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Mediator of DNA damage checkpoint protein 1 (Nuclear factor with BRCT domains 1)

 MDC1_HUMAN              Reviewed;        2089 AA.
Q14676; A2AB04; A2BF04; A2RRA8; A7YY86; B0S8A2; Q0EFC2; Q2L6H7;
Q2TAZ4; Q5JP55; Q5JP56; Q5ST83; Q68CQ3; Q86Z06; Q96QC2;
05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
05-JUL-2005, sequence version 3.
23-MAY-2018, entry version 181.
RecName: Full=Mediator of DNA damage checkpoint protein 1;
AltName: Full=Nuclear factor with BRCT domains 1;
Name=MDC1; Synonyms=KIAA0170, NFBD1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
MET-536; PRO-1540 AND ARG-1545.
TISSUE=Myelomonocyte;
PubMed=8724849; DOI=10.1093/dnares/3.1.17;
Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. V.
The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 3:17-24(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
LYS-268.
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS LYS-251;
ALA-586; ASP-1509; PRO-1540 AND ARG-1545.
Shiina S., Tamiya G., Oka A., Inoko H.;
"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS LYS-371;
LEU-386; PRO-1180; ASP-1509 AND ARG-1545.
TISSUE=Peripheral blood leukocyte;
PubMed=16702430; DOI=10.1534/genetics.106.057034;
Shiina T., Ota M., Shimizu S., Katsuyama Y., Hashimoto N., Takasu M.,
Anzai T., Kulski J.K., Kikkawa E., Naruse T., Kimura N., Yanagiya K.,
Watanabe A., Hosomichi K., Kohara S., Iwamoto C., Umehara Y.,
Meyer A., Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K.,
Gojobori T., Inoko H., Bahram S.;
"Rapid evolution of major histocompatibility complex class I genes in
primates generates new disease alleles in humans via hitchhiking
diversity.";
Genetics 173:1555-1570(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS LYS-268
AND ARG-1545.
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-1545.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 279-2089 (ISOFORM 4), AND VARIANTS
MET-536; PRO-1540 AND ARG-1545.
TISSUE=Pancreas;
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).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=14695167;
Mochan T.A., Venere M., DiTullio R.A. Jr., Halazonetis T.D.;
"53BP1 and NFBD1/MDC1-Nbs1 function in parallel interacting pathways
activating ataxia-telangiectasia mutated (ATM) in response to DNA
damage.";
Cancer Res. 63:8586-8591(2003).
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12475977; DOI=10.1074/jbc.M210749200;
Shang Y.L., Bodero A.J., Chen P.-L.;
"NFBD1, a novel nuclear protein with signature motifs of FHA and BRCT,
and an internal 41-amino acid repeat sequence, is an early participant
in DNA damage response.";
J. Biol. Chem. 278:6323-6329(2003).
[10]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ATM- AND CELL
CYCLE-DEPENDENT PHOSPHORYLATION, AND DOMAINS NLS1 AND NLS2.
PubMed=12499369; DOI=10.1074/jbc.M211392200;
Xu X., Stern D.F.;
"NFBD1/KIAA0170 is a chromatin-associated protein involved in DNA
damage signaling pathways.";
J. Biol. Chem. 278:8795-8803(2003).
[11]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CHEK2.
PubMed=12551934; DOI=10.1074/jbc.C300001200;
Peng A., Chen P.-L.;
"NFBD1, like 53BP1, is an early and redundant transducer mediating
Chk2 phosphorylation in response to DNA damage.";
J. Biol. Chem. 278:8873-8876(2003).
[12]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BRCA1 AND BARD1.
PubMed=12611903; DOI=10.1074/jbc.C300060200;
Lou Z., Chini C.C.S., Minter-Dykhouse K., Chen J.;
"Mediator of DNA damage checkpoint protein 1 regulates BRCA1
localization and phosphorylation in DNA damage checkpoint control.";
J. Biol. Chem. 278:13599-13602(2003).
[13]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION,
INTERACTION WITH THE MRN COMPLEX, PHOSPHORYLATION BY ATM, AND
MUTAGENESIS OF ARG-58.
PubMed=12607003; DOI=10.1038/nature01445;
Goldberg M., Stucki M., Falck J., D'Amours D., Rahman D., Pappin D.,
Bartek J., Jackson S.P.;
"MDC1 is required for the intra-S-phase DNA damage checkpoint.";
Nature 421:952-956(2003).
[14]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CHEK2,
PHOSPHORYLATION BY ATM AND CHEK2, AND MUTAGENESIS OF ARG-58; SER-72;
ASN-96; GLY-97 AND THR-98.
PubMed=12607004; DOI=10.1038/nature01447;
Lou Z., Minter-Dykhouse K., Wu X., Chen J.;
"MDC1 is coupled to activated CHK2 in mammalian DNA damage response
pathways.";
Nature 421:957-961(2003).
[15]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH THE MRN COMPLEX; ATM;
FANCD2; H2AFX; SMC1A AND TP53BP1, AND PHOSPHORYLATION BY ATM.
PubMed=12607005; DOI=10.1038/nature01446;
Stewart G.S., Wang B., Bignell C.R., Taylor A.M.R., Elledge S.J.;
"MDC1 is a mediator of the mammalian DNA damage checkpoint.";
Nature 421:961-966(2003).
