位置:首页 > 蛋白库 > TOP2A_HUMAN
TOP2A_HUMAN
ID   TOP2A_HUMAN             Reviewed;        1531 AA.
AC   P11388; B2RTS1; Q71UN1; Q71UQ5; Q9HB24; Q9HB25; Q9HB26; Q9UP44; Q9UQP9;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   04-MAY-2001, sequence version 3.
DT   03-AUG-2022, entry version 252.
DE   RecName: Full=DNA topoisomerase 2-alpha;
DE            EC=5.6.2.2 {ECO:0000255|PROSITE-ProRule:PRU00995, ECO:0000269|PubMed:19222228, ECO:0000269|PubMed:19697956};
DE   AltName: Full=DNA topoisomerase II, alpha isozyme;
GN   Name=TOP2A; Synonyms=TOP2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=2845399; DOI=10.1073/pnas.85.19.7177;
RA   Tsai-Pflugfelder M., Liu L.F., Liu A.A., Tewey K.M., Whang-Peng J.,
RA   Knutsen T., Huebner K., Croce C.M., Wang J.C.;
RT   "Cloning and sequencing of cDNA encoding human DNA topoisomerase II and
RT   localization of the gene to chromosome region 17q21-22.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:7177-7181(1988).
RN   [2]
RP   SEQUENCE REVISION TO 109-114.
RX   PubMed=8393377;
RA   Wasserman R.A., Austin C.A., Fisher L.M., Wang J.C.;
RT   "Use of yeast in the study of anticancer drugs targeting DNA
RT   topoisomerases: expression of a functional recombinant human DNA
RT   topoisomerase II alpha in yeast.";
RL   Cancer Res. 53:3591-3596(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX   PubMed=9795238; DOI=10.1016/s0378-1119(98)00468-5;
RA   Lang A.J., Mirski S.E., Cummings H.J., Yu Q., Gerlach J.H., Cole S.P.;
RT   "Structural organization of the human TOP2A and TOP2B genes.";
RL   Gene 221:255-266(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX   PubMed=10095062; DOI=10.1016/s0167-4781(99)00020-2;
RA   Sng J.H., Heaton V.J., Bell M., Mani P., Austin C.A., Fisher L.M.;
RT   "Molecular cloning and characterization of the human topoisomerase IIalpha
RT   and IIbeta genes: evidence for isoform evolution through gene
RT   duplication.";
RL   Biochim. Biophys. Acta 1444:395-406(1999).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-500 (ISOFORMS 2; 3 AND 4).
RA   Petruti-Mot A.S., Earnshaw W.C.;
RT   "Two differentially spliced forms of topoisomerase II alpha and beta mRNAs
RT   are conserved between birds and humans.";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21 AND 48-72.
RA   Neri S., Govoni M., Perrotta L., Pozzi S., Pession A.;
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   PROTEIN SEQUENCE OF 1-17; 74-96; 124-131; 169-184; 243-251; 277-287;
RP   325-336; 387-397; 467-478; 481-487; 500-519; 569-579; 702-713; 805-815;
RP   828-835; 864-877; 937-958; 1021-1026 AND 1185-1196, ACETYLATION AT MET-1,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Ovarian carcinoma;
RA   Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [11]
RP   PROTEIN SEQUENCE OF 135-157; 228-241; 307-321; 325-336; 387-397; 401-416;
RP   467-478; 536-550; 569-579; 640-655; 702-713; 805-815; 1011-1020; 1097-1114;
RP   1169-1184; 1239-1259 AND 1374-1411, PHOSPHORYLATION AT SER-1106, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RA   Bienvenut W.V., Waridel P., Quadroni M.;
RL   Submitted (MAR-2009) to UniProtKB.
RN   [12]
RP   SUBCELLULAR LOCATION.
RX   PubMed=8299728; DOI=10.1006/excr.1994.1046;
RA   Zini N., Santi S., Ognibene A., Bavelloni A., Neri L.M., Valmori A.,
RA   Mariani E., Negri C., Astaldi-Ricotti G.C., Maraldi N.M.;
RT   "Discrete localization of different DNA topoisomerases in HeLa and K562
RT   cell nuclei and subnuclear fractions.";
RL   Exp. Cell Res. 210:336-348(1994).
RN   [13]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=9155056; DOI=10.1038/bjc.1997.227;
RA   Turley H., Comley M., Houlbrook S., Nozaki N., Kikuchi A., Hickson I.D.,
RA   Gatter K., Harris A.L.;
RT   "The distribution and expression of the two isoforms of DNA topoisomerase
RT   II in normal and neoplastic human tissues.";
RL   Br. J. Cancer 75:1340-1346(1997).
RN   [14]
RP   PHOSPHORYLATION AT SER-1469, AND MUTAGENESIS OF SER-1469.
RX   PubMed=10942766; DOI=10.1074/jbc.m005179200;
RA   Escargueil A.E., Plisov S.Y., Filhol O., Cochet C., Larsen A.K.;
RT   "Mitotic phosphorylation of DNA topoisomerase II alpha by protein kinase
RT   CK2 creates the MPM-2 phosphoepitope on Ser-1469.";
RL   J. Biol. Chem. 275:34710-34718(2000).
RN   [15]
RP   NUCLEAR EXPORT SIGNAL.
RX   PubMed=12821127; DOI=10.1016/s0006-291x(03)01077-5;
RA   Mirski S.E., Bielawski J.C., Cole S.P.;
RT   "Identification of functional nuclear export sequences in human
RT   topoisomerase IIalpha and beta.";
RL   Biochem. Biophys. Res. Commun. 306:905-911(2003).
RN   [16]
RP   INTERACTION WITH DHX9.
RX   PubMed=12711669; DOI=10.1093/nar/gkg328;
RA   Zhou K., Choe K.-T., Zaidi Z., Wang Q., Mathews M.B., Lee C.-G.;
RT   "RNA helicase A interacts with dsDNA and topoisomerase IIalpha.";
RL   Nucleic Acids Res. 31:2253-2260(2003).
RN   [17]
RP   INTERACTION WITH COPS5.
