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Double-strand break repair protein MRE11 (EC 3.1.-.-) (Double-strand break repair protein MRE11A) (Meiotic recombination 11 homolog 1) (MRE11 homolog 1) (Meiotic recombination 11 homolog A) (MRE11 homolog A)

 MRE11_HUMAN             Reviewed;         708 AA.
P49959; B3KTC7; O43475;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
26-SEP-2001, sequence version 3.
29-SEP-2021, entry version 223.
RecName: Full=Double-strand break repair protein MRE11;
EC=3.1.-.- {ECO:0000269|PubMed:29670289};
AltName: Full=Double-strand break repair protein MRE11A;
AltName: Full=Meiotic recombination 11 homolog 1;
Short=MRE11 homolog 1;
AltName: Full=Meiotic recombination 11 homolog A;
Short=MRE11 homolog A;
Name=MRE11 {ECO:0000312|HGNC:HGNC:7230}; Synonyms=HNGS1, MRE11A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=8530104; DOI=10.1006/geno.1995.1217;
Petrini J.H.J., Walsh M.E., Dimare C., Chen X.-N., Korenberg J.R.,
Weaver D.T.;
"Isolation and characterization of the human MRE11 homologue.";
Genomics 29:80-86(1995).
[2]
SEQUENCE REVISION TO C-TERMINUS.
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.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Chamankhah M., Wei Y., Xiao W.;
"Molecular cloning and functional characterization of hNGS1, a yeast and
human MRE11 homolog.";
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND INTERACTION WITH
RAD50.
PubMed=9651580; DOI=10.1016/s1097-2765(00)80097-0;
Paull T.T., Gellert M.;
"The 3' to 5' exonuclease activity of Mre 11 facilitates repair of DNA
double-strand breaks.";
Mol. Cell 1:969-979(1998).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=11371508; DOI=10.1093/hmg/10.11.1155;
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.;
"hMRE11: genomic structure and a null mutation identified in a transcript
protected from nonsense-mediated mRNA decay.";
Hum. Mol. Genet. 10:1155-1162(2001).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLY-468 AND VAL-698.
NIEHS SNPs program;
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
Hattori M., Rogers J., Lander E.S., Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
FUNCTION IN DSB REPAIR, AND IDENTIFICATION IN THE MRN COMPLEX WITH RAD50
AND NBN.
PubMed=9590181; DOI=10.1016/s0092-8674(00)81175-7;
Carney J.P., Maser R.S., Olivares H., Davis E.M., Le Beau M.,
Yates J.R. III, Hays L., Morgan W.F., Petrini J.H.J.;
"The hMre11/hRad50 protein complex and Nijmegen breakage syndrome: linkage
of double-strand break repair to the cellular DNA damage response.";
Cell 93:477-486(1998).
[11]
FUNCTION IN DSB REPAIR, AND IDENTIFICATION IN THE MRN COMPLEX WITH RAD50
AND NBN.
PubMed=9705271; DOI=10.1074/jbc.273.34.21447;
Trujillo K.M., Yuan S.-S.F., Lee E.Y.-H.P., Sung P.;
"Nuclease activities in a complex of human recombination and DNA repair
factors Rad50, Mre11, and p95.";
J. Biol. Chem. 273:21447-21450(1998).
[12]
SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE BASC COMPLEX WITH BRCA1;
MSH2; MSH6; MLH1; ATM; BLM; RAD50 AND NBN.
PubMed=10783165;
Wang Y., Cortez D., Yazdi P., Neff N., Elledge S.J., Qin J.;
"BASC, a super complex of BRCA1-associated proteins involved in the
recognition and repair of aberrant DNA structures.";
Genes Dev. 14:927-939(2000).
[13]
IDENTIFICATION IN THE MRN COMPLEX WITH RAD50 AND NBN.
PubMed=10839544; DOI=10.1038/35013083;
Zhao S., Weng Y.-C., Yuan S.-S.F., Lin Y.-T., Hsu H.-C., Lin S.-C.,
Gerbino E., Song M.-H., Zdzienicka M.Z., Gatti R.A., Shay J.W., Ziv Y.,
Shiloh Y., Lee E.Y.-H.P.;
"Functional link between ataxia-telangiectasia and Nijmegen breakage
syndrome gene products.";
Nature 405:473-477(2000).
[14]
FUNCTION IN TELOMERES, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION
IN THE A COMPLEX WITH TERF2, AND SUBCELLULAR LOCATION.
PubMed=10888888; DOI=10.1038/77139;
Zhu X.-D., Kuester B., Mann M., Petrini J.H.J., de Lange T.;
"Cell-cycle-regulated association of RAD50/MRE11/NBS1 with TRF2 and human
telomeres.";
Nat. Genet. 25:347-352(2000).
[15]
FUNCTION.
PubMed=11741547; DOI=10.1016/s1097-2765(01)00381-1;
de Jager M., van Noort J., van Gent D.C., Dekker C., Kanaar R., Wyman C.;
"Human Rad50/Mre11 is a flexible complex that can tether DNA ends.";
Mol. Cell 8:1129-1135(2001).
[16]
INTERACTION WITH DCLRE1C.
PubMed=15456891; DOI=10.1128/mcb.24.20.9207-9220.2004;
Zhang X., Succi J., Feng Z., Prithivirajsingh S., Story M.D.,
Legerski R.J.;
"Artemis is a phosphorylation target of ATM and ATR and is involved in the
G2/M DNA damage checkpoint response.";
Mol. Cell. Biol. 24:9207-9220(2004).
