ID TP53B_HUMAN Reviewed; 1972 AA. AC Q12888; F8VY86; Q2M1Z7; Q4LE46; Q5FWZ3; Q7Z3U4; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 27-MAR-2024, entry version 236. DE RecName: Full=TP53-binding protein 1 {ECO:0000305}; DE Short=53BP1 {ECO:0000303|PubMed:9748285}; DE Short=p53-binding protein 1 {ECO:0000303|PubMed:9748285}; DE Short=p53BP1; GN Name=TP53BP1 {ECO:0000312|HGNC:HGNC:11999}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION. RC TISSUE=Skeletal muscle; RX PubMed=9748285; DOI=10.1074/jbc.273.40.26061; RA Iwabuchi K., Li B., Massa H.F., Trask B.J., Date T., Fields S.; RT "Stimulation of p53-mediated transcriptional activation by the p53-binding RT proteins, 53BP1 and 53BP2."; RL J. Biol. Chem. 273:26061-26068(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Myeloid leukemia cell; RA Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., RA Okazaki N., Koga H., Nagase T., Ohara O.; RT "Preparation of a set of expression-ready clones of mammalian long cDNAs RT encoding large proteins by the ORF trap cloning method."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS GLU-353; RP SER-412 AND GLN-1136. RC TISSUE=Cervix; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLU-353; SER-412; VAL-648; RP ARG-699; GLY-1014; ALA-1026; GLN-1136; GLY-1170 AND VAL-1174. RG NIEHS SNPs program; RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16572171; DOI=10.1038/nature04601; RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S., RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.; RT "Analysis of the DNA sequence and duplication history of human chromosome RT 15."; RL Nature 440:671-675(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Cerebellum; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 946-1972. RX PubMed=8016121; DOI=10.1073/pnas.91.13.6098; RA Iwabuchi K., Bartel P.L., Li B., Marraccino R., Fields S.; RT "Two cellular proteins that bind to wild-type but not mutant p53."; RL Proc. Natl. Acad. Sci. U.S.A. 91:6098-6102(1994). RN [8] RP PHOSPHORYLATION. RX PubMed=11042216; DOI=10.1074/jbc.m007665200; RA Xia Z., Morales J.C., Dunphy W.G., Carpenter P.B.; RT "Negative cell cycle regulation and DNA-damage inducible phosphorylation of RT the BRCT protein 53BP1."; RL J. Biol. Chem. 276:2708-2718(2001). RN [9] RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION. RX PubMed=11331310; DOI=10.1083/jcb.153.3.613; RA Rappold I., Iwabuchi K., Date T., Chen J.; RT "Tumor suppressor p53 binding protein 1 (53BP1) is involved in DNA damage- RT signaling pathways."; RL J. Cell Biol. 153:613-620(2001). RN [10] RP FUNCTION IN DNA DAMAGE CHECKPOINT, AND INTERACTION WITH CHEK2. RX PubMed=12364621; DOI=10.1126/science.1076182; RA Wang B., Matsuoka S., Carpenter P.B., Elledge S.J.; RT "53BP1, a mediator of the DNA damage checkpoint."; RL Science 298:1435-1438(2002). RN [11] RP SUBCELLULAR LOCATION. RX PubMed=12824158; DOI=10.1074/jbc.m304066200; RA Iwabuchi K., Basu B.P., Kysela B., Kurihara T., Shibata M., Guan D., RA Cao Y., Hamada T., Imamura K., Jeggo P.A., Date T., Doherty A.J.; RT "Potential role for 53BP1 in DNA end-joining repair through direct RT interaction with DNA."; RL J. Biol. Chem. 278:36487-36495(2003). RN [12] RP INTERACTION WITH H2AX. RX PubMed=12607005; DOI=10.1038/nature01446; RA Stewart G.S., Wang B., Bignell C.R., Taylor A.M.R., Elledge S.J.; RT "MDC1 is a mediator of the mammalian DNA damage checkpoint."; RL Nature 421:961-966(2003). RN [13] RP CHROMOSOMAL TRANSLOCATION WITH PDGFRB. RX PubMed=15492236; DOI=10.1158/0008-5472.can-04-2005; RA Grand F.H., Burgstaller S., Kuhr T., Baxter E.J., Webersinke G., Thaler J., RA Chase A.J., Cross N.C.; RT "p53-Binding protein 1 is fused to the platelet-derived growth factor RT receptor beta in a patient with a t(5;15)(q33;q22) and an imatinib- RT responsive eosinophilic myeloproliferative disorder."; RL Cancer Res. 64:7216-7219(2004). RN [14] RP INTERACTION WITH DCLRE1C. RX PubMed=15574327; DOI=10.1016/j.molcel.2004.10.029; RA Riballo E., Kuehne M., Rief N., Doherty A., Smith G.C.M., Recio M.-J., RA Reis C., Dahm K., Fricke A., Krempler A., Parker A.R., Jackson S.P., RA Gennery A., Jeggo P.A., Loebrich M.; RT "A pathway of double-strand break rejoining dependent upon ATM, Artemis, RT and proteins locating to gamma-H2AX foci."; RL Mol. Cell 16:715-724(2004). RN [15] RP METHYLATION, MUTAGENESIS OF ARG-1396; ARG-1398; ARG-1400; ARG-1401 AND RP ARG-1403, SUBCELLULAR LOCATION, AND DNA-BINDING. RX PubMed=16294045; DOI=10.4161/cc.4.12.2250; RA Boisvert F.-M., Rhie A., Richard S., Doherty A.J.; RT "The GAR motif of 53BP1 is arginine methylated by PRMT1 and is necessary RT for 53BP1 DNA binding activity."; RL Cell Cycle 4:1834-1841(2005). RN [16] RP METHYLATION, MUTAGENESIS OF ARG-1396; ARG-1398; ARG-1400; ARG-1401 AND RP ARG-1403, SUBUNIT, SUBCELLULAR LOCATION, AND DNA-BINDING. RX PubMed=16294047; DOI=10.4161/cc.4.12.2282; RA Adams M.M., Wang B., Xia Z., Morales J.C., Lu X., Donehower L.A., RA Bochar D.A., Elledge S.J., Carpenter P.B.; RT "53BP1 oligomerization is independent of its methylation by PRMT1."; RL Cell Cycle 4:1854-1861(2005). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222; SER-294; SER-500; RP SER-635; SER-639; SER-640; SER-1094; SER-1219; SER-1362 AND SER-1678, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-834 AND SER-1426, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [19] RP PHOSPHORYLATION AT SER-166; SER-176; SER-178; SER-294; THR-302; SER-380; RP SER-452; SER-523; SER-552; SER-831; SER-1028; SER-1086; SER-1114 AND RP SER-1219, AND MUTAGENESIS OF 176-SER--SER-178. RX PubMed=17553757; DOI=10.1016/j.dnarep.2007.04.011; RA Jowsey P., Morrice N.A., Hastie C.J., McLauchlan H., Toth R., Rouse J.; RT "Characterisation of the sites of DNA damage-induced 53BP1 phosphorylation RT catalysed by ATM and ATR."; RL DNA Repair 6:1536-1544(2007). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; THR-302; SER-523; RP THR-543; THR-548; SER-552; SER-831; THR-855; THR-1214; SER-1216 AND RP SER-1219, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222; SER-265; SER-395; RP SER-398; SER-500; SER-523; SER-525; SER-552; SER-809; SER-831; SER-1028; RP SER-1094; SER-1216; SER-1219; SER-1368; THR-1372; SER-1426; SER-1430; RP SER-1462; THR-1609; SER-1701 AND SER-1759, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [23] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [24] RP PHOSPHORYLATION AT SER-25 AND SER-1778, DEPHOSPHORYLATION AT SER-25 AND RP SER-1778 BY PPP5C, AND SUBCELLULAR LOCATION. RX PubMed=19176521; DOI=10.1074/jbc.m809272200; RA Kang Y., Lee J.H., Hoan N.N., Sohn H.M., Chang I.Y., You H.J.; RT "Protein phosphatase 5 regulates the function of 53BP1 after RT neocarzinostatin-induced DNA damage."; RL J. Biol. Chem. 284:9845-9853(2009). RN [25] RP INTERACTION WITH EPSTEIN-BARR VIRUS BZLF1 PROTEIN (MICROBIAL INFECTION). RX PubMed=19656881; DOI=10.1128/jvi.00512-09; RA Bailey S.G., Verrall E., Schelcher C., Rhie A., Doherty A.J., RA Sinclair A.J.; RT "Functional interaction between Epstein-Barr virus replication protein Zta RT and host DNA damage response protein 53BP1."; RL J. Virol. 83:11116-11122(2009). RN [26] RP INTERACTION WITH MSL1. RX PubMed=19650074; DOI=10.1002/jcp.21889; RA Gironella M., Malicet C., Cano C., Sandi M.J., Hamidi T., Tauil R.M., RA Baston M., Valaco P., Moreno S., Lopez F., Neira J.L., Dagorn J.C., RA Iovanna J.L.; RT "p8/nupr1 regulates DNA-repair activity after double-strand gamma RT irradiation-induced DNA damage."; RL J. Cell. Physiol. 221:594-602(2009). RN [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-294; SER-366; SER-380; RP SER-500; SER-523; SER-525; THR-543; SER-552; SER-834; SER-1028; SER-1114; RP SER-1426; SER-1430; SER-1460; SER-1462 AND SER-1474, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [28] RP INTERACTION WITH PWWP3A. RX PubMed=20347427; DOI=10.1016/j.molcel.2009.12.040; RA Huen M.S., Huang J., Leung J.W., Sy S.M., Leung K.M., Ching Y.P., RA Tsao S.W., Chen J.; RT "Regulation of chromatin architecture by the PWWP domain-containing DNA RT damage-responsive factor EXPAND1/MUM1."; RL Mol. Cell 37:854-864(2010). RN [29] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; SER-294; SER-500; RP SER-525; SER-552; SER-566; SER-580; SER-639; SER-640; SER-809; THR-922; RP SER-970; SER-975; SER-1028; SER-1068; SER-1114; SER-1362; SER-1426; RP SER-1430; THR-1609; SER-1618 AND SER-1678, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [30] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [31] RP FUNCTION IN DNA DAMAGE RESPONSE, PHOSPHORYLATION AT SER-1778, AND RP SUBCELLULAR LOCATION. RX PubMed=21144835; DOI=10.1016/j.bbrc.2010.12.005; RA Kang Y., Cheong H.M., Lee J.H., Song P.I., Lee K.H., Kim S.Y., Jun J.Y., RA You H.J.; RT "Protein phosphatase 5 is necessary for ATR-mediated DNA repair."; RL Biochem. Biophys. Res. Commun. 