RX   PubMed=15126503; DOI=10.1074/jbc.m401411200;
RA   Yun J., Tomida A., Andoh T., Tsuruo T.;
RT   "Interaction between glucose-regulated destruction domain of DNA
RT   topoisomerase IIalpha and MPN domain of Jab1/CSN5.";
RL   J. Biol. Chem. 279:31296-31303(2004).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-1106; SER-1213;
RP   SER-1247; SER-1332; SER-1337; THR-1343; SER-1351; SER-1354; SER-1374;
RP   SER-1377 AND SER-1525, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1213; SER-1374; SER-1377 AND
RP   SER-1525, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein phosphorylation
RT   analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1247, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17924679; DOI=10.1021/pr070152u;
RA   Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT   "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT   and high confident phosphopeptide identification by cross-validation of
RT   MS/MS and MS/MS/MS spectra.";
RL   J. Proteome Res. 6:4150-4162(2007).
RN   [21]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PLSCR1.
RX   PubMed=17567603; DOI=10.1093/nar/gkm434;
RA   Wyles J.P., Wu Z., Mirski S.E., Cole S.P.;
RT   "Nuclear interactions of topoisomerase II alpha and beta with phospholipid
RT   scramblase 1.";
RL   Nucleic Acids Res. 35:4076-4085(2007).
RN   [22]
RP   PHOSPHORYLATION AT THR-1343.
RX   PubMed=18062778; DOI=10.1042/bj20071394;
RA   Iida M., Matsuda M., Komatani H.;
RT   "Plk3 phosphorylates topoisomerase IIalpha at Thr(1342), a site that is not
RT   recognized by Plk1.";
RL   Biochem. J. 411:27-32(2008).
RN   [23]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1504, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [24]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-1213; SER-1247;
RP   SER-1332; SER-1337 AND SER-1377, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [25]
RP   FUNCTION, AND INTERACTION WITH SETMAR.
RX   PubMed=18790802; DOI=10.1093/nar/gkn560;
RA   Williamson E.A., Rasila K.K., Corwin L.K., Wray J., Beck B.D., Severns V.,
RA   Mobarak C., Lee S.H., Nickoloff J.A., Hromas R.;
RT   "The SET and transposase domain protein Metnase enhances chromosome
RT   decatenation: regulation by automethylation.";
RL   Nucleic Acids Res. 36:5822-5831(2008).
RN   [26]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1106; SER-1213; SER-1332;
RP   SER-1337; THR-1343; SER-1351; SER-1392; SER-1393; SER-1449; SER-1469;
RP   THR-1470; SER-1471; SER-1474 AND SER-1525, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [27]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [28]
RP   CATALYTIC ACTIVITY, AND COFACTOR.
RX   PubMed=19222228; DOI=10.1021/bi8023256;
RA   Deweese J.E., Burch A.M., Burgin A.B., Osheroff N.;
RT   "Use of divalent metal ions in the DNA cleavage reaction of human type II
RT   topoisomerases.";
RL   Biochemistry 48:1862-1869(2009).
RN   [29]
RP   MUTAGENESIS OF GLU-461; ASP-541; ASP-543 AND ASP-545, PUTATIVE
RP   METAL-BINDING SITES, CATALYTIC ACTIVITY, AND COFACTOR.
RX   PubMed=19697956; DOI=10.1021/bi900875c;
RA   Deweese J.E., Guengerich F.P., Burgin A.B., Osheroff N.;
RT   "Metal ion interactions in the DNA cleavage/ligation active site of human
RT   topoisomerase IIalpha.";
RL   Biochemistry 48:8940-8947(2009).
RN   [30]
RP   PHOSPHORYLATION AT SER-1106 BY CSNK1D/CK1.
RX   PubMed=19043076; DOI=10.1093/nar/gkn934;
RA   Grozav A.G., Chikamori K., Kozuki T., Grabowski D.R., Bukowski R.M.,
RA   Willard B., Kinter M., Andersen A.H., Ganapathi R., Ganapathi M.K.;
RT   "Casein kinase I delta/epsilon phosphorylates topoisomerase IIalpha at
RT   serine-1106 and modulates DNA cleavage activity.";
RL   Nucleic Acids Res. 37:382-392(2009).
RN   [31]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1247; SER-1374; SER-1387;
RP   SER-1393; SER-1504 AND SER-1525, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [32]
RP   INTERACTION WITH SETMAR.
RX   PubMed=20457750; DOI=10.1093/nar/gkq339;
RA   De Haro L.P., Wray J., Williamson E.A., Durant S.T., Corwin L.,
RA   Gentry A.C., Osheroff N., Lee S.H., Hromas R., Nickoloff J.A.;
RT   "Metnase promotes restart and repair of stalled and collapsed replication
RT   forks.";
RL   Nucleic Acids Res. 38:5681-5691(2010).
RN   [33]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP   ANALYSIS] AT SER-4; THR-282; SER-1106; THR-1205; SER-1213; SER-1247;
RP   SER-1332; SER-1337; THR-1343; SER-1351; SER-1354; SER-1374; SER-1377;
RP   SER-1471; SER-1474; SER-1495; SER-1504 AND SER-1525, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [34]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [35]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP   ANALYSIS] AT SER-4; SER-1106; SER-1213; SER-1247; SER-1295; SER-1297;
RP   SER-1299; SER-1302; SER-1332; SER-1337; THR-1343; SER-1351; SER-1354;
RP   SER-1374; SER-1377; SER-1469; THR-1470; SER-1471; SER-1474; SER-1476 AND
RP   SER-1525, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [36]
RP   MUTAGENESIS OF 342-LYS--LYS-344.
RX   PubMed=23022727; DOI=10.1038/nsmb.2388;
RA   Schmidt B.H., Osheroff N., Berger J.M.;
RT   "Structure of a topoisomerase II-DNA-nucleotide complex reveals a new
RT   control mechanism for ATPase activity.";
RL   Nat. Struct. Mol. Biol. 19:1147-1154(2012).
RN   [37]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RECQL5.
RX   PubMed=22013166; DOI=10.1093/nar/gkr844;
RA   Ramamoorthy M., Tadokoro T., Rybanska I., Ghosh A.K., Wersto R., May A.,
RA   Kulikowicz T., Sykora P., Croteau D.L., Bohr V.A.;
RT   "RECQL5 cooperates with Topoisomerase II alpha in DNA decatenation and cell
RT   cycle progression.";
RL   Nucleic Acids Res. 40:1621-1635(2012).
