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MRE11A

Protein FULL name:

double-strand break repair protein MRE11A isoform 2 [Homo sapiens].


MRE11A (Homo sapiens) is product of expression of MRE11A gene.

Human diseases related to this protein:

MRE11A is involved in:

DDS in Homo sapiens
     
HRR in Homo sapiens
     


Keywords:



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: 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.

INTERACTION: P24864:CCNE1; NbExp=1; IntAct=EBI-396513, EBI-519526; P16104:H2AFX; NbExp=1; IntAct=EBI-396513, EBI-494830; O60934:NBN; NbExp=1; IntAct=EBI-396513, EBI-494844;

SUBCELLULAR LOCATION: Nucleus (By similarity). Note=Localizes to discrete nuclear foci after treatment with genotoxic agents (By similarity).

PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.

DISEASE: Defects in MRE11A are a cause of ataxia telangiectasia- like disorder (ATLD) [MIM:604391]. ATLD is a disease with the same clinical feature than ataxia-telangiectasia but with a somewhat milder clinical course.

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.

SIMILARITY: Belongs to the MRE11/RAD32 family.

WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; [LINK]

WEB RESOURCE: Name=MRE11base; Note=MRE11A mutation db; [LINK]

WEB RESOURCE: Name=NIEHS-SNPs; [LINK]


NCBI GenPept GI number(s): 24234690
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot P49959 P49959
PFAM: - P49959 (Link - using uniprot id)
InterPro: - P49959 (Link - using uniprot id)
CATH: None  
SCOP: None  
PDB: - -


Protein sequence:
MSTADALDDENTFKILVATDIHLGFMEKDAVRGNDTFVTLDEILRLAQEN
EVDFILLGGDLFHENKPSRKTLHTCLELLRKYCMGDRPVQFEILSDQSVN
FGFSKFPWVNYQDGNLNISIPVFSIHGNHDDPTGADALCALDILSCAGFV
NHFGRSMSVEKIDISPVLLQKGSTKIALYGLGSIPDERLYRMFVNKKVTM
LRPKEDENSWFNLFVIHQNRSKHGSTNFIPEQFLDDFIDLVIWGHEHECK
IAPTKNEQQLFYISQPGSSVVTSLSPGEAVKKHVGLLRIKGRKMNMHKIP
LHTVRQFFMEDIVLANHPDIFNPDNPKVTQAIQSFCLEKIEEMLENAERE
RLGNSHQPEKPLVRLRVDYSGGFEPFSVLRFSQKFVDRVANPKDIIHFFR
HREQKEKTGEEINFGKLITKPSEGTTLRVEDLVKQYFQTAEKNVQLSLLT
ERGMGEAVQEFVDKEEKDAIEELVKYQLEKTQRFLKERHIDALEDKIDEE
VRRFRETRQKNTNEEDDEVREAMTRARALRSQSEESASAFSADDLMSIDL
AEQMANDSDDSISAATNKGRGRGRGRRGGRGQNSASRGGSQRGRAFKSTR
QQPSRNVTTKNYSEVIEVDESDVEEDIFPTTSKTDQRWSSTSSSKIMSQS
QVSKGVDFESSEDDDDDPFMNTSSLRRNRR

MRE11A (Homo sapiens) is able to recognize following damages:
MRE11A (Homo sapiens) belongs to following protein families:
References:

Title Authors Journal
Isolation and characterization of the human MRE11 homologue. Petrini JH, Walsh ME, DiMare C, Chen XN, Korenberg JR, Weaver DT Genomics Sept. 1, 1995
The 3' to 5' exonuclease activity of Mre 11 facilitates repair of DNA double-strand breaks. Paull TT, Gellert M Mol Cell June 1, 1998
The DNA double-strand break repair gene hMRE11 is mutated in individuals with an ataxia-telangiectasia-like disorder. Stewart GS, Maser RS, Stankovic T, Bressan DA, Kaplan MI, Jaspers NG, Raams A, Byrd PJ, Petrini JH, Taylor AM Cell Dec. 10, 1999
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 Feb. 1, 2001
hMRE11: genomic structure and a null mutation identified in a transcript protected from nonsense-mediated mRNA decay. Pitts SA, Kullar HS, Stankovic T, Stewart GS, Last JI, Bedenham T, Armstrong SJ, Piane M, Chessa L, Taylor AM, Byrd PJ Hum Mol Genet May 15, 2001
Mutation screening of Mre11 complex genes: indication of RAD50 involvement in breast and ovarian cancer susceptibility. Heikkinen K, Karppinen SM, Soini Y, Makinen M, Winqvist R J Med Genet Dec. 1, 2003
Large-scale characterization of HeLa cell nuclear phosphoproteins. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP Proc Natl Acad Sci U S A Aug. 17, 2004
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J Genome Res Oct. 1, 2004
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 MD, Legerski RJ Mol Cell Biol Oct. 1, 2004
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 Jan. 1, 2005
Global phosphoproteome of HT-29 human colon adenocarcinoma cells. Kim JE, Tannenbaum SR, White FM J Proteome Res Jan. 1, 2005
The consensus coding sequences of human breast and colorectal cancers. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE Science Oct. 13, 2006
Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M Cell Nov. 3, 2006
ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ Science May 25, 2007
A quantitative atlas of mitotic phosphorylation. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP Proc Natl Acad Sci U S A Aug. 5, 2008
Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M Mol Cell Aug. 8, 2008
Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK Sci Signal Jan. 1, 2009
Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S Anal Chem June 1, 2009


Last modification of this entry: Oct. 13, 2010.

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