[16]
REVIEW.
PubMed=15279781; DOI=10.1016/j.dnarep.2004.03.007;
Stucki M., Jackson S.P.;
"MDC1/NFBD1: a key regulator of the DNA damage response in higher
eukaryotes.";
DNA Repair 3:953-957(2004).
[17]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH H2AFX.
PubMed=15201865; DOI=10.1038/sj.emboj.7600269;
Lukas C., Melander F., Stucki M., Falck J., Bekker-Jensen S.,
Goldberg M., Lerenthal Y., Jackson S.P., Bartek J., Lukas J.;
"Mdc1 couples DNA double-strand break recognition by Nbs1 with its
H2AX-dependent chromatin retention.";
EMBO J. 23:2674-2683(2004).
[18]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH THE PRKDC
COMPLEX.
PubMed=15377652; DOI=10.1074/jbc.C400375200;
Lou Z., Chen B.P.-C., Asaithamby A., Minter-Dykhouse K., Chen D.J.,
Chen J.;
"MDC1 regulates DNA-PK autophosphorylation in response to DNA
damage.";
J. Biol. Chem. 279:46359-46362(2004).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, AND 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).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17693683; DOI=10.1074/mcp.M700120-MCP200;
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,
Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
network: indicating the involvement of ribonucleoside-diphosphate
reductase M2 subunit phosphorylation at residue serine 20 in canonical
Wnt signal transduction.";
Mol. Cell. Proteomics 6:1952-1967(2007).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372; SER-376; THR-378;
SER-513; THR-523 AND SER-780, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[22]
INTERACTION WITH RNF8.
PubMed=18006705; DOI=10.1126/science.1150034;
Kolas N.K., Chapman J.R., Nakada S., Ylanko J., Chahwan R.,
Sweeney F.D., Panier S., Mendez M., Wildenhain J., Thomson T.M.,
Pelletier L., Jackson S.P., Durocher D.;
"Orchestration of the DNA-damage response by the RNF8 ubiquitin
ligase.";
Science 318:1637-1640(2007).
[23]
INTERACTION WITH CEP164.
PubMed=18283122; DOI=10.1101/gad.1627708;
Sivasubramaniam S., Sun X., Pan Y.R., Wang S., Lee E.Y.;
"Cep164 is a mediator protein required for the maintenance of genomic
stability through modulation of MDC1, RPA, and CHK1.";
Genes Dev. 22:587-600(2008).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1403 AND THR-1425, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; THR-301; SER-394;
SER-397; SER-402; THR-404; THR-449; SER-453; THR-455; SER-495;
SER-498; SER-513; SER-780; SER-793; SER-1033; SER-1068; THR-1198;
SER-1399; SER-1400; THR-1403; THR-1425; THR-1466; THR-1548; THR-1589;
SER-1604; THR-1630; THR-1664; THR-1671; SER-1681; THR-1697; SER-1702;
SER-1711; SER-1775 AND THR-1858, VARIANT [LARGE SCALE ANALYSIS]
PRO-1540, 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).
[26]
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).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168; SER-329; THR-331;
SER-372; SER-376; THR-378; SER-402; THR-404; SER-411; THR-449;
SER-453; THR-455; THR-1157 AND THR-1466, 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).
[28]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-812 AND LYS-1402, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[29]
SUBCELLULAR LOCATION, AND INTERACTION WITH APTX.
PubMed=20008512; DOI=10.1093/nar/gkp1149;
Becherel O.J., Jakob B., Cherry A.L., Gueven N., Fusser M.,
Kijas A.W., Peng C., Katyal S., McKinnon P.J., Chen J., Epe B.,
Smerdon S.J., Taucher-Scholz G., Lavin M.F.;
"CK2 phosphorylation-dependent interaction between aprataxin and MDC1
in the DNA damage response.";
Nucleic Acids Res. 38:1489-1503(2010).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; SER-168; SER-329;
THR-331; SER-402; THR-404; SER-485; SER-513; SER-955; SER-1068;
SER-1399; THR-1403; THR-1425; THR-1589; SER-1775; THR-1800 AND
SER-1820, 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).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; THR-301; SER-329;
SER-402; THR-404; THR-455; SER-495; SER-498; THR-1567 AND SER-1820,
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).
[32]
SUMOYLATION AT LYS-1840, UBIQUITINATION BY RNF4, MUTAGENESIS OF
LYS-1840, AND INTERACTION WITH TP53BP1.
PubMed=22635276; DOI=10.1038/emboj.2012.158;
Luo K., Zhang H., Wang L., Yuan J., Lou Z.;
"Sumoylation of MDC1 is important for proper DNA damage response.";
EMBO J. 31:3008-3019(2012).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; THR-146; SER-168;
SER-299; SER-376; SER-453; THR-455; SER-485; SER-495; SER-498;
SER-513; THR-523; SER-780; SER-998; SER-1086; THR-1157; SER-1399;
SER-1400; THR-1403; THR-1425; SER-1564; THR-1589; THR-1671; SER-1775
AND SER-1820, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; SER-168; SER-329;
SER-485; SER-780; THR-1157; THR-1198; THR-1239; THR-1280; THR-1302 AND
THR-1608, 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).