RN   [38]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [39]
RP   FUNCTION, MUTAGENESIS OF GLU-461; ASP-541 AND ASP-543, AND COFACTOR.
RX   PubMed=22323612; DOI=10.1073/pnas.1115704109;
RA   Lee S., Jung S.R., Heo K., Byl J.A., Deweese J.E., Osheroff N., Hohng S.;
RT   "DNA cleavage and opening reactions of human topoisomerase IIalpha are
RT   regulated via Mg2+-mediated dynamic bending of gate-DNA.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:2925-2930(2012).
RN   [40]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-1106; SER-1213;
RP   THR-1244; SER-1247; SER-1374; SER-1377; SER-1391; SER-1449; SER-1469;
RP   SER-1471; SER-1474; SER-1495 AND SER-1504, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [41]
RP   INTERACTION WITH MCM3AP.
RX   PubMed=23652018; DOI=10.1038/ncomms2823;
RA   Singh S.K., Maeda K., Eid M.M., Almofty S.A., Ono M., Pham P.,
RA   Goodman M.F., Sakaguchi N.;
RT   "GANP regulates recruitment of AID to immunoglobulin variable regions by
RT   modulating transcription and nucleosome occupancy.";
RL   Nat. Commun. 4:1830-1830(2013).
RN   [42]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1228; LYS-1240; LYS-1385 AND
RP   LYS-1492, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
RN   [43]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1240, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA   Impens F., Radoshevich L., Cossart P., Ribet D.;
RT   "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT   external stimuli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN   [44]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-639; LYS-662; LYS-676; LYS-1075;
RP   LYS-1196; LYS-1228; LYS-1240; LYS-1385 AND LYS-1442, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA   Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL   Cell Rep. 10:1778-1791(2015).
RN   [45]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1228 AND LYS-1240, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA   Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "System-wide analysis of SUMOylation dynamics in response to replication
RT   stress reveals novel small ubiquitin-like modified target proteins and
RT   acceptor lysines relevant for genome stability.";
RL   Mol. Cell. Proteomics 14:1419-1434(2015).
RN   [46]
RP   INTERACTION WITH ERCC6.
RX   PubMed=26030138; DOI=10.1371/journal.pone.0128558;
RA   Nicolai S., Filippi S., Caputo M., Cipak L., Gregan J., Ammerer G.,
RA   Frontini M., Willems D., Prantera G., Balajee A.S., Proietti-De-Santis L.;
RT   "Identification of Novel Proteins Co-Purifying with Cockayne Syndrome Group
RT   B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and Chromatin
RT   Dynamics.";
RL   PLoS ONE 10:E0128558-E0128558(2015).
RN   [47]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-17; LYS-156; LYS-157; LYS-261;
RP   LYS-352; LYS-386; LYS-397; LYS-416; LYS-418; LYS-425; LYS-440; LYS-466;
RP   LYS-480; LYS-529; LYS-584; LYS-599; LYS-614; LYS-622; LYS-625; LYS-632;
RP   LYS-639; LYS-655; LYS-662; LYS-676; LYS-1075; LYS-1114; LYS-1196; LYS-1204;
RP   LYS-1228; LYS-1240; LYS-1259; LYS-1276; LYS-1283; LYS-1286; LYS-1363;
RP   LYS-1367; LYS-1373; LYS-1385; LYS-1422; LYS-1442; LYS-1454; LYS-1459;
RP   LYS-1484 AND LYS-1492, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [48]
RP   X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 29-428 IN COMPLEX WITH ADP, AND
RP   X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 29-428 IN COMPLEX WITH AMPPNP.
RX   PubMed=16100112; DOI=10.1074/jbc.m506520200;
RA   Wei H., Ruthenburg A.J., Bechis S.K., Verdine G.L.;
RT   "Nucleotide-dependent domain movement in the ATPase domain of a human type
RT   IIA DNA topoisomerase.";
RL   J. Biol. Chem. 280:37041-37047(2005).
RN   [49]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 431-1193 IN COMPLEX WITH DNA AND
RP   MAGNESIUM ION, SUBUNIT, AND COFACTOR.
RX   PubMed=22841979; DOI=10.1016/j.jmb.2012.07.014;
RA   Wendorff T.J., Schmidt B.H., Heslop P., Austin C.A., Berger J.M.;
RT   "The structure of DNA-bound human topoisomerase II alpha: conformational
RT   mechanisms for coordinating inter-subunit interactions with DNA cleavage.";
RL   J. Mol. Biol. 424:109-124(2012).
RN   [50]
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 29-428 IN COMPLEX WITH ADP AND
RP   ATP ANALOGS, AND DOMAIN.
RX   PubMed=25202966; DOI=10.1371/journal.pone.0107289;
RA   Stanger F.V., Dehio C., Schirmer T.;
RT   "Structure of the N-terminal Gyrase B fragment in complex with ADPPi
RT   reveals rigid-body motion induced by ATP hydrolysis.";
RL   PLoS ONE 9:E107289-E107289(2014).
RN   [51]
RP   VARIANT AMSACRINE-RESISTANT LYS-487.
RX   PubMed=1651812;
RA   Hinds M., Deisseroth K., Mayes J., Altschuler E., Jansen R., Ledley F.D.,
RA   Zwelling L.A.;
RT   "Identification of a point mutation in the topoisomerase II gene from a
RT   human leukemia cell line containing an amsacrine-resistant form of
RT   topoisomerase II.";
RL   Cancer Res. 51:4729-4731(1991).
RN   [52]
RP   VARIANT TENIPOSIDE-RESISTANT GLN-450.
RX   PubMed=1652758; DOI=10.1073/pnas.88.17.7654;
RA   Bugg B.Y., Danks M.K., Beck W.T., Suttle D.P.;
RT   "Expression of a mutant DNA topoisomerase II in CCRF-CEM human leukemic
RT   cells selected for resistance to teniposide.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:7654-7658(1991).
