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

 TOP2B_HUMAN             Reviewed;        1626 AA.
Q02880; Q13600; Q9UMG8; Q9UQP8;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
31-JAN-2002, sequence version 3.
22-NOV-2017, entry version 198.
RecName: Full=DNA topoisomerase 2-beta;
EC=5.99.1.3;
AltName: Full=DNA topoisomerase II, beta isozyme;
Name=TOP2B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1333583; DOI=10.1093/nar/20.21.5587;
Jenkins J.R., Ayton P., Jones T., Davies S.L., Simmons D.L.,
Harris A.L., Sheer D., Hickson I.D.;
"Isolation of cDNA clones encoding the beta isozyme of human DNA
topoisomerase II and localisation of the gene to chromosome 3p24.";
Nucleic Acids Res. 20:5587-5592(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8383537; DOI=10.1016/0167-4781(93)90215-Y;
Austin C.A., Sng J.H., Patel S., Fisher L.M.;
"Novel HeLa topoisomerase II is the II beta isoform: complete coding
sequence and homology with other type II topoisomerases.";
Biochim. Biophys. Acta 1172:283-291(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 149-1034.
PubMed=2556712; DOI=10.1073/pnas.86.23.9431;
Chung T.D., Drake F.H., Tan K.B., Per S.R., Crooke S.T.,
Mirabelli C.K.;
"Characterization and immunological identification of cDNA clones
encoding two human DNA topoisomerase II isozymes.";
Proc. Natl. Acad. Sci. U.S.A. 86:9431-9435(1989).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 910-1626.
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 OF 1038-1271.
PubMed=2163884; DOI=10.1016/0014-5793(90)81520-X;
Austin C.A., Fisher L.M.;
"Isolation and characterization of a human cDNA clone encoding a novel
DNA topoisomerase II homologue from HeLa cells.";
FEBS Lett. 266:115-117(1990).
[6]
NUCLEOTIDE SEQUENCE OF 1277-1626.
PubMed=9168988; DOI=10.1006/bbrc.1997.6539;
Yuwen H., Hsia C.C., Nakashima Y., Evangelista A., Tabor E.;
"Binding of wild-type p53 by topoisomerase II and overexpression of
topoisomerase II in human hepatocellular carcinoma.";
Biochem. Biophys. Res. Commun. 234:194-197(1997).
[7]
ALTERNATIVE SPLICING.
PubMed=8396237; DOI=10.1093/nar/21.16.3719;
Davies S.L., Jenkins J.R., Hickson I.D.;
"Human cells express two differentially spliced forms of topoisomerase
II beta mRNA.";
Nucleic Acids Res. 21:3719-3723(1993).
[8]
COFACTOR, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLU-482;
SER-485; ARG-508; LYS-510 AND ARG-515.
PubMed=10684600; DOI=10.1021/bi991328b;
West K.L., Meczes E.L., Thorn R., Turnbull R.M., Marshall R.,
Austin C.A.;
"Mutagenesis of E477 or K505 in the B' domain of human topoisomerase
II beta increases the requirement for magnesium ions during strand
passage.";
Biochemistry 39:1223-1233(2000).
[9]
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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1336; SER-1340; SER-1400
AND SER-1413, 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).
[11]
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).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Prostate cancer;
PubMed=17487921; DOI=10.1002/elps.200600782;
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
"Toward a global characterization of the phosphoproteome in prostate
cancer cells: identification of phosphoproteins in the LNCaP cell
line.";
Electrophoresis 28:2027-2034(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1454, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1400; SER-1413 AND
SER-1581, 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).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1336; SER-1340;
SER-1342; SER-1344; SER-1375; SER-1400; SER-1413; TYR-1421; SER-1424;
SER-1466; SER-1550; SER-1552; SER-1581; THR-1592; SER-1596; TYR-1609
AND SER-1613, 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).