[35]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1943, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[36]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1840, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[37]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-616 AND LYS-1413, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[38]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-616; LYS-1413; LYS-1740;
LYS-1790 AND LYS-1840, 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]
X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 1883-2089 IN COMPLEX WITH
PHOSPHORYLATED H2AFX.
PubMed=16377563; DOI=10.1016/j.cell.2005.09.038;
Stucki M., Clapperton J.A., Mohammad D., Yaffe M.B., Smerdon S.J.,
Jackson S.P.;
"MDC1 directly binds phosphorylated histone H2AX to regulate cellular
responses to DNA double-strand breaks.";
Cell 123:1213-1226(2005).
[40]
X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 1891-2086, AND INTERACTION
WITH PHOSPHORYLATED H2AFX.
PubMed=16049003; DOI=10.1074/jbc.C500273200;
Lee M.S., Edwards R.A., Thede G.L., Glover J.N.M.;
"Structure of the BRCT repeat domain of MDC1 and its specificity for
the free COOH-terminal end of the gamma-H2AX histone tail.";
J. Biol. Chem. 280:32053-32056(2005).
[41]
X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF 1891-2089 IN COMPLEX WITH
PHOSPHORYLATED HISTONE TETRAPEPTIDE.
PubMed=20159462; DOI=10.1016/j.str.2009.12.008;
Campbell S.J., Edwards R.A., Glover J.N.;
"Comparison of the structures and peptide binding specificities of the
BRCT domains of MDC1 and BRCA1.";
Structure 18:167-176(2010).
[42]
X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF 1884-2089.
PubMed=22139841; DOI=10.1074/jbc.M111.307868;
Singh N., Wiltshire T.D., Thompson J.R., Mer G., Couch F.J.;
"Molecular basis for the association of microcephalin (MCPH1) protein
with the cell division cycle protein 27 (Cdc27) subunit of the
anaphase-promoting complex.";
J. Biol. Chem. 287:2854-2862(2012).
[43]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-10 AND 19-138, AND
PHOSPHORYLATION AT THR-4.
PubMed=22234877; DOI=10.1093/nar/gkr1296;
Liu J., Luo S., Zhao H., Liao J., Li J., Yang C., Xu B., Stern D.F.,
Xu X., Ye K.;
"Structural mechanism of the phosphorylation-dependent dimerization of
the MDC1 forkhead-associated domain.";
Nucleic Acids Res. 40:3898-3912(2012).
-!- FUNCTION: Required for checkpoint mediated cell cycle arrest in
response to DNA damage within both the S phase and G2/M phases of
the cell cycle. May serve as a scaffold for the recruitment of DNA
repair and signal transduction proteins to discrete foci of DNA
damage marked by 'Ser-139' phosphorylation of histone H2AFX. Also
required for downstream events subsequent to the recruitment of
these proteins. These include phosphorylation and activation of
the ATM, CHEK1 and CHEK2 kinases, and stabilization of TP53 and
apoptosis. ATM and CHEK2 may also be activated independently by a
parallel pathway mediated by TP53BP1.
{ECO:0000269|PubMed:12475977, ECO:0000269|PubMed:12499369,
ECO:0000269|PubMed:12551934, ECO:0000269|PubMed:12607003,
ECO:0000269|PubMed:12607004, ECO:0000269|PubMed:12607005,
ECO:0000269|PubMed:12611903, ECO:0000269|PubMed:14695167,
ECO:0000269|PubMed:15201865, ECO:0000269|PubMed:15377652}.
-!- SUBUNIT: Homodimer. Interacts with several proteins involved in
the DNA damage response, although not all these interactions may
be direct. Interacts with H2AFX, which requires phosphorylation of
H2AFX on 'Ser-139'. Interacts with the MRN complex, composed of
MRE11, RAD50, and NBN. Interacts with CHEK2, which requires ATM-
mediated phosphorylation of 'Thr-68' within the FHA domain of
CHEK2. Interacts constitutively with the BRCA1-BARD1 complex,
SMC1A and TP53BP1. Interacts with ATM and FANCD2, and these
interactions are reduced upon DNA damage. Also interacts with the
PRKDC complex, composed of XRCC6/KU70, XRCC5/KU80 and PRKDC/XRCC7.
This interaction may be required for PRKDC autophosphorylation,
which is essential for DNA double strand break (DSB) repair. When
phosphorylated by ATM, interacts with RNF8 (via FHA domain).
Interacts with CEP164. When phosphorylated, interacts with APTX
(via FHA-like domain). {ECO:0000269|PubMed:12551934,
ECO:0000269|PubMed:12607003, ECO:0000269|PubMed:12607004,
ECO:0000269|PubMed:12607005, ECO:0000269|PubMed:12611903,
ECO:0000269|PubMed:15201865, ECO:0000269|PubMed:15377652,
ECO:0000269|PubMed:16049003, ECO:0000269|PubMed:16377563,
ECO:0000269|PubMed:18006705, ECO:0000269|PubMed:18283122,
ECO:0000269|PubMed:20008512, ECO:0000269|PubMed:20159462,
ECO:0000269|PubMed:22635276}.