404:476-481(2011). RN [32] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222; SER-294; SER-500; RP SER-525; SER-552; SER-809; SER-1028; SER-1101; SER-1114; SER-1362; RP SER-1430; SER-1618 AND SER-1678, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [33] RP FUNCTION. RX PubMed=22553214; DOI=10.1242/jcs.105353; RA Chapman J.R., Sossick A.J., Boulton S.J., Jackson S.P.; RT "BRCA1-associated exclusion of 53BP1 from DNA damage sites underlies RT temporal control of DNA repair."; RL J. Cell Sci. 125:3529-3534(2012). RN [34] RP FUNCTION, PHOSPHORYLATION, INTERACTION WITH RIF1 AND PAXIP1, AND RP MUTAGENESIS OF SER-6; SER-13; SER-25; SER-29; SER-105; SER-166; SER-176 AND RP SER-178. RX PubMed=23727112; DOI=10.1016/j.cell.2013.05.023; RA Callen E., Di Virgilio M., Kruhlak M.J., Nieto-Soler M., Wong N., RA Chen H.T., Faryabi R.B., Polato F., Santos M., Starnes L.M., Wesemann D.R., RA Lee J.E., Tubbs A., Sleckman B.P., Daniel J.A., Ge K., Alt F.W., RA Fernandez-Capetillo O., Nussenzweig M.C., Nussenzweig A.; RT "53BP1 mediates productive and mutagenic DNA repair through distinct RT phosphoprotein interactions."; RL Cell 153:1266-1280(2013). RN [35] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63; SER-124; SER-222; RP SER-265; SER-294; SER-366; SER-380; SER-398; SER-500; SER-507; SER-518; RP SER-523; SER-525; SER-552; SER-580; SER-771; SER-809; SER-834; THR-922; RP SER-1028; THR-1056; SER-1068; SER-1094; SER-1114; SER-1148; SER-1216; RP SER-1219; SER-1317; SER-1342; SER-1362; SER-1426; SER-1430; SER-1462; RP THR-1609; SER-1618; SER-1635; THR-1638; THR-1648; SER-1656; SER-1673; RP SER-1678 AND SER-1701, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [36] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RIF1, PHOSPHORYLATION, AND RP MUTAGENESIS OF SER-6; SER-13; SER-25; SER-29; SER-105; SER-166; SER-176; RP SER-178; THR-302; SER-437; SER-452; SER-523; THR-543; SER-580; SER-625; RP SER-674; THR-696; SER-698; SER-784; SER-831; THR-855; SER-892; SER-1068; RP SER-1086; SER-1104; SER-1148; THR-1171 AND SER-1219. RX PubMed=23333306; DOI=10.1016/j.molcel.2013.01.001; RA Escribano-Diaz C., Orthwein A., Fradet-Turcotte A., Xing M., Young J.T., RA Tkac J., Cook M.A., Rosebrock A.P., Munro M., Canny M.D., Xu D., RA Durocher D.; RT "A cell cycle-dependent regulatory circuit composed of 53BP1-RIF1 and RT BRCA1-CtIP controls DNA repair pathway choice."; RL Mol. Cell 49:872-883(2013). RN [37] RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF RP ASP-1521; LYS-1613; ASP-1616; ILE-1617; LEU-1619; ASN-1621; LEU-1622; RP GLU-1624 AND ARG-1627. RX PubMed=23760478; DOI=10.1038/nature12318; RA Fradet-Turcotte A., Canny M.D., Escribano-Diaz C., Orthwein A., Leung C.C., RA Huang H., Landry M.C., Kitevski-LeBlanc J., Noordermeer S.M., Sicheri F., RA Durocher D.; RT "53BP1 is a reader of the DNA-damage-induced H2A Lys 15 ubiquitin mark."; RL Nature 499:50-54(2013). RN [38] RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF SER-6; SER-13; SER-25; SER-29; RP SER-105; SER-166; SER-176; SER-178; THR-302; SER-437; SER-452; SER-523; RP THR-543; SER-580; SER-625; SER-674; THR-696; SER-698; SER-784; SER-831; RP THR-855; SER-892; SER-1068; SER-1086; SER-1104; SER-1148; THR-1171; RP SER-1219; 1398-ARG--ARG-1401 AND ASP-1521. RX PubMed=23345425; DOI=10.1073/pnas.1222617110; RA Lottersberger F., Bothmer A., Robbiani D.F., Nussenzweig M.C., de Lange T.; RT "Role of 53BP1 oligomerization in regulating double-strand break repair."; RL Proc. Natl. Acad. Sci. U.S.A. 110:2146-2151(2013). RN [39] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-294; SER-500; SER-552; RP SER-630; SER-692; SER-727; SER-1114; SER-1216 AND SER-1362, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [40] RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-1609 AND SER-1618, DOMAIN, AND RP MUTAGENESIS OF THR-1609 AND SER-1618. RX PubMed=24703952; DOI=10.1016/j.molcel.2014.03.020; RA Lee D.H., Acharya S.S., Kwon M., Drane P., Guan Y., Adelmant G., Kalev P., RA Shah J., Pellman D., Marto J.A., Chowdhury D.; RT "Dephosphorylation enables the recruitment of 53BP1 to double-strand DNA RT breaks."; RL Mol. Cell 54:512-525(2014). RN [41] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-930 AND LYS-1563, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [42] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-217; LYS-868; LYS-1434 AND RP LYS-1563, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [43] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-930, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [44] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1563, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [45] RP FUNCTION. RX PubMed=27153538; DOI=10.1016/j.molcel.2016.03.031; RA Jacquet K., Fradet-Turcotte A., Avvakumov N., Lambert J.P., Roques C., RA Pandita R.K., Paquet E., Herst P., Gingras A.C., Pandita T.K., Legube G., RA Doyon Y., Durocher D., Cote J.; RT "The TIP60 complex regulates bivalent chromatin recognition by 53BP1 RT through direct H4K20me binding and H2AK15 acetylation."; RL Mol. Cell 62:409-421(2016). RN [46] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-217; LYS-868; LYS-930; LYS-984; RP LYS-1365; LYS-1434 AND LYS-1563, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [47] RP FUNCTION, INTERACTION WITH NUDT16L1 AND RIF1, SUBCELLULAR LOCATION, RP PHOSPHORYLATION, AND MUTAGENESIS OF TRP-1495; ASP-1521; THR-1609 AND RP SER-1618. RX PubMed=28241136; DOI=10.1038/nature21358; RA Drane P., Brault M.E., Cui G., Meghani K., Chaubey S., Detappe A., RA Parnandi N., He Y., Zheng X.F., Botuyan M.V., Kalousi A., Yewdell W.T., RA Muench C., Harper J.W., Chaudhuri J., Soutoglou E., Mer G., Chowdhury D.; RT "TIRR regulates 53BP1 by masking its histone methyl-lysine binding RT function."; RL Nature 543:211-216(2017). RN [48] RP INTERACTION WITH SHLD2, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=29789392; DOI=10.15252/embj.201899543; RA Tomida J., Takata K.I., Bhetawal S., Person M.D., Chao H.P., Tang D.G., RA Wood R.D.; RT "FAM35A associates with REV7 and modulates DNA damage responses of normal RT and BRCA1-defective cells."; RL EMBO J. 37:0-0(2018). RN [49] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1722-1971 IN COMPLEX WITH TP53. RX PubMed=12110597; DOI=10.1093/emboj/cdf383; RA Derbyshire D.J., Basu B.P., Serpell L.C., Joo W.S., Date T., Iwabuchi K., RA Doherty A.J.; RT "Crystal structure of human 53BP1 BRCT domains bound to p53 tumour RT suppressor."; RL EMBO J. 21:3863-3872(2002). RN [50] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1714-1972 IN COMPLEX WITH TP53. RX PubMed=11877378; DOI=10.1101/gad.959202; RA Joo W.S., Jeffrey P.D., Cantor S.B., Finnin M.S., Livingston D.M., RA Pavletich N.P.; RT "Structure of the 53BP1 BRCT region bound to p53 and its comparison to the RT Brca1 BRCT structure."; RL Genes Dev. 16:583-593(2002). RN [51] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1485-1602, INTERACTION WITH RP METHYLATED HISTONE H3 AND HISTONE H4, SUBCELLULAR LOCATION, AND MUTAGENESIS RP OF TRP-1495; TYR-1502 AND ASP-1521. RX PubMed=15525939; DOI=10.1038/nature03114; RA Huyen Y., Zgheib O., Ditullio R.A. Jr., Gorgoulis V.G., Zacharatos P., RA Petty T.J., Sheston E.A., Mellert H.S., Stavridi E.S., Halazonetis T.D.; RT "Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand RT breaks."; RL Nature 432:406-411(2004). RN [52] RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 1484-1603 IN COMPLEX WITH HISTONE RP H4, SUBUNIT, FUNCTION, MUTAGENESIS OF TRP-1495; TYR-1500; TYR-1502; RP ASP-1521 AND TYR-1523, AND SUBCELLULAR LOCATION. RX PubMed=17190600; DOI=10.1016/j.cell.2006.10.043; RA Botuyan M.V., Lee J., Ward I.M., Kim J.-E., Thompson J.R., Chen J., Mer G.; RT "Structural basis for the methylation state-specific recognition of histone RT H4-K20 by 53BP1 and Crb2 in DNA repair."; RL Cell 127:1361-1373(2006). RN [53] {ECO:0007744|PDB:6RML, ECO:0007744|PDB:6RMM} RP X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 663-677 IN COMPLEX WITH TOPBP1, RP FUNCTION, INTERACTION WITH TOPBP1, PHOSPHORYLATION AT SER-366 AND THR-670, RP AND MUTAGENESIS OF SER-366 AND THR-670. RX PubMed=31135337; DOI=10.7554/elife.44353; RA Bigot N., Day M., Baldock R.A., Watts F.Z., Oliver A.W., Pearl L.H.; RT "Phosphorylation-mediated interactions with TOPBP1 couple 53BP1 and 9-1-1 RT to control the G1 DNA damage checkpoint."; RL Elife 8:e44353-e44353(2019). CC -!- FUNCTION: Double-strand break (DSB) repair protein involved in response CC to DNA damage, telomere dynamics and class-switch recombination (CSR) CC during antibody genesis (PubMed:12364621, PubMed:22553214, CC PubMed:23333306, PubMed:17190600, PubMed:21144835, PubMed:27153538, CC PubMed:28241136, PubMed:31135337). Plays a key role in the repair of CC double-strand DNA breaks (DSBs) in response to DNA damage by promoting CC non-homologous end joining (NHEJ)-mediated repair of DSBs and CC specifically counteracting the function of the homologous recombination CC (HR) repair protein BRCA1 (PubMed:22553214, PubMed:23727112, CC PubMed:23333306, PubMed:27153538, PubMed:31135337). In response to CC DSBs, phosphorylation by ATM promotes interaction with RIF1 and CC dissociation from NUDT16L1/TIRR, leading to recruitment to DSBs sites CC (PubMed:28241136). Recruited to DSBs sites by recognizing and binding CC histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 CC dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present CC at DSBs sites (PubMed:23760478, PubMed:27153538, PubMed:28241136, CC PubMed:17190600). Required for immunoglobulin class-switch CC recombination (CSR) during antibody genesis, a process that involves CC the generation of DNA DSBs (PubMed:23345425). Participates in the CC repair and the orientation of the broken DNA ends during CSR (By CC similarity). In contrast, it is not required for classic NHEJ and V(D)J CC recombination (By similarity). Promotes NHEJ of dysfunctional telomeres CC via interaction with PAXIP1 (PubMed:23727112). CC {ECO:0000250|UniProtKB:P70399, ECO:0000269|PubMed:12364621, CC ECO:0000269|PubMed:17190600, ECO:0000269|PubMed:21144835, CC ECO:0000269|PubMed:22553214, ECO:0000269|PubMed:23333306, CC ECO:0000269|PubMed:23345425, ECO:0000269|PubMed:23727112, CC ECO:0000269|PubMed:23760478, ECO:0000269|PubMed:27153538, CC ECO:0000269|PubMed:28241136, ECO:0000269|PubMed:31135337}. CC -!