[17]
FUNCTION IN ATM ACTIVATION.
PubMed=15064416; DOI=10.1126/science.1091496;
Lee J.-H., Paull T.T.;
"Direct activation of the ATM protein kinase by the Mre11/Rad50/Nbs1
complex.";
Science 304:93-96(2004).
[18]
INTERACTION WITH DCLRE1C.
PubMed=15723659; DOI=10.1111/j.1349-7006.2005.00019.x;
Chen L., Morio T., Minegishi Y., Nakada S., Nagasawa M., Komatsu K.,
Chessa L., Villa A., Lecis D., Delia D., Mizutani S.;
"Ataxia-telangiectasia-mutated dependent phosphorylation of Artemis in
response to DNA damage.";
Cancer Sci. 96:134-141(2005).
[19]
INTERACTION WITH ATF2, AND SUBCELLULAR LOCATION.
PubMed=15916964; DOI=10.1016/j.molcel.2005.04.015;
Bhoumik A., Takahashi S., Breitweiser W., Shiloh Y., Jones N., Ronai Z.;
"ATM-dependent phosphorylation of ATF2 is required for the DNA damage
response.";
Mol. Cell 18:577-587(2005).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling
networks.";
Cell 127:635-648(2006).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the
kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[22]
INTERACTION WITH DCLRE1B.
PubMed=18469862; DOI=10.1038/onc.2008.139;
Bae J.B., Mukhopadhyay S.S., Liu L., Zhang N., Tan J., Akhter S., Liu X.,
Shen X., Li L., Legerski R.J.;
"Snm1B/Apollo mediates replication fork collapse and S Phase checkpoint
activation in response to DNA interstrand cross-links.";
Oncogene 27:5045-5056(2008).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649; SER-688; SER-689 AND
SER-701, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[24]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in a
refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649; SER-688 AND SER-689, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[26]
INTERACTION WITH HERPES SIMPLEX VIRUS 1 UL12.
PubMed=20943970; DOI=10.1128/jvi.01506-10;
Balasubramanian N., Bai P., Buchek G., Korza G., Weller S.K.;
"Physical interaction between the herpes simplex virus type 1 exonuclease,
UL12, and the DNA double-strand break-sensing MRN complex.";
J. Virol. 84:12504-12514(2010).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-688 AND SER-689, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full phosphorylation
site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-688 AND SER-689, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
"System-wide temporal characterization of the proteome and phosphoproteome
of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[30]
INVOLVEMENT IN NPHP-RC.
PubMed=22863007; DOI=10.1016/j.cell.2012.06.028;
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.;
"Exome capture reveals ZNF423 and CEP164 mutations, linking renal
ciliopathies to DNA damage response signaling.";
Cell 150:533-548(2012).
[31]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.m111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275; SER-619; SER-678;
SER-688 AND SER-689, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649; SER-688 AND SER-689, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[34]
IDENTIFICATION IN THE MRN COMPLEX, INTERACTION WITH MCM9, AND SUBCELLULAR
LOCATION.
PubMed=26215093; DOI=10.1038/ncomms8744;
Lee K.Y., Im J.S., Shibata E., Park J., Handa N., Kowalczykowski S.C.,
Dutta A.;
"MCM8-9 complex promotes resection of double-strand break ends by MRE11-
RAD50-NBS1 complex.";
Nat. Commun. 6:7744-7744(2015).
[35]
INTERACTION WITH MRNIP.
PubMed=27568553; DOI=10.1016/j.celrep.2016.07.087;
Staples C.J., Barone G., Myers K.N., Ganesh A., Gibbs-Seymour I.,
Patil A.A., Beveridge R.D., Daye C., Beniston R., Maslen S., Ahel I.,
Skehel J.M., Collis S.J.;
"MRNIP/C5orf45 interacts with the MRN complex and contributes to the DNA
damage response.";
Cell Rep. 16:2565-2575(2016).
[36]
FUNCTION, AND INTERACTION WITH EXD2.
PubMed=26807646; DOI=10.1038/ncb3303;
Broderick R., Nieminuszczy J., Baddock H.T., Deshpande R.A., Gileadi O.,
Paull T.T., McHugh P.J., Niedzwiedz W.;
"EXD2 promotes homologous recombination by facilitating DNA end
resection.";
Nat. Cell Biol. 18:271-280(2016).
[37]
INTERACTION WITH SAMHD1.
PubMed=28834754; DOI=10.1016/j.celrep.2017.08.008;
Daddacha W., Koyen A.E., Bastien A.J., Head P.E., Dhere V.R., Nabeta G.N.,
Connolly E.C., Werner E., Madden M.Z., Daly M.B., Minten E.V., Whelan D.R.,
Schlafstein A.J., Zhang H., Anand R., Doronio C., Withers A.E., Shepard C.,
Sundaram R.K., Deng X., Dynan W.S., Wang Y., Bindra R.S., Cejka P.,
Rothenberg E., Doetsch P.W., Kim B., Yu D.S.;
"SAMHD1 promotes DNA end resection to facilitate DNA repair by homologous
recombination.";
Cell Rep. 20:1921-1935(2017).
[38]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-255; LYS-416 AND LYS-625, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-modification
with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[39]
FUNCTION, ACTIVITY REGULATION, AND INTERACTION WITH SAMHD1.