-!- INTERACTION:
Q13315:ATM; NbExp=2; IntAct=EBI-495644, EBI-495465;
P16104:H2AFX; NbExp=21; IntAct=EBI-495644, EBI-494830;
O60934:NBN; NbExp=32; IntAct=EBI-495644, EBI-494844;
O43070:nbs1 (xeno); NbExp=2; IntAct=EBI-495644, EBI-2125045;
O96028:NSD2; NbExp=3; IntAct=EBI-495644, EBI-2693298;
O96028-1:NSD2; NbExp=3; IntAct=EBI-495644, EBI-15910280;
Q06609:RAD51; NbExp=3; IntAct=EBI-495644, EBI-297202;
O76064:RNF8; NbExp=11; IntAct=EBI-495644, EBI-373337;
O76064-1:RNF8; NbExp=2; IntAct=EBI-495644, EBI-15964690;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12475977,
ECO:0000269|PubMed:12499369, ECO:0000269|PubMed:12551934,
ECO:0000269|PubMed:12607003, ECO:0000269|PubMed:12607004,
ECO:0000269|PubMed:12607005, ECO:0000269|PubMed:12611903,
ECO:0000269|PubMed:14695167, ECO:0000269|PubMed:15201865,
ECO:0000269|PubMed:15377652, ECO:0000269|PubMed:20008512}.
Chromosome {ECO:0000250}. Note=Associated with chromatin.
Relocalizes to discrete nuclear foci following DNA damage, this
requires 'Ser-139' phosphorylation of H2AFX. Colocalizes with APTX
at sites of DNA double-strand breaks.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q14676-1; Sequence=Displayed;
Name=2;
IsoId=Q14676-2; Sequence=VSP_014593;
Name=3;
IsoId=Q14676-3; Sequence=VSP_034104;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q14676-4; Sequence=VSP_014593, VSP_034103;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in testis.
{ECO:0000269|PubMed:12499369}.
-!- DOMAIN: Tandemly repeated BRCT domains are characteristic of
proteins involved in DNA damage signaling. In MDC1, these repeats
are required for localization to chromatin which flanks sites of
DNA damage marked by 'Ser-139' phosphorylation of H2AFX.
{ECO:0000269|PubMed:12499369}.
-!- PTM: Phosphorylated upon exposure to ionizing radiation (IR),
ultraviolet radiation (UV), and hydroxyurea (HU). Phosphorylation
in response to IR requires ATM, NBN, and possibly CHEK2. Also
phosphorylated during the G2/M phase of the cell cycle and during
activation of the mitotic spindle checkpoint. Phosphorylation at
Thr-4 by ATM stabilizes and enhances homodimerization via the FHA
domain. {ECO:0000269|PubMed:12607003, ECO:0000269|PubMed:12607004,
ECO:0000269|PubMed:12607005, ECO:0000269|PubMed:22234877}.
-!- PTM: Sumoylation at Lys-1840 by PIAS4 following DNA damage
promotes ubiquitin-mediated degradation.
{ECO:0000269|PubMed:22635276}.
-!- PTM: Ubiquitinated by RNF4, leading to proteasomal degradation;
undergoes 'Lys-48'-linked polyubiquitination.
{ECO:0000269|PubMed:22635276}.
-!- SEQUENCE CAUTION:
Sequence=BAA11487.2; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAH18685.1; Type=Erroneous termination; Positions=1804; Note=Translated as Gln.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; D79992; BAA11487.2; ALT_INIT; mRNA.
EMBL; CR749828; CAH18685.1; ALT_TERM; mRNA.
EMBL; BA000025; BAB63322.1; -; Genomic_DNA.
EMBL; AB088099; BAC54931.1; -; Genomic_DNA.
EMBL; AB202097; BAE78617.1; -; Genomic_DNA.
EMBL; AB103605; BAF31266.1; -; Genomic_DNA.
EMBL; AL662848; CAI17440.1; -; Genomic_DNA.
EMBL; AL662797; CAI18195.1; -; Genomic_DNA.
EMBL; AL845353; CAI41890.2; -; Genomic_DNA.
EMBL; AL845353; CAI41891.1; -; Genomic_DNA.
EMBL; AL662848; CAM24847.1; -; Genomic_DNA.
EMBL; AL662797; CAM25512.1; -; Genomic_DNA.
EMBL; BX248307; CAM25928.1; -; Genomic_DNA.
EMBL; BX248307; CAM25929.1; -; Genomic_DNA.
EMBL; BX927283; CAQ06769.1; -; Genomic_DNA.
EMBL; BX927283; CAQ06770.1; -; Genomic_DNA.
EMBL; CR936878; CAQ06813.1; -; Genomic_DNA.
EMBL; CR936878; CAQ06814.1; -; Genomic_DNA.
EMBL; CR788240; CAQ07571.1; -; Genomic_DNA.
EMBL; CR788240; CAQ07572.1; -; Genomic_DNA.
EMBL; CR759873; CAQ08690.1; -; Genomic_DNA.
EMBL; CR759873; CAQ08691.1; -; Genomic_DNA.
EMBL; CH471081; EAX03321.1; -; Genomic_DNA.
EMBL; BC110645; AAI10646.1; -; mRNA.
EMBL; BC152556; AAI52557.1; -; mRNA.
CCDS; CCDS34384.1; -. [Q14676-1]
RefSeq; NP_055456.2; NM_014641.2. [Q14676-1]
RefSeq; XP_005249551.1; XM_005249494.4. [Q14676-1]
RefSeq; XP_011513303.1; XM_011515001.2. [Q14676-1]
RefSeq; XP_011513305.1; XM_011515003.2. [Q14676-1]
RefSeq; XP_016867008.1; XM_017011519.1. [Q14676-1]
UniGene; Hs.653495; -.