[17]
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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1236; THR-1292;
SER-1342; SER-1344; SER-1375; SER-1400; THR-1403; SER-1413; SER-1424;
SER-1461; SER-1466; SER-1473; SER-1476; SER-1522; SER-1524; THR-1575
AND SER-1581, 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).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1236; SER-1336;
SER-1340; SER-1342; SER-1344; SER-1400; SER-1413; SER-1424; SER-1441;
SER-1452; SER-1454; SER-1466; SER-1476; SER-1522; SER-1524; SER-1526
AND SER-1613, 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).
[20]
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).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1336; SER-1340;
SER-1342; SER-1344; SER-1358; SER-1400; SER-1413; SER-1424; SER-1441;
SER-1454; SER-1466; SER-1522; SER-1524; SER-1550; SER-1581 AND
SER-1613, 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).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1236; SER-1400;
SER-1413; SER-1424; SER-1452; SER-1454; SER-1466; SER-1522; SER-1524;
SER-1550 AND SER-1552, 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).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1400; SER-1413;
SER-1522; SER-1524; SER-1550; SER-1552; THR-1575; SER-1576 AND
SER-1581, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[24]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-34; LYS-1227; LYS-1271;
LYS-1440 AND LYS-1456, SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-28
(ISOFORM BETA-1), 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).
[25]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-177; LYS-373; LYS-437;
LYS-605; LYS-643; LYS-1227; LYS-1440 AND LYS-1456, SUMOYLATION [LARGE
SCALE ANALYSIS] AT LYS-28 (ISOFORM BETA-1), 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).
[26]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1250, 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).
[27]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-33; LYS-177; LYS-178;
LYS-228; LYS-299; LYS-367; LYS-373; LYS-437; LYS-439; LYS-446;
LYS-600; LYS-605; LYS-635; LYS-643; LYS-646; LYS-676; LYS-712;
LYS-1092; LYS-1214; LYS-1217; LYS-1226; LYS-1227; LYS-1250; LYS-1262;
LYS-1271; LYS-1323; LYS-1327; LYS-1398; LYS-1440; LYS-1456 AND
LYS-1490, SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-28 AND LYS-29
(ISOFORM BETA-1), 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).
[28]
X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) OF 450-1206 IN COMPLEX WITH
DNA; MAGNESIUM AND ETOPOSIDE, ACTIVE SITE, COFACTOR, AND SUBUNIT.
PubMed=21778401; DOI=10.1126/science.1204117;
Wu C.C., Li T.K., Farh L., Lin L.Y., Lin T.S., Yu Y.J., Yen T.J.,
Chiang C.W., Chan N.L.;
"Structural basis of type II topoisomerase inhibition by the
anticancer drug etoposide.";
Science 333:459-462(2011).
[29]
VARIANT TYR-63, AND INVOLVEMENT IN AUTISM SPECTRUM DISORDER.
PubMed=28343847; DOI=10.1016/j.cca.2017.03.022;
Lam C.W., Yeung W.L., Law C.Y.;
"Global developmental delay and intellectual disability associated
with a de novo TOP2B mutation.";
Clin. Chim. Acta 469:63-68(2017).
-!- FUNCTION: Control of topological states of DNA by transient
breakage and subsequent rejoining of DNA strands. Topoisomerase II
makes double-strand breaks. {ECO:0000269|PubMed:10684600}.
-!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining
of double-stranded DNA. {ECO:0000255|PROSITE-ProRule:PRU00995,
ECO:0000269|PubMed:10684600}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00995,
ECO:0000269|PubMed:10684600, ECO:0000269|PubMed:21778401};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00995,
ECO:0000269|PubMed:10684600, ECO:0000269|PubMed:21778401};
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00995,
ECO:0000269|PubMed:10684600, ECO:0000269|PubMed:21778401};
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:0000255|PROSITE-ProRule:PRU00995,
ECO:0000269|PubMed:10684600, ECO:0000269|PubMed:21778401};
-!- SUBUNIT: Homodimer (PubMed:21778401). Interacts with KIAA1210 (By
similarity). {ECO:0000250|UniProtKB:Q64511,
ECO:0000269|PubMed:21778401}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Beta-2;
IsoId=Q02880-1; Sequence=Displayed;
Name=Beta-1;
IsoId=Q02880-2; Sequence=VSP_006532;
Note=Contains a glycyl lysine isopeptide (Lys-Gly) (interchain
with G-Cter in SUMO2) at position 28. Contains a glycyl lysine
isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) at
position 29. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364, ECO:0000244|PubMed:28112733};
-!- DISEASE: Note=A defect in TOP2B is associated with autism spectrum
disorder (ASD). {ECO:0000269|PubMed:28343847}.