PubMed=29670289; DOI=10.1038/s41586-018-0050-1;
Coquel F., Silva M.J., Techer H., Zadorozhny K., Sharma S.,
Nieminuszczy J., Mettling C., Dardillac E., Barthe A., Schmitz A.L.,
Promonet A., Cribier A., Sarrazin A., Niedzwiedz W., Lopez B., Costanzo V.,
Krejci L., Chabes A., Benkirane M., Lin Y.L., Pasero P.;
"SAMHD1 acts at stalled replication forks to prevent interferon
induction.";
Nature 557:57-61(2018).
[40]
FUNCTION, UBIQUITINATION, SUBCELLULAR LOCATION, AND INTERACTION WITH
UBQLN4.
PubMed=30612738; DOI=10.1016/j.cell.2018.11.024;
Jachimowicz R.D., Beleggia F., Isensee J., Velpula B.B., Goergens J.,
Bustos M.A., Doll M.A., Shenoy A., Checa-Rodriguez C., Wiederstein J.L.,
Baranes-Bachar K., Bartenhagen C., Hertwig F., Teper N., Nishi T.,
Schmitt A., Distelmaier F., Luedecke H.J., Albrecht B., Krueger M.,
Schumacher B., Geiger T., Hoon D.S.B., Huertas P., Fischer M., Hucho T.,
Peifer M., Ziv Y., Reinhardt H.C., Wieczorek D., Shiloh Y.;
"UBQLN4 represses homologous recombination and is overexpressed in
aggressive tumors.";
Cell 0:0-0(2019).
[41]
VARIANT ATLD1 SER-117.
PubMed=10612394; DOI=10.1016/s0092-8674(00)81547-0;
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.;
"The DNA double-strand break repair gene hMRE11 is mutated in individuals
with an ataxia-telangiectasia-like disorder.";
Cell 99:577-587(1999).
[42]
VARIANTS CANCER CYS-104; HIS-503 AND GLN-572.
PubMed=11196167;
Fukuda T., Sumiyoshi T., Takahashi M., Kataoka T., Asahara T., Inui H.,
Watatani M., Yasutomi M., Kamada N., Miyagawa K.;
"Alterations of the double-strand break repair gene MRE11 in cancer.";
Cancer Res. 61:23-26(2001).
[43]
VARIANT OVARIAN CANCER TRP-305.
PubMed=14684699; DOI=10.1136/jmg.40.12.e131;
Heikkinen K., Karppinen S.-M., Soini Y., Maekinen M., Winqvist R.;
"Mutation screening of Mre11 complex genes: indication of RAD50 involvement
in breast and ovarian cancer susceptibility.";
J. Med. Genet. 40:E131-E131(2003).
[44]
VARIANTS [LARGE SCALE ANALYSIS] CYS-237 AND TYR-302.
PubMed=16959974; DOI=10.1126/science.1133427;
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.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
-!- 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 (PubMed:9651580, PubMed:9590181,
PubMed:9705271, PubMed:11741547, PubMed:29670289). The complex
possesses single-strand endonuclease activity and double-strand-
specific 3'-5' exonuclease activity, which are provided by MRE11
(PubMed:9651580, PubMed:9590181, PubMed:9705271, PubMed:11741547,
PubMed:29670289). RAD50 may be required to bind DNA ends and hold them
in close proximity (PubMed:9651580, PubMed:9590181, PubMed:9705271,
PubMed:11741547, PubMed:29670289). 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, PubMed:30612738). 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).
{ECO:0000269|PubMed:10888888, ECO:0000269|PubMed:11741547,
ECO:0000269|PubMed:15064416, ECO:0000269|PubMed:29670289,
ECO:0000269|PubMed:30612738, ECO:0000269|PubMed:9590181,
ECO:0000269|PubMed:9705271}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- ACTIVITY REGULATION: Interaction with SAMHD1 stimulates the double-
strand-specific 3'-5' exonuclease activity.
{ECO:0000269|PubMed:29670289}.
-!- SUBUNIT: Component of the MRN complex composed of two heterodimers
RAD50/MRE11 associated with a single NBN (PubMed:9651580,
PubMed:9590181, PubMed:9705271, PubMed:10839544, PubMed:26215093). As
part of the MRN complex, interacts with MCM9; the interaction recruits
the complex to DNA repair sites (PubMed:26215093). 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). Interacts (when ubiquitinated) with UBQLN4 (via its
UBA domain) (PubMed:30612738). Interacts with CYREN (via XLF motif) (By
similarity). {ECO:0000250|UniProtKB:Q61216,
ECO:0000269|PubMed:10783165, ECO:0000269|PubMed:10839544,
ECO:0000269|PubMed:10888888, ECO:0000269|PubMed:15456891,
ECO:0000269|PubMed:15723659, ECO:0000269|PubMed:15916964,
ECO:0000269|PubMed:18469862, ECO:0000269|PubMed:26215093,
ECO:0000269|PubMed:26807646, ECO:0000269|PubMed:27568553,
ECO:0000269|PubMed:28834754, ECO:0000269|PubMed:29670289,
ECO:0000269|PubMed:30612738, ECO:0000269|PubMed:9590181,
ECO:0000269|PubMed:9651580, ECO:0000269|PubMed:9705271}.