PDB; 2ADO; X-ray; 1.45 A; A/B=1891-2086.
PDB; 2AZM; X-ray; 2.41 A; A/B=1883-2089.
PDB; 2ETX; X-ray; 1.33 A; A/B=1884-2089.
PDB; 3K05; X-ray; 1.33 A; A/B=1891-2089.
PDB; 3UEO; X-ray; 2.60 A; E/F=325-336.
PDB; 3UMZ; X-ray; 1.65 A; A/B=27-138.
PDB; 3UN0; X-ray; 2.30 A; A/B=26-138.
PDB; 3UNM; X-ray; 1.80 A; A/B=27-138.
PDB; 3UNN; X-ray; 1.70 A; A=27-138, B=1-8.
PDB; 3UOT; X-ray; 1.80 A; A/B=19-138, D/E=1-10.
PDBsum; 2ADO; -.
PDBsum; 2AZM; -.
PDBsum; 2ETX; -.
PDBsum; 3K05; -.
PDBsum; 3UEO; -.
PDBsum; 3UMZ; -.
PDBsum; 3UN0; -.
PDBsum; 3UNM; -.
PDBsum; 3UNN; -.
PDBsum; 3UOT; -.
ProteinModelPortal; Q14676; -.
SMR; Q14676; -.
BioGrid; 115014; 197.
CORUM; Q14676; -.
DIP; DIP-33603N; -.
IntAct; Q14676; 26.
MINT; Q14676; -.
STRING; 9606.ENSP00000365588; -.
iPTMnet; Q14676; -.
PhosphoSitePlus; Q14676; -.
SwissPalm; Q14676; -.
BioMuta; MDC1; -.
EPD; Q14676; -.
MaxQB; Q14676; -.
PaxDb; Q14676; -.
PeptideAtlas; Q14676; -.
PRIDE; Q14676; -.
Ensembl; ENST00000376406; ENSP00000365588; ENSG00000137337. [Q14676-1]
Ensembl; ENST00000383566; ENSP00000373060; ENSG00000206481.
Ensembl; ENST00000420019; ENSP00000396484; ENSG00000224587. [Q14676-1]
Ensembl; ENST00000420320; ENSP00000416511; ENSG00000225589. [Q14676-1]
Ensembl; ENST00000427406; ENSP00000387429; ENSG00000234012. [Q14676-1]
Ensembl; ENST00000435664; ENSP00000404318; ENSG00000231135.
Ensembl; ENST00000440369; ENSP00000415212; ENSG00000228575. [Q14676-1]
Ensembl; ENST00000449153; ENSP00000409167; ENSG00000237095. [Q14676-1]
GeneID; 9656; -.
KEGG; hsa:9656; -.
UCSC; uc003nrg.5; human. [Q14676-1]
CTD; 9656; -.
DisGeNET; 9656; -.
EuPathDB; HostDB:ENSG00000137337.14; -.
GeneCards; MDC1; -.
HGNC; HGNC:21163; MDC1.
HPA; HPA006915; -.
MIM; 607593; gene.
neXtProt; NX_Q14676; -.
OpenTargets; ENSG00000137337; -.
PharmGKB; PA134942837; -.
eggNOG; KOG2043; Eukaryota.
eggNOG; ENOG4111RPS; LUCA.
GeneTree; ENSGT00600000084454; -.
HOVERGEN; HBG080567; -.
InParanoid; Q14676; -.
KO; K20780; -.
OMA; FPLYLGK; -.
OrthoDB; EOG091G0V3Z; -.
PhylomeDB; Q14676; -.
TreeFam; TF329580; -.
Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
SignaLink; Q14676; -.
SIGNOR; Q14676; -.
ChiTaRS; MDC1; human.
EvolutionaryTrace; Q14676; -.
GeneWiki; MDC1; -.
GenomeRNAi; 9656; -.
PRO; PR:Q14676; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000137337; -.
ExpressionAtlas; Q14676; baseline and differential.
Genevisible; Q14676; HS.
GO; GO:0005694; C:chromosome; ISS:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:HPA.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0070975; F:FHA domain binding; IPI:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; TAS:Reactome.
GO; GO:0031573; P:intra-S DNA damage checkpoint; TAS:UniProtKB.
CDD; cd00027; BRCT; 1.
CDD; cd00060; FHA; 1.
Gene3D; 3.40.50.10190; -; 2.
InterPro; IPR001357; BRCT_dom.
InterPro; IPR036420; BRCT_dom_sf.
InterPro; IPR000253; FHA_dom.
InterPro; IPR008984; SMAD_FHA_dom_sf.
Pfam; PF00498; FHA; 1.
Pfam; PF16770; RTT107_BRCT_5; 1.
SMART; SM00240; FHA; 1.
SUPFAM; SSF49879; SSF49879; 1.
SUPFAM; SSF52113; SSF52113; 1.
PROSITE; PS50172; BRCT; 1.
PROSITE; PS50006; FHA_DOMAIN; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell cycle;
Chromosome; Complete proteome; DNA damage; DNA repair;
Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Ubl conjugation.
