P49959 (MRE11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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:	HNGS1, MRE11

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	708 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.8 Ref.9 Ref.12
Subcellular location	Nucleus By similarity. Note: Localizes to discrete nuclear foci after treatment with genotoxic agents By similarity.
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.19 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.18
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 process	DNA damage DNA repair Meiosis
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Ciliopathy Disease mutation
Ligand	Manganese
Molecular function	Endonuclease Exonuclease Hydrolase Nuclease
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA duplex unwinding Inferred from mutant phenotype PubMed 15790808. Source: BHF-UCL cell cycle checkpoint Inferred from electronic annotation. Source: Compara cell proliferation Inferred from electronic annotation. Source: Compara 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 negative regulation of DNA endoreduplication Inferred from mutant phenotype PubMed 15917200. Source: BHF-UCL 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 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: Compara telomere maintenance via telomerase Traceable author statement PubMed 9705271PubMed 9931460. Source: ProtInc
Cellular_component	Mre11 complex Non-traceable author statement PubMed 15790808. Source: BHF-UCL nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	3'-5' exonuclease activity Traceable author statement Ref.4. Source: ProtInc double-stranded DNA binding Traceable author statement PubMed 10802669. Source: ProtInc manganese ion binding Inferred from electronic annotation. Source: InterPro single-stranded DNA specific endodeoxyribonuclease activity Traceable author statement PubMed 9705271. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NBN	O60934	2	EBI-396513,EBI-494844

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 708

708

Double-strand break repair protein MRE11A

PRO_0000138672

Sites

Active site

129

1

Proton donor By similarity

Amino acid modifications

Modified residue

649

1

Phosphoserine Ref.13 Ref.14

Modified residue

688

1

Phosphoserine Ref.13 Ref.14 Ref.15 Ref.17

Modified residue

689

1

Phosphoserine Ref.13 Ref.14 Ref.15 Ref.17

Modified residue

701

1

Phosphoserine Ref.13

Natural variations

Alternative sequence

595 – 622

28

Missing in isoform 2.

VSP_003262

Natural variant

104

1

S → C in cancer. Ref.20

VAR_011625

Natural variant

117

1

N → S in ATLD. Ref.19

VAR_008513

Natural variant

157

1

M → V.

VAR_011626

Natural variant

237

1

F → C in a breast cancer sample; somatic mutation. Ref.22

VAR_036416

Natural variant

302

1

H → Y in a breast cancer sample; somatic mutation. Ref.22

VAR_036417

Natural variant

305

1

R → W in ovarian cancer. Ref.21

VAR_025528

Natural variant

468

1

D → G. Ref.6
Corresponds to variant rs1805367 [ dbSNP | Ensembl ].

VAR_019288

Natural variant

503

1

R → H in cancer. Ref.20

VAR_011627

Natural variant

572

1

R → Q in cancer. Ref.20

VAR_011628

Natural variant

698

1

M → V. Ref.6
Corresponds to variant rs1805362 [ dbSNP | Ensembl ].

VAR_019289

Experimental info

Sequence conflict

31

1

V → A in AAC78721. Ref.1

Secondary structure

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708

Helix Strand Turn

Details...

Helix

9 – 11

3

Beta strand

12 – 18

7

Turn

24 – 26

3

Turn

30 – 34

5

Helix

35 – 49

15

Beta strand

53 – 57

5

Beta strand

62 – 66

5

Helix

69 – 83

15

Beta strand

122 – 124

3

Beta strand

128 – 130

3

Turn

134 – 137

4

Helix

140 – 147

8

Beta strand

149 – 152

4

Beta strand

162 – 164

3

Beta strand

167 – 171

5

Beta strand

174 – 181

8

Helix

186 – 194

9

Beta strand

198 – 200

3

Helix

207 – 209

3

Beta strand

210 – 216

7

Beta strand

223 – 228

6

Helix

231 – 233

3

Beta strand

240 – 243

4

Beta strand

250 – 255

6

Turn

257 – 259

3

Beta strand

262 – 265

4

Helix

276 – 279

4

Beta strand

283 – 290

8

Beta strand

293 – 300

8

Beta strand

302 – 304

3

Beta strand

307 – 313

7

Helix

314 – 316

3

Turn

318 – 320

3

Helix

328 – 350

23

Turn

351 – 353

3

Beta strand

355 – 357

3

Beta strand

362 – 368

7

Turn

370 – 372

3

Helix

379 – 385

7

Turn

386 – 388

3

Beta strand

392 – 399

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 26, 2001. Version 3. Checksum: D94ABFBDDF6106AD	FASTA	708	80,593
	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
	Isoform 2 [UniParc]. Checksum: B36BA7EC8CE79BEE	FASTA	680	77,642
	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 QRGRAFKSTR 610 620 630 640 650 660 QQPSRNVTTK NYSEVIEVDE SDVEEDIFPT TSKTDQRWSS TSSSKIMSQS QVSKGVDFES 670 680 SEDDDDDPFM NTSSLRRNRR

References

	« Hide 'large scale' referencesShow '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]	"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.
[11]	"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.
[12]	"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.
[13]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[15]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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].
[17]	"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, MASS SPECTROMETRY.
[18]	"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.
[19]	"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.
[20]	"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.
[21]	"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.
[22]	"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. , 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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

MRE11base

MRE11A mutation db

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00218853.
IPI00940798.

RefSeq

NP_005581.2. NM_005590.3.
NP_005582.1. NM_005591.3.

UniGene

Hs.192649.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3T1I	X-ray	3.00	A/B/C/D	1-411	[»]

ProteinModelPortal

P49959.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33238N.

IntAct

P49959. 7 interactions.

MINT

MINT-131851.

STRING

9606.ENSP00000325863.

PTM databases

PhosphoSite

P49959.

Polymorphism databases

DMDM

17380137.

Proteomic databases

PaxDb

P49959.

PRIDE

P49959.

Protocols and materials databases

DNASU

4361.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000323929; ENSP00000325863; ENSG00000020922.
ENST00000323977; ENSP00000326094; ENSG00000020922.

GeneID

4361.

KEGG

hsa:4361.

UCSC

uc001peu.2. human.
uc001pev.2. human.

Organism-specific databases

CTD

4361.

GeneCards

GC11M094150.

HGNC

HGNC:7230. MRE11A.

HPA

CAB004081.
HPA002691.

MIM

600814. gene.
604391. phenotype.

neXtProt

NX_P49959.

Orphanet

251347. Ataxia-telangiectasia-like disorder.
145. Hereditary breast and ovarian cancer syndrome.

PharmGKB

PA30934.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0420.

HOGENOM

HOG000216581.

HOVERGEN

HBG052508.

InParanoid

P49959.

KO

K10865.

PhylomeDB

P49959.

Enzyme and pathway databases

Pathway_Interaction_DB

bard1pathway. BARD1 signaling events.
telomerasepathway. Regulation of Telomerase.

Reactome

REACT_111183. Meiosis.
REACT_216. DNA Repair.

Gene expression databases

ArrayExpress

P49959.

Bgee

P49959.

CleanEx

HS_MRE11A.

Genevestigator

P49959.

GermOnline

ENSG00000020922. Homo sapiens.

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

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Other

ChiTaRS

MRE11A. human.

GenomeRNAi

4361.

NextBio

17163.

PMAP-CutDB

P49959.

SOURCE

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Entry information

Entry name

MRE11_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 143 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.