- SUBUNIT: Homoligomer (PubMed:16294047, PubMed:23760478, CC PubMed:23345425). Interacts with p53/TP53 (via the central domain) CC (PubMed:12110597, PubMed:11877378). Interacts with DCLRE1C CC (PubMed:15574327). Interacts with histone H2AX and this requires CC phosphorylation of H2AX on 'Ser-139' (PubMed:12607005). Interacts with CC histone H4 that has been dimethylated at 'Lys-20' (H4K20me2) CC (PubMed:17190600). Has low affinity for histone H4 containing CC monomethylated 'Lys-20' (H4K20me1) (PubMed:17190600). Does not bind CC histone H4 containing unmethylated or trimethylated 'Lys-20' (H4K20me3) CC (PubMed:17190600). Has low affinity for histone H3 that has been CC dimethylated on 'Lys-79' (PubMed:15525939). Has very low affinity for CC histone H3 that has been monomethylated on 'Lys-79' (in vitro) CC (PubMed:15525939). Does not bind unmethylated histone H3 CC (PubMed:15525939). Interacts with histone H2A monoubiquitinated at CC 'Lys-15' (H2AK15Ub) (PubMed:23760478). Interacts with PWWP3A/EXPAND1 CC (PubMed:20347427). Interacts with CHEK2; modulates CHEK2 CC phosphorylation at 'Thr-68' in response to infrared (PubMed:12364621). CC Interacts with MSL1; this interaction may be required for MSL1 DNA CC repair activity, but not for histone acetyltransferase activity CC (PubMed:19650074). Interacts (when phosphorylated by ATM) with RIF1 CC (PubMed:23727112, PubMed:23333306, PubMed:28241136). Interacts (via the CC Tudor-like domain) with NUDT16L1/TIRR; interaction masks the Tudor-like CC domain and prevents recruitment to chromatin (PubMed:28241136). CC Interacts with PAXIP1 (PubMed:23727112). Interacts with SHLD2 CC (PubMed:29789392). Interacts (when phosphorylated) with TOPBP1 CC (PubMed:31135337). {ECO:0000269|PubMed:11877378, CC ECO:0000269|PubMed:12110597, ECO:0000269|PubMed:12364621, CC ECO:0000269|PubMed:12607005, ECO:0000269|PubMed:15525939, CC ECO:0000269|PubMed:15574327, ECO:0000269|PubMed:16294047, CC ECO:0000269|PubMed:17190600, ECO:0000269|PubMed:19650074, CC ECO:0000269|PubMed:20347427, ECO:0000269|PubMed:23333306, CC ECO:0000269|PubMed:23345425, ECO:0000269|PubMed:23727112, CC ECO:0000269|PubMed:23760478, ECO:0000269|PubMed:29789392, CC ECO:0000269|PubMed:31135337}. CC -!- SUBUNIT: (Microbial infection) Interacts (via C-terminus) with Epstein- CC Barr virus lytic switch protein BZLF1 (via C-terminus); this CC interaction is involved in the activation of the viral lytic cycle. CC {ECO:0000269|PubMed:19656881}. CC -!- INTERACTION: CC Q12888; Q49AR9: ANKS1A; NbExp=3; IntAct=EBI-396540, EBI-11954519; CC Q12888; Q13315: ATM; NbExp=2; IntAct=EBI-396540, EBI-495465; CC Q12888; P13637: ATP1A3; NbExp=3; IntAct=EBI-396540, EBI-948169; CC Q12888; P46379-2: BAG6; NbExp=3; IntAct=EBI-396540, EBI-10988864; CC Q12888; P41182: BCL6; NbExp=3; IntAct=EBI-396540, EBI-765407; CC Q12888; P38398: BRCA1; NbExp=5; IntAct=EBI-396540, EBI-349905; CC Q12888; Q5SWW7: C10orf55; NbExp=3; IntAct=EBI-396540, EBI-12809220; CC Q12888; P55212: CASP6; NbExp=3; IntAct=EBI-396540, EBI-718729; CC Q12888; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-396540, EBI-744556; CC Q12888; Q02930-3: CREB5; NbExp=3; IntAct=EBI-396540, EBI-10192698; CC Q12888; G5E9A7: DMWD; NbExp=3; IntAct=EBI-396540, EBI-10976677; CC Q12888; O75190-2: DNAJB6; NbExp=3; IntAct=EBI-396540, EBI-12593112; CC Q12888; O14645: DNALI1; NbExp=3; IntAct=EBI-396540, EBI-395638; CC Q12888; P50570-2: DNM2; NbExp=3; IntAct=EBI-396540, EBI-10968534; CC Q12888; P16104: H2AX; NbExp=6; IntAct=EBI-396540, EBI-494830; CC Q12888; P62807: H2BC8; NbExp=6; IntAct=EBI-396540, EBI-354552; CC Q12888; P68431: H3C12; NbExp=5; IntAct=EBI-396540, EBI-79722; CC Q12888; P62805: H4C9; NbExp=14; IntAct=EBI-396540, EBI-302023; CC Q12888; O14964: HGS; NbExp=3; IntAct=EBI-396540, EBI-740220; CC Q12888; P10809: HSPD1; NbExp=3; IntAct=EBI-396540, EBI-352528; CC Q12888; O14901: KLF11; NbExp=3; IntAct=EBI-396540, EBI-948266; CC Q12888; Q96G42: KLHDC7B; NbExp=3; IntAct=EBI-396540, EBI-9478422; CC Q12888; P13473-2: LAMP2; NbExp=3; IntAct=EBI-396540, EBI-21591415; CC Q12888; P50222: MEOX2; NbExp=3; IntAct=EBI-396540, EBI-748397; CC Q12888; Q14686: NCOA6; NbExp=3; IntAct=EBI-396540, EBI-78670; CC Q12888; Q8TDS5: OXER1; NbExp=3; IntAct=EBI-396540, EBI-12813389; CC Q12888; Q6ZW49: PAXIP1; NbExp=4; IntAct=EBI-396540, EBI-743225; CC Q12888; P16284: PECAM1; NbExp=3; IntAct=EBI-396540, EBI-716404; CC Q12888; P78337: PITX1; NbExp=3; IntAct=EBI-396540, EBI-748265; CC Q12888; Q13393: PLD1; NbExp=3; IntAct=EBI-396540, EBI-2827556; CC Q12888; P53350: PLK1; NbExp=6; IntAct=EBI-396540, EBI-476768; CC Q12888; D3DTS7: PMP22; NbExp=3; IntAct=EBI-396540, EBI-25882629; CC Q12888; P78424: POU6F2; NbExp=3; IntAct=EBI-396540, EBI-12029004; CC Q12888; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-396540, EBI-5280197; CC Q12888; P62826: RAN; NbExp=3; IntAct=EBI-396540, EBI-286642; CC Q12888; Q86V20-2: SHLD2; NbExp=3; IntAct=EBI-396540, EBI-20592761; CC Q12888; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-396540, EBI-5235340; CC Q12888; O43711: TLX3; NbExp=3; IntAct=EBI-396540, EBI-3939165; CC Q12888; P04637: TP53; NbExp=8; IntAct=EBI-396540, EBI-366083; CC Q12888; Q5T6F2: UBAP2; NbExp=3; IntAct=EBI-396540, EBI-2514383; CC Q12888; P61086: UBE2K; NbExp=3; IntAct=EBI-396540, EBI-473850; CC Q12888; Q08AM6: VAC14; NbExp=6; IntAct=EBI-396540, EBI-2107455; CC Q12888; P23763-3: VAMP1; NbExp=3; IntAct=EBI-396540, EBI-12097582; CC Q12888; P08670: VIM; NbExp=3; IntAct=EBI-396540, EBI-353844; CC Q12888; Q99986: VRK1; NbExp=8; IntAct=EBI-396540, EBI-1769146; CC Q12888; P04275-2: VWF; NbExp=3; IntAct=EBI-396540, EBI-25896548; CC Q12888; O43257: ZNHIT1; NbExp=2; IntAct=EBI-396540, EBI-347522; CC Q12888; Q6NZQ4: Paxip1; Xeno; NbExp=5; IntAct=EBI-396540, EBI-1395317; CC Q12888-1; P62805: H4C9; NbExp=3; IntAct=EBI-8022649, EBI-302023; CC Q12888-1; Q14686: NCOA6; NbExp=3; IntAct=EBI-8022649, EBI-78670; CC Q12888-1; P63165: SUMO1; NbExp=2; IntAct=EBI-8022649, EBI-80140; CC Q12888-1; P04637: TP53; NbExp=17; IntAct=EBI-8022649, EBI-366083; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11331310, CC ECO:0000269|PubMed:15525939, ECO:0000269|PubMed:16294045, CC ECO:0000269|PubMed:16294047, ECO:0000269|PubMed:17190600, CC ECO:0000269|PubMed:19176521, ECO:0000269|PubMed:21144835, CC ECO:0000269|PubMed:28241136, ECO:0000269|PubMed:9748285}. Chromosome CC {ECO:0000269|PubMed:12824158, ECO:0000269|PubMed:15525939, CC ECO:0000269|PubMed:17190600, ECO:0000269|PubMed:23333306, CC ECO:0000269|PubMed:23760478, ECO:0000269|PubMed:24703952, CC ECO:0000269|PubMed:28241136, ECO:0000269|PubMed:31135337}. Chromosome, CC centromere, kinetochore {ECO:0000250|UniProtKB:P70399}. Note=Localizes CC to the nucleus in absence of DNA damage (PubMed:28241136). Following CC DNA damage, recruited to sites of DNA damage, such as double stand CC breaks (DSBs): recognizes and binds histone H2A monoubiquitinated at CC 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), CC two histone marks that are present at DSBs sites (PubMed:23333306, CC PubMed:23760478, PubMed:24703952, PubMed:28241136, PubMed:17190600, CC PubMed:31135337). Associated with kinetochores during mitosis (By CC similarity). {ECO:0000250|UniProtKB:P70399, CC ECO:0000269|PubMed:17190600, ECO:0000269|PubMed:23333306, CC ECO:0000269|PubMed:23760478, ECO:0000269|PubMed:28241136}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q12888-1; Sequence=Displayed; CC Name=2; CC IsoId=Q12888-2; Sequence=VSP_018390; CC Name=3; CC IsoId=Q12888-3; Sequence=VSP_018390, VSP_055062; CC -!- DOMAIN: The Tudor-like region mediates binding to histone H4 CC dimethylated at 'Lys-20' (H4K20me2) (PubMed:17190600). Interaction with CC NUDT16L1/TIRR masks the Tudor-like domain and prevents recruitment to CC chromatin (PubMed:28241136). {ECO:0000269|PubMed:17190600, CC ECO:0000269|PubMed:28241136}. CC -!- DOMAIN: The UDR (ubiquitin-dependent recruitment) motif specifically CC recognizes and binds histone H2A monoubiquitinated at 'Lys-15' CC (H2AK15ub) (PubMed:23760478, PubMed:24703952). Phosphorylation of the CC UDR blocks interaction with H2AK15ub (PubMed:24703952). CC {ECO:0000269|PubMed:23760478, ECO:0000269|PubMed:24703952}. CC -!- PTM: Asymmetrically dimethylated on Arg residues by PRMT1. Methylation CC is required for DNA binding. {ECO:0000269|PubMed:16294045, CC ECO:0000269|PubMed:16294047}. CC -!- PTM: Phosphorylated at basal level in the absence of DNA damage CC (PubMed:11042216, PubMed:11331310). Phosphorylated by ATM in response CC to DNA damage: phosphorylation at different sites promotes interaction CC with different set of proteins: phosphorylation at the N-terminus by CC ATM (residues from 6-178) promotes interaction with PAXIP1 and non- CC homologous end joining (NHEJ) of dysfunctional telomeres CC (PubMed:23727112). Phosphorylation by ATM at residues that are located CC more C-terminus (residues 300-650) leads to promote interaction with CC RIF1 (PubMed:23727112, PubMed:23333306, PubMed:28241136). Interaction CC with RIF1 leads to disrupt interaction with NUDT16L1/TIRR CC (PubMed:28241136). Phosphorylation at Thr-1609 and Ser-1618 in the UDR CC motif blocks interaction with H2AK15ub (PubMed:24703952). CC Dephosphorylated by PPP4C (PubMed:24703952). Hyperphosphorylation CC during mitosis correlates with its exclusion from chromatin and DNA CC lesions. Hyperphosphorylated in an ATR-dependent manner in response to CC DNA damage induced by UV irradiation (PubMed:17553757, CC PubMed:21144835). Dephosphorylated by PPP5C (PubMed:19176521). CC Phosphorylation at Ser-366 and Thr-670 promotes interaction with TOPBP1 CC (PubMed:31135337). {ECO:0000269|PubMed:11042216, CC ECO:0000269|PubMed:11331310, ECO:0000269|PubMed:17553757, CC ECO:0000269|PubMed:19176521, ECO:0000269|PubMed:21144835, CC ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23727112, CC ECO:0000269|PubMed:24703952, ECO:0000269|PubMed:28241136, CC ECO:0000269|PubMed:31135337}. CC -!