CC   -!- FUNCTION: Key decatenating enzyme that alters DNA topology by binding
CC       to two double-stranded DNA molecules, generating a double-stranded
CC       break in one of the strands, passing the intact strand through the
CC       broken strand, and religating the broken strand (PubMed:17567603,
CC       PubMed:18790802, PubMed:22013166, PubMed:22323612). May play a role in
CC       regulating the period length of ARNTL/BMAL1 transcriptional oscillation
CC       (By similarity). {ECO:0000250|UniProtKB:Q01320,
CC       ECO:0000269|PubMed:17567603, ECO:0000269|PubMed:18790802,
CC       ECO:0000269|PubMed:22013166, ECO:0000269|PubMed:22323612}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent breakage, passage and rejoining of double-
CC         stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00995, ECO:0000269|PubMed:19222228,
CC         ECO:0000269|PubMed:19697956};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000305|PubMed:19222228, ECO:0000305|PubMed:19697956,
CC         ECO:0000305|PubMed:22323612, ECO:0000305|PubMed:22841979};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000305|PubMed:19222228, ECO:0000305|PubMed:19697956,
CC         ECO:0000305|PubMed:22323612, ECO:0000305|PubMed:22841979};
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000305|PubMed:19222228, ECO:0000305|PubMed:19697956,
CC         ECO:0000305|PubMed:22323612, ECO:0000305|PubMed:22841979};
CC       Note=Binds two Mg(2+) per subunit. The magnesium ions form salt bridges
CC       with both the protein and the DNA. Can also accept other divalent metal
CC       cations, such as Mn(2+) or Ca(2+). {ECO:0000305|PubMed:19222228,
CC       ECO:0000305|PubMed:19697956, ECO:0000305|PubMed:22323612,
CC       ECO:0000305|PubMed:22841979};
CC   -!- ACTIVITY REGULATION: Specifically inhibited by the intercalating agent
CC       amsacrine.
CC   -!- SUBUNIT: Homodimer. Interacts with COPS5. Interacts with RECQL5; this
CC       stimulates DNA decatenation. Interacts with SETMAR; stimulates the
CC       topoisomerase activity (PubMed:18790802, PubMed:20457750). Interacts
CC       with DHX9; this interaction occurs in a E2 enzyme UBE2I- and RNA-
CC       dependent manner, negatively regulates DHX9-mediated double-stranded
CC       DNA and RNA duplex helicase activity and stimulates TOP2A-mediated
CC       supercoiled DNA relaxation activity (PubMed:12711669). Interacts with
CC       HNRNPU (via C-terminus); this interaction protects the topoisomerase
CC       TOP2A from degradation and positively regulates the relaxation of
CC       supercoiled DNA in a RNA-dependent manner (By similarity). Interacts
CC       with MCM3AP isoform GANP (PubMed:23652018). Interacts with ERCC6
CC       (PubMed:26030138). Interacts with PLSCR1 (PubMed:17567603). Interacts
CC       with GCNA; this interaction allows the resolution of topoisomerase II
CC       (TOP2A) DNA-protein cross-links (By similarity).
CC       {ECO:0000250|UniProtKB:P41516, ECO:0000250|UniProtKB:Q01320,
CC       ECO:0000269|PubMed:12711669, ECO:0000269|PubMed:15126503,
CC       ECO:0000269|PubMed:16100112, ECO:0000269|PubMed:17567603,
CC       ECO:0000269|PubMed:20457750, ECO:0000269|PubMed:22013166,
CC       ECO:0000269|PubMed:22841979, ECO:0000269|PubMed:23652018,
CC       ECO:0000269|PubMed:26030138}.
CC   -!- INTERACTION:
CC       P11388; O14497-1: ARID1A; NbExp=2; IntAct=EBI-539628, EBI-15956509;
CC       P11388; P38398: BRCA1; NbExp=3; IntAct=EBI-539628, EBI-349905;
CC       P11388; P35222: CTNNB1; NbExp=5; IntAct=EBI-539628, EBI-491549;
CC       P11388; Q05655: PRKCD; NbExp=10; IntAct=EBI-539628, EBI-704279;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9155056}. Nucleus,
CC       nucleoplasm {ECO:0000269|PubMed:8299728}. Nucleus
CC       {ECO:0000269|PubMed:17567603, ECO:0000269|PubMed:22013166,
CC       ECO:0000269|PubMed:8299728, ECO:0000269|PubMed:9155056}. Nucleus,
CC       nucleolus {ECO:0000269|PubMed:9155056}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=P11388-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P11388-2; Sequence=VSP_006531;
CC       Name=3;
CC         IsoId=P11388-3; Sequence=VSP_006529;
CC       Name=4;
CC         IsoId=P11388-4; Sequence=VSP_006530;
CC   -!- TISSUE SPECIFICITY: Expressed in the tonsil, spleen, lymph node,
CC       thymus, skin, pancreas, testis, colon, kidney, liver, brain and lung
CC       (PubMed:9155056). Also found in high-grade lymphomas, squamous cell
CC       lung tumors and seminomas (PubMed:9155056).
CC       {ECO:0000269|PubMed:9155056}.
CC   -!- DOMAIN: The N-terminus has several structural domains; the ATPase
CC       domain (about residues 1-265), the transducer domain (about 266-428)
CC       and the toprim domain (455-572) (PubMed:25202966). Comparing different
CC       structures shows ATP hydrolysis induces domain shifts in the N-terminus
CC       that are probably part of the mechanism of DNA cleavage and rejoining
CC       (PubMed:25202966). {ECO:0000250|UniProtKB:P0AES6,
CC       ECO:0000269|PubMed:25202966}.
CC   -!- PTM: Phosphorylation has no effect on catalytic activity. However,
CC       phosphorylation at Ser-1106 by CSNK1D/CK1 promotes DNA cleavable
CC       complex formation. {ECO:0000269|PubMed:10942766,
CC       ECO:0000269|PubMed:18062778, ECO:0000269|PubMed:19043076,
CC       ECO:0000269|Ref.11}.
CC   -!- MISCELLANEOUS: Eukaryotic topoisomerase I and II can relax both
CC       negative and positive supercoils, whereas prokaryotic enzymes relax
CC       only negative supercoils.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; J04088; AAA61209.1; -; mRNA.