-!- SUBUNIT: (Microbial infection) Interacts with herpes simplex virus 1
protein UL12 (PubMed:20943970). {ECO:0000269|PubMed:20943970}.
-!- INTERACTION:
P49959; Q9BXW9: FANCD2; NbExp=6; IntAct=EBI-396513, EBI-359343;
P49959; P16104: H2AX; NbExp=7; IntAct=EBI-396513, EBI-494830;
P49959; P42858: HTT; NbExp=5; IntAct=EBI-396513, EBI-466029;
P49959; P49959: MRE11; NbExp=3; IntAct=EBI-396513, EBI-396513;
P49959; O60934: NBN; NbExp=5; IntAct=EBI-396513, EBI-494844;
P49959; O75943: RAD17; NbExp=2; IntAct=EBI-396513, EBI-968231;
P49959; Q99708: RBBP8; NbExp=3; IntAct=EBI-396513, EBI-745715;
P49959; P03243-1; Xeno; NbExp=2; IntAct=EBI-396513, EBI-1927377;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10783165,
ECO:0000269|PubMed:26215093}. Chromosome, telomere
{ECO:0000269|PubMed:10888888}. Chromosome {ECO:0000269|PubMed:26215093,
ECO:0000269|PubMed:30612738}. Note=Localizes to discrete nuclear foci
after treatment with genotoxic agents. {ECO:0000269|PubMed:10783165,
ECO:0000269|PubMed:26215093, ECO:0000269|PubMed:30612738}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P49959-1; Sequence=Displayed;
Name=2;
IsoId=P49959-2; Sequence=VSP_003262;
Name=3;
IsoId=P49959-3; Sequence=VSP_057350;
-!- PTM: Ubiquitinated following DNA damage. Ubiquitination triggers
interaction with UBQLN4, leading to MRE11 removal from chromatin and
degradation by the proteasome. {ECO:0000269|PubMed:30612738}.
-!- DISEASE: Ataxia-telangiectasia-like disorder 1 (ATLD1) [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. {ECO:0000269|PubMed:10612394}.
Note=The disease is caused by variants affecting the gene represented
in this entry.
-!- DISEASE: Note=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. {ECO:0000269|PubMed:22863007}.
-!- 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. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MRE11ID247.html";
-!- WEB RESOURCE: Name=MRE11base; Note=MRE11A mutation db;
URL="http://structure.bmc.lu.se/idbase/MRE11Abase/";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/mre11a/";
---------------------------------------------------------------------------
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EMBL; U37359; AAC78721.1; -; mRNA.
EMBL; AF022778; AAD10197.1; -; mRNA.
EMBL; AF073362; AAC36249.1; -; mRNA.
EMBL; AF303395; AAK18790.1; -; Genomic_DNA.
EMBL; AF303379; AAK18790.1; JOINED; Genomic_DNA.
EMBL; AF303380; AAK18790.1; JOINED; Genomic_DNA.
EMBL; AF303381; AAK18790.1; JOINED; Genomic_DNA.
EMBL; AF303382; AAK18790.1; JOINED; Genomic_DNA.
EMBL; AF303383; AAK18790.1; JOINED; Genomic_DNA.
EMBL; AF303384; AAK18790.1; JOINED; Genomic_DNA.
EMBL; AF303385; AAK18790.1; JOINED; Genomic_DNA.
EMBL; AF303386; AAK18790.1; JOINED; Genomic_DNA.
EMBL; AF303387; AAK18790.1; JOINED; Genomic_DNA.
EMBL; AF303388; AAK18790.1; JOINED; Genomic_DNA.
EMBL; AF303389; AAK18790.1; JOINED; Genomic_DNA.
EMBL; AF303390; AAK18790.1; JOINED; Genomic_DNA.
EMBL; AF303391; AAK18790.1; JOINED; Genomic_DNA.
EMBL; AF303392; AAK18790.1; JOINED; Genomic_DNA.
EMBL; AF303393; AAK18790.1; JOINED; Genomic_DNA.
EMBL; AF303394; AAK18790.1; JOINED; Genomic_DNA.
EMBL; AK095388; BAG53039.1; -; mRNA.
EMBL; AY584241; AAS79320.1; -; Genomic_DNA.
EMBL; AP000765; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP000786; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; KF455448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC063458; AAH63458.1; -; mRNA.
CCDS; CCDS8298.1; -. [P49959-2]
CCDS; CCDS8299.1; -. [P49959-1]
RefSeq; NP_005581.2; NM_005590.3. [P49959-2]
RefSeq; NP_005582.1; NM_005591.3. [P49959-1]
RefSeq; XP_011541139.1; XM_011542837.2. [P49959-1]
RefSeq; XP_016873261.1; XM_017017772.1. [P49959-1]
PDB; 3T1I; X-ray; 3.00 A; A/B/C/D=1-411.
PDBsum; 3T1I; -.
SMR; P49959; -.
BioGRID; 110501; 193.
ComplexPortal; CPX-4442; MRN complex.
CORUM; P49959; -.
DIP; DIP-33238N; -.
IntAct; P49959; 55.
MINT; P49959; -.
STRING; 9606.ENSP00000325863; -.
BindingDB; P49959; -.
ChEMBL; CHEMBL3308929; -.
GlyGen; P49959; 1 site, 1 O-linked glycan (1 site).
iPTMnet; P49959; -.
PhosphoSitePlus; P49959; -.
SwissPalm; P49959; -.
