ID TP2B_HUMAN STANDARD; PRT; 1626 AA. AC Q02880; Q9UQP8; Q13600; Q9UMG8; DT 01-JUL-1993 (Rel. 26, Created) DT 01-MAR-2002 (Rel. 41, Last sequence update) DT 01-MAR-2002 (Rel. 41, Last annotation update) DE DNA topoisomerase II, beta isozyme (EC 5.99.1.3). GN TOP2B. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93087165; PubMed=1333583; RA Jenkins J.R., Ayton P., Jones T., Davies S.L., Simmons D.L., RA Harris A.L., Sheer D., Hickson I.D.; RT "Isolation of cDNA clones encoding the beta isozyme of human DNA RT topoisomerase II and localisation of the gene to chromosome 3p24."; RL Nucleic Acids Res. 20:5587-5592(1992). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=93192319; PubMed=8383537; RA Austin C.A., Sng J.H., Patel S., Fisher L.M.; RT "Novel HeLa topoisomerase II is the II beta isoform: complete coding RT sequence and homology with other type II topoisomerases."; RL Biochim. Biophys. Acta 1172:283-291(1993). RN [3] RP SEQUENCE OF 149-1034 FROM N.A. RX MEDLINE=90083281; PubMed=2556712; RA Chung T.D., Drake F.H., Tan K.B., Per S.R., Crooke S.T., RA Mirabelli C.K.; RT "Characterization and immunological identification of cDNA clones RT encoding two human DNA topoisomerase II isozymes."; RL Proc. Natl. Acad. Sci. U.S.A. 86:9431-9435(1989). RN [4] RP SEQUENCE OF 910-1626 FROM N.A. RX MEDLINE=99196712; PubMed=10095062; 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 RT IIalpha and IIbeta genes: evidence for isoform evolution through gene RT duplication."; RL Biochim. Biophys. Acta 1444:395-406(1999). RN [5] RP SEQUENCE OF 1038-1271 FROM N.A. RX MEDLINE=90306333; PubMed=2163884; RA Austin C.A., Fisher L.M.; RT "Isolation and characterization of a human cDNA clone encoding a RT novel DNA topoisomerase II homologue from HeLa cells."; RL FEBS Lett. 266:115-117(1990). RN [6] RP SEQUENCE OF 1277-1626 FROM N.A. RA Yuwen H.; RT "Binding of wild-type p53 by topoisomerase II and overexpression of RT topoisomerase II in human hepatocellular carcinoma."; RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases. RN [7] RP ALTERNATIVE SPLICING. RX MEDLINE=93376494; PubMed=8396237; RA Davies S.L., Jenkins J.R., Hickson I.D.; RT "Human cells express two differentially spliced forms of RT topoisomerase II beta mRNA."; RL Nucleic Acids Res. 21:3719-3723(1993). CC -!- FUNCTION: CONTROL OF TOPOLOGICAL STATES OF DNA BY TRANSIENT CC BREAKAGE AND SUBSEQUENT REJOINING OF DNA STRANDS. TOPOISOMERASE II CC MAKES DOUBLE-STRAND BREAKS. CC -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining CC of double-stranded DNA. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: NUCLEAR; NUCLEOLUS. CC -!- ALTERNATIVE PRODUCTS: 2 ISOFORMS; BETA-1 AND BETA-2 (SHOWN HERE); CC ARE PRODUCED BY ALTERNATIVE SPLICING. CC -!- PTM: PHOSPHORYLATED. CC -!- MISCELLANEOUS: EUKARYOTIC TOPOISOMERASE I AND II CAN RELAX BOTH CC NEGATIVE AND POSITIVE SUPERCOILS, WHEREAS PROKARYOTIC ENZYMES CC RELAX ONLY NEGATIVE SUPERCOILS. CC -!- SIMILARITY: BELONGS TO THE TYPE II TOPOISOMERASE FAMILY. 