- DISEASE: Note=A chromosomal aberration involving TP53BP1 is found in a CC form of myeloproliferative disorder chronic with eosinophilia. CC Translocation t(5;15)(q33;q22) with PDGFRB creating a TP53BP1-PDGFRB CC fusion protein. {ECO:0000269|PubMed:15492236}. CC -!- SEQUENCE CAUTION: CC Sequence=BAE06107.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/tp53bp1/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF078776; AAC62018.1; -; mRNA. DR EMBL; AB210025; BAE06107.1; ALT_INIT; mRNA. DR EMBL; BX537418; CAD97660.1; -; mRNA. DR EMBL; AY904026; AAW69392.1; -; Genomic_DNA. DR EMBL; AC018924; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC112161; AAI12162.1; -; mRNA. DR EMBL; U09477; AAA21596.1; -; mRNA. DR CCDS; CCDS10096.1; -. [Q12888-1] DR CCDS; CCDS45250.1; -. [Q12888-2] DR CCDS; CCDS45251.1; -. [Q12888-3] DR PIR; I38604; I38604. DR RefSeq; NP_001135451.1; NM_001141979.1. [Q12888-3] DR RefSeq; NP_001135452.1; NM_001141980.1. [Q12888-2] DR RefSeq; NP_005648.1; NM_005657.2. [Q12888-1] DR PDB; 1GZH; X-ray; 2.60 A; B/D=1724-1972. DR PDB; 1KZY; X-ray; 2.50 A; C/D=1714-1972. DR PDB; 1XNI; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J=1485-1602. DR PDB; 2G3R; X-ray; 1.25 A; A=1484-1603. DR PDB; 2IG0; X-ray; 1.70 A; A=1484-1603. DR PDB; 2LVM; NMR; -; A=1484-1603. DR PDB; 2MWO; NMR; -; A=1484-1603. DR PDB; 2MWP; NMR; -; A=1484-1603. DR PDB; 3LGF; X-ray; 1.50 A; A=1484-1603. DR PDB; 3LGL; X-ray; 1.60 A; A=1484-1603. DR PDB; 3LH0; X-ray; 1.90 A; A=1484-1603. DR PDB; 4CRI; X-ray; 2.35 A; A/B=1459-1634. DR PDB; 4RG2; X-ray; 1.50 A; A/B=1483-1606. DR PDB; 4X34; X-ray; 1.80 A; A/B=1484-1603. DR PDB; 5ECG; X-ray; 3.00 A; C/D=1713-1972. DR PDB; 5J26; X-ray; 2.50 A; A=1487-1603. DR PDB; 5KGF; EM; 4.54 A; K/L=1611-1631. DR PDB; 5Z78; X-ray; 1.76 A; C=1484-1603. DR PDB; 5ZCJ; X-ray; 2.00 A; C=1459-1634. DR PDB; 6CO1; X-ray; 2.18 A; E/F=1484-1603. DR PDB; 6CO2; X-ray; 2.49 A; C/D=1484-1603. DR PDB; 6IU7; X-ray; 1.90 A; B=1665-1686. DR PDB; 6IUA; X-ray; 1.70 A; B=1665-1686. DR PDB; 6MXX; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/J=1484-1603. DR PDB; 6MXY; X-ray; 1.62 A; A/B=1484-1603. DR PDB; 6MXZ; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J=1484-1603. DR PDB; 6MY0; X-ray; 2.20 A; A/B=1484-1603. DR PDB; 6RML; X-ray; 2.81 A; C=663-677. DR PDB; 6RMM; X-ray; 3.53 A; P/R=359-373. DR PDB; 6UPT; X-ray; 1.96 A; A/B=1483-1606. DR PDB; 6VA5; X-ray; 1.28 A; A=1483-1606. DR PDB; 6VIP; X-ray; 1.36 A; A/B=1483-1606. DR PDB; 7LIN; X-ray; 1.44 A; B=1636-1650. DR PDB; 7LIO; X-ray; 3.01 A; C/D=1636-1650. DR PDB; 7YQK; EM; 3.38 A; K=1613-1630, N=1485-1602. DR PDB; 8EOM; X-ray; 1.70 A; A/B=1483-1606. DR PDB; 8F0W; X-ray; 1.52 A; A/B=1483-1606. DR PDB; 8HKW; X-ray; 1.90 A; C/D=1665-1686. DR PDB; 8SWJ; X-ray; 1.60 A; A/B/C/D=1483-1606. DR PDB; 8U4U; X-ray; 3.79 A; A/B/C/D/E/F/G/H/I/J=1484-1603. DR PDBsum; 1GZH; -. DR PDBsum; 1KZY; -. DR PDBsum; 1XNI; -. DR PDBsum; 2G3R; -. DR PDBsum; 2IG0; -. DR PDBsum; 2LVM; -. DR PDBsum; 2MWO; -. DR PDBsum; 2MWP; -. DR PDBsum; 3LGF; -. DR PDBsum; 3LGL; -. DR PDBsum; 3LH0; -. DR PDBsum; 4CRI; -. DR PDBsum; 4RG2; -. DR PDBsum; 4X34; -. DR PDBsum; 5ECG; -. DR PDBsum; 5J26; -. DR PDBsum; 5KGF; -. DR PDBsum; 5Z78; -. DR PDBsum; 5ZCJ; -. DR PDBsum; 6CO1; -. DR PDBsum; 6CO2; -. DR PDBsum; 6IU7; -. DR PDBsum; 6IUA; -. DR PDBsum; 6MXX; -. DR PDBsum; 6MXY; -. DR PDBsum; 6MXZ; -. DR PDBsum; 6MY0; -. DR PDBsum; 6RML; -. DR PDBsum; 6RMM; -. DR PDBsum; 6UPT; -. DR PDBsum; 6VA5; -. DR PDBsum; 6VIP; -. DR PDBsum; 7LIN; -. DR PDBsum; 7LIO; -. DR PDBsum; 7YQK; -. DR PDBsum; 8EOM; -. DR PDBsum; 8F0W; -. DR PDBsum; 8HKW; -. DR PDBsum; 8SWJ; -. DR PDBsum; 8U4U; -. DR AlphaFoldDB; Q12888; -. DR BMRB; Q12888; -. DR SMR; Q12888; -. DR BioGRID; 113011; 520. DR CORUM; Q12888; -. DR DIP; DIP-5978N; -. DR IntAct; Q12888; 369. DR MINT; Q12888; -. DR STRING; 9606.ENSP00000371475; -. DR BindingDB; Q12888; -. DR ChEMBL; CHEMBL2424509; -. DR GlyCosmos; Q12888; 3 sites, 1 glycan. DR GlyGen; Q12888; 10 sites, 1 O-linked glycan (10 sites). DR iPTMnet; Q12888; -. DR MetOSite; Q12888; -. DR PhosphoSitePlus; Q12888; -. DR SwissPalm; Q12888; -. DR BioMuta; TP53BP1; -. DR DMDM; 8928568; -. DR CPTAC; CPTAC-1014; -. DR CPTAC; CPTAC-1015; -. DR CPTAC; CPTAC-1334; -. DR CPTAC; CPTAC-2608; -. DR CPTAC; CPTAC-2609; -. DR CPTAC; CPTAC-5914; -. DR CPTAC; CPTAC-5915; -. DR CPTAC; CPTAC-5916; -. DR CPTAC; CPTAC-5917; -. DR EPD; Q12888; -. DR jPOST; Q12888; -. DR MassIVE; Q12888; -. DR MaxQB; Q12888; -. DR PaxDb; 9606-ENSP00000371475; -. DR PeptideAtlas; Q12888; -. DR ProteomicsDB; 29194; -. DR ProteomicsDB; 59003; -. [Q12888-1] DR ProteomicsDB; 59004; -. [Q12888-2] DR Pumba; Q12888; -. DR ABCD; Q12888; 6 sequenced antibodies. DR Antibodypedia; 1749; 1100 antibodies from 41 providers. DR CPTC; Q12888; 1 antibody. DR DNASU; 7158; -. DR Ensembl; ENST00000263801.7; ENSP00000263801.3; ENSG00000067369.14. [Q12888-1] DR Ensembl; ENST00000382044.9; ENSP00000371475.5; ENSG00000067369.14. [Q12888-2] DR Ensembl; ENST00000450115.6; ENSP00000393497.2; ENSG00000067369.14. [Q12888-3] DR GeneID; 7158; -. DR KEGG; hsa:7158; -. DR MANE-Select; ENST00000382044.9; ENSP00000371475.5; NM_001141980.3; NP_001135452.1. [Q12888-2] DR UCSC; uc001zrq.5; human. [Q12888-1] DR AGR; HGNC:11999; -. DR CTD; 7158; -. DR DisGeNET; 7158; -. DR GeneCards; TP53BP1; -. DR HGNC; HGNC:11999; TP53BP1. DR HPA; ENSG00000067369; Low tissue specificity. DR MalaCards; TP53BP1; -. DR MIM; 605230; gene. DR neXtProt; NX_Q12888; -. DR OpenTargets; ENSG00000067369; -. DR PharmGKB; PA36680; -. DR VEuPathDB; HostDB:ENSG00000067369; -. DR eggNOG; KOG3548; Eukaryota. DR GeneTree; ENSGT00390000011891; -. DR HOGENOM; CLU_002167_0_0_1; -. DR InParanoid; Q12888; -. DR OMA; EPCVENR; -. DR OrthoDB; 5403076at2759; -. DR PhylomeDB; Q12888; -. DR TreeFam; TF350227; -. DR PathwayCommons; Q12888; -. DR Reactome; R-HSA-3232118; SUMOylation of transcription factors. DR Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks. DR Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ). DR Reactome; R-HSA-5693607; Processing of DNA double-strand break ends. DR Reactome; R-HSA-69473; G2/M DNA damage checkpoint. DR SignaLink; Q12888; -. DR SIGNOR; Q12888; -. DR BioGRID-ORCS; 7158; 38 hits in 1177 CRISPR screens. DR ChiTaRS; TP53BP1; human. DR EvolutionaryTrace; Q12888; -. DR GeneWiki; TP53BP1; -. DR GenomeRNAi; 7158; -. DR Pharos; Q12888; Tbio. DR PRO; PR:Q12888; -. DR Proteomes; UP000005640; Chromosome 15. DR RNAct; Q12888; Protein. DR Bgee; ENSG00000067369; Expressed in pituitary gland and 200 other cell types or tissues. DR ExpressionAtlas; Q12888; baseline and differential. DR GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; IDA:ProtInc. DR GO; GO:1990391; C:DNA repair complex; IEA:Ensembl. DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005657; C:replication fork; IEA:Ensembl. DR GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB. DR GO; GO:0003684; F:damaged DNA binding; IEA:Ensembl. DR GO; GO:0042393; F:histone binding; IBA:GO_Central. DR GO; GO:0140566; F:histone reader activity; IDA:UniProtKB. DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB. DR GO; GO:0002039; F:p53 binding; IPI:AgBase. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL. DR GO; GO:0042162; F:telomeric DNA binding; IEA:Ensembl. DR GO; GO:0003712; F:transcription coregulator activity; IMP:BHF-UCL. DR GO; GO:0061649; F:ubiquitin modification-dependent histone binding; IDA:UniProtKB. DR GO; GO:0071481; P:cellular response to X-ray; IEA:Ensembl. DR GO; GO:0000077; P:DNA damage checkpoint signaling; IBA:GO_Central. DR GO; GO:0006974; P:DNA damage response; IDA:UniProtKB. DR GO; GO:0097680; P:double-strand break repair via classical nonhomologous end joining; IDA:UniProt. DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IDA:UniProtKB. DR GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; IDA:UniProtKB. DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IC:BHF-UCL. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; NAS:UniProtKB. DR GO; GO:0045830; P:positive regulation of isotype switching; IDA:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL. DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB. DR CDD; cd17745; BRCT_p53bp1_rpt1; 1. DR CDD; cd17724; BRCT_p53bp1_rpt2; 1. DR CDD; cd20383; Tudor_53BP1; 1. DR DisProt; DP02954; -. DR Gene3D; 2.30.30.140; -; 1. DR Gene3D; 2.30.30.30; -; 1. DR Gene3D; 3.40.50.10190; BRCT domain; 2. DR IDEAL; IID00123; -. DR InterPro; IPR015125; 53-BP1_Tudor. DR InterPro; IPR001357; BRCT_dom. DR InterPro; IPR036420; BRCT_dom_sf. DR InterPro; IPR047249; BRCT_p53bp1-like_rpt1. DR InterPro; IPR047250; BRCT_p53bp1-like_rpt2. DR InterPro; IPR014722; Rib_uL2_dom2. DR InterPro; IPR047252; TP53BP1-like. DR PANTHER; PTHR15321:SF3; TP53-BINDING PROTEIN 1; 1. DR PANTHER; PTHR15321; TUMOR SUPPRESSOR P53-BINDING PROTEIN 1; 1. DR Pfam; PF09038; 53-BP1_Tudor; 1. DR Pfam; PF18428; BRCT_3; 1. DR SMART; SM00292; BRCT; 2. DR SUPFAM; SSF52113; BRCT domain; 2. DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 2. DR PROSITE; PS50172; BRCT; 2. DR Genevisible; Q12888; HS. PE 1: Evidence at protein level; KW 3D-structure; Activator; Alternative splicing; Centromere; KW Chromosomal rearrangement; Chromosome; DNA damage; DNA repair; DNA-binding; KW Host-virus interaction; Isopeptide bond; Kinetochore; Methylation; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; Transcription; KW Transcription regulation; Ubl conjugation. FT CHAIN 1..1972 FT /note="TP53-binding protein 1" FT /id="PRO_0000072643" FT DOMAIN 1724..1848 FT /note="BRCT 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033" FT DOMAIN 1864..1964 