BioMuta; MRE11; -.
DMDM; 17380137; -.
EPD; P49959; -.
jPOST; P49959; -.
MassIVE; P49959; -.
MaxQB; P49959; -.
PaxDb; P49959; -.
PeptideAtlas; P49959; -.
PRIDE; P49959; -.
ProteomicsDB; 3675; -.
ProteomicsDB; 56186; -. [P49959-1]
ProteomicsDB; 56187; -. [P49959-2]
Antibodypedia; 706; 705 antibodies.
CPTC; P49959; 1 antibody.
DNASU; 4361; -.
Ensembl; ENST00000323929; ENSP00000325863; ENSG00000020922. [P49959-1]
Ensembl; ENST00000323977; ENSP00000326094; ENSG00000020922. [P49959-2]
Ensembl; ENST00000407439; ENSP00000385614; ENSG00000020922. [P49959-3]
GeneID; 4361; -.
KEGG; hsa:4361; -.
UCSC; uc001peu.4; human. [P49959-1]
CTD; 4361; -.
DisGeNET; 4361; -.
GeneCards; MRE11; -.
HGNC; HGNC:7230; MRE11.
HPA; ENSG00000020922; Low tissue specificity.
MalaCards; MRE11; -.
MIM; 600814; gene.
MIM; 604391; phenotype.
neXtProt; NX_P49959; -.
OpenTargets; ENSG00000020922; -.
Orphanet; 251347; Ataxia-telangiectasia-like disorder.
Orphanet; 145; Hereditary breast and ovarian cancer syndrome.
Orphanet; 240760; Nijmegen breakage syndrome-like disorder.
PharmGKB; PA30934; -.
VEuPathDB; HostDB:ENSG00000020922; -.
eggNOG; KOG2310; Eukaryota.
GeneTree; ENSGT00390000017288; -.
HOGENOM; CLU_009535_3_1_1; -.
InParanoid; P49959; -.
OMA; NRPSRDC; -.
PhylomeDB; P49959; -.
TreeFam; TF101105; -.
PathwayCommons; P49959; -.
Reactome; R-HSA-1834949; Cytosolic sensors of pathogen-associated DNA.
Reactome; R-HSA-2559586; DNA Damage/Telomere Stress Induced Senescence.
Reactome; R-HSA-3270619; IRF3-mediated induction of type I IFN.
Reactome; R-HSA-5685938; HDR through Single Strand Annealing (SSA).
Reactome; R-HSA-5685939; HDR through MMEJ (alt-NHEJ).
Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
Reactome; R-HSA-5693548; Sensing of DNA Double Strand Breaks.
Reactome; R-HSA-5693554; Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-HSA-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
Reactome; R-HSA-5693579; Homologous DNA Pairing and Strand Exchange.
Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
Reactome; R-HSA-912446; Meiotic recombination.
SIGNOR; P49959; -.
BioGRID-ORCS; 4361; 323 hits in 1023 CRISPR screens.
ChiTaRS; MRE11A; human.
GeneWiki; MRE11A; -.
GenomeRNAi; 4361; -.
Pharos; P49959; Tbio.
PRO; PR:P49959; -.
Proteomes; UP000005640; Chromosome 11.
RNAct; P49959; protein.
Bgee; ENSG00000020922; Expressed in calcaneal tendon and 224 other tissues.
ExpressionAtlas; P49959; baseline and differential.
Genevisible; P49959; HS.
GO; GO:0000781; C:chromosome, telomeric region; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030870; C:Mre11 complex; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0016605; C:PML body; IDA:BHF-UCL.
GO; GO:0005657; C:replication fork; IDA:UniProtKB.
GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB.
GO; GO:0008408; F:3'-5' exonuclease activity; IDA:CACAO.
GO; GO:0008296; F:3'-5'-exodeoxyribonuclease activity; IEA:InterPro.
GO; GO:0008409; F:5'-3' exonuclease activity; IDA:UniProtKB.
GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
GO; GO:0003690; F:double-stranded DNA binding; TAS:ProtInc.
GO; GO:0004520; F:endodeoxyribonuclease activity; IDA:CACAO.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
GO; GO:0004518; F:nuclease activity; TAS:BHF-UCL.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IDA:CACAO.
GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0000729; P:DNA double-strand break processing; TAS:Reactome.
GO; GO:0032508; P:DNA duplex unwinding; IMP:BHF-UCL.
GO; GO:0006310; P:DNA recombination; TAS:ProtInc.
GO; GO:0006281; P:DNA repair; TAS:ProtInc.
GO; GO:0110025; P:DNA strand resection involved in replication fork processing; IDA:UniProtKB.
GO; GO:0006302; P:double-strand break repair; TAS:ProtInc.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:UniProtKB.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IDA:CACAO.
GO; GO:0007129; P:homologous chromosome pairing at meiosis; IEA:Ensembl.
GO; GO:0042138; P:meiotic DNA double-strand break formation; IBA:GO_Central.
GO; GO:0097552; P:mitochondrial double-strand break repair via homologous recombination; IBA:GO_Central.
GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IBA:GO_Central.
GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IBA:GO_Central.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:BHF-UCL.
GO; GO:0033674; P:positive regulation of kinase activity; IDA:BHF-UCL.
GO; GO:0031954; P:positive regulation of protein autophosphorylation; IDA:BHF-UCL.