-!- 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; X68060; CAA48197.1; -; mRNA.
EMBL; X71911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z15111; CAA78815.1; -; mRNA.
EMBL; Z15115; CAA78821.1; -; mRNA.
EMBL; M27504; AAA61210.1; -; mRNA.
EMBL; AJ011721; CAA09753.1; -; Genomic_DNA.
EMBL; AJ011722; CAA09753.1; JOINED; Genomic_DNA.
EMBL; AJ011723; CAA09753.1; JOINED; Genomic_DNA.
EMBL; AJ011724; CAA09753.1; JOINED; Genomic_DNA.
EMBL; AJ011725; CAA09753.1; JOINED; Genomic_DNA.
EMBL; AJ011726; CAA09753.1; JOINED; Genomic_DNA.
EMBL; AJ011727; CAA09753.1; JOINED; Genomic_DNA.
EMBL; AJ011728; CAA09753.1; JOINED; Genomic_DNA.
EMBL; AJ011729; CAA09753.1; JOINED; Genomic_DNA.
EMBL; AJ011730; CAA09753.1; JOINED; Genomic_DNA.
EMBL; AJ011731; CAA09753.1; JOINED; Genomic_DNA.
EMBL; AJ011732; CAA09753.1; JOINED; Genomic_DNA.
EMBL; X53662; CAA37706.1; -; mRNA.
EMBL; U54831; AAB01982.1; -; mRNA.
CCDS; CCDS46776.1; -. [Q02880-2]
CCDS; CCDS82746.1; -. [Q02880-1]
PIR; S26730; A39242.
RefSeq; NP_001059.2; NM_001068.3. [Q02880-2]
RefSeq; NP_001317629.1; NM_001330700.1. [Q02880-1]
UniGene; Hs.475733; -.
PDB; 3QX3; X-ray; 2.16 A; A/B=450-1206.
PDB; 4G0U; X-ray; 2.70 A; A/B=450-1206.
PDB; 4G0V; X-ray; 2.55 A; A/B=450-1206.
PDB; 4G0W; X-ray; 2.70 A; A/B=450-1206.
PDB; 4J3N; X-ray; 2.30 A; A/B=450-1206.
PDB; 5GWI; X-ray; 2.74 A; A/B=450-1206.
PDB; 5GWJ; X-ray; 2.57 A; A/B=450-1206.
PDBsum; 3QX3; -.
PDBsum; 4G0U; -.
PDBsum; 4G0V; -.
PDBsum; 4G0W; -.
PDBsum; 4J3N; -.
PDBsum; 5GWI; -.
PDBsum; 5GWJ; -.
ProteinModelPortal; Q02880; -.
SMR; Q02880; -.
BioGrid; 113008; 73.
CORUM; Q02880; -.
IntAct; Q02880; 19.
MINT; MINT-155585; -.
STRING; 9606.ENSP00000396704; -.
BindingDB; Q02880; -.
ChEMBL; CHEMBL3396; -.
DrugBank; DB08651; 3'-THIO-THYMIDINE-5'-PHOSPHATE.
DrugBank; DB05488; 99mTc-ciprofloxacin.
DrugBank; DB05022; Amonafide.
DrugBank; DB00970; Dactinomycin.
DrugBank; DB00694; Daunorubicin.
DrugBank; DB00380; Dexrazoxane.
DrugBank; DB00773; Etoposide.
DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DrugBank; DB06042; ZEN-012.
iPTMnet; Q02880; -.
PhosphoSitePlus; Q02880; -.