CHAIN 1 2089 Mediator of DNA damage checkpoint protein
1.
/FTId=PRO_0000096316.
DOMAIN 54 105 FHA. {ECO:0000255|PROSITE-
ProRule:PRU00086}.
DOMAIN 1892 1970 BRCT 1. {ECO:0000255|PROSITE-
ProRule:PRU00033}.
DOMAIN 1991 2082 BRCT 2. {ECO:0000255|PROSITE-
ProRule:PRU00033}.
REGION 1 150 Interaction with CHEK2.
REGION 2 220 Interaction with the MRN complex.
REGION 145 568 Required for nuclear localization (NLS1).
REGION 1148 1610 Interaction with the PRKDC complex.
REGION 1698 2089 Required for nuclear localization (NLS2).
COMPBIAS 1034 1469 Pro-rich.
MOD_RES 4 4 Phosphothreonine; by ATM.
{ECO:0000269|PubMed:22234877}.
MOD_RES 108 108 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 146 146 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 168 168 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:17693683,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 176 176 Phosphoserine.
{ECO:0000250|UniProtKB:Q5U2M8}.
MOD_RES 299 299 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 301 301 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
MOD_RES 329 329 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 331 331 Phosphothreonine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231}.
MOD_RES 372 372 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:19690332}.
MOD_RES 376 376 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 378 378 Phosphothreonine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:19690332}.
MOD_RES 394 394 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 397 397 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 402 402 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 404 404 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 411 411 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 449 449 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 453 453 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 455 455 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 485 485 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 495 495 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 498 498 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 504 504 Phosphoserine.
{ECO:0000250|UniProtKB:Q5PSV9}.
MOD_RES 505 505 Phosphoserine.
{ECO:0000250|UniProtKB:Q5PSV9}.
MOD_RES 513 513 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 523 523 Phosphothreonine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:23186163}.
MOD_RES 590 590 Phosphoserine.
{ECO:0000250|UniProtKB:Q5U2M8}.
MOD_RES 780 780 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 793 793 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 812 812 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 955 955 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 998 998 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1033 1033 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1068 1068 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 1086 1086 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1157 1157 Phosphothreonine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1198 1198 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 1235 1235 Phosphoserine.
{ECO:0000250|UniProtKB:Q5PSV9}.
MOD_RES 1239 1239 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1280 1280 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1302 1302 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1399 1399 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1400 1400 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1402 1402 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1403 1403 Phosphothreonine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1425 1425 Phosphothreonine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1466 1466 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 1548 1548 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1564 1564 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1567 1567 Phosphothreonine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1589 1589 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1604 1604 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1608 1608 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1630 1630 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1664 1664 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1671 1671 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1681 1681 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1697 1697 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1702 1702 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1711 1711 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1775 1775 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1800 1800 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1820 1820 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1858 1858 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1943 1943 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
CROSSLNK 616 616 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 616 616 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 1413 1413 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 1413 1413 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 1740 1740 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1790 1790 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1840 1840 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000269|PubMed:22635276}.
CROSSLNK 1840 1840 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 741 1004 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_014593.
VAR_SEQ 1029 1787 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_034103.
VAR_SEQ 1124 1410 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_034104.
VARIANT 179 179 R -> C (in dbSNP:rs28986464).
/FTId=VAR_051160.
VARIANT 251 251 E -> K (in dbSNP:rs2517560).
{ECO:0000269|Ref.3}.
/FTId=VAR_022843.
VARIANT 268 268 R -> K (in dbSNP:rs9262152).
{ECO:0000269|PubMed:14574404,
ECO:0000269|PubMed:17974005}.
/FTId=VAR_022844.
VARIANT 371 371 E -> K (in dbSNP:rs2075015).
{ECO:0000269|PubMed:16702430}.
/FTId=VAR_022845.
VARIANT 386 386 P -> L (in dbSNP:rs28986465).
{ECO:0000269|PubMed:16702430}.
/FTId=VAR_051161.
VARIANT 536 536 I -> M (in dbSNP:rs58344693).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:8724849}.
/FTId=VAR_043922.
VARIANT 586 586 S -> A (in dbSNP:rs2844707).
{ECO:0000269|Ref.3}.
/FTId=VAR_022846.
VARIANT 917 917 R -> S (in dbSNP:rs28986467).
/FTId=VAR_051162.
VARIANT 1100 1100 P -> A (in dbSNP:rs28994869).
/FTId=VAR_051163.
VARIANT 1112 1112 S -> F (in dbSNP:rs28987085).
/FTId=VAR_051164.
VARIANT 1180 1180 S -> P (in dbSNP:rs9461623).
{ECO:0000269|PubMed:16702430}.
/FTId=VAR_051165.
VARIANT 1509 1509 E -> D (in dbSNP:rs3132589).
{ECO:0000269|PubMed:16702430,
ECO:0000269|Ref.3}.
/FTId=VAR_022847.
VARIANT 1540 1540 S -> P (in dbSNP:rs3130645).
{ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:8724849,
ECO:0000269|Ref.3}.
/FTId=VAR_022848.
VARIANT 1545 1545 Q -> R (in dbSNP:rs17292678).
{ECO:0000269|PubMed:14574404,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16702430,
ECO:0000269|PubMed:8724849,
ECO:0000269|Ref.3, ECO:0000269|Ref.6}.