GO; GO:0032206; P:positive regulation of telomere maintenance; IMP:BHF-UCL.
GO; GO:0007131; P:reciprocal meiotic recombination; TAS:ProtInc.
GO; GO:0000019; P:regulation of mitotic recombination; TAS:ProtInc.
GO; GO:0007062; P:sister chromatid cohesion; IMP:BHF-UCL.
GO; GO:0000723; P:telomere maintenance; IBA:GO_Central.
GO; GO:0007004; P:telomere maintenance via telomerase; TAS:ProtInc.
GO; GO:0031860; P:telomeric 3' overhang formation; IMP:BHF-UCL.
CDD; cd00840; MPP_Mre11_N; 1.
Gene3D; 3.30.110.110; -; 1.
Gene3D; 3.60.21.10; -; 1.
InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
InterPro; IPR029052; Metallo-depent_PP-like.
InterPro; IPR003701; Mre11.
InterPro; IPR038487; Mre11_capping_dom.
InterPro; IPR007281; Mre11_DNA-bd.
InterPro; IPR041796; Mre11_N.
Pfam; PF00149; Metallophos; 1.
Pfam; PF04152; Mre11_DNA_bind; 1.
PIRSF; PIRSF000882; DSB_repair_MRE11; 1.
SMART; SM01347; Mre11_DNA_bind; 1.
SUPFAM; SSF56300; SSF56300; 1.
TIGRFAMs; TIGR00583; mre11; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Chromosome; Ciliopathy;
Disease variant; DNA damage; DNA repair; Endonuclease; Exonuclease;
Host-virus interaction; Hydrolase; Isopeptide bond; Manganese; Meiosis;
Nuclease; Nucleus; Phosphoprotein; Reference proteome; Telomere;
Ubl conjugation.
INIT_MET 1
/note="Removed"
/evidence="ECO:0007744|PubMed:19413330,
ECO:0007744|PubMed:22223895"
CHAIN 2..708
/note="Double-strand break repair protein MRE11"
/id="PRO_0000138672"
REGION 507..540
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 556..614
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 651..708
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 507..528
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 583..614
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 660..684
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
ACT_SITE 129
/note="Proton donor"
/evidence="ECO:0000250"
MOD_RES 2
/note="N-acetylserine"
/evidence="ECO:0007744|PubMed:19413330,
ECO:0007744|PubMed:22223895"
MOD_RES 2
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q61216"
MOD_RES 275
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 619
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 641
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q61216"
MOD_RES 649
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569"
MOD_RES 678
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 688
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
ECO:0007744|PubMed:24275569"
MOD_RES 689
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
ECO:0007744|PubMed:24275569"
MOD_RES 701
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648"
CROSSLNK 255
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:28112733"
CROSSLNK 416
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:28112733"
CROSSLNK 625
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:28112733"
VAR_SEQ 1..7
/note="MSTADAL -> MNRNISHQKG (in isoform 3)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_057350"
VAR_SEQ 595..622
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:8530104"
/id="VSP_003262"
VARIANT 104
/note="S -> C (in cancer; dbSNP:rs748434421)"
/evidence="ECO:0000269|PubMed:11196167"
/id="VAR_011625"
VARIANT 117
/note="N -> S (in ATLD1; dbSNP:rs137852760)"
/evidence="ECO:0000269|PubMed:10612394"
/id="VAR_008513"
VARIANT 157
/note="M -> V (in dbSNP:rs147771140)"
/id="VAR_011626"
VARIANT 237
/note="F -> C (in a breast cancer sample; somatic
mutation)"
/evidence="ECO:0000269|PubMed:16959974"
/id="VAR_036416"
VARIANT 302
/note="H -> Y (in a breast cancer sample; somatic
mutation)"
/evidence="ECO:0000269|PubMed:16959974"
/id="VAR_036417"
VARIANT 305
/note="R -> W (in ovarian cancer; dbSNP:rs372000848)"
/evidence="ECO:0000269|PubMed:14684699"
/id="VAR_025528"
VARIANT 468
/note="D -> G (in dbSNP:rs1805367)"
/evidence="ECO:0000269|Ref.7"
/id="VAR_019288"
VARIANT 503
/note="R -> H (in cancer; dbSNP:rs774057024)"
/evidence="ECO:0000269|PubMed:11196167"
/id="VAR_011627"
VARIANT 572