DR   EMBL; AF071747; AAC77388.1; -; Genomic_DNA.
DR   EMBL; AF071738; AAC77388.1; JOINED; Genomic_DNA.
DR   EMBL; AF071739; AAC77388.1; JOINED; Genomic_DNA.
DR   EMBL; AF071740; AAC77388.1; JOINED; Genomic_DNA.
DR   EMBL; AF071741; AAC77388.1; JOINED; Genomic_DNA.
DR   EMBL; AF071742; AAC77388.1; JOINED; Genomic_DNA.
DR   EMBL; AF071743; AAC77388.1; JOINED; Genomic_DNA.
DR   EMBL; AF071744; AAC77388.1; JOINED; Genomic_DNA.
DR   EMBL; AF071745; AAC77388.1; JOINED; Genomic_DNA.
DR   EMBL; AF071746; AAC77388.1; JOINED; Genomic_DNA.
DR   EMBL; AJ011741; CAA09762.1; -; Genomic_DNA.
DR   EMBL; AJ011742; CAA09762.1; JOINED; Genomic_DNA.
DR   EMBL; AJ011743; CAA09762.1; JOINED; Genomic_DNA.
DR   EMBL; AJ011744; CAA09762.1; JOINED; Genomic_DNA.
DR   EMBL; AJ011745; CAA09762.1; JOINED; Genomic_DNA.
DR   EMBL; AJ011746; CAA09762.1; JOINED; Genomic_DNA.
DR   EMBL; AJ011747; CAA09762.1; JOINED; Genomic_DNA.
DR   EMBL; AJ011748; CAA09762.1; JOINED; Genomic_DNA.
DR   EMBL; AJ011749; CAA09762.1; JOINED; Genomic_DNA.
DR   EMBL; AJ011750; CAA09762.1; JOINED; Genomic_DNA.
DR   EMBL; AJ011751; CAA09762.1; JOINED; Genomic_DNA.
DR   EMBL; AJ011752; CAA09762.1; JOINED; Genomic_DNA.
DR   EMBL; AJ011753; CAA09762.1; JOINED; Genomic_DNA.
DR   EMBL; AJ011754; CAA09762.1; JOINED; Genomic_DNA.
DR   EMBL; AJ011755; CAA09762.1; JOINED; Genomic_DNA.
DR   EMBL; AJ011756; CAA09762.1; JOINED; Genomic_DNA.
DR   EMBL; AJ011757; CAA09762.1; JOINED; Genomic_DNA.
DR   EMBL; AJ011758; CAA09762.1; JOINED; Genomic_DNA.
DR   EMBL; AC080112; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF285157; AAG13403.1; -; mRNA.
DR   EMBL; AF285158; AAG13404.1; -; mRNA.
DR   EMBL; CH471152; EAW60663.1; -; Genomic_DNA.
DR   EMBL; BC140791; AAI40792.1; -; mRNA.
DR   EMBL; AF285159; AAG13405.1; -; mRNA.
DR   EMBL; AF069522; AAC23518.1; -; Genomic_DNA.
DR   EMBL; AF064590; AAC16736.1; -; Genomic_DNA.
DR   CCDS; CCDS45672.1; -. [P11388-1]
DR   PIR; A40493; A40493.
DR   RefSeq; NP_001058.2; NM_001067.3. [P11388-1]
DR   PDB; 1ZXM; X-ray; 1.87 A; A/B=29-428.
DR   PDB; 1ZXN; X-ray; 2.51 A; A/B/C/D=29-428.
DR   PDB; 4FM9; X-ray; 2.90 A; A=431-1193.
DR   PDB; 4R1F; X-ray; 2.51 A; A/B/C/D=29-428.
DR   PDB; 5GWK; X-ray; 3.15 A; A/B=429-1188.
DR   PDB; 5NNE; X-ray; 1.15 A; C=1198-1207.
DR   PDB; 6ZY5; EM; 3.60 A; A/B=1-1531.
DR   PDB; 6ZY6; EM; 4.10 A; A/B=1-1531.
DR   PDB; 6ZY7; EM; 4.64 A; A/B=1-1531.
DR   PDB; 6ZY8; EM; 7.40 A; A/B=1-1531.
DR   PDBsum; 1ZXM; -.
DR   PDBsum; 1ZXN; -.
DR   PDBsum; 4FM9; -.
DR   PDBsum; 4R1F; -.
DR   PDBsum; 5GWK; -.
DR   PDBsum; 5NNE; -.
DR   PDBsum; 6ZY5; -.
DR   PDBsum; 6ZY6; -.
DR   PDBsum; 6ZY7; -.
DR   PDBsum; 6ZY8; -.
DR   AlphaFoldDB; P11388; -.
DR   SMR; P11388; -.
DR   BioGRID; 113006; 254.
DR   CORUM; P11388; -.
DR   DIP; DIP-33887N; -.
DR   IntAct; P11388; 98.
DR   MINT; P11388; -.
DR   STRING; 9606.ENSP00000411532; -.
DR   BindingDB; P11388; -.
DR   ChEMBL; CHEMBL1806; -.
DR   DrugBank; DB05706; 13-deoxydoxorubicin.
DR   DrugBank; DB06013; Aldoxorubicin.
DR   DrugBank; DB05022; Amonafide.
DR   DrugBank; DB06263; Amrubicin.
DR   DrugBank; DB00276; Amsacrine.
DR   DrugBank; DB06420; Annamycin.
DR   DrugBank; DB04975; Banoxantrone.
DR   DrugBank; DB06362; Becatecarin.
DR   DrugBank; DB00537; Ciprofloxacin.
DR   DrugBank; DB00970; Dactinomycin.
DR   DrugBank; DB00694; Daunorubicin.
DR   DrugBank; DB06421; Declopramide.
DR   DrugBank; DB00380; Dexrazoxane.
DR   DrugBank; DB00997; Doxorubicin.
DR   DrugBank; DB05129; Elsamitrucin.
DR   DrugBank; DB00467; Enoxacin.
DR   DrugBank; DB00445; Epirubicin.
DR   DrugBank; DB00773; Etoposide.
DR   DrugBank; DB09047; Finafloxacin.
DR   DrugBank; DB04576; Fleroxacin.