/FTId=VAR_043923.
VARIANT 1745 1745 P -> R (in dbSNP:rs28994871).
/FTId=VAR_051166.
VARIANT 1791 1791 V -> E (in dbSNP:rs28994873).
/FTId=VAR_051167.
VARIANT 1855 1855 D -> E (in dbSNP:rs28994874).
/FTId=VAR_051168.
VARIANT 1883 1883 R -> Q (in dbSNP:rs28994875).
/FTId=VAR_051169.
VARIANT 1904 1904 R -> Q (in dbSNP:rs28994876).
/FTId=VAR_051170.
MUTAGEN 58 58 R->A: Abrogates binding to the MRE11
complex and to CHEK2.
{ECO:0000269|PubMed:12607003,
ECO:0000269|PubMed:12607004}.
MUTAGEN 72 72 S->A: Abrogates binding to CHEK2.
{ECO:0000269|PubMed:12607004}.
MUTAGEN 96 96 N->A: Abrogates binding to CHEK2; when
associated with A-97 and A-98.
{ECO:0000269|PubMed:12607004}.
MUTAGEN 97 97 G->A: Abrogates binding to CHEK2; when
associated with A-96 and A-98.
{ECO:0000269|PubMed:12607004}.
MUTAGEN 98 98 T->A: Abrogates binding to CHEK2; when
associated with A-96 and A-97.
{ECO:0000269|PubMed:12607004}.
MUTAGEN 1840 1840 K->R: Suppresses RNF4-mediated
ubiquitination, accumulates at sites of
DNA damage, defective homologous
recombination.
{ECO:0000269|PubMed:22635276}.
CONFLICT 638 638 L -> P (in Ref. 2; CAH18685).
{ECO:0000305}.
CONFLICT 645 1326 Missing (in Ref. 2; CAH18685).
{ECO:0000305}.
CONFLICT 1005 1005 G -> GS (in Ref. 3; BAB63322).
{ECO:0000305}.
CONFLICT 1041 1041 T -> A (in Ref. 1; BAA11487 and 7;
AAI52557). {ECO:0000305}.
CONFLICT 1266 1266 Y -> S (in Ref. 4; BAE78617).
{ECO:0000305}.
CONFLICT 1283 1283 P -> T (in Ref. 4; BAE78617).
{ECO:0000305}.
CONFLICT 1533 1533 A -> T (in Ref. 4; BAC54931/BAF31266).
{ECO:0000305}.
CONFLICT 1536 1536 E -> A (in Ref. 5; CAM25929).
{ECO:0000305}.
CONFLICT 1664 1664 T -> S (in Ref. 4; BAE78617).
{ECO:0000305}.
CONFLICT 1668 1668 Q -> R (in Ref. 2; CAH18685).
{ECO:0000305}.
CONFLICT 1734 1734 A -> T (in Ref. 4; BAE78617).
{ECO:0000305}.
CONFLICT 1843 1843 E -> K (in Ref. 2). {ECO:0000305}.
CONFLICT 2048 2048 H -> R (in Ref. 2). {ECO:0000305}.
HELIX 21 24 {ECO:0000244|PDB:3UOT}.
STRAND 32 36 {ECO:0000244|PDB:3UMZ}.
STRAND 39 42 {ECO:0000244|PDB:3UN0}.
STRAND 45 49 {ECO:0000244|PDB:3UMZ}.
STRAND 51 59 {ECO:0000244|PDB:3UMZ}.
STRAND 62 65 {ECO:0000244|PDB:3UMZ}.
STRAND 76 80 {ECO:0000244|PDB:3UMZ}.
STRAND 88 91 {ECO:0000244|PDB:3UMZ}.
STRAND 98 100 {ECO:0000244|PDB:3UMZ}.
TURN 101 104 {ECO:0000244|PDB:3UMZ}.
STRAND 120 123 {ECO:0000244|PDB:3UMZ}.
STRAND 126 132 {ECO:0000244|PDB:3UMZ}.
STRAND 1894 1897 {ECO:0000244|PDB:2ETX}.
HELIX 1903 1911 {ECO:0000244|PDB:2ETX}.
TURN 1920 1922 {ECO:0000244|PDB:2ETX}.
STRAND 1924 1927 {ECO:0000244|PDB:2ETX}.
HELIX 1935 1943 {ECO:0000244|PDB:2ETX}.
HELIX 1951 1959 {ECO:0000244|PDB:2ETX}.
HELIX 1966 1968 {ECO:0000244|PDB:2ETX}.
HELIX 1973 1978 {ECO:0000244|PDB:2ETX}.
HELIX 1983 1992 {ECO:0000244|PDB:2ETX}.
TURN 1995 1998 {ECO:0000244|PDB:2ETX}.
STRAND 2000 2003 {ECO:0000244|PDB:2ETX}.
HELIX 2011 2020 {ECO:0000244|PDB:2ETX}.
STRAND 2024 2026 {ECO:0000244|PDB:3K05}.
STRAND 2037 2040 {ECO:0000244|PDB:2ETX}.
HELIX 2043 2048 {ECO:0000244|PDB:2ETX}.
HELIX 2050 2055 {ECO:0000244|PDB:2ETX}.
HELIX 2063 2071 {ECO:0000244|PDB:2ETX}.