/note="R -> Q (in cancer; dbSNP:rs200085146)"
/evidence="ECO:0000269|PubMed:11196167"
/id="VAR_011628"
VARIANT 698
/note="M -> V (in dbSNP:rs1805362)"
/evidence="ECO:0000269|Ref.7"
/id="VAR_019289"
CONFLICT 31
/note="V -> A (in Ref. 1; AAC78721)"
/evidence="ECO:0000305"
HELIX 9..11
/evidence="ECO:0007829|PDB:3T1I"
STRAND 12..18
/evidence="ECO:0007829|PDB:3T1I"
TURN 24..26
/evidence="ECO:0007829|PDB:3T1I"
TURN 30..34
/evidence="ECO:0007829|PDB:3T1I"
HELIX 35..49
/evidence="ECO:0007829|PDB:3T1I"
STRAND 53..57
/evidence="ECO:0007829|PDB:3T1I"
STRAND 62..66
/evidence="ECO:0007829|PDB:3T1I"
HELIX 69..83
/evidence="ECO:0007829|PDB:3T1I"
STRAND 122..124
/evidence="ECO:0007829|PDB:3T1I"
STRAND 128..130
/evidence="ECO:0007829|PDB:3T1I"
TURN 134..137
/evidence="ECO:0007829|PDB:3T1I"
HELIX 140..147
/evidence="ECO:0007829|PDB:3T1I"
STRAND 149..152
/evidence="ECO:0007829|PDB:3T1I"
STRAND 162..164
/evidence="ECO:0007829|PDB:3T1I"
STRAND 167..171
/evidence="ECO:0007829|PDB:3T1I"
STRAND 174..181
/evidence="ECO:0007829|PDB:3T1I"
HELIX 186..194
/evidence="ECO:0007829|PDB:3T1I"
STRAND 198..200
/evidence="ECO:0007829|PDB:3T1I"
HELIX 207..209
/evidence="ECO:0007829|PDB:3T1I"
STRAND 210..216
/evidence="ECO:0007829|PDB:3T1I"
STRAND 223..228
/evidence="ECO:0007829|PDB:3T1I"
HELIX 231..233
/evidence="ECO:0007829|PDB:3T1I"
STRAND 240..243
/evidence="ECO:0007829|PDB:3T1I"
STRAND 250..255
/evidence="ECO:0007829|PDB:3T1I"
TURN 257..259
/evidence="ECO:0007829|PDB:3T1I"
STRAND 262..265
/evidence="ECO:0007829|PDB:3T1I"
HELIX 276..279
/evidence="ECO:0007829|PDB:3T1I"
STRAND 283..290
/evidence="ECO:0007829|PDB:3T1I"
STRAND 293..300
/evidence="ECO:0007829|PDB:3T1I"
STRAND 302..304
/evidence="ECO:0007829|PDB:3T1I"
STRAND 307..313
/evidence="ECO:0007829|PDB:3T1I"
HELIX 314..316
/evidence="ECO:0007829|PDB:3T1I"
TURN 318..320
/evidence="ECO:0007829|PDB:3T1I"
HELIX 328..350
/evidence="ECO:0007829|PDB:3T1I"
TURN 351..353
/evidence="ECO:0007829|PDB:3T1I"
STRAND 355..357
/evidence="ECO:0007829|PDB:3T1I"
STRAND 362..368
/evidence="ECO:0007829|PDB:3T1I"
TURN 370..372
/evidence="ECO:0007829|PDB:3T1I"
HELIX 379..385
/evidence="ECO:0007829|PDB:3T1I"
TURN 386..388
/evidence="ECO:0007829|PDB:3T1I"
STRAND 392..399
/evidence="ECO:0007829|PDB:3T1I"
SEQUENCE 708 AA; 80593 MW; D94ABFBDDF6106AD CRC64;
MSTADALDDE NTFKILVATD IHLGFMEKDA VRGNDTFVTL DEILRLAQEN EVDFILLGGD
LFHENKPSRK TLHTCLELLR KYCMGDRPVQ FEILSDQSVN FGFSKFPWVN YQDGNLNISI
PVFSIHGNHD DPTGADALCA LDILSCAGFV NHFGRSMSVE KIDISPVLLQ KGSTKIALYG
LGSIPDERLY RMFVNKKVTM LRPKEDENSW FNLFVIHQNR SKHGSTNFIP EQFLDDFIDL
VIWGHEHECK IAPTKNEQQL FYISQPGSSV VTSLSPGEAV KKHVGLLRIK GRKMNMHKIP
LHTVRQFFME DIVLANHPDI FNPDNPKVTQ AIQSFCLEKI EEMLENAERE RLGNSHQPEK
PLVRLRVDYS GGFEPFSVLR FSQKFVDRVA NPKDIIHFFR HREQKEKTGE EINFGKLITK
PSEGTTLRVE DLVKQYFQTA EKNVQLSLLT ERGMGEAVQE FVDKEEKDAI EELVKYQLEK
TQRFLKERHI DALEDKIDEE VRRFRETRQK NTNEEDDEVR EAMTRARALR SQSEESASAF
SADDLMSIDL AEQMANDSDD SISAATNKGR GRGRGRRGGR GQNSASRGGS QRGRADTGLE
TSTRSRNSKT AVSASRNMSI IDAFKSTRQQ PSRNVTTKNY SEVIEVDESD VEEDIFPTTS
KTDQRWSSTS SSKIMSQSQV SKGVDFESSE DDDDDPFMNT SSLRRNRR


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Pathways :
WP1807: Double-Strand Break Repair
WP377: Genes of Meiotic Recombination
WP1205: Homologous recombination
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP32: Translation Factors
WP1663: Homologous recombination
WP1678: Nucleotide excision repair
WP1625: Base excision repair
WP1672: Mismatch repair
WP2341: vitamin B1 (thiamin) biosynthesis and salvage pathway
WP1576: Homologous recombination
WP1201: Non-homologous end joining
WP1530: miRNA regulation of DNA Damage Response
WP186: Homologous recombination
WP1216: Homologous recombination
WP1234: Homologous recombination
WP1579: DNA damage response
WP1258: Homologous recombination
WP1296: Homologous recombination
WP917: Homologous recombination
WP1362: Homologous recombination
WP707: DNA damage response
WP1035: Mismatch repair
WP1888: Post-translational protein modification
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Related Genes :
