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TP53-binding protein 1 (53BP1) (p53-binding protein 1) (p53BP1)

 TP53B_HUMAN             Reviewed;        1972 AA.
Q12888; F8VY86; Q2M1Z7; Q4LE46; Q5FWZ3; Q7Z3U4;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 2.
05-DEC-2018, entry version 203.
RecName: Full=TP53-binding protein 1 {ECO:0000305};
Short=53BP1 {ECO:0000303|PubMed:9748285};
Short=p53-binding protein 1 {ECO:0000303|PubMed:9748285};
Short=p53BP1;
Name=TP53BP1 {ECO:0000312|HGNC:HGNC:11999};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
TISSUE=Skeletal muscle;
PubMed=9748285; DOI=10.1074/jbc.273.40.26061;
Iwabuchi K., Li B., Massa H.F., Trask B.J., Date T., Fields S.;
"Stimulation of p53-mediated transcriptional activation by the p53-
binding proteins, 53BP1 and 53BP2.";
J. Biol. Chem. 273:26061-26068(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Myeloid leukemia cell;
Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M.,
Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.;
"Preparation of a set of expression-ready clones of mammalian long
cDNAs encoding large proteins by the ORF trap cloning method.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS
GLU-353; SER-412 AND GLN-1136.
TISSUE=Cervix;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLU-353; SER-412;
VAL-648; ARG-699; GLY-1014; ALA-1026; GLN-1136; GLY-1170 AND VAL-1174.
NIEHS SNPs program;
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Cerebellum;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 946-1972.
PubMed=8016121; DOI=10.1073/pnas.91.13.6098;
Iwabuchi K., Bartel P.L., Li B., Marraccino R., Fields S.;
"Two cellular proteins that bind to wild-type but not mutant p53.";
Proc. Natl. Acad. Sci. U.S.A. 91:6098-6102(1994).
[8]
PHOSPHORYLATION.
PubMed=11042216; DOI=10.1074/jbc.M007665200;
Xia Z., Morales J.C., Dunphy W.G., Carpenter P.B.;
"Negative cell cycle regulation and DNA-damage inducible
phosphorylation of the BRCT protein 53BP1.";
J. Biol. Chem. 276:2708-2718(2001).
[9]
SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
PubMed=11331310; DOI=10.1083/jcb.153.3.613;
Rappold I., Iwabuchi K., Date T., Chen J.;
"Tumor suppressor p53 binding protein 1 (53BP1) is involved in DNA
damage-signaling pathways.";
J. Cell Biol. 153:613-620(2001).
[10]
FUNCTION IN DNA DAMAGE CHECKPOINT, AND INTERACTION WITH CHEK2.
PubMed=12364621; DOI=10.1126/science.1076182;
Wang B., Matsuoka S., Carpenter P.B., Elledge S.J.;
"53BP1, a mediator of the DNA damage checkpoint.";
Science 298:1435-1438(2002).
[11]
SUBCELLULAR LOCATION.
PubMed=12824158; DOI=10.1074/jbc.M304066200;
Iwabuchi K., Basu B.P., Kysela B., Kurihara T., Shibata M., Guan D.,
Cao Y., Hamada T., Imamura K., Jeggo P.A., Date T., Doherty A.J.;
"Potential role for 53BP1 in DNA end-joining repair through direct
interaction with DNA.";
J. Biol. Chem. 278:36487-36495(2003).
[12]
INTERACTION WITH H2AFX.
PubMed=12607005; DOI=10.1038/nature01446;
Stewart G.S., Wang B., Bignell C.R., Taylor A.M.R., Elledge S.J.;
"MDC1 is a mediator of the mammalian DNA damage checkpoint.";
Nature 421:961-966(2003).
[13]
CHROMOSOMAL TRANSLOCATION WITH PDGFRB.
PubMed=15492236; DOI=10.1158/0008-5472.CAN-04-2005;
Grand F.H., Burgstaller S., Kuhr T., Baxter E.J., Webersinke G.,
Thaler J., Chase A.J., Cross N.C.;
"p53-Binding protein 1 is fused to the platelet-derived growth factor
receptor beta in a patient with a t(5;15)(q33;q22) and an imatinib-
responsive eosinophilic myeloproliferative disorder.";
Cancer Res. 64:7216-7219(2004).
[14]
INTERACTION WITH DCLRE1C.
PubMed=15574327; DOI=10.1016/j.molcel.2004.10.029;
Riballo E., Kuehne M., Rief N., Doherty A., Smith G.C.M., Recio M.-J.,
Reis C., Dahm K., Fricke A., Krempler A., Parker A.R., Jackson S.P.,
Gennery A., Jeggo P.A., Loebrich M.;
"A pathway of double-strand break rejoining dependent upon ATM,
Artemis, and proteins locating to gamma-H2AX foci.";
Mol. Cell 16:715-724(2004).
[15]
METHYLATION, MUTAGENESIS OF ARG-1396; ARG-1398; ARG-1400; ARG-1401 AND
ARG-1403, SUBCELLULAR LOCATION, AND DNA-BINDING.
PubMed=16294045; DOI=10.4161/cc.4.12.2250;
Boisvert F.-M., Rhie A., Richard S., Doherty A.J.;
"The GAR motif of 53BP1 is arginine methylated by PRMT1 and is
necessary for 53BP1 DNA binding activity.";
Cell Cycle 4:1834-1841(2005).
[16]
METHYLATION, MUTAGENESIS OF ARG-1396; ARG-1398; ARG-1400; ARG-1401 AND
ARG-1403, SUBUNIT, SUBCELLULAR LOCATION, AND DNA-BINDING.
PubMed=16294047; DOI=10.4161/cc.4.12.2282;
Adams M.M., Wang B., Xia Z., Morales J.C., Lu X., Donehower L.A.,
Bochar D.A., Elledge S.J., Carpenter P.B.;
"53BP1 oligomerization is independent of its methylation by PRMT1.";
Cell Cycle 4:1854-1861(2005).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222; SER-294; SER-500;
SER-635; SER-639; SER-640; SER-1094; SER-1219; SER-1362 AND SER-1678,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-834 AND SER-1426, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[19]
PHOSPHORYLATION AT SER-166; SER-176; SER-178; SER-294; THR-302;
SER-380; SER-452; SER-523; SER-552; SER-831; SER-1028; SER-1086;
SER-1114 AND SER-1219, AND MUTAGENESIS OF 176-SER--SER-178.
PubMed=17553757; DOI=10.1016/j.dnarep.2007.04.011;
Jowsey P., Morrice N.A., Hastie C.J., McLauchlan H., Toth R.,
Rouse J.;
"Characterisation of the sites of DNA damage-induced 53BP1
phosphorylation catalysed by ATM and ATR.";
DNA Repair 6:1536-1544(2007).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; THR-302; SER-523;
THR-543; THR-548; SER-552; SER-831; THR-855; THR-1214; SER-1216 AND
SER-1219, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222; SER-265; SER-395;
SER-398; SER-500; SER-523; SER-525; SER-552; SER-809; SER-831;
SER-1028; SER-1094; SER-1216; SER-1219; SER-1368; THR-1372; SER-1426;
SER-1430; SER-1462; THR-1609; SER-1701 AND SER-1759, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[24]
PHOSPHORYLATION AT SER-25 AND SER-1778, DEPHOSPHORYLATION AT SER-25
AND SER-1778 BY PPP5C, AND SUBCELLULAR LOCATION.
PubMed=19176521; DOI=10.1074/jbc.M809272200;
Kang Y., Lee J.H., Hoan N.N., Sohn H.M., Chang I.Y., You H.J.;
"Protein phosphatase 5 regulates the function of 53BP1 after
neocarzinostatin-induced DNA damage.";
J. Biol. Chem. 284:9845-9853(2009).
[25]
INTERACTION WITH MSL1.
PubMed=19650074; DOI=10.1002/jcp.21889;
Gironella M., Malicet C., Cano C., Sandi M.J., Hamidi T., Tauil R.M.,
Baston M., Valaco P., Moreno S., Lopez F., Neira J.L., Dagorn J.C.,
Iovanna J.L.;
"p8/nupr1 regulates DNA-repair activity after double-strand gamma
irradiation-induced DNA damage.";
J. Cell. Physiol. 221:594-602(2009).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-294; SER-366; SER-380;
SER-500; SER-523; SER-525; THR-543; SER-552; SER-834; SER-1028;
SER-1114; SER-1426; SER-1430; SER-1460; SER-1462 AND SER-1474, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[27]
INTERACTION WITH MUM1.
PubMed=20347427; DOI=10.1016/j.molcel.2009.12.040;
Huen M.S., Huang J., Leung J.W., Sy S.M., Leung K.M., Ching Y.P.,
Tsao S.W., Chen J.;
"Regulation of chromatin architecture by the PWWP domain-containing
DNA damage-responsive factor EXPAND1/MUM1.";
Mol. Cell 37:854-864(2010).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; SER-294; SER-500;
SER-525; SER-552; SER-566; SER-580; SER-639; SER-640; SER-809;
THR-922; SER-970; SER-975; SER-1028; SER-1068; SER-1114; SER-1362;
SER-1426; SER-1430; THR-1609; SER-1618 AND SER-1678, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[30]
FUNCTION IN DNA DAMAGE RESPONSE, PHOSPHORYLATION AT SER-1778, AND
SUBCELLULAR LOCATION.
PubMed=21144835; DOI=10.1016/j.bbrc.2010.12.005;
Kang Y., Cheong H.M., Lee J.H., Song P.I., Lee K.H., Kim S.Y.,
Jun J.Y., You H.J.;
"Protein phosphatase 5 is necessary for ATR-mediated DNA repair.";
Biochem. Biophys. Res. Commun. 404:476-481(2011).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222; SER-294; SER-500;
SER-525; SER-552; SER-809; SER-1028; SER-1101; SER-1114; SER-1362;
SER-1430; SER-1618 AND SER-1678, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[32]
FUNCTION.
PubMed=22553214; DOI=10.1242/jcs.105353;
Chapman J.R., Sossick A.J., Boulton S.J., Jackson S.P.;
"BRCA1-associated exclusion of 53BP1 from DNA damage sites underlies
temporal control of DNA repair.";
J. Cell Sci. 125:3529-3534(2012).
[33]
FUNCTION, PHOSPHORYLATION, INTERACTION WITH RIF1 AND PAXIP1, AND
MUTAGENESIS OF SER-6; SER-13; SER-25; SER-29; SER-105; SER-166;
SER-176 AND SER-178.
PubMed=23727112; DOI=10.1016/j.cell.2013.05.023;
Callen E., Di Virgilio M., Kruhlak M.J., Nieto-Soler M., Wong N.,
Chen H.T., Faryabi R.B., Polato F., Santos M., Starnes L.M.,
Wesemann D.R., Lee J.E., Tubbs A., Sleckman B.P., Daniel J.A., Ge K.,
Alt F.W., Fernandez-Capetillo O., Nussenzweig M.C., Nussenzweig A.;
"53BP1 mediates productive and mutagenic DNA repair through distinct
phosphoprotein interactions.";
Cell 153:1266-1280(2013).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63; SER-124; SER-222;
SER-265; SER-294; SER-366; SER-380; SER-398; SER-500; SER-507;
SER-518; SER-523; SER-525; SER-552; SER-580; SER-771; SER-809;
SER-834; THR-922; SER-1028; THR-1056; SER-1068; SER-1094; SER-1114;
SER-1148; SER-1216; SER-1219; SER-1317; SER-1342; SER-1362; SER-1426;
SER-1430; SER-1462; THR-1609; SER-1618; SER-1635; THR-1638; THR-1648;
SER-1656; SER-1673; SER-1678 AND SER-1701, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[35]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RIF1,
PHOSPHORYLATION, AND MUTAGENESIS OF SER-6; SER-13; SER-25; SER-29;
SER-105; SER-166; SER-176; SER-178; THR-302; SER-437; SER-452;
SER-523; THR-543; SER-580; SER-625; SER-674; THR-696; SER-698;
SER-784; SER-831; THR-855; SER-892; SER-1068; SER-1086; SER-1104;
SER-1148; THR-1171 AND SER-1219.
PubMed=23333306; DOI=10.1016/j.molcel.2013.01.001;
Escribano-Diaz C., Orthwein A., Fradet-Turcotte A., Xing M.,
Young J.T., Tkac J., Cook M.A., Rosebrock A.P., Munro M., Canny M.D.,
Xu D., Durocher D.;
"A cell cycle-dependent regulatory circuit composed of 53BP1-RIF1 and
BRCA1-CtIP controls DNA repair pathway choice.";
Mol. Cell 49:872-883(2013).
[36]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF
ASP-1521; LYS-1613; ASP-1616; ILE-1617; LEU-1619; ASN-1621; LEU-1622;
GLU-1624 AND ARG-1627.
PubMed=23760478; DOI=10.1038/nature12318;
Fradet-Turcotte A., Canny M.D., Escribano-Diaz C., Orthwein A.,
Leung C.C., Huang H., Landry M.C., Kitevski-LeBlanc J.,
Noordermeer S.M., Sicheri F., Durocher D.;
"53BP1 is a reader of the DNA-damage-induced H2A Lys 15 ubiquitin
mark.";
Nature 499:50-54(2013).
[37]
FUNCTION, SUBUNIT, AND MUTAGENESIS OF SER-6; SER-13; SER-25; SER-29;
SER-105; SER-166; SER-176; SER-178; THR-302; SER-437; SER-452;
SER-523; THR-543; SER-580; SER-625; SER-674; THR-696; SER-698;
SER-784; SER-831; THR-855; SER-892; SER-1068; SER-1086; SER-1104;
SER-1148; THR-1171; SER-1219; 1398-ARG--ARG-1401 AND ASP-1521.
PubMed=23345425; DOI=10.1073/pnas.1222617110;
Lottersberger F., Bothmer A., Robbiani D.F., Nussenzweig M.C.,
de Lange T.;
"Role of 53BP1 oligomerization in regulating double-strand break
repair.";
Proc. Natl. Acad. Sci. U.S.A. 110:2146-2151(2013).
[38]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-294; SER-500; SER-552;
SER-630; SER-692; SER-727; SER-1114; SER-1216 AND SER-1362, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[39]
SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-1609 AND SER-1618,
DOMAIN, AND MUTAGENESIS OF THR-1609 AND SER-1618.
PubMed=24703952; DOI=10.1016/j.molcel.2014.03.020;
Lee D.H., Acharya S.S., Kwon M., Drane P., Guan Y., Adelmant G.,
Kalev P., Shah J., Pellman D., Marto J.A., Chowdhury D.;
"Dephosphorylation enables the recruitment of 53BP1 to double-strand
DNA breaks.";
Mol. Cell 54:512-525(2014).
[40]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-930 AND LYS-1563, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[41]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-217; LYS-868; LYS-1434 AND
LYS-1563, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[42]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-930, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[43]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1563, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[44]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-217; LYS-868; LYS-930;
LYS-984; LYS-1365; LYS-1434 AND LYS-1563, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[45]
FUNCTION, INTERACTION WITH NUDT16L1 AND RIF1, SUBCELLULAR LOCATION,
PHOSPHORYLATION, AND MUTAGENESIS OF TRP-1495; ASP-1521; THR-1609 AND
SER-1618.
PubMed=28241136; DOI=10.1038/nature21358;
Drane P., Brault M.E., Cui G., Meghani K., Chaubey S., Detappe A.,
Parnandi N., He Y., Zheng X.F., Botuyan M.V., Kalousi A.,
Yewdell W.T., Muench C., Harper J.W., Chaudhuri J., Soutoglou E.,
Mer G., Chowdhury D.;
"TIRR regulates 53BP1 by masking its histone methyl-lysine binding
function.";
Nature 543:211-216(2017).
[46]
INTERACTION WITH SHLD2, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=29789392; DOI=10.15252/embj.201899543;
Tomida J., Takata K.I., Bhetawal S., Person M.D., Chao H.P.,
Tang D.G., Wood R.D.;
"FAM35A associates with REV7 and modulates DNA damage responses of
normal and BRCA1-defective cells.";
EMBO J. 37:0-0(2018).
[47]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1722-1971 IN COMPLEX WITH
TP53.
PubMed=12110597; DOI=10.1093/emboj/cdf383;
Derbyshire D.J., Basu B.P., Serpell L.C., Joo W.S., Date T.,
Iwabuchi K., Doherty A.J.;
"Crystal structure of human 53BP1 BRCT domains bound to p53 tumour
suppressor.";
EMBO J. 21:3863-3872(2002).
[48]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1714-1972 IN COMPLEX WITH
TP53.
PubMed=11877378; DOI=10.1101/gad.959202;
Joo W.S., Jeffrey P.D., Cantor S.B., Finnin M.S., Livingston D.M.,
Pavletich N.P.;
"Structure of the 53BP1 BRCT region bound to p53 and its comparison to
the Brca1 BRCT structure.";
Genes Dev. 16:583-593(2002).
[49]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1485-1602, INTERACTION WITH
METHYLATED HISTONE H3 AND HISTONE H4, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF TRP-1495; TYR-1502 AND ASP-1521.
PubMed=15525939; DOI=10.1038/nature03114;
Huyen Y., Zgheib O., Ditullio R.A. Jr., Gorgoulis V.G., Zacharatos P.,
Petty T.J., Sheston E.A., Mellert H.S., Stavridi E.S.,
Halazonetis T.D.;
"Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand
breaks.";
Nature 432:406-411(2004).
[50]
X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 1484-1603 IN COMPLEX WITH
HISTONE H4, SUBUNIT, FUNCTION, MUTAGENESIS OF TRP-1495; TYR-1500;
TYR-1502; ASP-1521 AND TYR-1523, AND SUBCELLULAR LOCATION.
PubMed=17190600; DOI=10.1016/j.cell.2006.10.043;
Botuyan M.V., Lee J., Ward I.M., Kim J.-E., Thompson J.R., Chen J.,
Mer G.;
"Structural basis for the methylation state-specific recognition of
histone H4-K20 by 53BP1 and Crb2 in DNA repair.";
Cell 127:1361-1373(2006).
-!- FUNCTION: Double-strand break (DSB) repair protein involved in
response to DNA damage, telomere dynamics and class-switch
recombination (CSR) during antibody genesis (PubMed:12364621,
PubMed:22553214, PubMed:23333306, PubMed:17190600,
PubMed:21144835, PubMed:28241136). Plays a key role in the repair
of double-strand DNA breaks (DSBs) in response to DNA damage by
promoting non-homologous end joining (NHEJ)-mediated repair of
DSBs and specifically counteracting the function of the homologous
recombination (HR) repair protein BRCA1 (PubMed:22553214,
PubMed:23727112, PubMed:23333306). In response to DSBs,
phosphorylation by ATM promotes interaction with RIF1 and
dissociation from NUDT16L1/TIRR, leading to recruitment to DSBs
sites (PubMed:28241136). Recruited to DSBs sites by recognizing
and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub)
and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone
marks that are present at DSBs sites (PubMed:23760478,
PubMed:28241136, PubMed:17190600). Required for immunoglobulin
class-switch recombination (CSR) during antibody genesis, a
process that involves the generation of DNA DSBs
(PubMed:23345425). Participates to the repair and the orientation
of the broken DNA ends during CSR (By similarity). In contrast, it
is not required for classic NHEJ and V(D)J recombination (By
similarity). Promotes NHEJ of dysfunctional telomeres via
interaction with PAXIP1 (PubMed:23727112).
{ECO:0000250|UniProtKB:P70399, ECO:0000269|PubMed:12364621,
ECO:0000269|PubMed:17190600, ECO:0000269|PubMed:21144835,
ECO:0000269|PubMed:22553214, ECO:0000269|PubMed:23333306,
ECO:0000269|PubMed:23345425, ECO:0000269|PubMed:23727112,
ECO:0000269|PubMed:23760478, ECO:0000269|PubMed:28241136}.
-!- SUBUNIT: Homoligomer (PubMed:16294047, PubMed:23760478,
PubMed:23345425). Interacts with p53/TP53 (via the central domain)
(PubMed:12110597, PubMed:11877378). Interacts with DCLRE1C
(PubMed:15574327). Interacts with histone H2AFX and this requires
phosphorylation of H2AFX on 'Ser-139' (PubMed:12607005). Interacts
with histone H4 that has been dimethylated at 'Lys-20' (H4K20me2)
(PubMed:17190600). Has low affinity for histone H4 containing
monomethylated 'Lys-20' (H4K20me1) (PubMed:17190600). Does not
bind histone H4 containing unmethylated or trimethylated 'Lys-20'
(H4K20me3) (PubMed:17190600). Has low affinity for histone H3 that
has been dimethylated on 'Lys-79' (PubMed:15525939). Has very low
affinity for histone H3 that has been monomethylated on 'Lys-79'
(in vitro) (PubMed:15525939). Does not bind unmethylated histone
H3 (PubMed:15525939). Interacts with histone H2A monoubiquitinated
at 'Lys-15' (H2AK15Ub) (PubMed:23760478). Interacts with
MUM1/EXPAND1 (PubMed:20347427). Interacts with CHEK2; modulates
CHEK2 phosphorylation at 'Thr-68' in response to infrared
(PubMed:12364621). Interacts with MSL1; this interaction may be
required for MSL1 DNA repair activity, but not for histone
acetyltransferase activity (PubMed:19650074). Interacts (when
phosphorylated by ATM) with RIF1 (PubMed:23727112,
PubMed:23333306, PubMed:28241136). Interacts (via the Tudor-like
domain) with NUDT16L1/TIRR; interaction masks the Tudor-like
domain and prevents recruitment to chromatin (PubMed:28241136).
Interacts with PAXIP1 (PubMed:23727112). Interacts with IFI202A
(By similarity). Interacts with SHLD2 (PubMed:29789392).
{ECO:0000250|UniProtKB:P70399, ECO:0000269|PubMed:11877378,
ECO:0000269|PubMed:12110597, ECO:0000269|PubMed:12364621,
ECO:0000269|PubMed:12607005, ECO:0000269|PubMed:15525939,
ECO:0000269|PubMed:15574327, ECO:0000269|PubMed:16294047,
ECO:0000269|PubMed:17190600, ECO:0000269|PubMed:19650074,
ECO:0000269|PubMed:20347427, ECO:0000269|PubMed:23333306,
ECO:0000269|PubMed:23345425, ECO:0000269|PubMed:23727112,
ECO:0000269|PubMed:23760478, ECO:0000269|PubMed:29789392}.
-!- INTERACTION:
Q13315:ATM; NbExp=2; IntAct=EBI-396540, EBI-495465;
P38398:BRCA1; NbExp=5; IntAct=EBI-396540, EBI-349905;
P16104:H2AFX; NbExp=6; IntAct=EBI-396540, EBI-494830;
P68431:HIST1H3D; NbExp=5; IntAct=EBI-396540, EBI-79722;
P62805:HIST2H4B; NbExp=11; IntAct=EBI-396540, EBI-302023;
P50222:MEOX2; NbExp=3; IntAct=EBI-396540, EBI-748397;
P01106:MYC; NbExp=2; IntAct=EBI-396540, EBI-447544;
Q14686:NCOA6; NbExp=3; IntAct=EBI-396540, EBI-78670;
Q6ZW49:PAXIP1; NbExp=4; IntAct=EBI-396540, EBI-743225;
Q6NZQ4:Paxip1 (xeno); NbExp=5; IntAct=EBI-396540, EBI-1395317;
P53350:PLK1; NbExp=5; IntAct=EBI-396540, EBI-476768;
Q86V20-2:SHLD2; NbExp=3; IntAct=EBI-396540, EBI-20592761;
P63165:SUMO1; NbExp=2; IntAct=EBI-396540, EBI-80140;
P04637:TP53; NbExp=17; IntAct=EBI-8022649, EBI-366083;
Q08AM6:VAC14; NbExp=5; IntAct=EBI-396540, EBI-2107455;
Q99986:VRK1; NbExp=8; IntAct=EBI-396540, EBI-1769146;
O43257:ZNHIT1; NbExp=2; IntAct=EBI-396540, EBI-347522;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11331310,
ECO:0000269|PubMed:15525939, ECO:0000269|PubMed:16294045,
ECO:0000269|PubMed:16294047, ECO:0000269|PubMed:17190600,
ECO:0000269|PubMed:19176521, ECO:0000269|PubMed:21144835,
ECO:0000269|PubMed:28241136, ECO:0000269|PubMed:9748285}.
Chromosome {ECO:0000269|PubMed:12824158,
ECO:0000269|PubMed:15525939, ECO:0000269|PubMed:17190600,
ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23760478,
ECO:0000269|PubMed:24703952, ECO:0000269|PubMed:28241136}.
Chromosome, centromere, kinetochore
{ECO:0000250|UniProtKB:P70399}. Note=Localizes to the nucleus in
absence of DNA damage (PubMed:28241136). Following DNA damage,
recruited to sites of DNA damage, such as double stand breaks
(DSBs): recognizes and binds histone H2A monoubiquitinated at
'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20'
(H4K20me2), two histone marks that are present at DSBs sites
(PubMed:23333306, PubMed:23760478, PubMed:24703952,
PubMed:28241136, PubMed:17190600). Associated with kinetochores
during mitosis (By similarity). {ECO:0000250|UniProtKB:P70399,
ECO:0000269|PubMed:17190600, ECO:0000269|PubMed:23333306,
ECO:0000269|PubMed:23760478, ECO:0000269|PubMed:28241136}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q12888-1; Sequence=Displayed;
Name=2;
IsoId=Q12888-2; Sequence=VSP_018390;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q12888-3; Sequence=VSP_018390, VSP_055062;
Note=No experimental confirmation available.;
-!- DOMAIN: The Tudor-like region mediates binding to histone H4
dimethylated at 'Lys-20' (H4K20me2) (PubMed:17190600). Interaction
with NUDT16L1/TIRR masks the Tudor-like domain and prevents
recruitment to chromatin (PubMed:28241136).
{ECO:0000269|PubMed:17190600, ECO:0000269|PubMed:28241136}.
-!- DOMAIN: The UDR (ubiquitin-dependent recruitment) motif
specifically recognizes and binds histone H2A monoubiquitinated at
'Lys-15' (H2AK15ub) (PubMed:23760478, PubMed:24703952).
Phosphorylation of the UDR blocks interaction with H2AK15ub
(PubMed:24703952). {ECO:0000269|PubMed:23760478,
ECO:0000269|PubMed:24703952}.
-!- PTM: Asymmetrically dimethylated on Arg residues by PRMT1.
Methylation is required for DNA binding.
{ECO:0000269|PubMed:16294045, ECO:0000269|PubMed:16294047}.
-!- PTM: Phosphorylated at basal level in the absence of DNA damage
(PubMed:11042216, PubMed:11331310). Phosphorylated by ATM in
response to DNA damage: phosphorylation at different sites
promotes interaction with different set of proteins:
phosphorylation at the N-terminus by ATM (residues from 6-178)
promotes interaction with PAXIP1 and non-homologous end joining
(NHEJ) of dysfunctional telomeres (PubMed:23727112).
Phosphorylation by ATM at residues that are located more C-
terminus (residues 300-650) leads to promote interaction with RIF1
(PubMed:23727112, PubMed:23333306, PubMed:28241136). Interaction
with RIF1 leads to disrupt interaction with NUDT16L1/TIRR
(PubMed:28241136). Phosphorylation at Thr-1609 and Ser-1618 in the
UDR motif blocks interaction with H2AK15ub (PubMed:24703952).
Dephosphorylated by PPP4C (PubMed:24703952). Hyperphosphorylation
during mitosis correlates with its exclusion from chromatin and
DNA lesions. Hyperphosphorylated in an ATR-dependent manner in
response to DNA damage induced by UV irradiation (PubMed:17553757,
PubMed:21144835). Dephosphorylated by PPP5C (PubMed:19176521).
{ECO:0000269|PubMed:11042216, ECO:0000269|PubMed:11331310,
ECO:0000269|PubMed:17553757, ECO:0000269|PubMed:19176521,
ECO:0000269|PubMed:21144835, ECO:0000269|PubMed:23333306,
ECO:0000269|PubMed:23727112, ECO:0000269|PubMed:24703952,
ECO:0000269|PubMed:28241136}.
-!- DISEASE: Note=A chromosomal aberration involving TP53BP1 is found
in a form of myeloproliferative disorder chronic with
eosinophilia. Translocation t(5;15)(q33;q22) with PDGFRB creating
a TP53BP1-PDGFRB fusion protein. {ECO:0000269|PubMed:15492236}.
-!- SEQUENCE CAUTION:
Sequence=BAE06107.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/tp53bp1/";
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EMBL; AF078776; AAC62018.1; -; mRNA.
EMBL; AB210025; BAE06107.1; ALT_INIT; mRNA.
EMBL; BX537418; CAD97660.1; -; mRNA.
EMBL; AY904026; AAW69392.1; -; Genomic_DNA.
EMBL; AC018924; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC112161; AAI12162.1; -; mRNA.
EMBL; U09477; AAA21596.1; -; mRNA.
CCDS; CCDS10096.1; -. [Q12888-1]
CCDS; CCDS45250.1; -. [Q12888-2]
CCDS; CCDS45251.1; -. [Q12888-3]
PIR; I38604; I38604.
RefSeq; NP_001135451.1; NM_001141979.1. [Q12888-3]
RefSeq; NP_001135452.1; NM_001141980.1. [Q12888-2]
RefSeq; NP_005648.1; NM_005657.2. [Q12888-1]
UniGene; Hs.440968; -.
UniGene; Hs.584887; -.
UniGene; Hs.718479; -.
PDB; 1GZH; X-ray; 2.60 A; B/D=1724-1972.
PDB; 1KZY; X-ray; 2.50 A; C/D=1714-1972.
PDB; 1XNI; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J=1485-1602.
PDB; 2G3R; X-ray; 1.25 A; A=1484-1603.
PDB; 2IG0; X-ray; 1.70 A; A=1484-1603.
PDB; 2LVM; NMR; -; A=1484-1603.
PDB; 2MWO; NMR; -; A=1484-1603.
PDB; 2MWP; NMR; -; A=1484-1603.
PDB; 3LGF; X-ray; 1.50 A; A=1484-1603.
PDB; 3LGL; X-ray; 1.60 A; A=1484-1603.
PDB; 3LH0; X-ray; 1.90 A; A=1484-1603.
PDB; 4CRI; X-ray; 2.35 A; A/B=1459-1634.
PDB; 4RG2; X-ray; 1.50 A; A/B=1483-1606.
PDB; 4X34; X-ray; 1.80 A; A/B=1484-1603.
PDB; 5ECG; X-ray; 3.00 A; C/D=1713-1972.
PDB; 5J26; X-ray; 2.50 A; A=1487-1603.
PDB; 5KGF; EM; 4.54 A; K/L=1611-1631.
PDB; 5Z78; X-ray; 1.76 A; C=1484-1603.
PDB; 5ZCJ; X-ray; 2.00 A; C=1459-1634.
PDB; 6CO1; X-ray; 2.18 A; E/F=1484-1603.
PDB; 6CO2; X-ray; 2.49 A; C/D=1484-1603.
PDBsum; 1GZH; -.
PDBsum; 1KZY; -.
PDBsum; 1XNI; -.
PDBsum; 2G3R; -.
PDBsum; 2IG0; -.
PDBsum; 2LVM; -.
PDBsum; 2MWO; -.
PDBsum; 2MWP; -.
PDBsum; 3LGF; -.
PDBsum; 3LGL; -.
PDBsum; 3LH0; -.
PDBsum; 4CRI; -.
PDBsum; 4RG2; -.
PDBsum; 4X34; -.
PDBsum; 5ECG; -.
PDBsum; 5J26; -.
PDBsum; 5KGF; -.
PDBsum; 5Z78; -.
PDBsum; 5ZCJ; -.
PDBsum; 6CO1; -.
PDBsum; 6CO2; -.
ProteinModelPortal; Q12888; -.
SMR; Q12888; -.
BioGrid; 113011; 147.
CORUM; Q12888; -.
DIP; DIP-5978N; -.
IntAct; Q12888; 320.
MINT; Q12888; -.
STRING; 9606.ENSP00000371475; -.
BindingDB; Q12888; -.
ChEMBL; CHEMBL2424509; -.
iPTMnet; Q12888; -.
PhosphoSitePlus; Q12888; -.
BioMuta; TP53BP1; -.
DMDM; 8928568; -.
EPD; Q12888; -.
MaxQB; Q12888; -.
PaxDb; Q12888; -.
PeptideAtlas; Q12888; -.
PRIDE; Q12888; -.
ProteomicsDB; 59003; -.
ProteomicsDB; 59004; -. [Q12888-2]
Ensembl; ENST00000263801; ENSP00000263801; ENSG00000067369. [Q12888-1]
Ensembl; ENST00000382044; ENSP00000371475; ENSG00000067369. [Q12888-2]
Ensembl; ENST00000450115; ENSP00000393497; ENSG00000067369. [Q12888-3]
GeneID; 7158; -.
KEGG; hsa:7158; -.
UCSC; uc001zrq.5; human. [Q12888-1]
CTD; 7158; -.
DisGeNET; 7158; -.
EuPathDB; HostDB:ENSG00000067369.13; -.
GeneCards; TP53BP1; -.
HGNC; HGNC:11999; TP53BP1.
HPA; CAB004083; -.
HPA; HPA008788; -.
HPA; HPA022133; -.
MIM; 605230; gene.
neXtProt; NX_Q12888; -.
OpenTargets; ENSG00000067369; -.
PharmGKB; PA36680; -.
eggNOG; KOG3548; Eukaryota.
eggNOG; ENOG411075K; LUCA.
GeneTree; ENSGT00390000011891; -.
HOGENOM; HOG000231961; -.
HOVERGEN; HBG060882; -.
InParanoid; Q12888; -.
KO; K20915; -.
OMA; QTGTPVC; -.
OrthoDB; EOG091G0BHF; -.
PhylomeDB; Q12888; -.
TreeFam; TF350227; -.
Reactome; R-HSA-3232118; SUMOylation of transcription factors.
Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
SIGNOR; Q12888; -.
ChiTaRS; TP53BP1; human.
EvolutionaryTrace; Q12888; -.
GeneWiki; TP53BP1; -.
GenomeRNAi; 7158; -.
PMAP-CutDB; Q12888; -.
PRO; PR:Q12888; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000067369; Expressed in 222 organ(s), highest expression level in lung.
CleanEx; HS_TP53BP1; -.
ExpressionAtlas; Q12888; baseline and differential.
Genevisible; Q12888; HS.
GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:ProtInc.
GO; GO:1990391; C:DNA repair complex; IEA:Ensembl.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005657; C:replication fork; IEA:Ensembl.
GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB.
GO; GO:0003684; F:damaged DNA binding; IEA:Ensembl.
GO; GO:0042393; F:histone binding; IBA:GO_Central.
GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
GO; GO:0002039; F:p53 binding; IPI:AgBase.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; IPI:BHF-UCL.
GO; GO:0042162; F:telomeric DNA binding; IEA:Ensembl.
GO; GO:0003712; F:transcription coregulator activity; IMP:BHF-UCL.
GO; GO:0061649; F:ubiquitin modification-dependent histone binding; IDA:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0071481; P:cellular response to X-ray; IEA:Ensembl.
GO; GO:0000077; P:DNA damage checkpoint; IBA:GO_Central.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IDA:UniProtKB.
GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; IDA:UniProtKB.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IC:BHF-UCL.
GO; GO:0045830; P:positive regulation of isotype switching; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
CDD; cd00027; BRCT; 2.
Gene3D; 2.30.30.30; -; 1.
Gene3D; 3.40.50.10190; -; 2.
InterPro; IPR015125; 53-BP1_Tudor.
InterPro; IPR001357; BRCT_dom.
InterPro; IPR036420; BRCT_dom_sf.
InterPro; IPR014722; Rib_L2_dom2.
Pfam; PF09038; 53-BP1_Tudor; 1.
SMART; SM00292; BRCT; 2.
SUPFAM; SSF52113; SSF52113; 2.
PROSITE; PS50172; BRCT; 2.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Centromere;
Chromosomal rearrangement; Chromosome; Complete proteome; DNA damage;
DNA repair; DNA-binding; Isopeptide bond; Kinetochore; Methylation;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 1972 TP53-binding protein 1.
/FTId=PRO_0000072643.
DOMAIN 1724 1848 BRCT 1. {ECO:0000255|PROSITE-
ProRule:PRU00033}.
DOMAIN 1864 1964 BRCT 2. {ECO:0000255|PROSITE-
ProRule:PRU00033}.
REGION 1484 1603 Tudor-like.
{ECO:0000305|PubMed:17190600}.
REGION 1495 1523 Interaction with dimethylated histone H4.
{ECO:0000269|PubMed:17190600}.
MOTIF 1396 1403 GAR. {ECO:0000269|PubMed:16294045}.
MOTIF 1604 1631 UDR. {ECO:0000269|PubMed:23760478}.
COMPBIAS 1642 1646 Poly-Ser.
COMPBIAS 1760 1764 Poly-Glu.
MOD_RES 25 25 Phosphoserine.
{ECO:0000269|PubMed:19176521}.
MOD_RES 63 63 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 105 105 Phosphoserine.
{ECO:0000244|PubMed:17525332}.
MOD_RES 124 124 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 166 166 Phosphoserine.
{ECO:0000269|PubMed:17553757}.
MOD_RES 176 176 Phosphoserine.
{ECO:0000305|PubMed:17553757}.
MOD_RES 178 178 Phosphoserine.
{ECO:0000305|PubMed:17553757}.
MOD_RES 222 222 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 265 265 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 294 294 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:17553757}.
MOD_RES 302 302 Phosphothreonine.
{ECO:0000244|PubMed:17525332,
ECO:0000269|PubMed:17553757}.
MOD_RES 366 366 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 380 380 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:17553757}.
MOD_RES 395 395 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 398 398 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 429 429 Phosphoserine.
{ECO:0000250|UniProtKB:P70399}.
MOD_RES 452 452 Phosphoserine.
{ECO:0000269|PubMed:17553757}.
MOD_RES 464 464 Phosphoserine.
{ECO:0000250|UniProtKB:P70399}.
MOD_RES 500 500 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 507 507 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 518 518 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 523 523 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:17553757}.
MOD_RES 525 525 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 543 543 Phosphothreonine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:19690332}.
MOD_RES 548 548 Phosphothreonine.
{ECO:0000244|PubMed:17525332}.
MOD_RES 552 552 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:17553757}.
MOD_RES 566 566 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 580 580 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 630 630 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 635 635 Phosphoserine.
{ECO:0000244|PubMed:17081983}.
MOD_RES 639 639 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231}.
MOD_RES 640 640 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231}.
MOD_RES 692 692 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 724 724 Phosphoserine.
{ECO:0000250|UniProtKB:P70399}.
MOD_RES 727 727 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 771 771 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 809 809 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 830 830 Phosphoserine.
{ECO:0000250|UniProtKB:P70399}.
MOD_RES 831 831 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:17553757}.
MOD_RES 834 834 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 855 855 Phosphothreonine.
{ECO:0000244|PubMed:17525332}.
MOD_RES 922 922 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 970 970 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 975 975 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1028 1028 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:17553757}.
MOD_RES 1056 1056 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1068 1068 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1086 1086 Phosphoserine.
{ECO:0000269|PubMed:17553757}.
MOD_RES 1094 1094 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1101 1101 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1114 1114 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:17553757}.
MOD_RES 1148 1148 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1214 1214 Phosphothreonine.
{ECO:0000244|PubMed:17525332}.
MOD_RES 1216 1216 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1219 1219 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:17553757}.
MOD_RES 1317 1317 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1342 1342 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1355 1355 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P70399}.
MOD_RES 1362 1362 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1368 1368 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1372 1372 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1426 1426 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1430 1430 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1460 1460 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 1462 1462 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 1474 1474 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 1609 1609 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:24703952}.
MOD_RES 1618 1618 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:24703952}.
MOD_RES 1631 1631 Phosphoserine.
{ECO:0000250|UniProtKB:P70399}.
MOD_RES 1635 1635 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1638 1638 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1648 1648 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1656 1656 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1673 1673 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1678 1678 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1701 1701 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1759 1759 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1778 1778 Phosphoserine.
{ECO:0000269|PubMed:19176521,
ECO:0000269|PubMed:21144835}.
CROSSLNK 217 217 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 217 217 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:28112733}.
CROSSLNK 868 868 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 868 868 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 930 930 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 984 984 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1365 1365 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1434 1434 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 1434 1434 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:28112733}.
CROSSLNK 1563 1563 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 1563 1563 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 1 M -> MPGEQM (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:17974005,
ECO:0000303|Ref.2}.
/FTId=VSP_018390.
VAR_SEQ 1692 1693 Missing (in isoform 3).
{ECO:0000303|Ref.2}.
/FTId=VSP_055062.
VARIANT 353 353 D -> E (in dbSNP:rs560191).
{ECO:0000269|PubMed:17974005,
ECO:0000269|Ref.4}.
/FTId=VAR_022172.
VARIANT 412 412 G -> S (in dbSNP:rs689647).
{ECO:0000269|PubMed:17974005,
ECO:0000269|Ref.4}.
/FTId=VAR_022173.
VARIANT 648 648 M -> V (in dbSNP:rs45443496).
{ECO:0000269|Ref.4}.
/FTId=VAR_022174.
VARIANT 699 699 Q -> R (in dbSNP:rs34823068).
{ECO:0000269|Ref.4}.
/FTId=VAR_022175.
VARIANT 841 841 D -> G (in dbSNP:rs34185035).
/FTId=VAR_034558.
VARIANT 1014 1014 E -> G (in dbSNP:rs45470395).
{ECO:0000269|Ref.4}.
/FTId=VAR_022176.
VARIANT 1026 1026 V -> A (in dbSNP:rs45482998).
{ECO:0000269|Ref.4}.
/FTId=VAR_022177.
VARIANT 1136 1136 K -> Q (in dbSNP:rs2602141).
{ECO:0000269|PubMed:17974005,
ECO:0000269|Ref.4}.
/FTId=VAR_022178.
VARIANT 1137 1137 E -> K (in dbSNP:rs34740611).
/FTId=VAR_034559.
VARIANT 1170 1170 A -> G (in dbSNP:rs45500399).
{ECO:0000269|Ref.4}.
/FTId=VAR_022179.
VARIANT 1174 1174 I -> V (in dbSNP:rs3803339).
{ECO:0000269|Ref.4}.
/FTId=VAR_022180.
VARIANT 1442 1442 R -> Q (in dbSNP:rs2230449).
/FTId=VAR_034560.
VARIANT 1488 1488 G -> W (in dbSNP:rs11554564).
/FTId=VAR_038689.
MUTAGEN 6 6 S->A: In 28A: Defects in recruitment to
double strand breaks (DSBs), abolished
interaction with RIF1 and abolished
ability to repair DSBs; when associated
with A-13; A-25; A-29; A-105; A-166; A-
176; A-178; A-302; A-437; A-452; A-523;
A-543; A-580; A-625; A-674; A-696; A-698;
A-784; A-831; A-855; A-892; A-1068; A-
1086; A-1104; A-1148; A-1171 and A-1219.
In 8A: Does not affect interaction with
RIF1 and ability to promote
immunoglobulin class-switch recombination
(CSR), but abolishes interaction with
PAXIP1 and ability to promote NHEJ of
dysfunctional telomeres; when associated
with A-13; A-25; A-29; A-105; A-166; A-
176 and A-178.
{ECO:0000269|PubMed:23333306,
ECO:0000269|PubMed:23345425,
ECO:0000269|PubMed:23727112}.
MUTAGEN 13 13 S->A: In 28A: Defects in recruitment to
double strand breaks (DSBs), abolished
interaction with RIF1 and abolished
ability to repair DSBs; when associated
with A-6; A-25; A-29; A-105; A-166; A-
176; A-178; A-302; A-437; A-452; A-523;
A-543; A-580; A-625; A-674; A-696; A-698;
A-784; A-831; A-855; A-892; A-1068; A-
1086; A-1104; A-1148; A-1171 and A-1219.
In 8A: Does not affect interaction with
RIF1 and ability to promote
immunoglobulin class-switch recombination
(CSR), but abolishes interaction with
PAXIP1 and ability to promote NHEJ of
dysfunctional telomeres; when associated
with A-6; A-25; A-29; A-105; A-166; A-176
and A-178. {ECO:0000269|PubMed:23333306,
ECO:0000269|PubMed:23345425,
ECO:0000269|PubMed:23727112}.
MUTAGEN 25 25 S->A: In 28A: Defects in recruitment to
double strand breaks (DSBs), abolished
interaction with RIF1 and abolished
ability to repair DSBs; when associated
with A-6; A-13; A-29; A-105; A-166; A-
176; A-178; A-302; A-437; A-452; A-523;
A-543; A-580; A-625; A-674; A-696; A-698;
A-784; A-831; A-855; A-892; A-1068; A-
1086; A-1104; A-1148; A-1171 and A-1219.
In 8A: Does not affect interaction with
RIF1 and ability to promote
immunoglobulin class-switch recombination
(CSR), but abolishes interaction with
PAXIP1 and ability to promote NHEJ of
dysfunctional telomeres; when associated
with A-6; A-13; A-29; A-105; A-166; A-176
and A-178. {ECO:0000269|PubMed:23333306,
ECO:0000269|PubMed:23345425,
ECO:0000269|PubMed:23727112}.
MUTAGEN 29 29 S->A: In 28A: Defects in recruitment to
double strand breaks (DSBs), abolished
interaction with RIF1 and abolished
ability to repair DSBs; when associated
with A-6; A-13; A-25; A-105; A-166; A-
176; A-178; A-302; A-437; A-452; A-523;
A-543; A-580; A-625; A-674; A-696; A-698;
A-784; A-831; A-855; A-892; A-1068; A-
1086; A-1104; A-1148; A-1171 and A-1219.
In 8A: Does not affect interaction with
RIF1 and ability to promote
immunoglobulin class-switch recombination
(CSR), but abolishes interaction with
PAXIP1 and ability to promote NHEJ of
dysfunctional telomeres; when associated
with A-6; A-13; A-25; A-105; A-166; A-176
and A-178. {ECO:0000269|PubMed:23333306,
ECO:0000269|PubMed:23345425,
ECO:0000269|PubMed:23727112}.
MUTAGEN 105 105 S->A: In 28A: Defects in recruitment to
double strand breaks (DSBs), abolished
interaction with RIF1 and abolished
ability to repair DSBs; when associated
with A-6; A-13; A-25; A-29; A-166; A-176;
A-178; A-302; A-437; A-452; A-523; A-543;
A-580; A-625; A-674; A-696; A-698; A-784;
A-831; A-855; A-892; A-1068; A-1086; A-
1104; A-1148; A-1171 and A-1219. In 8A:
Does not affect interaction with RIF1 and
ability to promote immunoglobulin class-
switch recombination (CSR), but abolishes
interaction with PAXIP1 and ability to
promote NHEJ of dysfunctional telomeres;
when associated with A-6; A-13; A-25; A-
29; A-166; A-176 and A-178.
{ECO:0000269|PubMed:23333306,
ECO:0000269|PubMed:23345425,
ECO:0000269|PubMed:23727112}.
MUTAGEN 166 166 S->A: In 28A: Defects in recruitment to
double strand breaks (DSBs), abolished
interaction with RIF1 and abolished
ability to repair DSBs; when associated
with A-6; A-13; A-25; A-29; A-105; A-176;
A-178; A-302; A-437; A-452; A-523; A-543;
A-580; A-625; A-674; A-696; A-698; A-784;
A-831; A-855; A-892; A-1068; A-1086; A-
1104; A-1148; A-1171 and A-1219. In 8A:
Does not affect interaction with RIF1 and
ability to promote immunoglobulin class-
switch recombination (CSR), but abolishes
interaction with PAXIP1 and ability to
promote NHEJ of dysfunctional telomeres;
when associated with A-6; A-13; A-25; A-
29; A-105; A-176 and A-178.
{ECO:0000269|PubMed:23333306,
ECO:0000269|PubMed:23345425,
ECO:0000269|PubMed:23727112}.
MUTAGEN 176 178 SQS->AQA: Loss of phosphorylation site.
{ECO:0000269|PubMed:17553757}.
MUTAGEN 176 176 S->A: In 28A: Defects in recruitment to
double strand breaks (DSBs), abolished
interaction with RIF1 and abolished
ability to repair DSBs; when associated
with A-6; A-13; A-25; A-29; A-105; A-166;
A-178; A-302; A-437; A-452; A-523; A-543;
A-580; A-625; A-674; A-696; A-698; A-784;
A-831; A-855; A-892; A-1068; A-1086; A-
1104; A-1148; A-1171 and A-1219. In 8A:
Does not affect interaction with RIF1 and
ability to promote immunoglobulin class-
switch recombination (CSR), but abolishes
interaction with PAXIP1 and ability to
promote NHEJ of dysfunctional telomeres;
when associated with A-6; A-13; A-25; A-
29; A-105; A-166 and A-178.
{ECO:0000269|PubMed:23333306,
ECO:0000269|PubMed:23345425,
ECO:0000269|PubMed:23727112}.
MUTAGEN 178 178 S->A: In 28A: Defects in recruitment to
double strand breaks (DSBs), abolished
interaction with RIF1 and abolished
ability to repair DSBs; when associated
with A-6; A-13; A-25; A-29; A-105; A-166;
A-176; A-302; A-437; A-452; A-523; A-543;
A-580; A-625; A-674; A-696; A-698; A-784;
A-831; A-855; A-892; A-1068; A-1086; A-
1104; A-1148; A-1171 and A-1219. In 8A:
Does not affect interaction with RIF1 and
ability to promote immunoglobulin class-
switch recombination (CSR), but abolishes
interaction with PAXIP1 and ability to
promote NHEJ of dysfunctional telomeres;
when associated with A-6; A-13; A-25; A-
29; A-105; A-166 and A-176.
{ECO:0000269|PubMed:23333306,
ECO:0000269|PubMed:23345425,
ECO:0000269|PubMed:23727112}.
MUTAGEN 302 302 T->A: In 28A: Defects in recruitment to
double strand breaks (DSBs), abolished
interaction with RIF1 and abolished
ability to repair DSBs; when associated
with A-6; A-13; A-25; A-29; A-105; A-166;
A-176; A-178; A-437; A-452; A-523; A-543;
A-580; A-625; A-674; A-696; A-698; A-784;
A-831; A-855; A-892; A-1068; A-1086; A-
1104; A-1148; A-1171 and A-1219.
{ECO:0000269|PubMed:23333306,
ECO:0000269|PubMed:23345425}.
MUTAGEN 437 437 S->A: In 28A: Defects in recruitment to
double strand breaks (DSBs), abolished
interaction with RIF1 and abolished
ability to repair DSBs; when associated
with A-6; A-13; A-25; A-29; A-105; A-166;
A-176; A-178; A-302; A-452; A-523; A-543;
A-580; A-625; A-674; A-696; A-698; A-784;
A-831; A-855; A-892; A-1068; A-1086; A-
1104; A-1148; A-1171 and A-1219.
{ECO:0000269|PubMed:23333306,
ECO:0000269|PubMed:23345425}.
MUTAGEN 452 452 S->A: In 28A: Defects in recruitment to
double strand breaks (DSBs), abolished
interaction with RIF1 and abolished
ability to repair DSBs; when associated
with A-6; A-13; A-25; A-29; A-105; A-166;
A-176; A-178; A-302; A-437; A-523; A-543;
A-580; A-625; A-674; A-696; A-698; A-784;
A-831; A-855; A-892; A-1068; A-1086; A-
1104; A-1148; A-1171 and A-1219.
{ECO:0000269|PubMed:23333306,
ECO:0000269|PubMed:23345425}.
MUTAGEN 523 523 S->A: In 28A: Defects in recruitment to
double strand breaks (DSBs), abolished
interaction with RIF1 and abolished
ability to repair DSBs; when associated
with A-6; A-13; A-25; A-29; A-105; A-166;
A-176; A-178; A-302; A-437; A-452; A-543;
A-580; A-625; A-674; A-696; A-698; A-784;
A-831; A-855; A-892; A-1068; A-1086; A-
1104; A-1148; A-1171 and A-1219.
{ECO:0000269|PubMed:23333306,
ECO:0000269|PubMed:23345425}.
MUTAGEN 543 543 T->A: In 28A: Defects in recruitment to
double strand breaks (DSBs), abolished
interaction with RIF1 and abolished
ability to repair DSBs; when associated
with A-6; A-13; A-25; A-29; A-105; A-166;
A-176; A-178; A-302; A-437; A-452; A-523;
A-580; A-625; A-674; A-696; A-698; A-784;
A-831; A-855; A-892; A-1068; A-1086; A-
1104; A-1148; A-1171 and A-1219.
{ECO:0000269|PubMed:23333306,
ECO:0000269|PubMed:23345425}.
MUTAGEN 580 580 S->A: In 28A: Defects in recruitment to
double strand breaks (DSBs), abolished
interaction with RIF1 and abolished
ability to repair DSBs; when associated
with A-6; A-13; A-25; A-29; A-105; A-166;
A-176; A-178; A-302; A-437; A-452; A-523;
A-543; A-625; A-674; A-696; A-698; A-784;
A-831; A-855; A-892; A-1068; A-1086; A-
1104; A-1148; A-1171 and A-1219.
{ECO:0000269|PubMed:23333306,
ECO:0000269|PubMed:23345425}.
MUTAGEN 625 625 S->A: In 28A: Defects in recruitment to
double strand breaks (DSBs), abolished
interaction with RIF1 and abolished
ability to repair DSBs; when associated
with A-6; A-13; A-25; A-29; A-105; A-166;
A-176; A-178; A-302; A-437; A-452; A-523;
A-543; A-580; A-674; A-696; A-698; A-784;
A-831; A-855; A-892; A-1068; A-1086; A-
1104; A-1148; A-1171 and A-1219.
{ECO:0000269|PubMed:23333306,
ECO:0000269|PubMed:23345425}.
MUTAGEN 674 674 S->A: In 28A: Defects in recruitment to
double strand breaks (DSBs), abolished
interaction with RIF1 and abolished
ability to repair DSBs; when associated
with A-6; A-13; A-25; A-29; A-105; A-166;
A-176; A-178; A-302; A-437; A-452; A-523;
A-543; A-580; A-625; A-696; A-698; A-784;
A-831; A-855; A-892; A-1068; A-1086; A-
1104; A-1148; A-1171 and A-1219.
{ECO:0000269|PubMed:23333306,
ECO:0000269|PubMed:23345425}.
MUTAGEN 696 696 T->A: In 28A: Defects in recruitment to
double strand breaks (DSBs), abolished
interaction with RIF1 and abolished
ability to repair DSBs; when associated
with A-6; A-13; A-25; A-29; A-105; A-166;
A-176; A-178; A-302; A-437; A-452; A-523;
A-543; A-580; A-625; A-674; A-698; A-784;
A-831; A-855; A-892; A-1068; A-1086; A-
1104; A-1148; A-1171 and A-1219.
{ECO:0000269|PubMed:23333306,
ECO:0000269|PubMed:23345425}.
MUTAGEN 698 698 S->A: In 28A: Defects in recruitment to
double strand breaks (DSBs), abolished
interaction with RIF1 and abolished
ability to repair DSBs; when associated
with A-6; A-13; A-25; A-29; A-105; A-166;
A-176; A-178; A-302; A-437; A-452; A-523;
A-543; A-580; A-625; A-674; A-696; A-784;
A-831; A-855; A-892; A-1068; A-1086; A-
1104; A-1148; A-1171 and A-1219.
{ECO:0000269|PubMed:23333306,
ECO:0000269|PubMed:23345425}.
MUTAGEN 784 784 S->A: In 28A: Defects in recruitment to
double strand breaks (DSBs), abolished
interaction with RIF1 and abolished
ability to repair DSBs; when associated
with A-6; A-13; A-25; A-29; A-105; A-166;
A-176; A-178; A-302; A-437; A-452; A-523;
A-543; A-580; A-625; A-674; A-696; A-698;
A-831; A-855; A-892; A-1068; A-1086; A-
1104; A-1148; A-1171 and A-1219.
{ECO:0000269|PubMed:23333306,
ECO:0000269|PubMed:23345425}.
MUTAGEN 831 831 S->A: In 28A: Defects in recruitment to
double strand breaks (DSBs), abolished
interaction with RIF1 and abolished
ability to repair DSBs; when associated
with A-6; A-13; A-25; A-29; A-105; A-166;
A-176; A-178; A-302; A-437; A-452; A-523;
A-543; A-580; A-625; A-674; A-696; A-698;
A-784; A-855; A-892; A-1068; A-1086; A-
1104; A-1148; A-1171 and A-1219.
{ECO:0000269|PubMed:23333306,
ECO:0000269|PubMed:23345425}.
MUTAGEN 855 855 T->A: In 28A: Defects in recruitment to
double strand breaks (DSBs), abolished
interaction with RIF1 and abolished
ability to repair DSBs; when associated
with A-6; A-13; A-25; A-29; A-105; A-166;
A-176; A-178; A-302; A-437; A-452; A-523;
A-543; A-580; A-625; A-674; A-696; A-698;
A-784; A-831; A-892; A-1068; A-1086; A-
1104; A-1148; A-1171 and A-1219.
{ECO:0000269|PubMed:23333306,
ECO:0000269|PubMed:23345425}.
MUTAGEN 892 892 S->A: In 28A: Defects in recruitment to
double strand breaks (DSBs), abolished
interaction with RIF1 and abolished
ability to repair DSBs; when associated
with A-6; A-13; A-25; A-29; A-105; A-166;
A-176; A-178; A-302; A-437; A-452; A-523;
A-543; A-580; A-625; A-674; A-696; A-698;
A-784; A-831; A-855; A-1068; A-1086; A-
1104; A-1148; A-1171 and A-1219.
{ECO:0000269|PubMed:23333306,
ECO:0000269|PubMed:23345425}.
MUTAGEN 1068 1068 S->A: In 28A: Defects in recruitment to
double strand breaks (DSBs), abolished
interaction with RIF1 and abolished
ability to repair DSBs; when associated
with A-6; A-13; A-25; A-29; A-105; A-166;
A-176; A-178; A-302; A-437; A-452; A-523;
A-543; A-580; A-625; A-674; A-696; A-698;
A-784; A-831; A-855; A-892; A-1086; A-
1104; A-1148; A-1171 and A-1219.
{ECO:0000269|PubMed:23333306,
ECO:0000269|PubMed:23345425}.
MUTAGEN 1086 1086 S->A: In 28A: Defects in recruitment to
double strand breaks (DSBs), abolished
interaction with RIF1 and abolished
ability to repair DSBs; when associated
with A-6; A-13; A-25; A-29; A-105; A-166;
A-176; A-178; A-302; A-437; A-452; A-523;
A-543; A-580; A-625; A-674; A-696; A-698;
A-784; A-831; A-855; A-892; A-1068; A-
1104; A-1148; A-1171 and A-1219.
{ECO:0000269|PubMed:23333306,
ECO:0000269|PubMed:23345425}.
MUTAGEN 1104 1104 S->A: In 28A: Defects in recruitment to
double strand breaks (DSBs), abolished
interaction with RIF1 and abolished
ability to repair DSBs; when associated
with A-6; A-13; A-25; A-29; A-105; A-166;
A-176; A-178; A-302; A-437; A-452; A-523;
A-543; A-580; A-625; A-674; A-696; A-698;
A-784; A-831; A-855; A-892; A-1068; A-
1086; A-1148; A-1171 and A-1219.
{ECO:0000269|PubMed:23333306,
ECO:0000269|PubMed:23345425}.
MUTAGEN 1148 1148 S->A: In 28A: Defects in recruitment to
double strand breaks (DSBs), abolished
interaction with RIF1 and abolished
ability to repair DSBs; when associated
with A-6; A-13; A-25; A-29; A-105; A-166;
A-176; A-178; A-302; A-437; A-452; A-523;
A-543; A-580; A-625; A-674; A-696; A-698;
A-784; A-831; A-855; A-892; A-1068; A-
1086; A-1104; A-1171 and A-1219.
{ECO:0000269|PubMed:23333306,
ECO:0000269|PubMed:23345425}.
MUTAGEN 1171 1171 T->A: In 28A: Defects in recruitment to
double strand breaks (DSBs), abolished
interaction with RIF1 and abolished
ability to repair DSBs; when associated
with A-6; A-13; A-25; A-29; A-105; A-166;
A-176; A-178; A-302; A-437; A-452; A-523;
A-543; A-580; A-625; A-674; A-696; A-698;
A-784; A-831; A-855; A-892; A-1068; A-
1086; A-1104; A-1148 and A-1219.
{ECO:0000269|PubMed:23333306,
ECO:0000269|PubMed:23345425}.
MUTAGEN 1219 1219 S->A: In 28A: Defects in recruitment to
double strand breaks (DSBs), abolished
interaction with RIF1 and abolished
ability to repair DSBs; when associated
with A-6; A-13; A-25; A-29; A-105; A-166;
A-176; A-178; A-302; A-437; A-452; A-523;
A-543; A-580; A-625; A-674; A-696; A-698;
A-784; A-831; A-855; A-892; A-1068; A-
1086; A-1104; A-1148 and A-1171.
{ECO:0000269|PubMed:23333306,
ECO:0000269|PubMed:23345425}.
MUTAGEN 1396 1396 R->A: No detectable effect on methylation
by PRMT1 (in vitro). Loss of methylation;
when associated with A-1398; A-1400; A-
1401 and A-1403.
{ECO:0000269|PubMed:16294045,
ECO:0000269|PubMed:16294047}.
MUTAGEN 1396 1396 R->K: No detectable effect on methylation
by PRMT1 (in vitro).
{ECO:0000269|PubMed:16294045,
ECO:0000269|PubMed:16294047}.
MUTAGEN 1398 1401 RGRR->AGAA: No effect on in class-switch
recombination (CSR).
{ECO:0000269|PubMed:23345425}.
MUTAGEN 1398 1398 R->A: No detectable effect on methylation
by PRMT1 (in vitro). Loss of methylation;
when associated with A-1396; A-1400; A-
1401 and A-1403.
{ECO:0000269|PubMed:16294045,
ECO:0000269|PubMed:16294047}.
MUTAGEN 1398 1398 R->K: Reduced methylation by PRMT1 (in
vitro). Strongly reduced methylation;
when associated with K-1400. Strongly
reduced methylation; when associated with
K-1401. {ECO:0000269|PubMed:16294045,
ECO:0000269|PubMed:16294047}.
MUTAGEN 1400 1400 R->A: No detectable effect on methylation
by PRMT1 (in vitro). Loss of methylation;
when associated with A-1396; A-1398; A-
1401 and A-1403.
{ECO:0000269|PubMed:16294045,
ECO:0000269|PubMed:16294047}.
MUTAGEN 1400 1400 R->K: Reduced methylation by PRMT1 (in
vitro). Strongly reduced methylation;
when associated with K-1398. Strongly
reduced methylation; when associated with
K-1401. {ECO:0000269|PubMed:16294045,
ECO:0000269|PubMed:16294047}.
MUTAGEN 1401 1401 R->A: No detectable effect on methylation
by PRMT1 (in vitro). Loss of methylation;
when associated with A-1396; A-1398; A-
1400 and A-1403.
{ECO:0000269|PubMed:16294045,
ECO:0000269|PubMed:16294047}.
MUTAGEN 1401 1401 R->K: Reduced methylation by PRMT1 (in
vitro). Strongly reduced methylation;
when associated with K-1398. Strongly
reduced methylation; when associated with
K-1400. {ECO:0000269|PubMed:16294045,
ECO:0000269|PubMed:16294047}.
MUTAGEN 1403 1403 R->A: No detectable effect on methylation
by PRMT1 (in vitro). Loss of methylation;
when associated with A-1396; A-1398; A-
1400 and A-1401.
{ECO:0000269|PubMed:16294045,
ECO:0000269|PubMed:16294047}.
MUTAGEN 1403 1403 R->K: No detectable effect on methylation
by PRMT1 (in vitro).
{ECO:0000269|PubMed:16294045,
ECO:0000269|PubMed:16294047}.
MUTAGEN 1495 1495 W->A,H: Loss of interaction with histone
H4 that has been dimethylated at 'Lys-20'
(H4K20me2). Abolishes recruitment to
double strand breaks. Loss of interaction
with histone H4 that has been
dimethylated at 'Lys-20' (H4K20me2).
Abolishes recruitment to double strand
breaks; when associated with A-1521.
{ECO:0000269|PubMed:15525939,
ECO:0000269|PubMed:17190600,
ECO:0000269|PubMed:28241136}.
MUTAGEN 1495 1495 W->F: No effect on recruitment to double
strand breaks.
{ECO:0000269|PubMed:15525939,
ECO:0000269|PubMed:17190600}.
MUTAGEN 1495 1495 W->V: Reduces recruitment to double
strand breaks.
{ECO:0000269|PubMed:15525939,
ECO:0000269|PubMed:17190600}.
MUTAGEN 1500 1500 Y->A: Reduces affinity for histone H4
that has been dimethylated at 'Lys-20'.
{ECO:0000269|PubMed:17190600}.
MUTAGEN 1502 1502 Y->A: Reduces affinity for histone H4
that has been dimethylated at 'Lys-20'.
{ECO:0000269|PubMed:15525939,
ECO:0000269|PubMed:17190600}.
MUTAGEN 1502 1502 Y->L,Q: Abolishes recruitment to double
strand breaks.
{ECO:0000269|PubMed:15525939,
ECO:0000269|PubMed:17190600}.
MUTAGEN 1521 1521 D->A: Loss of interaction with histone H4
that has been dimethylated at 'Lys-20'
(H4K20me2). Abolishes recruitment to
double strand breaks. Loss of interaction
with histone H4 that has been
dimethylated at 'Lys-20' (H4K20me2).
Abolishes recruitment to double strand
breaks; when associated with A-1495.
{ECO:0000269|PubMed:15525939,
ECO:0000269|PubMed:17190600,
ECO:0000269|PubMed:28241136}.
MUTAGEN 1521 1521 D->R: Abolishes recruitment to double
strand breaks and induces defects in
class-switch recombination (CSR).
{ECO:0000269|PubMed:15525939,
ECO:0000269|PubMed:17190600,
ECO:0000269|PubMed:23345425,
ECO:0000269|PubMed:23760478}.
MUTAGEN 1523 1523 Y->A: Increases affinity for histone H4
that has been dimethylated at 'Lys-20'.
No effect on recruitment to double strand
breaks. {ECO:0000269|PubMed:17190600}.
MUTAGEN 1523 1523 Y->S: Decreases affinity for histone H4
that has been dimethylated at 'Lys-20'.
{ECO:0000269|PubMed:17190600}.
MUTAGEN 1609 1609 T->A: Constitutive recruitment to mitotic
DNA lesions, leading to mitotic defects;
when associated with A-1618.
{ECO:0000269|PubMed:24703952}.
MUTAGEN 1609 1609 T->E: Phosphomimetic mutant that
abolishes recruitment to double strand
breaks; when associated with D-1618.
{ECO:0000269|PubMed:24703952}.
MUTAGEN 1613 1613 K->A: Does not affect recruitment to
double strand breaks.
{ECO:0000269|PubMed:23760478}.
MUTAGEN 1616 1616 D->A: Does not affect recruitment to
double strand breaks.
{ECO:0000269|PubMed:23760478}.
MUTAGEN 1617 1617 I->A: Strongly reduced recruitment to
double strand breaks. Defects in class-
switch recombination (CSR).
{ECO:0000269|PubMed:23760478}.
MUTAGEN 1618 1618 S->A: Constitutive recruitment to mitotic
DNA lesions, leading to mitotic defects;
when associated with A-1609.
{ECO:0000269|PubMed:24703952}.
MUTAGEN 1618 1618 S->D: Phosphomimetic mutant that
abolishes recruitment to double strand
breaks; when associated with E-1609.
{ECO:0000269|PubMed:24703952}.
MUTAGEN 1619 1619 L->A: Strongly reduced recruitment to
double strand breaks. Defects in class-
switch recombination (CSR). Does not
affect interaction with histone H4
dimethylated at 'Lys-20' (H4K20me2).
Impaired interaction with histone H2A
monoubiquitinated at 'Lys-15' (H2AK15ub).
{ECO:0000269|PubMed:23760478}.
MUTAGEN 1621 1621 N->A: Reduced recruitment to double
strand breaks.
{ECO:0000269|PubMed:23760478}.
MUTAGEN 1622 1622 L->A: Reduced recruitment to double
strand breaks.
{ECO:0000269|PubMed:23760478}.
MUTAGEN 1624 1624 E->A: Does not affect recruitment to
double strand breaks.
{ECO:0000269|PubMed:23760478}.
MUTAGEN 1627 1627 R->A: Reduced recruitment to double
strand breaks.
{ECO:0000269|PubMed:23760478}.
CONFLICT 796 796 P -> S (in Ref. 3; CAD97660).
{ECO:0000305}.
CONFLICT 1600 1600 Y -> C (in Ref. 3; CAD97660).
{ECO:0000305}.
CONFLICT 1958 1958 G -> R (in Ref. 3; CAD97660).
{ECO:0000305}.
STRAND 1490 1494 {ECO:0000244|PDB:2G3R}.
TURN 1496 1498 {ECO:0000244|PDB:2G3R}.
STRAND 1501 1511 {ECO:0000244|PDB:2G3R}.
STRAND 1514 1519 {ECO:0000244|PDB:2G3R}.
STRAND 1524 1528 {ECO:0000244|PDB:2G3R}.
HELIX 1529 1531 {ECO:0000244|PDB:2G3R}.
STRAND 1532 1535 {ECO:0000244|PDB:2LVM}.
STRAND 1543 1547 {ECO:0000244|PDB:2G3R}.
STRAND 1549 1551 {ECO:0000244|PDB:5Z78}.
STRAND 1553 1564 {ECO:0000244|PDB:2G3R}.
STRAND 1567 1574 {ECO:0000244|PDB:2G3R}.
STRAND 1577 1582 {ECO:0000244|PDB:2G3R}.
HELIX 1583 1585 {ECO:0000244|PDB:2G3R}.
STRAND 1586 1588 {ECO:0000244|PDB:2G3R}.
HELIX 1590 1594 {ECO:0000244|PDB:2G3R}.
HELIX 1597 1600 {ECO:0000244|PDB:2G3R}.
HELIX 1715 1719 {ECO:0000244|PDB:1KZY}.
TURN 1726 1731 {ECO:0000244|PDB:1KZY}.
STRAND 1732 1736 {ECO:0000244|PDB:1KZY}.
HELIX 1741 1745 {ECO:0000244|PDB:1GZH}.
HELIX 1773 1781 {ECO:0000244|PDB:1KZY}.
TURN 1782 1784 {ECO:0000244|PDB:1KZY}.
TURN 1793 1799 {ECO:0000244|PDB:1KZY}.
STRAND 1801 1808 {ECO:0000244|PDB:1KZY}.
HELIX 1813 1821 {ECO:0000244|PDB:1KZY}.
STRAND 1825 1827 {ECO:0000244|PDB:1KZY}.
HELIX 1829 1837 {ECO:0000244|PDB:1KZY}.
HELIX 1843 1845 {ECO:0000244|PDB:1KZY}.
STRAND 1851 1853 {ECO:0000244|PDB:1KZY}.
TURN 1854 1857 {ECO:0000244|PDB:1KZY}.
STRAND 1858 1860 {ECO:0000244|PDB:1KZY}.
TURN 1868 1871 {ECO:0000244|PDB:1KZY}.
STRAND 1873 1879 {ECO:0000244|PDB:1KZY}.
TURN 1881 1884 {ECO:0000244|PDB:1KZY}.
HELIX 1885 1894 {ECO:0000244|PDB:1KZY}.
STRAND 1898 1908 {ECO:0000244|PDB:1KZY}.
HELIX 1914 1916 {ECO:0000244|PDB:1KZY}.
STRAND 1918 1922 {ECO:0000244|PDB:1KZY}.
HELIX 1928 1937 {ECO:0000244|PDB:1KZY}.
HELIX 1944 1953 {ECO:0000244|PDB:1KZY}.
HELIX 1963 1965 {ECO:0000244|PDB:1KZY}.
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


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