1 Publication

Keywords - Diseasei

Ciliopathy, Disease mutation

Organism-specific databases

DisGeNETi4361
MalaCardsiMRE11
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 MRE11Add BLAST707

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei2PhosphoserineBy similarity1
Cross-linki255Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei275PhosphoserineCombined sources1
Cross-linki416Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei619PhosphoserineCombined sources1
Cross-linki625Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei641PhosphoserineBy similarity1
Modified residuei649PhosphoserineCombined sources1
Modified residuei678PhosphoserineCombined sources1
Modified residuei688PhosphoserineCombined sources1
Modified residuei689PhosphoserineCombined sources1
Modified residuei701PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP49959
MaxQBiP49959
PaxDbiP49959
PeptideAtlasiP49959
PRIDEiP49959
ProteomicsDBi56186
56187 [P49959-2]

PTM databases

iPTMnetiP49959
PhosphoSitePlusiP49959

Miscellaneous databases

PMAP-CutDBiP49959

Expressioni

Gene expression databases

BgeeiENSG00000020922 Expressed in 208 organ(s), highest expression level in kidney
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/MRE11 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, MRE11 and NBN (PubMed:10783165). Found in a complex with TERF2 (PubMed:10888888). Interacts with DCLRE1C/Artemis and DCLRE1B/Apollo (PubMed:15456891, PubMed:15723659, PubMed:18469862). Interacts with ATF2 (PubMed:15916964). Interacts with EXD2 (PubMed:26807646). Interacts with MRNIP (PubMed:27568553). Interacts with SAMHD1; leading to stimulate 3'-5' exonuclease activity (PubMed:28834754, PubMed:29670289).14 Publications
(Microbial infection) Interacts with herpes simplex virus 1 protein UL12 (PubMed:20943970).1 Publication

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi110501, 128 interactors
CORUMiP49959
DIPiDIP-33238N
IntActiP49959, 40 interactors
MINTiP49959
STRINGi9606.ENSP00000325863

Chemistry databases

BindingDBiP49959

Structurei

Secondary structure

1708
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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
OMAiIHFFRHR
OrthoDBiEOG091G06P4
PhylomeDBiP49959
TreeFamiTF101105

Family and domain databases

Gene3Di3.30.110.110, 1 hit
3.60.21.10, 1 hit
InterProiView protein in InterPro
IPR004843 Calcineurin-like_PHP_ApaH
IPR029052 Metallo-depent_PP-like
IPR003701 Mre11
IPR007281 Mre11_DNA-bd
IPR038487 Mre11_DNA-bd_sf
PANTHERiPTHR10139 PTHR10139, 1 hit
PfamiView protein in Pfam
PF00149 Metallophos, 1 hit
PF04152 Mre11_DNA_bind, 1 hit
PIRSFiPIRSF000882 DSB_repair_MRE11, 1 hit
SMARTiView protein in SMART
SM01347 Mre11_DNA_bind, 1 hit
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

This entry has 3 described isoforms and 4 potential isoforms that are computationally mapped.iShow all

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

Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F8W7U8F8W7U8_HUMAN
Double-strand break repair protein ...
MRE11
707Annotation score:
F5GXT0F5GXT0_HUMAN
Double-strand break repair protein ...
MRE11
221Annotation score:
F5H256F5H256_HUMAN
Double-strand break repair protein ...
MRE11
127Annotation score:
F5H742F5H742_HUMAN
Double-strand break repair protein ...
MRE11
111Annotation score:

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 dbSNP:rs748434421EnsemblClinVar.1
Natural variantiVAR_008513117N → S in ATLD1. 1 PublicationCorresponds to variant dbSNP:rs137852760EnsemblClinVar.1
Natural variantiVAR_011626157M → V. Corresponds to variant dbSNP:rs147771140EnsemblClinVar.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 dbSNP:rs372000848EnsemblClinVar.1
Natural variantiVAR_019288468D → G1 PublicationCorresponds to variant dbSNP:rs1805367Ensembl.1
Natural variantiVAR_011627503R → H in cancer. 1 PublicationCorresponds to variant dbSNP:rs774057024EnsemblClinVar.1
Natural variantiVAR_011628572R → Q in cancer. 1 PublicationCorresponds to variant dbSNP:rs200085146EnsemblClinVar.1
Natural variantiVAR_019289698M → V1 PublicationCorresponds to variant dbSNP:rs1805362EnsemblClinVar.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

Similar proteinsi

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, 128 interactors
CORUMiP49959
DIPiDIP-33238N
IntActiP49959, 40 interactors
MINTiP49959
STRINGi9606.ENSP00000325863

Chemistry databases

BindingDBiP49959
ChEMBLiCHEMBL3308929

PTM databases

iPTMnetiP49959
PhosphoSitePlusiP49959

Polymorphism and mutation databases

BioMutaiMRE11A
DMDMi17380137

Proteomic databases

EPDiP49959
MaxQBiP49959
PaxDbiP49959
PeptideAtlasiP49959
PRIDEiP49959
ProteomicsDBi56186
56187 [P49959-2]

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
EuPathDBiHostDB:ENSG00000020922.12
GeneCardsiMRE11
HGNCiHGNC:7230 MRE11
HPAiCAB004081
HPA002691
MalaCardsiMRE11
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
OMAiIHFFRHR
OrthoDBiEOG091G06P4
PhylomeDBiP49959
TreeFamiTF101105

Enzyme and pathway databases

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-CutDBiP49959
PROiPR:P49959
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000020922 Expressed in 208 organ(s), highest expression level in kidney
CleanExiHS_MRE11A
ExpressionAtlasiP49959 baseline and differential
GenevisibleiP49959 HS

Family and domain databases

Gene3Di3.30.110.110, 1 hit
3.60.21.10, 1 hit
InterProiView protein in InterPro
IPR004843 Calcineurin-like_PHP_ApaH
IPR029052 Metallo-depent_PP-like
IPR003701 Mre11
IPR007281 Mre11_DNA-bd
IPR038487 Mre11_DNA-bd_sf
PANTHERiPTHR10139 PTHR10139, 1 hit
PfamiView protein in Pfam
PF00149 Metallophos, 1 hit
PF04152 Mre11_DNA_bind, 1 hit
PIRSFiPIRSF000882 DSB_repair_MRE11, 1 hit
SMARTiView protein in SMART
SM01347 Mre11_DNA_bind, 1 hit
TIGRFAMsiTIGR00583 mre11, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiMRE11_HUMAN
AccessioniPrimary (citable) accession number: P49959
Secondary accession number(s): B3KTC7, O43475
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 26, 2001
Last modified: September 12, 2018
This is version 200 of the entry and version 3 of the sequence. See 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health

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