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; X68060; CAA48197.1; -. DR EMBL; X71911; -; NOT_ANNOTATED_CDS. DR EMBL; Z15111; CAA78815.1; -. DR EMBL; Z15115; CAA78821.1; -. DR EMBL; M27504; AAA61210.1; -. DR EMBL; AJ011721; CAA09753.1; -. DR EMBL; AJ011722; CAA09753.1; JOINED. DR EMBL; AJ011723; CAA09753.1; JOINED. DR EMBL; AJ011724; CAA09753.1; JOINED. DR EMBL; AJ011725; CAA09753.1; JOINED. DR EMBL; AJ011726; CAA09753.1; JOINED. DR EMBL; AJ011727; CAA09753.1; JOINED. DR EMBL; AJ011728; CAA09753.1; JOINED. DR EMBL; AJ011729; CAA09753.1; JOINED. DR EMBL; AJ011730; CAA09753.1; JOINED. DR EMBL; AJ011731; CAA09753.1; JOINED. DR EMBL; AJ011732; CAA09753.1; JOINED. DR EMBL; X53662; CAA37706.1; -. DR EMBL; U54831; AAB01982.1; -. DR PIR; S26730; S26730. DR PIR; S10710; S10710. DR PIR; S41641; S41641. DR HSSP; P06786; 1BGW. DR MIM; 126431; -. DR InterPro; IPR003957; CBFA_NFYB_topis. DR InterPro; IPR001241; DNA_topoisoII. DR InterPro; IPR002205; DNA_topoisoIV. DR InterPro; IPR003594; HATPase_c. DR Pfam; PF00204; DNA_gyraseB; 1. DR Pfam; PF00521; DNA_topoisoIV; 1. DR Pfam; PF02518; HATPase_c; 1. DR PRINTS; PR00615; CCAATSUBUNTA. DR PRINTS; PR00418; TPI2FAMILY. DR ProDom; PD000742; DNA_topoisoIV; 1. DR SMART; SM00433; TOP2c; 1. DR SMART; SM00434; TOP4c; 1. DR PROSITE; PS00177; TOPOISOMERASE_II; 1. KW Isomerase; Topoisomerase; DNA-binding; ATP-binding; Phosphorylation; KW Alternative splicing; Nuclear protein. FT NP_BIND 182 187 ATP (POTENTIAL). FT ACT_SITE 826 826 DNA CLEAVAGE (BY SIMILARITY). FT VARSPLIC 24 28 MISSING (IN ISOFORM BETA-1). FT CONFLICT 1431 1431 T -> S (IN REF. 4). FT CONFLICT 1611 1611 A -> T (IN REF. 1). FT CONFLICT 1621 1621 D -> H (IN REF. 4). SQ SEQUENCE 1626 AA; 183266 MW; E60E9262CC68B05D CRC64; MAKSGGCGAG AGVGGGNGAL TWVTLFDQNN AAKKEESETA NKNDSSKKLS VERVYQKKTQ LEHILLRPDT YIGSVEPLTQ FMWVYDEDVG MNCREVTFVP GLYKIFDEIL VNAADNKQRD KNMTCIKVSI DPESNIISIW NNGKGIPVVE HKVEKVYVPA LIFGQLLTSS NYDDDEKKVT GGRNGYGAKL CNIFSTKFTV ETACKEYKHS FKQTWMNNMM KTSEAKIKHF DGEDYTCITF QPDLSKFKME KLDKDIVALM TRRAYDLAGS CRGVKVMFNG KKLPVNGFRS YVDLYVKDKL DETGVALKVI HELANERWDV CLTLSEKGFQ QISFVNSIAT TKGGRHVDYV VDQVVGKLIE VVKKKNKAGV SVKPFQVKNH IWVFINCLIE NPTFDSQTKE NMTLQPKSFG SKCQLSEKFF KAASNCGIVE SILNWVKFKA QTQLNKKCSS VKYSKIKGIP KLDDANDAGG KHSLECTLIL TEGDSAKSLA VSGLGVIGRD RYGVFPLRGK ILNVREASHK QIMENAEINN IIKIVGLQYK KSYDDAESLK TLRYGKIMIM TDQDQDGSHI KGLLINFIHH NWPSLLKHGF LEEFITPIVK ASKNKQELSF YSIPEFDEWK KHIENQKAWK IKYYKGLGTS TAKEAKEYFA DMERHRILFR YAGPEDDAAI TLAFSKKKID DRKEWLTNFM EDRRQRRLHG LPEQFLYGTA TKHLTYNDFI NKELILFSNS DNERSIPSLV DGFKPGQRKV LFTCFKRNDK REVKVAQLAG SVAEMSAYHH GEQALMMTIV NLAQNFVGSN NINLLQPIGQ FGTRLHGGKD AASPRYIFTM LSTLARLLFP AVDDNLLKFL YDDNQRVEPE WYIPIIPMVL INGAEGIGTG WACKLPNYDA REIVNNVRRM LDGLDPHPML PNYKNFKGTI QELGQNQYAV SGEIFVVDRN TVEITELPVR TWTQVYKEQV LEPMLNGTDK TPALISDYKE YHTDTTVKFV VKMTEEKLAQ AEAAGLHKVF KLQTTLTCNS MVLFDHMGCL KKYETVQDIL KEFFDLRLSY YGLRKEWLVG MLGAESTKLN NQARFILEKI QGKITIENRS KKDLIQMLVQ RGYESDPVKA WKEAQEKAAE EDETQNQHDD SSSDSGTPSG PDFNYILNMS LWSLTKEKVE ELIKQRDAKG REVNDLKRKS PSDLWKEDLA AFVEELDKVE SQEREDVLAG MSGKAIKGKV GKPKVKKLQL EETMPSPYGR RIIPEITAMK ADASKKLLKK KKGDLDTAAV KVEFDEEFSG APVEGAGEEA LTPSVPINKG PKPKREKKEP GTRVRKTPTS SGKPSAKKVK KRNPWSDDES KSESDLEETE PVVIPRDSLL RRAAAERPKY TFDFSEEEDD DADDDDDDNN DLEELKVKAS PITNDGEDEF VPSDGLDKDE YTFSPGKSKA TPEKSLHDKK SQDFGNLFSF PSYSQKSEDD SAKFDSNEED SASVFSPSFG LKQTDKVPSK TVAAKKGKPS SDTVPKPKRA PKQKKVVEAV NSDSDSEFGI PKKTTTPKGK GRGAKKRKAS GSENEGDYNP GRKTSKTTSK KPKKTSFDQD SDVDIFPSDF PTEPPSLPRT GRARKEVKYF AESDEEEDDV DFAMFN //