FT /note="BRCT 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033" FT REGION 24..273 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 290..332 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 346..507 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 520..556 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 568..595 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 649..687 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 742..911 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 997..1028 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1045..1103 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1127..1148 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1188..1232 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1269..1478 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1484..1603 FT /note="Tudor-like" FT /evidence="ECO:0000305|PubMed:17190600" FT REGION 1495..1523 FT /note="Interaction with dimethylated histone H4" FT /evidence="ECO:0000269|PubMed:17190600" FT REGION 1622..1719 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1745..1768 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 1396..1403 FT /note="GAR" FT /evidence="ECO:0000269|PubMed:16294045" FT MOTIF 1604..1631 FT /note="UDR" FT /evidence="ECO:0000269|PubMed:23760478" FT COMPBIAS 31..63 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 76..92 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 93..124 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 130..152 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 153..209 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 346..366 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 424..441 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 452..469 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 580..595 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 794..822 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 848..878 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 887..905 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1068..1082 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1188..1202 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1216..1232 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1284..1329 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1632..1655 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1669..1683 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 25 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:19176521" FT MOD_RES 63 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 105 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332" FT MOD_RES 124 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 166 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:17553757" FT MOD_RES 176 FT /note="Phosphoserine" FT /evidence="ECO:0000305|PubMed:17553757" FT MOD_RES 178 FT /note="Phosphoserine" FT /evidence="ECO:0000305|PubMed:17553757" FT MOD_RES 222 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 265 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 294 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:17553757, FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 302 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:17553757, FT ECO:0007744|PubMed:17525332" FT MOD_RES 366 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:31135337, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" FT MOD_RES 380 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:17553757, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" FT MOD_RES 395 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 398 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 429 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P70399" FT MOD_RES 452 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:17553757" FT MOD_RES 464 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P70399" FT MOD_RES 500 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 507 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 518 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 523 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:17553757, FT ECO:0007744|PubMed:17525332, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" FT MOD_RES 525 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 543 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17525332, FT ECO:0007744|PubMed:19690332" FT MOD_RES 548 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17525332" FT MOD_RES 552 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:17553757, FT ECO:0007744|PubMed:17525332, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 566 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 580 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 630 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 635 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983" FT MOD_RES 639 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231" FT MOD_RES 640 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231" FT MOD_RES 670 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:31135337" FT MOD_RES 692 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 724 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P70399" FT MOD_RES 727 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 771 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 809 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 830 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P70399" FT MOD_RES 831 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:17553757, FT ECO:0007744|PubMed:17525332, ECO:0007744|PubMed:18669648" FT MOD_RES 834 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" FT MOD_RES 855 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17525332" FT MOD_RES 922 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 970 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 975 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 1028 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:17553757, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1056 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1068 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1086 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:17553757" FT MOD_RES 1094 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163" FT MOD_RES 1101 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 1114 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:17553757, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 1148 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1214 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17525332" FT MOD_RES 1216 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 1219 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:17553757, FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17525332, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163" FT MOD_RES 1317 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1342 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1355 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:P70399" FT MOD_RES 1362 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 1368 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1372 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1426 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 1430 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 1460 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 1462 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" FT MOD_RES 1474 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 1609 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:24703952, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1618 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:24703952, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1631 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P70399" FT MOD_RES 1635 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1638 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1648 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1656 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1673 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1678 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1701 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1759 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1778 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:19176521, FT ECO:0000269|PubMed:21144835" FT CROSSLNK 217 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 217 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25114211, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 868 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 868 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 930 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 984 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1365 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1434 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 1434 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25114211, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 1563 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 1563 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25114211, FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:28112733" FT VAR_SEQ 1 FT /note="M -> MPGEQM (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:17974005, ECO:0000303|Ref.2" FT /id="VSP_018390" FT VAR_SEQ 1692..1693 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_055062" FT VARIANT 353 FT /note="D -> E (in dbSNP:rs560191)" FT /evidence="ECO:0000269|PubMed:17974005, ECO:0000269|Ref.4" FT /id="VAR_022172" FT VARIANT 412 FT /note="G -> S (in dbSNP:rs689647)" FT /evidence="ECO:0000269|PubMed:17974005, ECO:0000269|Ref.4" FT /id="VAR_022173" FT VARIANT 648 FT /note="M -> V (in dbSNP:rs45443496)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_022174" FT VARIANT 699 FT /note="Q -> R (in dbSNP:rs34823068)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_022175" FT VARIANT 841 FT /note="D -> G (in dbSNP:rs34185035)" FT /id="VAR_034558" FT VARIANT 1014 FT /note="E -> G (in dbSNP:rs45470395)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_022176" FT VARIANT 1026 FT /note="V -> A (in dbSNP:rs45482998)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_022177" FT VARIANT 1136 FT /note="K -> Q (in dbSNP:rs2602141)" FT /evidence="ECO:0000269|PubMed:17974005, ECO:0000269|Ref.4" FT /id="VAR_022178" FT VARIANT 1137 FT /note="E -> K (in dbSNP:rs34740611)" FT /id="VAR_034559" FT VARIANT 1170 FT /note="A -> G (in dbSNP:rs45500399)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_022179" FT VARIANT 1174 FT /note="I -> V (in dbSNP:rs3803339)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_022180" FT VARIANT 1442 FT /note="R -> Q (in dbSNP:rs2230449)" FT /id="VAR_034560" FT VARIANT 1488 FT /note="G -> W (in dbSNP:rs11554564)" FT /id="VAR_038689" FT MUTAGEN 6 FT /note="S->A: In 28A: Defects in recruitment to double FT strand breaks (DSBs), abolished interaction with RIF1 and FT abolished ability to repair DSBs; when associated with FT A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; FT A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; FT A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; FT A-1171 and A-1219. In 8A: Does not affect interaction with FT RIF1 and ability to promote immunoglobulin class-switch FT recombination (CSR), but abolishes interaction with PAXIP1 FT and ability to promote NHEJ of dysfunctional telomeres; FT when associated with A-13; A-25; A-29; A-105; A-166; A-176 FT and A-178." FT /evidence="ECO:0000269|PubMed:23333306, FT ECO:0000269|PubMed:23345425, ECO:0000269|PubMed:23727112" FT MUTAGEN 13 FT /note="S->A: In 28A: Defects in recruitment to double FT strand breaks (DSBs), abolished interaction with RIF1 and FT abolished ability to repair DSBs; when associated with A-6; FT A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; FT A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; FT A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; FT A-1171 and A-1219. In 8A: Does not affect interaction with FT RIF1 and ability to promote immunoglobulin class-switch FT recombination (CSR), but abolishes interaction with PAXIP1 FT and ability to promote NHEJ of dysfunctional telomeres; FT when associated with A-6; A-25; A-29; A-105; A-166; A-176 FT and A-178." FT /evidence="ECO:0000269|PubMed:23333306, FT ECO:0000269|PubMed:23345425, ECO:0000269|PubMed:23727112" FT MUTAGEN 25 FT /note="S->A: In 28A: Defects in recruitment to double FT strand breaks (DSBs), abolished interaction with RIF1 and FT abolished ability to repair DSBs; when associated with A-6; FT A-13; A-29; A-105; A-166; A-176; A-178; A-302; A-437; FT A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; FT A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; FT A-1171 and A-1219. In 8A: Does not affect interaction with FT RIF1 and ability to promote immunoglobulin class-switch FT recombination (CSR), but abolishes interaction with PAXIP1 FT and ability to promote NHEJ of dysfunctional telomeres; FT when associated with A-6; A-13; A-29; A-105; A-166; A-176 FT and A-178." FT /evidence="ECO:0000269|PubMed:23333306, FT ECO:0000269|PubMed:23345425, ECO:0000269|PubMed:23727112" FT MUTAGEN 29 FT /note="S->A: In 28A: Defects in recruitment to double FT strand breaks (DSBs), abolished interaction with RIF1 and FT abolished ability to repair DSBs; when associated with A-6; FT A-13; A-25; A-105; A-166; A-176; A-178; A-302; A-437; FT A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; FT A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; FT A-1171 and A-1219. In 8A: Does not affect interaction with FT RIF1 and ability to promote immunoglobulin class-switch FT recombination (CSR), but abolishes interaction with PAXIP1 FT and ability to promote NHEJ of dysfunctional telomeres; FT when associated with A-6; A-13; A-25; A-105; A-166; A-176 FT and A-178." FT /evidence="ECO:0000269|PubMed:23333306, FT ECO:0000269|PubMed:23345425, ECO:0000269|PubMed:23727112" FT MUTAGEN 105 FT /note="S->A: In 28A: Defects in recruitment to double FT strand breaks (DSBs), abolished interaction with RIF1 and FT abolished ability to repair DSBs; when associated with A-6; FT A-13; A-25; A-29; A-166; A-176; A-178; A-302; A-437; A-452; FT A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; FT A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 FT and A-1219. In 8A: Does not affect interaction with RIF1 FT and ability to promote immunoglobulin class-switch FT recombination (CSR), but abolishes interaction with PAXIP1 FT and ability to promote NHEJ of dysfunctional telomeres; FT when associated with A-6; A-13; A-25; A-29; A-166; A-176 FT and A-178." FT /evidence="ECO:0000269|PubMed:23333306, FT ECO:0000269|PubMed:23345425, ECO:0000269|PubMed:23727112" FT MUTAGEN 166 FT /note="S->A: In 28A: Defects in recruitment to double FT strand breaks (DSBs), abolished interaction with RIF1 and FT abolished ability to repair DSBs; when associated with A-6; FT A-13; A-25; A-29; A-105; A-176; A-178; A-302; A-437; A-452; FT A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; FT A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 FT and A-1219. In 8A: Does not affect interaction with RIF1 FT and ability to promote immunoglobulin class-switch FT recombination (CSR), but abolishes interaction with PAXIP1 FT and ability to promote NHEJ of dysfunctional telomeres; FT when associated with A-6; A-13; A-25; A-29; A-105; A-176 FT and A-178." FT /evidence="ECO:0000269|PubMed:23333306, FT ECO:0000269|PubMed:23345425, ECO:0000269|PubMed:23727112" FT MUTAGEN 176..178 FT /note="SQS->AQA: Loss of phosphorylation site." FT /evidence="ECO:0000269|PubMed:17553757" FT MUTAGEN 176 FT /note="S->A: In 28A: Defects in recruitment to double FT strand breaks (DSBs), abolished interaction with RIF1 and FT abolished ability to repair DSBs; when associated with A-6; FT A-13; A-25; A-29; A-105; A-166; A-178; A-302; A-437; A-452; FT A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; FT A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 FT and A-1219. In 8A: Does not affect interaction with RIF1 FT and ability to promote immunoglobulin class-switch FT recombination (CSR), but abolishes interaction with PAXIP1 FT and ability to promote NHEJ of dysfunctional telomeres; FT when associated with A-6; A-13; A-25; A-29; A-105; A-166 FT and A-178." FT /evidence="ECO:0000269|PubMed:23333306, FT ECO:0000269|PubMed:23345425, ECO:0000269|PubMed:23727112" FT MUTAGEN 178 FT /note="S->A: In 28A: Defects in recruitment to double FT strand breaks (DSBs), abolished interaction with RIF1 and FT abolished ability to repair DSBs; when associated with A-6; FT A-13; A-25; A-29; A-105; A-166; A-176; A-302; A-437; A-452; FT A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; FT A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 FT and A-1219. In 8A: Does not affect interaction with RIF1 FT and ability to promote immunoglobulin class-switch FT recombination (CSR), but abolishes interaction with PAXIP1 FT and ability to promote NHEJ of dysfunctional telomeres; FT when associated with A-6; A-13; A-25; A-29; A-105; A-166 FT and A-176." FT /evidence="ECO:0000269|PubMed:23333306, FT ECO:0000269|PubMed:23345425, ECO:0000269|PubMed:23727112" FT MUTAGEN 302 FT /note="T->A: In 28A: Defects in recruitment to double FT strand breaks (DSBs), abolished interaction with RIF1 and FT abolished ability to repair DSBs; when associated with A-6; FT A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-437; A-452; FT A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; FT A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 FT and A-1219." FT /evidence="ECO:0000269|PubMed:23333306, FT ECO:0000269|PubMed:23345425" FT MUTAGEN 366 FT /note="S->A: Decreased interaction with TOPBP1." FT /evidence="ECO:0000269|PubMed:31135337" FT MUTAGEN 437 FT /note="S->A: In 28A: Defects in recruitment to double FT strand breaks (DSBs), abolished interaction with RIF1 and FT abolished ability to repair DSBs; when associated with A-6; FT A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-452; FT A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; FT A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 FT and A-1219." FT /evidence="ECO:0000269|PubMed:23333306, FT ECO:0000269|PubMed:23345425" FT MUTAGEN 452 FT /note="S->A: In 28A: Defects in recruitment to double FT strand breaks (DSBs), abolished interaction with RIF1 and FT abolished ability to repair DSBs; when associated with A-6; FT A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; FT A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; FT A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 FT and A-1219." FT /evidence="ECO:0000269|PubMed:23333306, FT ECO:0000269|PubMed:23345425" FT MUTAGEN 523 FT /note="S->A: In 28A: Defects in recruitment to double FT strand breaks (DSBs), abolished interaction with RIF1 and FT abolished ability to repair DSBs; when associated with A-6; FT A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; FT A-452; A-543; A-580; A-625; A-674; A-696; A-698; A-784; FT A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 FT and A-1219." FT /evidence="ECO:0000269|PubMed:23333306, FT