Double-strand break repair protein MRE11A

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Q9JIM0 (MRE11_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 88. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	Mre11a
Synonyms:	Mre11

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	706 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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 By similarity.
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. Interacts with DCLRE1C/Artemis and DCLRE1B/Apollo By similarity.
Subcellular location	Nucleus By similarity. Note: Localizes to discrete nuclear foci after treatment with genotoxic agents By similarity.
Sequence similarities	Belongs to the MRE11/RAD32 family.

Ontologies

Keywords
Biological process	DNA damage DNA repair Meiosis
Cellular component	Nucleus
Ligand	Manganese
Molecular function	Endonuclease Exonuclease Hydrolase Nuclease
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle checkpoint Traceable author statement Ref.1. Source: RGD double-strand break repair Traceable author statement Ref.1. Source: RGD heart development Inferred from expression pattern Ref.1. Source: RGD nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC reciprocal meiotic recombination Traceable author statement Ref.1. Source: RGD telomere maintenance Traceable author statement Ref.1. Source: RGD
Cellular_component	Mre11 complex Traceable author statement Ref.1. Source: RGD condensed nuclear chromosome Inferred from direct assay PubMed 10855503. Source: RGD nuclear chromatin Inferred from direct assay PubMed 10855503. Source: RGD nucleoplasm Inferred from direct assay PubMed 16706843. Source: RGD perinuclear region of cytoplasm Inferred from direct assay PubMed 18212738. Source: RGD
Molecular_function	endonuclease activity Inferred from electronic annotation. Source: UniProtKB-KW exonuclease activity Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 706

706

Double-strand break repair protein MRE11A

PRO_0000138675

Sites

Active site

129

Proton donor By similarity

Amino acid modifications

Modified residue

648

Phosphoserine By similarity

Modified residue

686

Phosphoserine By similarity

Modified residue

699

Phosphoserine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q9JIM0 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 0183A41BC015FDA0
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FASTA

706

80,122

        10         20         30         40         50         60 
MSPTDPLDDE DTFKILVATD IHLGFMEKDA VRGNDTFVTF DEILRLALEN EVDFILLGGD 

        70         80         90        100        110        120 
LFHENKPSRK TLHSCLELLR KYCMGDRPVQ FEIISDQSVN FGFSKFPWVN YRDGNLNISI 

       130        140        150        160        170        180 
PVFSIHGNHD DPTGADALCA LDVLSCAGFV NHFGRSMSVE KVDISPVLLQ KGSTKLALYG 

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

       250        260        270        280        290        300 
VIWGHEHECK IGPTRNEQQL FYVSQPGSSV VTALSPGETV KKHVGLLRVK GRKMNMQKLP 

       310        320        330        340        350        360 
LRTVRQFFME DVVLANHPSL FNPDNPKVTQ AIQSFCLEKI EEMLDSAERE RLGNPQQPEK 

       370        380        390        400        410        420 
PLIRLRVDYS GGFEPFNVLR FSQKFVDRVA NPKDVIHFFR HREQKGKTGE EINFGKLIIK 

       430        440        450        460        470        480 
PASEGTTLRV EDLVKQYFQT AEKNVQLSLL TERGMGEAVQ EFVDKEEKDA IEELVKYQLE 

       490        500        510        520        530        540 
KTQRFLKERH IDALEDKIDE EVRRFRESRQ RNTNEEDDEV REAMSRARAL RSQSENAASA 

       550        560        570        580        590        600 
FSADDLSFDI TEQTADDSDD SQSAVPSRGR GRGRGRRGGR GQSTAPRGGS QRGRDTGLGI 

       610        620        630        640        650        660 
STRGRSSKAT ASTSRNMSII DAFRSTRQQP SRNVATKNYS ETIEVDESDD DDSFPTSSRA 

       670        680        690        700 
DQRWSGTAPS KRMSQSQTAK GVDFESDEDD DDDPFMSGSC PRRNRR

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References

[1]	"The MRE11-NBS1-RAD50 pathway is perturbed in SV40 large T antigen-immortalized AT-1, AT-2 and HL-1 cardiomyocytes." Lanson N.A. Jr., Egeland D.B., Royals B.A., Claycomb W.C. Nucleic Acids Res. 28:2882-2892(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF218574 mRNA. Translation: AAF91227.1.
IPI	IPI00200709.
RefSeq	NP_071615.1. NM_022279.1.
UniGene	Rn.209040.
3D structure databases
ProteinModelPortal	Q9JIM0.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000012940.
PTM databases
PhosphoSite	Q9JIM0.
Proteomic databases
PRIDE	Q9JIM0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	64046.
KEGG	rno:64046.
UCSC	RGD:69263. rat.
Organism-specific databases
CTD	4361.
RGD	69263. Mre11a.
Phylogenomic databases
eggNOG	COG0420.
HOGENOM	HOG000216581.
HOVERGEN	HBG052508.
InParanoid	Q9JIM0.
KO	K10865.
OrthoDB	EOG46WZ82.
Gene expression databases
ArrayExpress	Q9JIM0.
Genevestigator	Q9JIM0.
GermOnline	ENSRNOG00000009506. Rattus norvegicus.
Family and domain databases
InterPro	IPR003701. DNA_repair_Mre11. IPR004843. Metallo_PEstase_dom. IPR007281. Mre11_DNA-bd. [Graphical view]
PANTHER	PTHR10139. PTHR10139. 1 hit.
Pfam	PF00149. Metallophos. 1 hit. PF04152. Mre11_DNA_bind. 1 hit. [Graphical view]
PIRSF	PIRSF000882. DSB_repair_MRE11. 1 hit.
TIGRFAMs	TIGR00583. mre11. 1 hit.
ProtoNet	Search...
Other
NextBio	612709.

Entry information

Entry name

MRE11_RAT

Accession

Primary (citable) accession number: Q9JIM0

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	October 1, 2000
Last modified:	April 3, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents