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DNA topoisomerase 2-alpha (EC 5.99.1.3) (DNA topoisomerase II, alpha isozyme)

 TOP2A_HUMAN             Reviewed;        1531 AA.
P11388; B2RTS1; Q71UN1; Q71UQ5; Q9HB24; Q9HB25; Q9HB26; Q9UP44;
Q9UQP9;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
04-MAY-2001, sequence version 3.
22-NOV-2017, entry version 219.
RecName: Full=DNA topoisomerase 2-alpha;
EC=5.99.1.3;
AltName: Full=DNA topoisomerase II, alpha isozyme;
Name=TOP2A; Synonyms=TOP2;
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).
PubMed=2845399; DOI=10.1073/pnas.85.19.7177;
Tsai-Pflugfelder M., Liu L.F., Liu A.A., Tewey K.M., Whang-Peng J.,
Knutsen T., Huebner K., Croce C.M., Wang J.C.;
"Cloning and sequencing of cDNA encoding human DNA topoisomerase II
and localization of the gene to chromosome region 17q21-22.";
Proc. Natl. Acad. Sci. U.S.A. 85:7177-7181(1988).
[2]
SEQUENCE REVISION TO 109-114.
PubMed=8393377;
Wasserman R.A., Austin C.A., Fisher L.M., Wang J.C.;
"Use of yeast in the study of anticancer drugs targeting DNA
topoisomerases: expression of a functional recombinant human DNA
topoisomerase II alpha in yeast.";
Cancer Res. 53:3591-3596(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=9795238; DOI=10.1016/S0378-1119(98)00468-5;
Lang A.J., Mirski S.E., Cummings H.J., Yu Q., Gerlach J.H., Cole S.P.;
"Structural organization of the human TOP2A and TOP2B genes.";
Gene 221:255-266(1998).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=10095062; DOI=10.1016/S0167-4781(99)00020-2;
Sng J.H., Heaton V.J., Bell M., Mani P., Austin C.A., Fisher L.M.;
"Molecular cloning and characterization of the human topoisomerase
IIalpha and IIbeta genes: evidence for isoform evolution through gene
duplication.";
Biochim. Biophys. Acta 1444:395-406(1999).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-500 (ISOFORMS 2; 3 AND 4).
Petruti-Mot A.S., Earnshaw W.C.;
"Two differentially spliced forms of topoisomerase II alpha and beta
mRNAs are conserved between birds and humans.";
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21 AND 48-72.
Neri S., Govoni M., Perrotta L., Pozzi S., Pession A.;
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
[10]
PROTEIN SEQUENCE OF 1-17; 74-96; 124-131; 169-184; 243-251; 277-287;
325-336; 387-397; 467-478; 481-487; 500-519; 569-579; 702-713;
805-815; 828-835; 864-877; 937-958; 1021-1026 AND 1185-1196,
ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[11]
PROTEIN SEQUENCE OF 135-157; 228-241; 307-321; 325-336; 387-397;
401-416; 467-478; 536-550; 569-579; 640-655; 702-713; 805-815;
1011-1020; 1097-1114; 1169-1184; 1239-1259 AND 1374-1411,
PHOSPHORYLATION AT SER-1106, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Cervix carcinoma;
Bienvenut W.V., Waridel P., Quadroni M.;
Submitted (MAR-2009) to UniProtKB.
[12]
PHOSPHORYLATION AT SER-1469, AND MUTAGENESIS OF SER-1469.
PubMed=10942766; DOI=10.1074/jbc.M005179200;
Escargueil A.E., Plisov S.Y., Filhol O., Cochet C., Larsen A.K.;
"Mitotic phosphorylation of DNA topoisomerase II alpha by protein
kinase CK2 creates the MPM-2 phosphoepitope on Ser-1469.";
J. Biol. Chem. 275:34710-34718(2000).
[13]
NUCLEAR EXPORT SIGNAL.
PubMed=12821127; DOI=10.1016/S0006-291X(03)01077-5;
Mirski S.E., Bielawski J.C., Cole S.P.;
"Identification of functional nuclear export sequences in human
topoisomerase IIalpha and beta.";
Biochem. Biophys. Res. Commun. 306:905-911(2003).
[14]
INTERACTION WITH DHX9.
PubMed=12711669; DOI=10.1093/nar/gkg328;
Zhou K., Choe K.-T., Zaidi Z., Wang Q., Mathews M.B., Lee C.-G.;
"RNA helicase A interacts with dsDNA and topoisomerase IIalpha.";
Nucleic Acids Res. 31:2253-2260(2003).
[15]
INTERACTION WITH COPS5.
PubMed=15126503; DOI=10.1074/jbc.M401411200;
Yun J., Tomida A., Andoh T., Tsuruo T.;
"Interaction between glucose-regulated destruction domain of DNA
topoisomerase IIalpha and MPN domain of Jab1/CSN5.";
J. Biol. Chem. 279:31296-31303(2004).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-1106; SER-1213;
SER-1247; SER-1332; SER-1337; THR-1343; SER-1351; SER-1354; SER-1374;
SER-1377 AND SER-1525, 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).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1213; SER-1374; SER-1377
AND SER-1525, 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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1247, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[19]
PHOSPHORYLATION AT THR-1343.
PubMed=18062778; DOI=10.1042/BJ20071394;
Iida M., Matsuda M., Komatani H.;
"Plk3 phosphorylates topoisomerase IIalpha at Thr(1342), a site that
is not recognized by Plk1.";
Biochem. J. 411:27-32(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1504, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-1213; SER-1247;
SER-1332; SER-1337 AND SER-1377, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[22]
FUNCTION, AND INTERACTION WITH SETMAR.
PubMed=18790802; DOI=10.1093/nar/gkn560;
Williamson E.A., Rasila K.K., Corwin L.K., Wray J., Beck B.D.,
Severns V., Mobarak C., Lee S.H., Nickoloff J.A., Hromas R.;
"The SET and transposase domain protein Metnase enhances chromosome
decatenation: regulation by automethylation.";
Nucleic Acids Res. 36:5822-5831(2008).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1106; SER-1213;
SER-1332; SER-1337; THR-1343; SER-1351; SER-1392; SER-1393; SER-1449;
SER-1469; THR-1470; SER-1471; SER-1474 AND SER-1525, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[25]
CATALYTIC ACTIVITY, AND COFACTOR.
PubMed=19222228; DOI=10.1021/bi8023256;
Deweese J.E., Burch A.M., Burgin A.B., Osheroff N.;
"Use of divalent metal ions in the DNA cleavage reaction of human type
II topoisomerases.";
Biochemistry 48:1862-1869(2009).
[26]
MUTAGENESIS OF GLU-461; ASP-541; ASP-543 AND ASP-545, PUTATIVE
METAL-BINDING SITES, CATALYTIC ACTIVITY, AND COFACTOR.
PubMed=19697956; DOI=10.1021/bi900875c;
Deweese J.E., Guengerich F.P., Burgin A.B., Osheroff N.;
"Metal ion interactions in the DNA cleavage/ligation active site of
human topoisomerase IIalpha.";
Biochemistry 48:8940-8947(2009).
[27]
PHOSPHORYLATION AT SER-1106 BY CSNK1D/CK1.
PubMed=19043076; DOI=10.1093/nar/gkn934;
Grozav A.G., Chikamori K., Kozuki T., Grabowski D.R., Bukowski R.M.,
Willard B., Kinter M., Andersen A.H., Ganapathi R., Ganapathi M.K.;
"Casein kinase I delta/epsilon phosphorylates topoisomerase IIalpha at
serine-1106 and modulates DNA cleavage activity.";
Nucleic Acids Res. 37:382-392(2009).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1247; SER-1374;
SER-1387; SER-1393; SER-1504 AND SER-1525, 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).
[29]
INTERACTION WITH SETMAR.
PubMed=20457750; DOI=10.1093/nar/gkq339;
De Haro L.P., Wray J., Williamson E.A., Durant S.T., Corwin L.,
Gentry A.C., Osheroff N., Lee S.H., Hromas R., Nickoloff J.A.;
"Metnase promotes restart and repair of stalled and collapsed
replication forks.";
Nucleic Acids Res. 38:5681-5691(2010).
[30]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-4; THR-282; SER-1106; THR-1205; SER-1213;
SER-1247; SER-1332; SER-1337; THR-1343; SER-1351; SER-1354; SER-1374;
SER-1377; SER-1471; SER-1474; SER-1495; SER-1504 AND SER-1525, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[31]
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).
[32]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-4; SER-1106; SER-1213; SER-1247; SER-1295;
SER-1297; SER-1299; SER-1302; SER-1332; SER-1337; THR-1343; SER-1351;
SER-1354; SER-1374; SER-1377; SER-1469; THR-1470; SER-1471; SER-1474;
SER-1476 AND SER-1525, 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).
[33]
MUTAGENESIS OF 342-LYS--LYS-344.
PubMed=23022727; DOI=10.1038/nsmb.2388;
Schmidt B.H., Osheroff N., Berger J.M.;
"Structure of a topoisomerase II-DNA-nucleotide complex reveals a new
control mechanism for ATPase activity.";
Nat. Struct. Mol. Biol. 19:1147-1154(2012).
[34]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RECQL5.
PubMed=22013166; DOI=10.1093/nar/gkr844;
Ramamoorthy M., Tadokoro T., Rybanska I., Ghosh A.K., Wersto R.,
May A., Kulikowicz T., Sykora P., Croteau D.L., Bohr V.A.;
"RECQL5 cooperates with Topoisomerase II alpha in DNA decatenation and
cell cycle progression.";
Nucleic Acids Res. 40:1621-1635(2012).
[35]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[36]
FUNCTION, MUTAGENESIS OF GLU-461; ASP-541 AND ASP-543, AND COFACTOR.
PubMed=22323612; DOI=10.1073/pnas.1115704109;
Lee S., Jung S.R., Heo K., Byl J.A., Deweese J.E., Osheroff N.,
Hohng S.;
"DNA cleavage and opening reactions of human topoisomerase IIalpha are
regulated via Mg2+-mediated dynamic bending of gate-DNA.";
Proc. Natl. Acad. Sci. U.S.A. 109:2925-2930(2012).
[37]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-1106; SER-1213;
THR-1244; SER-1247; SER-1374; SER-1377; SER-1391; SER-1449; SER-1469;
SER-1471; SER-1474; SER-1495 AND SER-1504, 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).
[38]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1228; LYS-1240; LYS-1385 AND
LYS-1492, 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).
[39]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1240, 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).
[40]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-639; LYS-662; LYS-676;
LYS-1075; LYS-1196; LYS-1228; LYS-1240; LYS-1385 AND LYS-1442, 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).
[41]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1228 AND LYS-1240, 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).
[42]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-17; LYS-156; LYS-157;
LYS-261; LYS-352; LYS-386; LYS-397; LYS-416; LYS-418; LYS-425;
LYS-440; LYS-466; LYS-480; LYS-529; LYS-584; LYS-599; LYS-614;
LYS-622; LYS-625; LYS-632; LYS-639; LYS-655; LYS-662; LYS-676;
LYS-1075; LYS-1114; LYS-1196; LYS-1204; LYS-1228; LYS-1240; LYS-1259;
LYS-1276; LYS-1283; LYS-1286; LYS-1363; LYS-1367; LYS-1373; LYS-1385;
LYS-1422; LYS-1442; LYS-1454; LYS-1459; LYS-1484 AND LYS-1492, 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).
[43]
X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 29-428 IN COMPLEX WITH ADP,
AND X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 29-428 IN COMPLEX WITH
AMPPNP.
PubMed=16100112; DOI=10.1074/jbc.M506520200;
Wei H., Ruthenburg A.J., Bechis S.K., Verdine G.L.;
"Nucleotide-dependent domain movement in the ATPase domain of a human
type IIA DNA topoisomerase.";
J. Biol. Chem. 280:37041-37047(2005).
[44]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 431-1193 IN COMPLEX WITH DNA
AND MAGNESIUM ION, SUBUNIT, AND COFACTOR.
PubMed=22841979; DOI=10.1016/j.jmb.2012.07.014;
Wendorff T.J., Schmidt B.H., Heslop P., Austin C.A., Berger J.M.;
"The structure of DNA-bound human topoisomerase II alpha:
conformational mechanisms for coordinating inter-subunit interactions
with DNA cleavage.";
J. Mol. Biol. 424:109-124(2012).
[45]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 29-428 IN COMPLEX WITH ADP
AND ATP ANALOGS, AND DOMAIN.
PubMed=25202966; DOI=10.1371/journal.pone.0107289;
Stanger F.V., Dehio C., Schirmer T.;
"Structure of the N-terminal Gyrase B fragment in complex with ADPPi
reveals rigid-body motion induced by ATP hydrolysis.";
PLoS ONE 9:E107289-E107289(2014).
[46]
VARIANT AMSACRINE-RESISTANT LYS-487.
PubMed=1651812;
Hinds M., Deisseroth K., Mayes J., Altschuler E., Jansen R.,
Ledley F.D., Zwelling L.A.;
"Identification of a point mutation in the topoisomerase II gene from
a human leukemia cell line containing an amsacrine-resistant form of
topoisomerase II.";
Cancer Res. 51:4729-4731(1991).
[47]
VARIANT TENIPOSIDE-RESISTANT GLN-450.
PubMed=1652758; DOI=10.1073/pnas.88.17.7654;
Bugg B.Y., Danks M.K., Beck W.T., Suttle D.P.;
"Expression of a mutant DNA topoisomerase II in CCRF-CEM human
leukemic cells selected for resistance to teniposide.";
Proc. Natl. Acad. Sci. U.S.A. 88:7654-7658(1991).
-!- FUNCTION: Control of topological states of DNA by transient
breakage and subsequent rejoining of DNA strands. Topoisomerase II
makes double-strand breaks. Essential during mitosis and meiosis
for proper segregation of daughter chromosomes. May play a role in
regulating the period length of ARNTL/BMAL1 transcriptional
oscillation (By similarity). {ECO:0000250|UniProtKB:Q01320,
ECO:0000269|PubMed:18790802, ECO:0000269|PubMed:22013166,
ECO:0000269|PubMed:22323612}.
-!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining
of double-stranded DNA. {ECO:0000255|PROSITE-ProRule:PRU00995,
ECO:0000269|PubMed:19222228, ECO:0000269|PubMed:19697956}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000305|PubMed:19222228,
ECO:0000305|PubMed:19697956, ECO:0000305|PubMed:22323612,
ECO:0000305|PubMed:22841979};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000305|PubMed:19222228,
ECO:0000305|PubMed:19697956, ECO:0000305|PubMed:22323612,
ECO:0000305|PubMed:22841979};
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000305|PubMed:19222228,
ECO:0000305|PubMed:19697956, ECO:0000305|PubMed:22323612,
ECO:0000305|PubMed:22841979};
Note=Binds two Mg(2+) per subunit. The magnesium ions form salt
bridges with both the protein and the DNA. Can also accept other
divalent metal cations, such as Mn(2+) or Ca(2+).
{ECO:0000305|PubMed:19222228, ECO:0000305|PubMed:19697956,
ECO:0000305|PubMed:22323612, ECO:0000305|PubMed:22841979};
-!- ENZYME REGULATION: Specifically inhibited by the intercalating
agent amsacrine.
-!- SUBUNIT: Homodimer. Interacts with COPS5. Interacts with RECQL5;
this stimulates DNA decatenation. Interacts with SETMAR;
stimulates the topoisomerase activity (PubMed:18790802,
PubMed:20457750). Interacts with DHX9; this interaction occurs in
a E2 enzyme UBE2I- and RNA-dependent manner, negatively regulates
DHX9-mediated double-stranded DNA and RNA duplex helicase activity
and stimulates TOP2A-mediated supercoiled DNA relaxation activity
(PubMed:12711669). Interacts with HNRNPU (via C-terminus); this
interaction protects the topoisomerase TOP2A from degradation and
positively regulates the relaxation of supercoiled DNA in a RNA-
dependent manner (By similarity). {ECO:0000250|UniProtKB:P41516,
ECO:0000269|PubMed:12711669, ECO:0000269|PubMed:15126503,
ECO:0000269|PubMed:16100112, ECO:0000269|PubMed:20457750,
ECO:0000269|PubMed:22013166, ECO:0000269|PubMed:22841979}.
-!- INTERACTION:
O14497-1:ARID1A; NbExp=2; IntAct=EBI-539628, EBI-15956509;
P38398:BRCA1; NbExp=3; IntAct=EBI-539628, EBI-349905;
P35222:CTNNB1; NbExp=5; IntAct=EBI-539628, EBI-491549;
Q05655:PRKCD; NbExp=10; IntAct=EBI-539628, EBI-704279;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22013166}.
Nucleus, nucleoplasm {ECO:0000269|PubMed:22013166}. Note=Generally
located in the nucleoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=P11388-1; Sequence=Displayed;
Name=2;
IsoId=P11388-2; Sequence=VSP_006531;
Name=3;
IsoId=P11388-3; Sequence=VSP_006529;
Name=4;
IsoId=P11388-4; Sequence=VSP_006530;
-!- DOMAIN: The N-terminus has several structural domains; the ATPase
domain (about residues 1-265), the transducer domain (about 266-
428) and the toprim domain (455-572) (PubMed:25202966). Comparing
different structures shows ATP hydrolysis induces domain shifts in
the N-terminus that are probably part of the mechanism of DNA
cleavage and rejoining (PubMed:25202966).
{ECO:0000250|UniProtKB:P0AES6, ECO:0000269|PubMed:25202966}.
-!- PTM: Phosphorylation has no effect on catalytic activity. However,
phosphorylation at Ser-1106 by CSNK1D/CK1 promotes DNA cleavable
complex formation. {ECO:0000269|PubMed:10942766,
ECO:0000269|PubMed:18062778, ECO:0000269|PubMed:19043076,
ECO:0000269|Ref.11}.
-!- MISCELLANEOUS: Eukaryotic topoisomerase I and II can relax both
negative and positive supercoils, whereas prokaryotic enzymes
relax only negative supercoils.
-!- SIMILARITY: Belongs to the type II topoisomerase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; J04088; AAA61209.1; -; mRNA.
EMBL; AF071747; AAC77388.1; -; Genomic_DNA.
EMBL; AF071738; AAC77388.1; JOINED; Genomic_DNA.
EMBL; AF071739; AAC77388.1; JOINED; Genomic_DNA.
EMBL; AF071740; AAC77388.1; JOINED; Genomic_DNA.
EMBL; AF071741; AAC77388.1; JOINED; Genomic_DNA.
EMBL; AF071742; AAC77388.1; JOINED; Genomic_DNA.
EMBL; AF071743; AAC77388.1; JOINED; Genomic_DNA.
EMBL; AF071744; AAC77388.1; JOINED; Genomic_DNA.
EMBL; AF071745; AAC77388.1; JOINED; Genomic_DNA.
EMBL; AF071746; AAC77388.1; JOINED; Genomic_DNA.
EMBL; AJ011741; CAA09762.1; -; Genomic_DNA.
EMBL; AJ011742; CAA09762.1; JOINED; Genomic_DNA.
EMBL; AJ011743; CAA09762.1; JOINED; Genomic_DNA.
EMBL; AJ011744; CAA09762.1; JOINED; Genomic_DNA.
EMBL; AJ011745; CAA09762.1; JOINED; Genomic_DNA.
EMBL; AJ011746; CAA09762.1; JOINED; Genomic_DNA.
EMBL; AJ011747; CAA09762.1; JOINED; Genomic_DNA.
EMBL; AJ011748; CAA09762.1; JOINED; Genomic_DNA.
EMBL; AJ011749; CAA09762.1; JOINED; Genomic_DNA.
EMBL; AJ011750; CAA09762.1; JOINED; Genomic_DNA.
EMBL; AJ011751; CAA09762.1; JOINED; Genomic_DNA.
EMBL; AJ011752; CAA09762.1; JOINED; Genomic_DNA.
EMBL; AJ011753; CAA09762.1; JOINED; Genomic_DNA.
EMBL; AJ011754; CAA09762.1; JOINED; Genomic_DNA.
EMBL; AJ011755; CAA09762.1; JOINED; Genomic_DNA.
EMBL; AJ011756; CAA09762.1; JOINED; Genomic_DNA.
EMBL; AJ011757; CAA09762.1; JOINED; Genomic_DNA.
EMBL; AJ011758; CAA09762.1; JOINED; Genomic_DNA.
EMBL; AC080112; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF285157; AAG13403.1; -; mRNA.
EMBL; AF285158; AAG13404.1; -; mRNA.
EMBL; CH471152; EAW60663.1; -; Genomic_DNA.
EMBL; BC140791; AAI40792.1; -; mRNA.
EMBL; AF285159; AAG13405.1; -; mRNA.
EMBL; AF069522; AAC23518.1; -; Genomic_DNA.
EMBL; AF064590; AAC16736.1; -; Genomic_DNA.
CCDS; CCDS45672.1; -. [P11388-1]
PIR; A40493; A40493.
RefSeq; NP_001058.2; NM_001067.3. [P11388-1]
UniGene; Hs.156346; -.
PDB; 1LWZ; Model; -; A=431-1200.
PDB; 1ZXM; X-ray; 1.87 A; A/B=29-428.
PDB; 1ZXN; X-ray; 2.51 A; A/B/C/D=29-428.
PDB; 4FM9; X-ray; 2.90 A; A=431-1193.
PDB; 4R1F; X-ray; 2.51 A; A/B/C/D=29-428.
PDB; 5GWK; X-ray; 3.15 A; A/B=429-1188.
PDBsum; 1LWZ; -.
PDBsum; 1ZXM; -.
PDBsum; 1ZXN; -.
PDBsum; 4FM9; -.
PDBsum; 4R1F; -.
PDBsum; 5GWK; -.
ProteinModelPortal; P11388; -.
SMR; P11388; -.
BioGrid; 113006; 107.
CORUM; P11388; -.
DIP; DIP-33887N; -.
IntAct; P11388; 48.
MINT; MINT-98770; -.
STRING; 9606.ENSP00000411532; -.
BindingDB; P11388; -.
ChEMBL; CHEMBL1806; -.
DrugBank; DB05022; Amonafide.
DrugBank; DB06263; Amrubicin.
DrugBank; DB00276; Amsacrine.
DrugBank; DB04975; Banoxantrone.
DrugBank; DB00537; Ciprofloxacin.
DrugBank; DB00970; Dactinomycin.
DrugBank; DB00694; Daunorubicin.
DrugBank; DB00380; Dexrazoxane.
DrugBank; DB00997; Doxorubicin.
DrugBank; DB05129; Elsamitrucin.
DrugBank; DB00467; Enoxacin.
DrugBank; DB00445; Epirubicin.
DrugBank; DB00773; Etoposide.
DrugBank; DB09047; Finafloxacin.
DrugBank; DB04576; Fleroxacin.
DrugBank; DB01645; Genistein.
DrugBank; DB01177; Idarubicin.
DrugBank; DB01137; Levofloxacin.
DrugBank; DB00978; Lomefloxacin.
DrugBank; DB04967; Lucanthone.
DrugBank; DB01204; Mitoxantrone.
DrugBank; DB00218; Moxifloxacin.
DrugBank; DB01059; Norfloxacin.
DrugBank; DB01165; Ofloxacin.
DrugBank; DB00487; Pefloxacin.
DrugBank; DB01179; Podofilox.
DrugBank; DB05920; RTA 744.
DrugBank; DB04978; SP1049C.
DrugBank; DB01208; Sparfloxacin.
DrugBank; DB00444; Teniposide.
DrugBank; DB00685; Trovafloxacin.
DrugBank; DB00385; Valrubicin.
DrugBank; DB06042; ZEN-012.
GuidetoPHARMACOLOGY; 2637; -.
iPTMnet; P11388; -.
PhosphoSitePlus; P11388; -.
SwissPalm; P11388; -.
BioMuta; TOP2A; -.
DMDM; 13959709; -.
UCD-2DPAGE; P11388; -.
EPD; P11388; -.
MaxQB; P11388; -.
PaxDb; P11388; -.
PeptideAtlas; P11388; -.
PRIDE; P11388; -.
Ensembl; ENST00000423485; ENSP00000411532; ENSG00000131747. [P11388-1]
GeneID; 7153; -.
KEGG; hsa:7153; -.
UCSC; uc002huq.4; human. [P11388-1]
CTD; 7153; -.
DisGeNET; 7153; -.
EuPathDB; HostDB:ENSG00000131747.14; -.
GeneCards; TOP2A; -.
H-InvDB; HIX0013797; -.
HGNC; HGNC:11989; TOP2A.
HPA; CAB002448; -.
HPA; HPA006458; -.
HPA; HPA026773; -.
MalaCards; TOP2A; -.
MIM; 126430; gene.
neXtProt; NX_P11388; -.
OpenTargets; ENSG00000131747; -.
Orphanet; 635; Neuroblastoma.
PharmGKB; PA354; -.
eggNOG; KOG0355; Eukaryota.
eggNOG; COG0187; LUCA.
eggNOG; COG0188; LUCA.
GeneTree; ENSGT00390000016222; -.
HOVERGEN; HBG052998; -.
InParanoid; P11388; -.
KO; K03164; -.
OMA; DNMGRAG; -.
OrthoDB; EOG091G00U2; -.
PhylomeDB; P11388; -.
TreeFam; TF105282; -.
BRENDA; 5.99.1.3; 2681.
Reactome; R-HSA-1362277; Transcription of E2F targets under negative control by DREAM complex.
Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins.
SignaLink; P11388; -.
SIGNOR; P11388; -.
EvolutionaryTrace; P11388; -.
GeneWiki; TOP2A; -.
GenomeRNAi; 7153; -.
PRO; PR:P11388; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000131747; -.
CleanEx; HS_TOP2A; -.
ExpressionAtlas; P11388; baseline and differential.
Genevisible; P11388; HS.
GO; GO:0000793; C:condensed chromosome; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0009330; C:DNA topoisomerase complex (ATP-hydrolyzing); IDA:UniProtKB.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0008301; F:DNA binding, bending; IDA:UniProtKB.
GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IDA:UniProtKB.
GO; GO:0008094; F:DNA-dependent ATPase activity; IDA:UniProtKB.
GO; GO:0008144; F:drug binding; IDA:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0005080; F:protein kinase C binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0043130; F:ubiquitin binding; IMP:UniProtKB.
GO; GO:0030263; P:apoptotic chromosome condensation; IDA:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
GO; GO:0006266; P:DNA ligation; IDA:UniProtKB.
GO; GO:0006265; P:DNA topological change; IDA:UniProtKB.
GO; GO:0040016; P:embryonic cleavage; IEA:Ensembl.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
GO; GO:0044774; P:mitotic DNA integrity checkpoint; IBA:GO_Central.
GO; GO:1905463; P:negative regulation of DNA duplex unwinding; IMP:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0045870; P:positive regulation of single stranded viral RNA replication via double stranded DNA intermediate; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0045070; P:positive regulation of viral genome replication; IMP:UniProtKB.
GO; GO:0016925; P:protein sumoylation; TAS:Reactome.
GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0000819; P:sister chromatid segregation; IBA:GO_Central.
CDD; cd00075; HATPase_c; 1.
CDD; cd03365; TOPRIM_TopoIIA; 1.
Gene3D; 1.10.268.10; -; 1.
Gene3D; 3.30.1360.40; -; 1.
Gene3D; 3.30.230.10; -; 1.
Gene3D; 3.30.565.10; -; 1.
Gene3D; 3.40.50.670; -; 2.
Gene3D; 3.90.199.10; -; 1.
InterPro; IPR024946; Arg_repress-like_C.
InterPro; IPR012542; DTHCT.
InterPro; IPR003594; HATPase_C.
InterPro; IPR036890; HATPase_C_sf.
InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
InterPro; IPR001241; Topo_IIA.
InterPro; IPR013760; Topo_IIA-like_dom_sf.
InterPro; IPR002205; Topo_IIA_A/C.
InterPro; IPR013758; Topo_IIA_A/C_ab.
InterPro; IPR013757; Topo_IIA_A_a_sf.
InterPro; IPR013759; Topo_IIA_B_C.
InterPro; IPR013506; Topo_IIA_bsu_dom2.
InterPro; IPR018522; TopoIIA_CS.
InterPro; IPR031660; TOPRIM_C.
InterPro; IPR006171; TOPRIM_domain.
InterPro; IPR034157; TOPRIM_TopoII.
PANTHER; PTHR10169; PTHR10169; 1.
Pfam; PF00204; DNA_gyraseB; 1.
Pfam; PF00521; DNA_topoisoIV; 1.
Pfam; PF08070; DTHCT; 1.
Pfam; PF02518; HATPase_c; 1.
Pfam; PF01751; Toprim; 1.
Pfam; PF16898; TOPRIM_C; 1.
SMART; SM00433; TOP2c; 1.
SMART; SM00434; TOP4c; 1.
SUPFAM; SSF54211; SSF54211; 1.
SUPFAM; SSF55874; SSF55874; 1.
SUPFAM; SSF56719; SSF56719; 1.
PROSITE; PS00177; TOPOISOMERASE_II; 1.
PROSITE; PS50880; TOPRIM; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Biological rhythms; Complete proteome; Cytoplasm;
Direct protein sequencing; DNA-binding; Isomerase; Isopeptide bond;
Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Topoisomerase; Ubl conjugation.
CHAIN 1 1531 DNA topoisomerase 2-alpha.
/FTId=PRO_0000145363.
DOMAIN 455 572 Toprim. {ECO:0000255|PROSITE-
ProRule:PRU00995}.
NP_BIND 148 150 ATP. {ECO:0000269|PubMed:16100112,
ECO:0000269|PubMed:25202966}.
NP_BIND 161 168 ATP. {ECO:0000269|PubMed:16100112,
ECO:0000269|PubMed:25202966}.
NP_BIND 376 378 ATP. {ECO:0000269|PubMed:16100112,
ECO:0000305|PubMed:25202966}.
REGION 342 344 Interaction with DNA.
{ECO:0000305|PubMed:23022727}.
REGION 990 999 Interaction with DNA.
{ECO:0000269|PubMed:22841979}.
MOTIF 1018 1028 Nuclear export signal.
ACT_SITE 805 805 O-(5'-phospho-DNA)-tyrosine intermediate.
{ECO:0000250|UniProtKB:P06786}.
METAL 461 461 Magnesium 1; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00995}.
METAL 541 541 Magnesium 1; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00995}.
METAL 541 541 Magnesium 2.
{ECO:0000269|PubMed:22841979}.
METAL 543 543 Magnesium 2.
{ECO:0000269|PubMed:22841979}.
BINDING 91 91 ATP. {ECO:0000269|PubMed:16100112,
ECO:0000269|PubMed:25202966}.
BINDING 120 120 ATP. {ECO:0000269|PubMed:16100112,
ECO:0000269|PubMed:25202966}.
SITE 489 489 Interaction with DNA.
{ECO:0000255|PROSITE-ProRule:PRU00995}.
SITE 492 492 Interaction with DNA.
{ECO:0000269|PubMed:22841979}.
SITE 661 661 Interaction with DNA.
{ECO:0000269|PubMed:22841979}.
SITE 662 662 Interaction with DNA.
{ECO:0000269|PubMed:22841979}.
SITE 723 723 Interaction with DNA.
{ECO:0000269|PubMed:22841979}.
SITE 757 757 Interaction with DNA.
{ECO:0000269|PubMed:22841979}.
SITE 763 763 Interaction with DNA.
{ECO:0000269|PubMed:22841979}.
SITE 804 804 Transition state stabilizer.
{ECO:0000250}.
SITE 856 856 Important for DNA bending; intercalates
between base pairs of target DNA.
{ECO:0000250}.
SITE 931 931 Interaction with DNA.
{ECO:0000269|PubMed:22841979}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.10}.
MOD_RES 4 4 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 282 282 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1106 1106 Phosphoserine; by CK1.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:19043076,
ECO:0000269|Ref.11}.
MOD_RES 1205 1205 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1213 1213 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1244 1244 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1247 1247 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1295 1295 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1297 1297 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1299 1299 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1302 1302 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1327 1327 Phosphothreonine.
{ECO:0000250|UniProtKB:Q01320}.
MOD_RES 1332 1332 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 1337 1337 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 1343 1343 Phosphothreonine; by PLK3.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000269|PubMed:18062778}.
MOD_RES 1351 1351 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 1354 1354 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 1374 1374 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1377 1377 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1387 1387 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 1391 1391 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1392 1392 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1393 1393 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 1422 1422 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q01320}.
MOD_RES 1442 1442 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q01320}.
MOD_RES 1449 1449 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1469 1469 Phosphoserine; by CK2.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:10942766}.
MOD_RES 1470 1470 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
MOD_RES 1471 1471 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1474 1474 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1476 1476 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1495 1495 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1504 1504 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1525 1525 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
CROSSLNK 17 17 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 156 156 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 157 157 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 261 261 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 352 352 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 386 386 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 397 397 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 416 416 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 418 418 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 425 425 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 440 440 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 466 466 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 480 480 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 529 529 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 584 584 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 599 599 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 614 614 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 622 622 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 625 625 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 632 632 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 639 639 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 655 655 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 662 662 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 676 676 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 1075 1075 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 1114 1114 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1196 1196 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 1204 1204 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1228 1228 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 1240 1240 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 1240 1240 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 1259 1259 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1276 1276 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1283 1283 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1286 1286 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1363 1363 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1367 1367 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1373 1373 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1385 1385 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 1422 1422 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 1442 1442 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 1454 1454 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1459 1459 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1484 1484 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1492 1492 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 321 321 K -> KSSKYWSSRKSKQHILLNFFVLFKFINDAFFGICPF
K (in isoform 3). {ECO:0000303|Ref.8}.
/FTId=VSP_006529.
VAR_SEQ 355 355 Q -> QRELCNGAILAHCNLRLMGSSDSPASASRVAGIAGG
CHHTQLIFVFLVETGFHHVGQAGLERLTSGDPPASASQSSG
ITDVK (in isoform 4).
{ECO:0000303|Ref.8}.
/FTId=VSP_006530.
VAR_SEQ 401 401 A -> AHLYSRFLIDPFFPNMIPNMIFSFSKA (in
isoform 2). {ECO:0000303|Ref.8}.
/FTId=VSP_006531.
VARIANT 450 450 R -> Q (in teniposide (VM-26) resistant
cells; dbSNP:rs746765101).
{ECO:0000269|PubMed:1652758}.
/FTId=VAR_007532.
VARIANT 487 487 R -> K (in amsacrine resistant cells;
dbSNP:rs267607133).
{ECO:0000269|PubMed:1651812}.
/FTId=VAR_007533.
VARIANT 1324 1324 T -> K (in dbSNP:rs28969502).
/FTId=VAR_029245.
VARIANT 1386 1386 G -> D (in dbSNP:rs34300454).
/FTId=VAR_052594.
VARIANT 1515 1515 A -> S (in dbSNP:rs11540720).
/FTId=VAR_052595.
MUTAGEN 342 344 KKK->AAA: Reduced enzyme activity;
abolishes stimulation of ATPase activity
upon DNA binding.
{ECO:0000269|PubMed:23022727}.
MUTAGEN 342 344 KKK->EEE: Strongly reduced enzyme
activity; abolishes stimulation of ATPase
activity upon DNA binding.
{ECO:0000269|PubMed:23022727}.
MUTAGEN 461 461 E->A,C: Impairs bending of target DNA.
Strongly reduced DNA cleavage.
{ECO:0000269|PubMed:19697956,
ECO:0000269|PubMed:22323612}.
MUTAGEN 541 541 D->A,C: Impairs bending of target DNA.
Strongly reduced DNA cleavage.
{ECO:0000269|PubMed:19697956,
ECO:0000269|PubMed:22323612}.
MUTAGEN 543 543 D->A,C: Impairs bending of target DNA.
Strongly reduced DNA cleavage.
{ECO:0000269|PubMed:19697956,
ECO:0000269|PubMed:22323612}.
MUTAGEN 545 545 D->A,C: Strongly reduced DNA cleavage.
{ECO:0000269|PubMed:19697956}.
MUTAGEN 1469 1469 S->A: Abolishes binding to the antibody
MPM2. {ECO:0000269|PubMed:10942766}.
CONFLICT 152 152 D -> H (in Ref. 4; CAA09762).
{ECO:0000305}.
CONFLICT 180 180 E -> Q (in Ref. 4; CAA09762).
{ECO:0000305}.
CONFLICT 327 327 D -> H (in Ref. 4; CAA09762).
{ECO:0000305}.
CONFLICT 1022 1022 F -> L (in Ref. 4; CAA09762).
{ECO:0000305}.
CONFLICT 1274 1274 T -> S (in Ref. 4; CAA09762).
{ECO:0000305}.
CONFLICT 1295 1295 S -> P (in Ref. 1; AAA61209).
{ECO:0000305}.
HELIX 30 33 {ECO:0000244|PDB:1ZXM}.
STRAND 34 36 {ECO:0000244|PDB:1ZXM}.
HELIX 39 45 {ECO:0000244|PDB:1ZXM}.
HELIX 48 51 {ECO:0000244|PDB:1ZXM}.
STRAND 57 65 {ECO:0000244|PDB:1ZXM}.
TURN 66 68 {ECO:0000244|PDB:1ZXM}.
STRAND 69 77 {ECO:0000244|PDB:1ZXM}.
HELIX 79 98 {ECO:0000244|PDB:1ZXM}.
STRAND 104 110 {ECO:0000244|PDB:1ZXM}.
TURN 111 114 {ECO:0000244|PDB:1ZXM}.
STRAND 115 123 {ECO:0000244|PDB:1ZXM}.
STRAND 128 130 {ECO:0000244|PDB:1ZXM}.
TURN 131 134 {ECO:0000244|PDB:1ZXM}.
HELIX 137 143 {ECO:0000244|PDB:1ZXM}.
STRAND 144 149 {ECO:0000244|PDB:1ZXM}.
HELIX 153 155 {ECO:0000244|PDB:1ZXM}.
HELIX 166 172 {ECO:0000244|PDB:1ZXM}.
STRAND 174 183 {ECO:0000244|PDB:1ZXM}.
TURN 184 187 {ECO:0000244|PDB:1ZXM}.
STRAND 188 195 {ECO:0000244|PDB:1ZXM}.
TURN 196 199 {ECO:0000244|PDB:1ZXM}.
STRAND 205 208 {ECO:0000244|PDB:1ZXM}.
STRAND 214 221 {ECO:0000244|PDB:1ZXM}.
HELIX 223 226 {ECO:0000244|PDB:1ZXM}.
HELIX 233 249 {ECO:0000244|PDB:1ZXM}.
STRAND 250 252 {ECO:0000244|PDB:1ZXM}.
STRAND 254 257 {ECO:0000244|PDB:1ZXM}.
HELIX 267 275 {ECO:0000244|PDB:1ZXM}.
STRAND 281 285 {ECO:0000244|PDB:1ZXM}.
STRAND 289 294 {ECO:0000244|PDB:1ZXM}.
STRAND 297 303 {ECO:0000244|PDB:1ZXM}.
STRAND 305 307 {ECO:0000244|PDB:1ZXM}.
STRAND 309 314 {ECO:0000244|PDB:1ZXM}.
HELIX 324 341 {ECO:0000244|PDB:1ZXM}.
STRAND 346 348 {ECO:0000244|PDB:1ZXN}.
HELIX 353 357 {ECO:0000244|PDB:1ZXM}.
STRAND 360 366 {ECO:0000244|PDB:1ZXM}.
STRAND 373 375 {ECO:0000244|PDB:1ZXM}.
HELIX 385 387 {ECO:0000244|PDB:1ZXM}.
STRAND 388 390 {ECO:0000244|PDB:1ZXM}.
HELIX 396 402 {ECO:0000244|PDB:1ZXM}.
HELIX 407 410 {ECO:0000244|PDB:1ZXM}.
HELIX 411 415 {ECO:0000244|PDB:1ZXN}.
STRAND 419 421 {ECO:0000244|PDB:1ZXN}.
STRAND 423 425 {ECO:0000244|PDB:1ZXN}.
TURN 445 448 {ECO:0000244|PDB:4FM9}.
HELIX 452 454 {ECO:0000244|PDB:4FM9}.
STRAND 456 462 {ECO:0000244|PDB:4FM9}.
HELIX 463 476 {ECO:0000244|PDB:4FM9}.
STRAND 478 486 {ECO:0000244|PDB:4FM9}.
HELIX 498 503 {ECO:0000244|PDB:4FM9}.
HELIX 505 514 {ECO:0000244|PDB:4FM9}.
STRAND 518 520 {ECO:0000244|PDB:4FM9}.
HELIX 525 530 {ECO:0000244|PDB:4FM9}.
STRAND 534 539 {ECO:0000244|PDB:4FM9}.
HELIX 544 560 {ECO:0000244|PDB:4FM9}.
HELIX 562 566 {ECO:0000244|PDB:4FM9}.
STRAND 570 573 {ECO:0000244|PDB:4FM9}.
STRAND 577 581 {ECO:0000244|PDB:4FM9}.
STRAND 586 590 {ECO:0000244|PDB:4FM9}.
HELIX 592 601 {ECO:0000244|PDB:4FM9}.
STRAND 607 612 {ECO:0000244|PDB:4FM9}.
HELIX 616 618 {ECO:0000244|PDB:4FM9}.
HELIX 621 629 {ECO:0000244|PDB:4FM9}.
HELIX 631 634 {ECO:0000244|PDB:4FM9}.
STRAND 635 639 {ECO:0000244|PDB:4FM9}.
HELIX 644 653 {ECO:0000244|PDB:4FM9}.
HELIX 658 678 {ECO:0000244|PDB:4FM9}.
STRAND 685 688 {ECO:0000244|PDB:4FM9}.
STRAND 691 694 {ECO:0000244|PDB:4FM9}.
HELIX 695 701 {ECO:0000244|PDB:4FM9}.
HELIX 703 714 {ECO:0000244|PDB:4FM9}.
TURN 718 720 {ECO:0000244|PDB:4FM9}.
HELIX 724 735 {ECO:0000244|PDB:4FM9}.
HELIX 744 754 {ECO:0000244|PDB:4FM9}.
HELIX 762 772 {ECO:0000244|PDB:4FM9}.
TURN 793 799 {ECO:0000244|PDB:4FM9}.
TURN 803 805 {ECO:0000244|PDB:4FM9}.
HELIX 812 817 {ECO:0000244|PDB:4FM9}.
HELIX 822 824 {ECO:0000244|PDB:4FM9}.
HELIX 831 833 {ECO:0000244|PDB:4FM9}.
STRAND 834 839 {ECO:0000244|PDB:5GWK}.
TURN 848 850 {ECO:0000244|PDB:4FM9}.
STRAND 853 856 {ECO:0000244|PDB:4FM9}.
STRAND 861 864 {ECO:0000244|PDB:4FM9}.
HELIX 869 881 {ECO:0000244|PDB:4FM9}.
STRAND 897 903 {ECO:0000244|PDB:4FM9}.
STRAND 906 910 {ECO:0000244|PDB:4FM9}.
STRAND 912 915 {ECO:0000244|PDB:5GWK}.
STRAND 921 923 {ECO:0000244|PDB:4FM9}.
HELIX 932 938 {ECO:0000244|PDB:4FM9}.
HELIX 940 944 {ECO:0000244|PDB:4FM9}.
STRAND 948 950 {ECO:0000244|PDB:4FM9}.
STRAND 955 959 {ECO:0000244|PDB:4FM9}.
STRAND 968 971 {ECO:0000244|PDB:4FM9}.
HELIX 974 983 {ECO:0000244|PDB:4FM9}.
HELIX 985 988 {ECO:0000244|PDB:4FM9}.
STRAND 992 996 {ECO:0000244|PDB:4FM9}.
STRAND 1000 1003 {ECO:0000244|PDB:4FM9}.
STRAND 1009 1011 {ECO:0000244|PDB:4FM9}.
HELIX 1015 1059 {ECO:0000244|PDB:4FM9}.
HELIX 1070 1080 {ECO:0000244|PDB:4FM9}.
HELIX 1086 1091 {ECO:0000244|PDB:4FM9}.
HELIX 1126 1129 {ECO:0000244|PDB:4FM9}.
HELIX 1133 1136 {ECO:0000244|PDB:5GWK}.
HELIX 1138 1160 {ECO:0000244|PDB:4FM9}.
HELIX 1163 1189 {ECO:0000244|PDB:4FM9}.
SEQUENCE 1531 AA; 174385 MW; 3DF40BC9E84789DC CRC64;
MEVSPLQPVN ENMQVNKIKK NEDAKKRLSV ERIYQKKTQL EHILLRPDTY IGSVELVTQQ
MWVYDEDVGI NYREVTFVPG LYKIFDEILV NAADNKQRDP KMSCIRVTID PENNLISIWN
NGKGIPVVEH KVEKMYVPAL IFGQLLTSSN YDDDEKKVTG GRNGYGAKLC NIFSTKFTVE
TASREYKKMF KQTWMDNMGR AGEMELKPFN GEDYTCITFQ PDLSKFKMQS LDKDIVALMV
RRAYDIAGST KDVKVFLNGN KLPVKGFRSY VDMYLKDKLD ETGNSLKVIH EQVNHRWEVC
LTMSEKGFQQ ISFVNSIATS KGGRHVDYVA DQIVTKLVDV VKKKNKGGVA VKAHQVKNHM
WIFVNALIEN PTFDSQTKEN MTLQPKSFGS TCQLSEKFIK AAIGCGIVES ILNWVKFKAQ
VQLNKKCSAV KHNRIKGIPK LDDANDAGGR NSTECTLILT EGDSAKTLAV SGLGVVGRDK
YGVFPLRGKI LNVREASHKQ IMENAEINNI IKIVGLQYKK NYEDEDSLKT LRYGKIMIMT
DQDQDGSHIK GLLINFIHHN WPSLLRHRFL EEFITPIVKV SKNKQEMAFY SLPEFEEWKS
STPNHKKWKV KYYKGLGTST SKEAKEYFAD MKRHRIQFKY SGPEDDAAIS LAFSKKQIDD
RKEWLTNFME DRRQRKLLGL PEDYLYGQTT TYLTYNDFIN KELILFSNSD NERSIPSMVD
GLKPGQRKVL FTCFKRNDKR EVKVAQLAGS VAEMSSYHHG EMSLMMTIIN LAQNFVGSNN
LNLLQPIGQF GTRLHGGKDS ASPRYIFTML SSLARLLFPP KDDHTLKFLY DDNQRVEPEW
YIPIIPMVLI NGAEGIGTGW SCKIPNFDVR EIVNNIRRLM DGEEPLPMLP SYKNFKGTIE
ELAPNQYVIS GEVAILNSTT IEISELPVRT WTQTYKEQVL EPMLNGTEKT PPLITDYREY
HTDTTVKFVV KMTEEKLAEA ERVGLHKVFK LQTSLTCNSM VLFDHVGCLK KYDTVLDILR
DFFELRLKYY GLRKEWLLGM LGAESAKLNN QARFILEKID GKIIIENKPK KELIKVLIQR
GYDSDPVKAW KEAQQKVPDE EENEESDNEK ETEKSDSVTD SGPTFNYLLD MPLWYLTKEK
KDELCRLRNE KEQELDTLKR KSPSDLWKED LATFIEELEA VEAKEKQDEQ VGLPGKGGKA
KGKKTQMAEV LPSPRGQRVI PRITIEMKAE AEKKNKKKIK NENTEGSPQE DGVELEGLKQ
RLEKKQKREP GTKTKKQTTL AFKPIKKGKK RNPWSDSESD RSSDESNFDV PPRETEPRRA
ATKTKFTMDL DSDEDFSDFD EKTDDEDFVP SDASPPKTKT SPKLSNKELK PQKSVVSDLE
ADDVKGSVPL SSSPPATHFP DETEITNPVP KKNVTVKKTA AKSQSSTSTT GAKKRAAPKG
TKRDPALNSG VSQKPDPAKT KNRRKRKPST SDDSDSNFEK IVSKAVTSKK SKGESDDFHM
DFDSAVAPRA KSVRAKKPIK YLEESDEDDL F


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20-272-191336 Topoisomerase II alpha - Mouse monoclonal [SWT3D1] to Topoisomerase II alpha; EC 5.99.1.3; DNA topoisomerase II. alpha isozyme Monoclonal 0.5 ml
EIAAB43432 DNA topoisomerase 2-alpha,DNA topoisomerase II, alpha isozyme,Homo sapiens,Human,TOP2,TOP2A
EIAAB43434 DNA topoisomerase 2-alpha,DNA topoisomerase II, alpha isozyme,Rat,Rattus norvegicus,Top2,Top-2,Top2a
EIAAB43435 DNA topoisomerase 2-alpha,DNA topoisomerase II, alpha isozyme,Mouse,Mus musculus,Top2,Top-2,Top2a
EIAAB43433 DNA topoisomerase 2-alpha,DNA topoisomerase II, alpha isozyme,Pig,Sus scrofa,TOP2A
18-003-42906 DNA topoisomerase 2-alpha - EC 5.99.1.3; DNA topoisomerase II. alpha isozyme Polyclonal 0.1 mg Protein A
EIAAB43436 Chicken,DNA topoisomerase 2-alpha,DNA topoisomerase II, alpha isozyme,Gallus gallus,TOP2A
EIAAB43441 DNA topoisomerase 3-alpha,DNA topoisomerase III alpha,Homo sapiens,Human,TOP3,TOP3A
EIAAB43440 DNA topoisomerase 3-alpha,DNA topoisomerase III alpha,Mouse,Mus musculus,Top3,Top3a
AVARP04007_T200 Anti-DNA topoisomerase II, alpha isozyme (TOP2A) Species_Reactivity: Human
EIAAB43439 DNA topoisomerase 2-beta,DNA topoisomerase II, beta isozyme,Homo sapiens,Human,TOP2B
EIAAB43438 DNA topoisomerase 2-beta,DNA topoisomerase II, beta isozyme,Mouse,Mus musculus,Top2b
18-272-196475 Topoisomerase II beta - Rabbit polyclonal to Topoisomerase II beta; EC 5.99.1.3; DNA topoisomerase II. beta isozyme Polyclonal 0.5 ml
18-272-196476 Topoisomerase II beta prediluted - Rabbit polyclonal to Topoisomerase II beta prediluted; EC 5.99.1.3; DNA topoisomerase II. beta isozyme Polyclonal 7 ml
EIAAB43437 Chicken,DNA topoisomerase 2-beta,DNA topoisomerase II, beta isozyme,Gallus gallus,TOP2B
orb70885 NES Topoisomerase 2 alpha (1017-1028) peptide This is NES Topoisomerase 2 alpha (1017-1028) peptide. For research use only. 1 mg
TOP2A11-P human Topoisomerase II alpha (TOP2 alpha) Control blocking peptide 100 ug
TOP2A11-P human Topoisomerase II alpha (TOP2 alpha) Control_blocking peptide 100 ug
TOP2A11-A Anti-human Topoisomerase II alpha (TOP2 alpha) IgG, aff pure 100 ug
bs-1203P Peptides: TOPO II Alpha_DNA TP II Alpha (DNA topoisomerase II Alpha) Protein Length:12-25 amino acids. 200ug lyophilized
TOP2A11-A Anti_human Topoisomerase II alpha (TOP2 alpha) IgG, aff pure 100 ug
20-272-190787 Topoisomerase I - Mouse monoclonal [Mab1] to Topoisomerase I; EC 5.99.1.2; DNA topoisomerase I Monoclonal 0.05 ml
EIAAB43428 DNA topoisomerase 1,DNA topoisomerase I,Homo sapiens,Human,TOP1
ABD-013 alpha-DNA Topoisomerase I 50


 

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