[MRE11 HNGS1 MRE11A] Double-strand break repair protein MRE11 (EC 3.1.-.-) (Double-strand break repair protein MRE11A) (Meiotic recombination 11 homolog 1) (MRE11 homolog 1) (Meiotic recombination 11 homolog A) (MRE11 homolog A)
[Mre11 Mre11a] Double-strand break repair protein MRE11 (EC 3.1.-.-) (Double-strand break repair protein MRE11A) (MmMRE11A) (Meiotic recombination 11 homolog 1) (MRE11 homolog 1) (Meiotic recombination 11 homolog A) (MRE11 homolog A)
[Mre11 Mre11a] Double-strand break repair protein MRE11 (EC 3.1.-.-) (Double-strand break repair protein MRE11A) (Meiotic recombination 11 homolog 1) (MRE11 homolog 1) (Meiotic recombination 11 homolog A) (MRE11 homolog A)
[MRE11 MRE11A QtrA-18006] Double-strand break repair protein MRE11 (EC 3.1.-.-) (Double-strand break repair protein MRE11A) (Meiotic recombination 11 homolog A) (MRE11 homolog A)
[MRE11] Double-strand break repair protein MRE11 (EC 3.1.-.-)
[rad21a rad21 SCC1] Double-strand-break repair protein rad21 homolog A (SCC1 homolog) [Cleaved into: 64-kDa C-terminal product (64-kDa carboxy-terminal product)]
[RAD21 HR21 KIAA0078 NXP1 SCC1] Double-strand-break repair protein rad21 homolog (hHR21) (Nuclear matrix protein 1) (NXP-1) (SCC1 homolog) [Cleaved into: 64-kDa C-terminal product (64-kDa carboxy-terminal product) (65-kDa carboxy-terminal product)]
[Rad21 Hr21 Scc1] Double-strand-break repair protein rad21 homolog (mHR21) (Pokeweed agglutinin-binding protein 29) (PW29) (SCC1 homolog) [Cleaved into: 64-kDa C-terminal product (64-kDa carboxy-terminal product)]
[Atm] Serine-protein kinase ATM (EC 2.7.11.1) (Ataxia telangiectasia mutated homolog) (A-T mutated homolog)
[mre11 VNG_0512G] DNA double-strand break repair protein Mre11 (EC 3.1.-.-)
[RAD21 SCC1] Double-strand-break repair protein rad21 homolog [Cleaved into: 64-kDa C-terminal product (64-kDa carboxy-terminal product)]
[SAE2 COM1 YGL175C G1639] DNA endonuclease SAE2 (EC 3.1.-.-) (Completion of meiotic recombination protein 1) (Sporulation in the absence of SPO11 protein 2)
[MLH1 COCA2] DNA mismatch repair protein Mlh1 (MutL protein homolog 1)
[brc-1 C36A4.8] Breast cancer type 1 susceptibility protein homolog (EC 2.3.2.27) (RING-type E3 ubiquitin transferase BRCA1)
[Mlh1] DNA mismatch repair protein Mlh1 (MutL protein homolog 1)
[mei-41 CG4252] Serine/threonine-protein kinase ATR (EC 2.7.11.1) (Ataxia telangiectasia and Rad3-related protein homolog) (ATR homolog) (dATR) (Meiotic protein 41)
[DMC1 LIM15 At3g22880 F5N5.6] Meiotic recombination protein DMC1 homolog (AtDMC1)
[Brca1] Breast cancer type 1 susceptibility protein homolog (EC 2.3.2.27) (RING-type E3 ubiquitin transferase BRCA1)
[RDH54 TID1 YBR073W YBR0715] DNA repair and recombination protein RDH54 (RAD homolog 54) (Recombination factor TID1) (Two hybrid interaction with DMC1 protein 1) [Includes: DNA topoisomerase (EC 5.99.1.-); Putative helicase (EC 3.6.4.12)]
[Rec8 Mei8 Rec8L1] Meiotic recombination protein REC8 homolog (Cohesin Rec8p)
[DCLRE1C ARTEMIS ASCID SCIDA SNM1C] Protein artemis (EC 3.1.-.-) (DNA cross-link repair 1C protein) (Protein A-SCID) (SNM1 homolog C) (hSNM1C) (SNM1-like protein)
[DMC1 DMC1H LIM15] Meiotic recombination protein DMC1/LIM15 homolog
[RAD54L RAD54A] DNA repair and recombination protein RAD54-like (EC 3.6.4.12) (RAD54 homolog) (hHR54) (hRAD54)
[mus-23 B11O9.50 NCU08730] Double-strand break repair protein mus-23 (Recombinational repair protein mus-23)
[MSH2] DNA mismatch repair protein Msh2 (hMSH2) (MutS protein homolog 2)
[Rad21l1 Gm14160 Rad21l] Double-strand-break repair protein rad21-like protein 1
[Dmc1 Dmc1h Lim15] Meiotic recombination protein DMC1/LIM15 homolog
[SPO11-1 At3g13170 MJG19.19] Meiotic recombination protein SPO11-1 (AtSPO11-1) (EC 5.6.2.2)
[DMC1A DMC1 Os12g0143800 LOC_Os12g04980] Meiotic recombination protein DMC1 homolog A (OsDMC1A) (OsDMC1) (RiLIM15A)
[Brca1] Breast cancer type 1 susceptibility protein homolog (EC 2.3.2.27) (RING-type E3 ubiquitin transferase BRCA1)

Bibliography :