SwissPalm; Q02880; -.
DMDM; 20141946; -.
EPD; Q02880; -.
MaxQB; Q02880; -.
PaxDb; Q02880; -.
PeptideAtlas; Q02880; -.
PRIDE; Q02880; -.
Ensembl; ENST00000264331; ENSP00000264331; ENSG00000077097. [Q02880-1]
Ensembl; ENST00000435706; ENSP00000396704; ENSG00000077097. [Q02880-2]
GeneID; 7155; -.
KEGG; hsa:7155; -.
UCSC; uc003cdj.4; human. [Q02880-1]
CTD; 7155; -.
DisGeNET; 7155; -.
EuPathDB; HostDB:ENSG00000077097.13; -.
GeneCards; TOP2B; -.
H-InvDB; HIX0030807; -.
HGNC; HGNC:11990; TOP2B.
HPA; CAB004601; -.
HPA; HPA024120; -.
HPA; HPA050441; -.
MIM; 126431; gene.
neXtProt; NX_Q02880; -.
OpenTargets; ENSG00000077097; -.
PharmGKB; PA36672; -.
eggNOG; KOG0355; Eukaryota.
eggNOG; COG0187; LUCA.
eggNOG; COG0188; LUCA.
GeneTree; ENSGT00390000016222; -.
HOGENOM; HOG000216693; -.
HOVERGEN; HBG052998; -.
InParanoid; Q02880; -.
KO; K03164; -.
OMA; ACKLPNY; -.
OrthoDB; EOG091G00U2; -.
PhylomeDB; Q02880; -.
TreeFam; TF105282; -.
BRENDA; 5.99.1.3; 2681.
Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins.
SIGNOR; Q02880; -.
ChiTaRS; TOP2B; human.
GeneWiki; TOP2B; -.
GenomeRNAi; 7155; -.
PRO; PR:Q02880; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000077097; -.
CleanEx; HS_TOP2B; -.
ExpressionAtlas; Q02880; baseline and differential.
Genevisible; Q02880; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; 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; IEA:UniProtKB-KW.
GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IDA:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
GO; GO:0005080; F:protein kinase C binding; IPI:UniProtKB.
GO; GO:0043021; F:ribonucleoprotein complex binding; ISS:UniProtKB.
GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
GO; GO:0006265; P:DNA topological change; IDA:UniProtKB.
GO; GO:0030900; P:forebrain development; IEA:Ensembl.
GO; GO:0044774; P:mitotic DNA integrity checkpoint; IBA:GO_Central.
GO; GO:0001764; P:neuron migration; IEA:Ensembl.
GO; GO:0016925; P:protein sumoylation; TAS:Reactome.
GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
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; -; 1.
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;
Autism spectrum disorder; Complete proteome; Cytoplasm;
Disease mutation; DNA-binding; Isomerase; Isopeptide bond; Magnesium;
Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Topoisomerase; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q64511}.
CHAIN 2 1626 DNA topoisomerase 2-beta.
/FTId=PRO_0000145369.
DOMAIN 476 593 Toprim. {ECO:0000255|PROSITE-
ProRule:PRU00995}.
NP_BIND 169 171 ATP. {ECO:0000250}.
NP_BIND 182 189 ATP. {ECO:0000250}.
NP_BIND 397 399 ATP. {ECO:0000250}.
REGION 363 365 Interaction with DNA. {ECO:0000250}.
REGION 1011 1020 Interaction with DNA.
MOTIF 1034 1044 Nuclear export signal.
ACT_SITE 826 826 O-(5'-phospho-DNA)-tyrosine intermediate.
{ECO:0000269|PubMed:21778401}.
METAL 482 482 Magnesium 1; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00995}.
METAL 562 562 Magnesium 1; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00995}.
METAL 562 562 Magnesium 2. {ECO:0000255|PROSITE-
ProRule:PRU00995,
ECO:0000269|PubMed:21778401}.
METAL 564 564 Magnesium 2. {ECO:0000255|PROSITE-
ProRule:PRU00995,
ECO:0000269|PubMed:21778401}.