DR   DrugBank; DB01645; Genistein.
DR   DrugBank; DB01177; Idarubicin.
DR   DrugBank; DB00978; Lomefloxacin.
DR   DrugBank; DB04967; Lucanthone.
DR   DrugBank; DB01204; Mitoxantrone.
DR   DrugBank; DB00218; Moxifloxacin.
DR   DrugBank; DB01059; Norfloxacin.
DR   DrugBank; DB01165; Ofloxacin.
DR   DrugBank; DB00487; Pefloxacin.
DR   DrugBank; DB01179; Podofilox.
DR   DrugBank; DB05920; RTA 744.
DR   DrugBank; DB04978; SP1049C.
DR   DrugBank; DB01208; Sparfloxacin.
DR   DrugBank; DB00444; Teniposide.
DR   DrugBank; DB00685; Trovafloxacin.
DR   DrugBank; DB00385; Valrubicin.
DR   DrugBank; DB06042; ZEN-012.
DR   DrugCentral; P11388; -.
DR   GuidetoPHARMACOLOGY; 2637; -.
DR   CarbonylDB; P11388; -.
DR   GlyGen; P11388; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P11388; -.
DR   MetOSite; P11388; -.
DR   PhosphoSitePlus; P11388; -.
DR   SwissPalm; P11388; -.
DR   BioMuta; TOP2A; -.
DR   DMDM; 13959709; -.
DR   UCD-2DPAGE; P11388; -.
DR   CPTAC; CPTAC-1187; -.
DR   EPD; P11388; -.
DR   jPOST; P11388; -.
DR   MassIVE; P11388; -.
DR   MaxQB; P11388; -.
DR   PaxDb; P11388; -.
DR   PeptideAtlas; P11388; -.
DR   PRIDE; P11388; -.
DR   ProteomicsDB; 52767; -. [P11388-1]
DR   ProteomicsDB; 52768; -. [P11388-2]
DR   ProteomicsDB; 52769; -. [P11388-3]
DR   ProteomicsDB; 52770; -. [P11388-4]
DR   Antibodypedia; 1583; 1483 antibodies from 45 providers.
DR   DNASU; 7153; -.
DR   Ensembl; ENST00000423485.6; ENSP00000411532.1; ENSG00000131747.15. [P11388-1]
DR   GeneID; 7153; -.
DR   KEGG; hsa:7153; -.
DR   MANE-Select; ENST00000423485.6; ENSP00000411532.1; NM_001067.4; NP_001058.2.
DR   UCSC; uc002huq.4; human. [P11388-1]
DR   CTD; 7153; -.
DR   DisGeNET; 7153; -.
DR   GeneCards; TOP2A; -.
DR   HGNC; HGNC:11989; TOP2A.
DR   HPA; ENSG00000131747; Tissue enhanced (lymphoid tissue, testis).
DR   MalaCards; TOP2A; -.
DR   MIM; 126430; gene.
DR   neXtProt; NX_P11388; -.
DR   OpenTargets; ENSG00000131747; -.
DR   Orphanet; 635; Neuroblastoma.
DR   PharmGKB; PA354; -.
DR   VEuPathDB; HostDB:ENSG00000131747; -.
DR   eggNOG; KOG0355; Eukaryota.
DR   GeneTree; ENSGT00940000157539; -.
DR   HOGENOM; CLU_001935_1_0_1; -.
DR   InParanoid; P11388; -.
DR   OMA; PMDDNIL; -.
DR   OrthoDB; 117851at2759; -.
DR   PhylomeDB; P11388; -.
DR   TreeFam; TF105282; -.
DR   BRENDA; 5.6.2.2; 2681.
DR   BRENDA; 5.99.1.3; 2681.
DR   PathwayCommons; P11388; -.
DR   Reactome; R-HSA-1362277; Transcription of E2F targets under negative control by DREAM complex.
DR   Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins.
DR   SignaLink; P11388; -.
DR   SIGNOR; P11388; -.
DR   BioGRID-ORCS; 7153; 809 hits in 1095 CRISPR screens.
DR   ChiTaRS; TOP2A; human.
DR   EvolutionaryTrace; P11388; -.
DR   GeneWiki; TOP2A; -.
DR   GenomeRNAi; 7153; -.
DR   Pharos; P11388; Tclin.
DR   PRO; PR:P11388; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; P11388; protein.
DR   Bgee; ENSG00000131747; Expressed in ventricular zone and 142 other tissues.
DR   ExpressionAtlas; P11388; baseline and differential.
DR   Genevisible; P11388; HS.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:Ensembl.
DR   GO; GO:0000793; C:condensed chromosome; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0009330; C:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; IDA:UniProtKB.
DR   GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0008301; F:DNA binding, bending; IDA:UniProtKB.
DR   GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IDA:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR   GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR   GO; GO:0005080; F:protein kinase C binding; IPI:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0043130; F:ubiquitin binding; IMP:UniProtKB.
DR   GO; GO:0030263; P:apoptotic chromosome condensation; IDA:UniProtKB.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR   GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
DR   GO; GO:0006266; P:DNA ligation; IDA:UniProtKB.
DR   GO; GO:0006265; P:DNA topological change; IDA:UniProtKB.
DR   GO; GO:0040016; P:embryonic cleavage; IEA:Ensembl.
DR   GO; GO:0007143; P:female meiotic nuclear division; IEA:Ensembl.
DR   GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR   GO; GO:1905463; P:negative regulation of DNA duplex unwinding; IMP:UniProtKB.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR   GO; GO:0045870; P:positive regulation of single stranded viral RNA replication via double stranded DNA intermediate; IMP:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR   GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR   GO; GO:0000819; P:sister chromatid segregation; IBA:GO_Central.
DR   CDD; cd00187; TOP4c; 1.
DR   CDD; cd03365; TOPRIM_TopoIIA; 1.
DR   Gene3D; 1.10.268.10; -; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   Gene3D; 3.40.50.670; -; 1.
DR   Gene3D; 3.90.199.10; -; 1.
DR   InterPro; IPR012542; DTHCT.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR001241; Topo_IIA.
DR   InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR013757; Topo_IIA_A_a_sf.
