TP53B_HUMAN
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 03-AUG-2022, entry version 227.
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 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 [26]
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 [27]
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 [28]
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 [29]
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 [30]
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 [31]
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 [32]
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 [33]
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 [34]
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 [35]
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 [36]
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 [37]
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 [38]
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 [39]
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 [40]
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 [41]
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 [42]
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 [43]
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 [44]
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 [45]
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 [46]
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 [47]
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 [48]
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 [49]
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 [50]
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 [51]
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).
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). Plays a key role in the repair of double-strand DNA
CC breaks (DSBs) in response to DNA damage by promoting non-homologous end
CC joining (NHEJ)-mediated repair of DSBs and specifically counteracting
CC the function of the homologous recombination (HR) repair protein BRCA1
CC (PubMed:22553214, PubMed:23727112, PubMed:23333306, PubMed:27153538).
CC In response to DSBs, phosphorylation by ATM promotes interaction with
CC RIF1 and dissociation from NUDT16L1/TIRR, leading to recruitment to
CC DSBs sites (PubMed:28241136). Recruited to DSBs sites by recognizing
CC and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and
CC histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that
CC are present at DSBs sites (PubMed:23760478, PubMed:27153538,
CC PubMed:28241136, PubMed:17190600). Required for immunoglobulin class-
CC switch recombination (CSR) during antibody genesis, a process that
CC involves the generation of DNA DSBs (PubMed:23345425). Participates in
CC the 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}.
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 IFI202A (By
CC similarity). Interacts with SHLD2 (PubMed:29789392).
CC {ECO:0000250|UniProtKB:P70399, 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 -!- 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=6; 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}. Chromosome, centromere, kinetochore
CC {ECO:0000250|UniProtKB:P70399}. Note=Localizes to the nucleus in
CC absence of DNA damage (PubMed:28241136). Following DNA damage,
CC recruited to sites of DNA damage, such as double stand breaks (DSBs):
CC recognizes and binds histone H2A monoubiquitinated at 'Lys-15'
CC (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two
CC histone marks that are present at DSBs sites (PubMed:23333306,
CC PubMed:23760478, PubMed:24703952, PubMed:28241136, PubMed:17190600).
CC Associated with kinetochores during mitosis (By similarity).
CC {ECO:0000250|UniProtKB:P70399, ECO:0000269|PubMed:17190600,
CC ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23760478,
CC 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 {ECO:0000269|PubMed:11042216, ECO:0000269|PubMed:11331310,
CC ECO:0000269|PubMed:17553757, ECO:0000269|PubMed:19176521,
CC ECO:0000269|PubMed:21144835, ECO:0000269|PubMed:23333306,
CC ECO:0000269|PubMed:23727112, ECO:0000269|PubMed:24703952,
CC ECO:0000269|PubMed:28241136}.
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/";
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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 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 AlphaFoldDB; Q12888; -.
DR BMRB; Q12888; -.
DR SMR; Q12888; -.
DR BioGRID; 113011; 463.
DR CORUM; Q12888; -.
DR DIP; DIP-5978N; -.
DR IntAct; Q12888; 367.
DR MINT; Q12888; -.
DR STRING; 9606.ENSP00000371475; -.
DR BindingDB; Q12888; -.
DR ChEMBL; CHEMBL2424509; -.
DR GlyGen; Q12888; 3 sites, 1 O-linked glycan (3 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 EPD; Q12888; -.
DR jPOST; Q12888; -.
DR MassIVE; Q12888; -.
DR MaxQB; Q12888; -.
DR PaxDb; Q12888; -.
DR PeptideAtlas; Q12888; -.
DR PRIDE; Q12888; -.
DR ProteomicsDB; 29194; -.
DR ProteomicsDB; 59003; -. [Q12888-1]
DR ProteomicsDB; 59004; -. [Q12888-2]
DR ABCD; Q12888; 6 sequenced antibodies.
DR Antibodypedia; 1749; 996 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 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; PIVDDTC; -.
DR OrthoDB; 27155at2759; -.
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; 35 hits in 1095 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 198 other tissues.
DR ExpressionAtlas; Q12888; baseline and differential.
DR Genevisible; Q12888; HS.
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: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:0006974; P:cellular response to DNA damage stimulus; 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: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: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:0045893; P:positive regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR CDD; cd04508; TUDOR; 1.
DR DisProt; DP02954; -.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 3.40.50.10190; -; 2.
DR IDEAL; IID00123; -.
DR InterPro; IPR015125; 53-BP1_Tudor.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR002999; Tudor.
DR Pfam; PF09038; 53-BP1_Tudor; 1.
DR SMART; SM00292; BRCT; 2.
DR SUPFAM; SSF52113; SSF52113; 2.
DR PROSITE; PS50172; BRCT; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Centromere;
KW Chromosomal rearrangement; Chromosome; DNA damage; DNA repair; DNA-binding;
KW Isopeptide bond; Kinetochore; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW 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:0007744|PubMed:19690332,
FT 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 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 A-
FT 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; A-
FT 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; A-
FT 452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-
FT 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; A-
FT 452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-
FT 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; A-
FT 452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-
FT 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; A-
FT 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; A-
FT 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; A-
FT 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; A-
FT 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; A-
FT 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 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; A-
FT 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; A-
FT 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; A-
FT 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; A-
FT 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; A-
FT 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; A-
FT 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 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; A-
FT 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; A-
FT 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; A-
FT 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; A-
FT 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; A-
FT 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; A-
FT 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; A-
FT 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; A-
FT 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; A-
FT 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; A-
FT 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; A-
FT 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; A-
FT 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; A-
FT 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 A-
FT 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 A-
FT 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 A-
FT 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 A-
FT 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 A-
FT 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 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