ECO:0000269|PubMed:23345425" FT MUTAGEN 543 FT /note="T->A: In 28A: Defects in recruitment to double FT strand breaks (DSBs), abolished interaction with RIF1 and FT abolished ability to repair DSBs; when associated with A-6; FT A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; FT A-452; A-523; A-580; A-625; A-674; A-696; A-698; A-784; FT A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 FT and A-1219." FT /evidence="ECO:0000269|PubMed:23333306, FT ECO:0000269|PubMed:23345425" FT MUTAGEN 580 FT /note="S->A: In 28A: Defects in recruitment to double FT strand breaks (DSBs), abolished interaction with RIF1 and FT abolished ability to repair DSBs; when associated with A-6; FT A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; FT A-452; A-523; A-543; A-625; A-674; A-696; A-698; A-784; FT A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 FT and A-1219." FT /evidence="ECO:0000269|PubMed:23333306, FT ECO:0000269|PubMed:23345425" FT MUTAGEN 625 FT /note="S->A: In 28A: Defects in recruitment to double FT strand breaks (DSBs), abolished interaction with RIF1 and FT abolished ability to repair DSBs; when associated with A-6; FT A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; FT A-452; A-523; A-543; A-580; A-674; A-696; A-698; A-784; FT A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 FT and A-1219." FT /evidence="ECO:0000269|PubMed:23333306, FT ECO:0000269|PubMed:23345425" FT MUTAGEN 670 FT /note="T->A: Decreased interaction with TOPBP1." FT /evidence="ECO:0000269|PubMed:31135337" FT MUTAGEN 674 FT /note="S->A: In 28A: Defects in recruitment to double FT strand breaks (DSBs), abolished interaction with RIF1 and FT abolished ability to repair DSBs; when associated with A-6; FT A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; FT A-452; A-523; A-543; A-580; A-625; A-696; A-698; A-784; FT A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 FT and A-1219." FT /evidence="ECO:0000269|PubMed:23333306, FT ECO:0000269|PubMed:23345425" FT MUTAGEN 696 FT /note="T->A: In 28A: Defects in recruitment to double FT strand breaks (DSBs), abolished interaction with RIF1 and FT abolished ability to repair DSBs; when associated with A-6; FT A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; FT A-452; A-523; A-543; A-580; A-625; A-674; A-698; A-784; FT A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 FT and A-1219." FT /evidence="ECO:0000269|PubMed:23333306, FT ECO:0000269|PubMed:23345425" FT MUTAGEN 698 FT /note="S->A: In 28A: Defects in recruitment to double FT strand breaks (DSBs), abolished interaction with RIF1 and FT abolished ability to repair DSBs; when associated with A-6; FT A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; FT A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-784; FT A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 FT and A-1219." FT /evidence="ECO:0000269|PubMed:23333306, FT ECO:0000269|PubMed:23345425" FT MUTAGEN 784 FT /note="S->A: In 28A: Defects in recruitment to double FT strand breaks (DSBs), abolished interaction with RIF1 and FT abolished ability to repair DSBs; when associated with A-6; FT A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; FT A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; FT A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 FT and A-1219." FT /evidence="ECO:0000269|PubMed:23333306, FT ECO:0000269|PubMed:23345425" FT MUTAGEN 831 FT /note="S->A: In 28A: Defects in recruitment to double FT strand breaks (DSBs), abolished interaction with RIF1 and FT abolished ability to repair DSBs; when associated with A-6; FT A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; FT A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; FT A-784; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 FT and A-1219." FT /evidence="ECO:0000269|PubMed:23333306, FT ECO:0000269|PubMed:23345425" FT MUTAGEN 855 FT /note="T->A: In 28A: Defects in recruitment to double FT strand breaks (DSBs), abolished interaction with RIF1 and FT abolished ability to repair DSBs; when associated with A-6; FT A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; FT A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; FT A-784; A-831; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 FT and A-1219." FT /evidence="ECO:0000269|PubMed:23333306, FT ECO:0000269|PubMed:23345425" FT MUTAGEN 892 FT /note="S->A: In 28A: Defects in recruitment to double FT strand breaks (DSBs), abolished interaction with RIF1 and FT abolished ability to repair DSBs; when associated with A-6; FT A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; FT A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; FT A-784; A-831; A-855; A-1068; A-1086; A-1104; A-1148; A-1171 FT and A-1219." FT /evidence="ECO:0000269|PubMed:23333306, FT ECO:0000269|PubMed:23345425" FT MUTAGEN 1068 FT /note="S->A: In 28A: Defects in recruitment to double FT strand breaks (DSBs), abolished interaction with RIF1 and FT abolished ability to repair DSBs; when associated with A-6; FT A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; FT A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; FT A-784; A-831; A-855; A-892; A-1086; A-1104; A-1148; A-1171 FT and A-1219." FT /evidence="ECO:0000269|PubMed:23333306, FT ECO:0000269|PubMed:23345425" FT MUTAGEN 1086 FT /note="S->A: In 28A: Defects in recruitment to double FT strand breaks (DSBs), abolished interaction with RIF1 and FT abolished ability to repair DSBs; when associated with A-6; FT A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; FT A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; FT A-784; A-831; A-855; A-892; A-1068; A-1104; A-1148; A-1171 FT and A-1219." FT /evidence="ECO:0000269|PubMed:23333306, FT ECO:0000269|PubMed:23345425" FT MUTAGEN 1104 FT /note="S->A: In 28A: Defects in recruitment to double FT strand breaks (DSBs), abolished interaction with RIF1 and FT abolished ability to repair DSBs; when associated with A-6; FT A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; FT A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; FT A-784; A-831; A-855; A-892; A-1068; A-1086; A-1148; A-1171 FT and A-1219." FT /evidence="ECO:0000269|PubMed:23333306, FT ECO:0000269|PubMed:23345425" FT MUTAGEN 1148 FT /note="S->A: In 28A: Defects in recruitment to double FT strand breaks (DSBs), abolished interaction with RIF1 and FT abolished ability to repair DSBs; when associated with A-6; FT A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; FT A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; FT A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1171 FT and A-1219." FT /evidence="ECO:0000269|PubMed:23333306, FT ECO:0000269|PubMed:23345425" FT MUTAGEN 1171 FT /note="T->A: In 28A: Defects in recruitment to double FT strand breaks (DSBs), abolished interaction with RIF1 and FT abolished ability to repair DSBs; when associated with A-6; FT A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; FT A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; FT A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148 FT and A-1219." FT /evidence="ECO:0000269|PubMed:23333306, FT ECO:0000269|PubMed:23345425" FT MUTAGEN 1219 FT /note="S->A: In 28A: Defects in recruitment to double FT strand breaks (DSBs), abolished interaction with RIF1 and FT abolished ability to repair DSBs; when associated with A-6; FT A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; FT A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; FT A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148 FT and A-1171." FT /evidence="ECO:0000269|PubMed:23333306, FT ECO:0000269|PubMed:23345425" FT MUTAGEN 1396 FT /note="R->A: No detectable effect on methylation by PRMT1 FT (in vitro). Loss of methylation; when associated with FT A-1398; A-1400; A-1401 and A-1403." FT /evidence="ECO:0000269|PubMed:16294045, FT ECO:0000269|PubMed:16294047" FT MUTAGEN 1396 FT /note="R->K: No detectable effect on methylation by PRMT1 FT (in vitro)." FT /evidence="ECO:0000269|PubMed:16294045, FT ECO:0000269|PubMed:16294047" FT MUTAGEN 1398..1401 FT /note="RGRR->AGAA: No effect on in class-switch FT recombination (CSR)." FT /evidence="ECO:0000269|PubMed:23345425" FT MUTAGEN 1398 FT /note="R->A: No detectable effect on methylation by PRMT1 FT (in vitro). Loss of methylation; when associated with FT A-1396; A-1400; A-1401 and A-1403." FT /evidence="ECO:0000269|PubMed:16294045, FT ECO:0000269|PubMed:16294047" FT MUTAGEN 1398 FT /note="R->K: Reduced methylation by PRMT1 (in vitro). FT Strongly reduced methylation; when associated with K-1400. FT Strongly reduced methylation; when associated with K-1401." FT /evidence="ECO:0000269|PubMed:16294045, FT ECO:0000269|PubMed:16294047" FT MUTAGEN 1400 FT /note="R->A: No detectable effect on methylation by PRMT1 FT (in vitro). Loss of methylation; when associated with FT A-1396; A-1398; A-1401 and A-1403." FT /evidence="ECO:0000269|PubMed:16294045, FT ECO:0000269|PubMed:16294047" FT MUTAGEN 1400 FT /note="R->K: Reduced methylation by PRMT1 (in vitro). FT Strongly reduced methylation; when associated with K-1398. FT Strongly reduced methylation; when associated with K-1401." FT /evidence="ECO:0000269|PubMed:16294045, FT ECO:0000269|PubMed:16294047" FT MUTAGEN 1401 FT /note="R->A: No detectable effect on methylation by PRMT1 FT (in vitro). Loss of methylation; when associated with FT A-1396; A-1398; A-1400 and A-1403." FT /evidence="ECO:0000269|PubMed:16294045, FT ECO:0000269|PubMed:16294047" FT MUTAGEN 1401 FT /note="R->K: Reduced methylation by PRMT1 (in vitro). FT Strongly reduced methylation; when associated with K-1398. FT Strongly reduced methylation; when associated with K-1400." FT /evidence="ECO:0000269|PubMed:16294045, FT