DR   InterPro; IPR013759; Topo_IIA_B_C.
DR   InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR   InterPro; IPR002205; Topo_IIA_dom_A.
DR   InterPro; IPR018522; TopoIIA_CS.
DR   InterPro; IPR031660; TOPRIM_C.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR034157; TOPRIM_TopoII.
DR   Pfam; PF00204; DNA_gyraseB; 1.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   Pfam; PF08070; DTHCT; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   Pfam; PF16898; TOPRIM_C; 1.
DR   SMART; SM00433; TOP2c; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   SUPFAM; SSF56719; SSF56719; 1.
DR   PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW   Biological rhythms; Cytoplasm; Direct protein sequencing; DNA-binding;
KW   Isomerase; Isopeptide bond; Magnesium; Metal-binding; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Reference proteome; Topoisomerase;
KW   Ubl conjugation.
FT   CHAIN           1..1531
FT                   /note="DNA topoisomerase 2-alpha"
FT                   /id="PRO_0000145363"
FT   DOMAIN          455..572
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT   REGION          342..344
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000305|PubMed:23022727"
FT   REGION          990..999
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000269|PubMed:22841979"
FT   REGION          1090..1123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1184..1531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1433..1439
FT                   /note="Interaction with PLSCR1"
FT                   /evidence="ECO:0000269|PubMed:17567603"
FT   MOTIF           1018..1028
FT                   /note="Nuclear export signal"
FT   COMPBIAS        1225..1274
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1289..1332
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1333..1347
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1354..1372
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1408..1434
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1466..1504
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        805
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P06786"
FT   BINDING         91
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:16100112,
FT                   ECO:0000269|PubMed:25202966"
FT   BINDING         120
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:16100112,
FT                   ECO:0000269|PubMed:25202966"
FT   BINDING         148..150
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:16100112,
FT                   ECO:0000269|PubMed:25202966"
FT   BINDING         161..168
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:16100112,
FT                   ECO:0000269|PubMed:25202966"
FT   BINDING         376..378
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:16100112,
FT                   ECO:0000305|PubMed:25202966"
FT   BINDING         461
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT   BINDING         541
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT   BINDING         541
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:22841979"
FT   BINDING         543
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:22841979"
FT   SITE            489
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT   SITE            492
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000269|PubMed:22841979"
FT   SITE            661
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000269|PubMed:22841979"
FT   SITE            662
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000269|PubMed:22841979"
FT   SITE            723
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000269|PubMed:22841979"
FT   SITE            757
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000269|PubMed:22841979"
FT   SITE            763
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000269|PubMed:22841979"
FT   SITE            804
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P06786"
FT   SITE            856
FT                   /note="Important for DNA bending; intercalates between base
FT                   pairs of target DNA"
FT                   /evidence="ECO:0000250|UniProtKB:P06786"
FT   SITE            931
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000269|PubMed:22841979"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000269|Ref.10, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22814378"
FT   MOD_RES         4
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         282
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         1106
FT                   /note="Phosphoserine; by CK1"
FT                   /evidence="ECO:0000269|PubMed:19043076, ECO:0000269|Ref.11,
FT                   ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1205
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         1213
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16964243,
FT                   ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         1244
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1247
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18691976,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         1295
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         1297
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         1299
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         1302
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         1327
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01320"
FT   MOD_RES         1332
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT   MOD_RES         1337
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT   MOD_RES         1343
FT                   /note="Phosphothreonine; by PLK3"
FT                   /evidence="ECO:0000269|PubMed:18062778,
FT                   ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT   MOD_RES         1351
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692"
FT   MOD_RES         1354
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT   MOD_RES         1374
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16964243,
FT                   ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1377
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16964243,
FT                   ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18691976,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1387
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         1391
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1392
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         1393
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332"
FT   MOD_RES         1422
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q01320"
FT   MOD_RES         1442
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q01320"
FT   MOD_RES         1449
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1469
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000269|PubMed:10942766,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1470
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:21406692"
FT   MOD_RES         1471
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1474
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1476
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         1495
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1504
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18220336,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1525
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16964243,
FT                   ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692"
FT   CROSSLNK        17
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        156
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        157
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        261
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        352
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        386
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        397
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        416
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        418
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        425
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        440
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        466
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        480
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        529
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        584
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        599
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        614
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        622
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        625
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        632
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        639
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25772364,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        655
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        662
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25772364,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        676
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25772364,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1075
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25772364,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1114
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1196
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25772364,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1204
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1228
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25218447,
FT                   ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1240
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0007744|PubMed:25114211"
FT   CROSSLNK        1240
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0007744|PubMed:25114211,
FT                   ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT                   ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1259
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1276
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1283
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1286
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1363
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1367
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1373
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1385
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25218447,
FT                   ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1422
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1442
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0007744|PubMed:25772364,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1454
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1459
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1484
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1492
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25218447,
FT                   ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         321
FT                   /note="K -> KSSKYWSSRKSKQHILLNFFVLFKFINDAFFGICPFK (in
FT                   isoform 3)"
FT                   /evidence="ECO:0000303|Ref.8"
FT                   /id="VSP_006529"
FT   VAR_SEQ         355
FT                   /note="Q -> QRELCNGAILAHCNLRLMGSSDSPASASRVAGIAGGCHHTQLIFVFL
FT                   VETGFHHVGQAGLERLTSGDPPASASQSSGITDVK (in isoform 4)"
FT                   /evidence="ECO:0000303|Ref.8"
FT                   /id="VSP_006530"
FT   VAR_SEQ         401
FT                   /note="A -> AHLYSRFLIDPFFPNMIPNMIFSFSKA (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.8"
FT                   /id="VSP_006531"
FT   VARIANT         450
FT                   /note="R -> Q (in teniposide (VM-26) resistant cells;
FT                   dbSNP:rs746765101)"
FT                   /evidence="ECO:0000269|PubMed:1652758"
FT                   /id="VAR_007532"
FT   VARIANT         487
FT                   /note="R -> K (in amsacrine resistant cells;
FT                   dbSNP:rs267607133)"
FT                   /evidence="ECO:0000269|PubMed:1651812"
FT                   /id="VAR_007533"
FT   VARIANT         1324
FT                   /note="T -> K (in dbSNP:rs28969502)"
FT                   /id="VAR_029245"
FT   VARIANT         1386
FT                   /note="G -> D (in dbSNP:rs34300454)"
FT                   /id="VAR_052594"
FT   VARIANT         1515
FT                   /note="A -> S (in dbSNP:rs11540720)"
FT                   /id="VAR_052595"
FT   MUTAGEN         342..344
FT                   /note="KKK->AAA: Reduced enzyme activity; abolishes
FT                   stimulation of ATPase activity upon DNA binding."