HELIX 2076 2079 {ECO:0000244|PDB:2ETX}.
SEQUENCE 2089 AA; 226666 MW; A8B880A25617EC96 CRC64;
MEDTQAIDWD VEEEEETEQS SESLRCNVEP VGRLHIFSGA HGPEKDFPLH LGKNVVGRMP
DCSVALPFPS ISKQHAEIEI LAWDKAPILR DCGSLNGTQI LRPPKVLSPG VSHRLRDQEL
ILFADLLCQY HRLDVSLPFV SRGPLTVEET PRVQGETQPQ RLLLAEDSEE EVDFLSERRM
VKKSRTTSSS VIVPESDEEG HSPVLGGLGP PFAFNLNSDT DVEEGQQPAT EEASSAARRG
ATVEAKQSEA EVVTEIQLEK DQPLVKERDN DTKVKRGAGN GVVPAGVILE RSQPPGEDSD
TDVDDDSRPP GRPAEVHLER AQPFGFIDSD TDAEEERIPA TPVVIPMKKR KIFHGVGTRG
PGAPGLAHLQ ESQAGSDTDV EEGKAPQAVP LEKSQASMVI NSDTDDEEEV SAALTLAHLK
ESQPAIWNRD AEEDMPQRVV LLQRSQTTTE RDSDTDVEEE ELPVENREAV LKDHTKIRAL
VRAHSEKDQP PFGDSDDSVE ADKSSPGIHL ERSQASTTVD INTQVEKEVP PGSAIIHIKK
HQVSVEGTNQ TDVKAVGGPA KLLVVSLEEA WPLHGDCETD AEEGTSLTAS VVADVRKSQL
PAEGDAGAEW AAAVLKQERA HEVGAQGGPP VAQVEQDLPI SRENLTDLVV DTDTLGESTQ
PQREGAQVPT GREREQHVGG TKDSEDNYGD SEDLDLQATQ CFLENQGLEA VQSMEDEPTQ
AFMLTPPQEL GPSHCSFQTT GTLDEPWEVL ATQPFCLRES EDSETQPFDT HLEAYGPCLS
PPRAIPGDQH PESPVHTEPM GIQGRGRQTV DKVMGIPKET AERVGPERGP LERETEKLLP
ERQTDVTGEE ELTKGKQDRE QKQLLARDTQ RQESDKNGES ASPERDRESL KVEIETSEEI
QEKQVQKQTL PSKAFEREVE RPVANRECDP AELEEKVPKV ILERDTQRGE PEGGSQDQKG
QASSPTPEPG VGAGDLPGPT SAPVPSGSQS GGRGSPVSPR RHQKGLLNCK MPPAEKASRI
RAAEKVSRGD QESPDACLPP TVPEAPAPPQ KPLNSQSQKH LAPPPLLSPL LPSIKPTVRK
TRQDGSQEAP EAPLSSELEP FHPKPKIRTR KSSRMTPFPA TSAAPEPHPS TSTAQPVTPK
PTSQATRSRT NRSSVKTPEP VVPTAPELQP STSTDQPVTS EPTSQVTRGR KSRSSVKTPE
TVVPTALELQ PSTSTDRPVT SEPTSQATRG RKNRSSVKTP EPVVPTAPEL QPSTSTDQPV
TSEPTYQATR GRKNRSSVKT PEPVVPTAPE LRPSTSTDRP VTPKPTSRTT RSRTNMSSVK
TPETVVPTAP ELQISTSTDQ PVTPKPTSRT TRSRTNMSSV KNPESTVPIA PELPPSTSTE
QPVTPEPTSR ATRGRKNRSS GKTPETLVPT APKLEPSTST DQPVTPEPTS QATRGRTNRS
SVKTPETVVP TAPELQPSTS TDQPVTPEPT SQATRGRTDR SSVKTPETVV PTAPELQASA
STDQPVTSEP TSRTTRGRKN RSSVKTPETV VPAAPELQPS TSTDQPVTPE PTSRATRGRT
NRSSVKTPES IVPIAPELQP STSRNQLVTP EPTSRATRCR TNRSSVKTPE PVVPTAPEPH
PTTSTDQPVT PKLTSRATRR KTNRSSVKTP KPVEPAASDL EPFTPTDQSV TPEAIAQGGQ
SKTLRSSTVR AMPVPTTPEF QSPVTTDQPI SPEPITQPSC IKRQRAAGNP GSLAAPIDHK
PCSAPLEPKS QASRNQRWGA VRAAESLTAI PEPASPQLLE TPIHASQIQK VEPAGRSRFT
PELQPKASQS RKRSLATMDS PPHQKQPQRG EVSQKTVIIK EEEEDTAEKP GKEEDVVTPK
PGKRKRDQAE EEPNRIPSRS LRRTKLNQES TAPKVLFTGV VDARGERAVL ALGGSLAGSA
AEASHLVTDR IRRTVKFLCA LGRGIPILSL DWLHQSRKAG FFLPPDEYVV TDPEQEKNFG
FSLQDALSRA RERRLLEGYE IYVTPGVQPP PPQMGEIISC CGGTYLPSMP RSYKPQRVVI
TCPQDFPHCS IPLRVGLPLL SPEFLLTGVL KQEAKPEAFV LSPLEMSST


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