ECO:0000269|PubMed:16294047" FT MUTAGEN 1403 FT /note="R->A: No detectable effect on methylation by PRMT1 FT (in vitro). Loss of methylation; when associated with FT A-1396; A-1398; A-1400 and A-1401." FT /evidence="ECO:0000269|PubMed:16294045, FT ECO:0000269|PubMed:16294047" FT MUTAGEN 1403 FT /note="R->K: No detectable effect on methylation by PRMT1 FT (in vitro)." FT /evidence="ECO:0000269|PubMed:16294045, FT ECO:0000269|PubMed:16294047" FT MUTAGEN 1495 FT /note="W->A,H: Loss of interaction with histone H4 that has FT been dimethylated at 'Lys-20' (H4K20me2). Abolishes FT recruitment to double strand breaks. Loss of interaction FT with histone H4 that has been dimethylated at 'Lys-20' FT (H4K20me2). Abolishes recruitment to double strand breaks; FT when associated with A-1521." FT /evidence="ECO:0000269|PubMed:15525939, FT ECO:0000269|PubMed:17190600, ECO:0000269|PubMed:28241136" FT MUTAGEN 1495 FT /note="W->F: No effect on recruitment to double strand FT breaks." FT /evidence="ECO:0000269|PubMed:15525939, FT ECO:0000269|PubMed:17190600" FT MUTAGEN 1495 FT /note="W->V: Reduces recruitment to double strand breaks." FT /evidence="ECO:0000269|PubMed:15525939, FT ECO:0000269|PubMed:17190600" FT MUTAGEN 1500 FT /note="Y->A: Reduces affinity for histone H4 that has been FT dimethylated at 'Lys-20'." FT /evidence="ECO:0000269|PubMed:17190600" FT MUTAGEN 1502 FT /note="Y->A: Reduces affinity for histone H4 that has been FT dimethylated at 'Lys-20'." FT /evidence="ECO:0000269|PubMed:15525939, FT ECO:0000269|PubMed:17190600" FT MUTAGEN 1502 FT /note="Y->L,Q: Abolishes recruitment to double strand FT breaks." FT /evidence="ECO:0000269|PubMed:15525939, FT ECO:0000269|PubMed:17190600" FT MUTAGEN 1521 FT /note="D->A: Loss of interaction with histone H4 that has FT been dimethylated at 'Lys-20' (H4K20me2). Abolishes FT recruitment to double strand breaks. Loss of interaction FT with histone H4 that has been dimethylated at 'Lys-20' FT (H4K20me2). Abolishes recruitment to double strand breaks; FT when associated with A-1495." FT /evidence="ECO:0000269|PubMed:15525939, FT ECO:0000269|PubMed:17190600, ECO:0000269|PubMed:28241136" FT MUTAGEN 1521 FT /note="D->R: Abolishes recruitment to double strand breaks FT and induces defects in class-switch recombination (CSR)." FT /evidence="ECO:0000269|PubMed:15525939, FT ECO:0000269|PubMed:17190600, ECO:0000269|PubMed:23345425, FT ECO:0000269|PubMed:23760478" FT MUTAGEN 1523 FT /note="Y->A: Increases affinity for histone H4 that has FT been dimethylated at 'Lys-20'. No effect on recruitment to FT double strand breaks." FT /evidence="ECO:0000269|PubMed:17190600" FT MUTAGEN 1523 FT /note="Y->S: Decreases affinity for histone H4 that has FT been dimethylated at 'Lys-20'." FT /evidence="ECO:0000269|PubMed:17190600" FT MUTAGEN 1609 FT /note="T->A: Constitutive recruitment to mitotic DNA FT lesions, leading to mitotic defects; when associated with FT A-1618." FT /evidence="ECO:0000269|PubMed:24703952" FT MUTAGEN 1609 FT /note="T->E: Phosphomimetic mutant that abolishes FT recruitment to double strand breaks; when associated with FT D-1618." FT /evidence="ECO:0000269|PubMed:24703952" FT MUTAGEN 1613 FT /note="K->A: Does not affect recruitment to double strand FT breaks." FT /evidence="ECO:0000269|PubMed:23760478" FT MUTAGEN 1616 FT /note="D->A: Does not affect recruitment to double strand FT breaks." FT /evidence="ECO:0000269|PubMed:23760478" FT MUTAGEN 1617 FT /note="I->A: Strongly reduced recruitment to double strand FT breaks. Defects in class-switch recombination (CSR)." FT /evidence="ECO:0000269|PubMed:23760478" FT MUTAGEN 1618 FT /note="S->A: Constitutive recruitment to mitotic DNA FT lesions, leading to mitotic defects; when associated with FT A-1609." FT /evidence="ECO:0000269|PubMed:24703952" FT MUTAGEN 1618 FT /note="S->D: Phosphomimetic mutant that abolishes FT recruitment to double strand breaks; when associated with FT E-1609." FT /evidence="ECO:0000269|PubMed:24703952" FT MUTAGEN 1619 FT /note="L->A: Strongly reduced recruitment to double strand FT breaks. Defects in class-switch recombination (CSR). Does FT not affect interaction with histone H4 dimethylated at FT 'Lys-20' (H4K20me2). Impaired interaction with histone H2A FT monoubiquitinated at 'Lys-15' (H2AK15ub)." FT /evidence="ECO:0000269|PubMed:23760478" FT MUTAGEN 1621 FT /note="N->A: Reduced recruitment to double strand breaks." FT /evidence="ECO:0000269|PubMed:23760478" FT MUTAGEN 1622 FT /note="L->A: Reduced recruitment to double strand breaks." FT /evidence="ECO:0000269|PubMed:23760478" FT MUTAGEN 1624 FT /note="E->A: Does not affect recruitment to double strand FT breaks." FT /evidence="ECO:0000269|PubMed:23760478" FT MUTAGEN 1627 FT /note="R->A: Reduced recruitment to double strand breaks." FT /evidence="ECO:0000269|PubMed:23760478" FT CONFLICT 796 FT /note="P -> S (in Ref. 3; CAD97660)" FT /evidence="ECO:0000305" FT CONFLICT 1600 FT /note="Y -> C (in Ref. 3; CAD97660)" FT /evidence="ECO:0000305" FT CONFLICT 1958 FT /note="G -> R (in Ref. 3; CAD97660)" FT /evidence="ECO:0000305" FT STRAND 1490..1494 FT /evidence="ECO:0007829|PDB:2G3R" FT TURN 1496..1498 FT /evidence="ECO:0007829|PDB:2G3R" FT STRAND 1501..1511 FT /evidence="ECO:0007829|PDB:2G3R" FT STRAND 1514..1519 FT /evidence="ECO:0007829|PDB:2G3R" FT STRAND 1524..1528 FT /evidence="ECO:0007829|PDB:2G3R" FT HELIX 1529..1531 FT /evidence="ECO:0007829|PDB:2G3R" FT STRAND 1532..1535 FT /evidence="ECO:0007829|PDB:2LVM" FT STRAND 1543..1547 FT /evidence="ECO:0007829|PDB:2G3R" FT TURN 1549..1551 FT /evidence="ECO:0007829|PDB:6VA5" FT STRAND 1553..1564 FT /evidence="ECO:0007829|PDB:2G3R" FT STRAND 1567..1574 FT /evidence="ECO:0007829|PDB:2G3R" FT STRAND 1577..1582 FT /evidence="ECO:0007829|PDB:2G3R" FT HELIX 1583..1585 FT /evidence="ECO:0007829|PDB:2G3R" FT STRAND 1586..1588 FT /evidence="ECO:0007829|PDB:2G3R" FT HELIX 1590..1594 FT /evidence="ECO:0007829|PDB:2G3R" FT HELIX 1597..1600 FT /evidence="ECO:0007829|PDB:2G3R" FT STRAND 1615..1617 FT /evidence="ECO:0007829|PDB:7YQK" FT TURN 1674..1676 FT /evidence="ECO:0007829|PDB:6IUA" FT HELIX 1715..1719 FT /evidence="ECO:0007829|PDB:1KZY" FT TURN 1726..1731 FT /evidence="ECO:0007829|PDB:1KZY" FT STRAND 1732..1736 FT /evidence="ECO:0007829|PDB:1KZY" FT HELIX 1741..1745 FT /evidence="ECO:0007829|PDB:1GZH" FT HELIX 1773..1781 FT /evidence="ECO:0007829|PDB:1KZY" FT TURN 1782..1784 FT /evidence="ECO:0007829|PDB:1KZY" FT TURN 1793..1799 FT /evidence="ECO:0007829|PDB:1KZY" FT STRAND 1801..1808 FT /evidence="ECO:0007829|PDB:1KZY" FT HELIX 1813..1821 FT /evidence="ECO:0007829|PDB:1KZY" FT STRAND 1825..1827 FT /evidence="ECO:0007829|PDB:1KZY" FT HELIX 1829..1837 FT /evidence="ECO:0007829|PDB:1KZY" FT HELIX 1843..1845 FT /evidence="ECO:0007829|PDB:1KZY" FT STRAND 1851..1853 FT /evidence="ECO:0007829|PDB:1KZY" FT TURN 1854..1857 FT /evidence="ECO:0007829|PDB:1KZY" FT STRAND 1858..1860 FT /evidence="ECO:0007829|PDB:1KZY" FT TURN 1868..1871 FT /evidence="ECO:0007829|PDB:1KZY" FT STRAND 1873..1879 FT /evidence="ECO:0007829|PDB:1KZY" FT TURN 1881..1884 FT /evidence="ECO:0007829|PDB:1KZY" FT HELIX 1885..1894 FT /evidence="ECO:0007829|PDB:1KZY" FT STRAND 1898..1908 FT /evidence="ECO:0007829|PDB:1KZY" FT HELIX 1914..1916 FT /evidence="ECO:0007829|PDB:1KZY" FT STRAND 1918..1922 FT /evidence="ECO:0007829|PDB:1KZY" FT HELIX 1928..1937 FT /evidence="ECO:0007829|PDB:1KZY" FT HELIX 1944..1953 FT /evidence="ECO:0007829|PDB:1KZY" FT HELIX 1963..1965 FT /evidence="ECO:0007829|PDB:1KZY" SQ SEQUENCE 1972 AA; 213574 MW; 13E2CC8A265F9D2A CRC64; MDPTGSQLDS DFSQQDTPCL IIEDSQPESQ VLEDDSGSHF SMLSRHLPNL QTHKENPVLD VVSNPEQTAG EERGDGNSGF NEHLKENKVA DPVDSSNLDT CGSISQVIEQ LPQPNRTSSV LGMSVESAPA VEEEKGEELE QKEKEKEEDT SGNTTHSLGA EDTASSQLGF GVLELSQSQD VEENTVPYEV DKEQLQSVTT NSGYTRLSDV DANTAIKHEE QSNEDIPIAE QSSKDIPVTA QPSKDVHVVK EQNPPPARSE DMPFSPKASV AAMEAKEQLS AQELMESGLQ IQKSPEPEVL STQEDLFDQS NKTVSSDGCS TPSREEGGCS LASTPATTLH LLQLSGQRSL VQDSLSTNSS DLVAPSPDAF RSTPFIVPSS PTEQEGRQDK PMDTSVLSEE GGEPFQKKLQ SGEPVELENP PLLPESTVSP QASTPISQST PVFPPGSLPI PSQPQFSHDI FIPSPSLEEQ SNDGKKDGDM HSSSLTVECS KTSEIEPKNS PEDLGLSLTG DSCKLMLSTS EYSQSPKMES LSSHRIDEDG ENTQIEDTEP MSPVLNSKFV PAENDSILMN PAQDGEVQLS QNDDKTKGDD TDTRDDISIL ATGCKGREET VAEDVCIDLT CDSGSQAVPS PATRSEALSS VLDQEEAMEI KEHHPEEGSS GSEVEEIPET PCESQGEELK EENMESVPLH LSLTETQSQG LCLQKEMPKK ECSEAMEVET SVISIDSPQK LAILDQELEH KEQEAWEEAT SEDSSVVIVD VKEPSPRVDV SCEPLEGVEK CSDSQSWEDI APEIEPCAEN RLDTKEEKSV EYEGDLKSGT AETEPVEQDS SQPSLPLVRA DDPLRLDQEL QQPQTQEKTS NSLTEDSKMA NAKQLSSDAE AQKLGKPSAH ASQSFCESSS ETPFHFTLPK EGDIIPPLTG ATPPLIGHLK LEPKRHSTPI GISNYPESTI ATSDVMSESM VETHDPILGS GKGDSGAAPD VDDKLCLRMK LVSPETEASE ESLQFNLEKP ATGERKNGST AVAESVASPQ KTMSVLSCIC EARQENEARS EDPPTTPIRG NLLHFPSSQG EEEKEKLEGD HTIRQSQQPM KPISPVKDPV SPASQKMVIQ GPSSPQGEAM VTDVLEDQKE GRSTNKENPS KALIERPSQN NIGIQTMECS LRVPETVSAA TQTIKNVCEQ GTSTVDQNFG KQDATVQTER GSGEKPVSAP GDDTESLHSQ GEEEFDMPQP PHGHVLHRHM RTIREVRTLV TRVITDVYYV DGTEVERKVT EETEEPIVEC QECETEVSPS QTGGSSGDLG DISSFSSKAS SLHRTSSGTS LSAMHSSGSS GKGAGPLRGK TSGTEPADFA LPSSRGGPGK LSPRKGVSQT GTPVCEEDGD AGLGIRQGGK APVTPRGRGR RGRPPSRTTG TRETAVPGPL GIEDISPNLS PDDKSFSRVV PRVPDSTRRT DVGAGALRRS DSPEIPFQAA AGPSDGLDAS SPGNSFVGLR VVAKWSSNGY FYSGKITRDV GAGKYKLLFD DGYECDVLGK DILLCDPIPL DTEVTALSED EYFSAGVVKG HRKESGELYY SIEKEGQRKW YKRMAVILSL EQGNRLREQY GLGPYEAVTP LTKAADISLD NLVEGKRKRR SNVSSPATPT ASSSSSTTPT RKITESPRAS MGVLSGKRKL ITSEEERSPA KRGRKSATVK PGAVGAGEFV SPCESGDNTG EPSALEEQRG PLPLNKTLFL GYAFLLTMAT TSDKLASRSK LPDGPTGSSE EEEEFLEIPP FNKQYTESQL RAGAGYILED FNEAQCNTAY QCLLIADQHC RTRKYFLCLA SGIPCVSHVW VHDSCHANQL QNYRNYLLPA GYSLEEQRIL DWQPRENPFQ NLKVLLVSDQ QQNFLELWSE ILMTGGAASV KQHHSSAHNK DIALGVFDVV VTDPSCPASV LKCAEALQLP VVSQEWVIQC LIVGERIGFK QHPKYKHDYV SH //