FT                   /evidence="ECO:0000269|PubMed:23022727"
FT   MUTAGEN         342..344
FT                   /note="KKK->EEE: Strongly reduced enzyme activity;
FT                   abolishes stimulation of ATPase activity upon DNA binding."
FT                   /evidence="ECO:0000269|PubMed:23022727"
FT   MUTAGEN         461
FT                   /note="E->A,C: Impairs bending of target DNA. Strongly
FT                   reduced DNA cleavage."
FT                   /evidence="ECO:0000269|PubMed:19697956,
FT                   ECO:0000269|PubMed:22323612"
FT   MUTAGEN         541
FT                   /note="D->A,C: Impairs bending of target DNA. Strongly
FT                   reduced DNA cleavage."
FT                   /evidence="ECO:0000269|PubMed:19697956,
FT                   ECO:0000269|PubMed:22323612"
FT   MUTAGEN         543
FT                   /note="D->A,C: Impairs bending of target DNA. Strongly
FT                   reduced DNA cleavage."
FT                   /evidence="ECO:0000269|PubMed:19697956,
FT                   ECO:0000269|PubMed:22323612"
FT   MUTAGEN         545
FT                   /note="D->A,C: Strongly reduced DNA cleavage."
FT                   /evidence="ECO:0000269|PubMed:19697956"
FT   MUTAGEN         1469
FT                   /note="S->A: Abolishes binding to the antibody MPM2."
FT                   /evidence="ECO:0000269|PubMed:10942766"
FT   CONFLICT        152
FT                   /note="D -> H (in Ref. 4; CAA09762)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        180
FT                   /note="E -> Q (in Ref. 4; CAA09762)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        327
FT                   /note="D -> H (in Ref. 4; CAA09762)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1022
FT                   /note="F -> L (in Ref. 4; CAA09762)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1274
FT                   /note="T -> S (in Ref. 4; CAA09762)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1295
FT                   /note="S -> P (in Ref. 1; AAA61209)"
FT                   /evidence="ECO:0000305"
FT   HELIX           30..33
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   STRAND          34..36
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   HELIX           39..45
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   HELIX           48..51
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   STRAND          57..65
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   TURN            66..68
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   STRAND          69..77
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   HELIX           79..98
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   STRAND          104..110
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   TURN            111..114
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   STRAND          115..123
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   STRAND          128..130
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   TURN            131..134
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   HELIX           137..143
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   STRAND          144..149
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   HELIX           153..155
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   HELIX           166..172
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   STRAND          174..183
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   TURN            184..187
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   STRAND          188..195
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   TURN            196..199
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   STRAND          205..208
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   STRAND          214..221
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   HELIX           223..226
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   HELIX           233..249
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   STRAND          250..252
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   STRAND          254..257
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   HELIX           267..275
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   STRAND          281..285
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   STRAND          289..294
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   STRAND          297..303
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   STRAND          305..307
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   STRAND          309..314
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   HELIX           324..341
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   STRAND          346..348
FT                   /evidence="ECO:0007829|PDB:1ZXN"
FT   HELIX           353..357
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   STRAND          360..366
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   STRAND          373..375
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   HELIX           385..387
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   STRAND          388..390
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   HELIX           396..402
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   HELIX           407..410
FT                   /evidence="ECO:0007829|PDB:1ZXM"
FT   HELIX           411..415
FT                   /evidence="ECO:0007829|PDB:1ZXN"
FT   STRAND          419..421
FT                   /evidence="ECO:0007829|PDB:1ZXN"
FT   STRAND          423..425
FT                   /evidence="ECO:0007829|PDB:1ZXN"
FT   TURN            445..448
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   HELIX           452..454
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   STRAND          456..462
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   HELIX           463..476
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   STRAND          478..486
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   HELIX           498..503
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   HELIX           505..514
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   STRAND          518..520
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   HELIX           525..530
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   STRAND          534..539
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   HELIX           544..560
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   HELIX           562..566
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   STRAND          570..573
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   STRAND          577..581
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   STRAND          586..590
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   HELIX           592..601
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   STRAND          607..612
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   HELIX           616..618
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   HELIX           621..629
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   HELIX           631..634
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   STRAND          635..639
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   HELIX           644..653
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   HELIX           658..678
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   STRAND          685..688
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   STRAND          691..694
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   HELIX           695..701
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   HELIX           703..714
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   TURN            718..720
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   HELIX           724..735
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   HELIX           744..754
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   HELIX           762..772
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   TURN            793..799
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   TURN            803..805
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   HELIX           812..817
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   HELIX           822..824
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   HELIX           831..833
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   STRAND          834..839
FT                   /evidence="ECO:0007829|PDB:5GWK"
FT   TURN            848..850
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   STRAND          853..856
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   STRAND          861..864
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   HELIX           869..881
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   STRAND          897..903
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   STRAND          906..910
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   STRAND          912..915
FT                   /evidence="ECO:0007829|PDB:5GWK"
FT   STRAND          921..923
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   HELIX           932..938
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   HELIX           940..944
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   STRAND          948..950
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   STRAND          955..959
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   STRAND          968..971
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   HELIX           974..983
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   HELIX           985..988
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   STRAND          992..996
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   STRAND          1000..1003
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   STRAND          1009..1011
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   HELIX           1015..1059
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   HELIX           1070..1080
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   HELIX           1086..1091
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   HELIX           1126..1129
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   HELIX           1133..1136
FT                   /evidence="ECO:0007829|PDB:5GWK"
FT   HELIX           1138..1160
FT                   /evidence="ECO:0007829|PDB:4FM9"
FT   HELIX           1163..1189
FT                   /evidence="ECO:0007829|PDB:4FM9"
SQ   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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024