BINDING 112 112 ATP. {ECO:0000250}.
BINDING 141 141 ATP. {ECO:0000250}.
SITE 510 510 Interaction with DNA.
SITE 513 513 Interaction with DNA.
SITE 682 682 Interaction with DNA.
SITE 683 683 Interaction with DNA.
SITE 744 744 Interaction with DNA.
SITE 778 778 Interaction with DNA.
{ECO:0000255|PROSITE-ProRule:PRU00995}.
SITE 825 825 Transition state stabilizer.
SITE 877 877 Important for DNA bending; intercalates
between base pairs of target DNA.
SITE 952 952 Interaction with DNA.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q64511}.
MOD_RES 3 3 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q64511}.
MOD_RES 1236 1236 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1292 1292 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 1336 1336 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 1340 1340 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 1342 1342 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 1344 1344 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 1358 1358 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1370 1370 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q64511}.
MOD_RES 1375 1375 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 1400 1400 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1403 1403 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 1413 1413 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1421 1421 Phosphotyrosine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1424 1424 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1441 1441 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 1452 1452 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1454 1454 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1461 1461 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 1466 1466 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1473 1473 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 1476 1476 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231}.
MOD_RES 1522 1522 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1524 1524 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1526 1526 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1550 1550 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1552 1552 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1575 1575 Phosphothreonine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:24275569}.
MOD_RES 1576 1576 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1581 1581 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 1592 1592 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1596 1596 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1609 1609 Phosphotyrosine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1613 1613 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
CROSSLNK 33 33 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 34 34 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447}.
CROSSLNK 177 177 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 178 178 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 228 228 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 299 299 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 367 367 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 373 373 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 437 437 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 439 439 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 446 446 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 600 600 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 605 605 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 635 635 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 643 643 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 646 646 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 676 676 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 712 712 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1092 1092 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1214 1214 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1217 1217 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1226 1226 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1227 1227 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 1250 1250 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 1262 1262 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1271 1271 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 1323 1323 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1327 1327 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1398 1398 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1440 1440 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 1456 1456 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 1490 1490 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 24 28 Missing (in isoform Beta-1).
{ECO:0000305}.
/FTId=VSP_006532.
VARIANT 63 63 H -> Y (probable disease-associated
mutation found in a patient with autism
spectrum disorder; dbSNP:rs886039770).
{ECO:0000269|PubMed:28343847}.
/FTId=VAR_079273.
MUTAGEN 482 482 E->Q: Strongly reduced enzyme activity.
{ECO:0000269|PubMed:10684600}.
MUTAGEN 485 485 S->A: Slightly reduced enzyme activity.
{ECO:0000269|PubMed:10684600}.
MUTAGEN 508 508 R->E: Slightly reduced enzyme activity.
{ECO:0000269|PubMed:10684600}.
MUTAGEN 510 510 K->E: Strongly reduced enzyme activity.
{ECO:0000269|PubMed:10684600}.
MUTAGEN 515 515 R->Q: Slightly reduced enzyme activity.
{ECO:0000269|PubMed:10684600}.
CONFLICT 1431 1431 T -> S (in Ref. 4; CAA78821/CAA09753).
{ECO:0000305}.
CONFLICT 1611 1611 A -> T (in Ref. 1; CAA48197).
{ECO:0000305}.
CONFLICT 1621 1621 D -> H (in Ref. 4; CAA09753).
{ECO:0000305}.
TURN 466 469 {ECO:0000244|PDB:3QX3}.
STRAND 470 472 {ECO:0000244|PDB:4G0U}.
HELIX 473 475 {ECO:0000244|PDB:3QX3}.
STRAND 477 482 {ECO:0000244|PDB:3QX3}.
HELIX 483 491 {ECO:0000244|PDB:3QX3}.
TURN 494 496 {ECO:0000244|PDB:5GWJ}.
HELIX 497 499 {ECO:0000244|PDB:3QX3}.
STRAND 502 507 {ECO:0000244|PDB:3QX3}.
HELIX 514 516 {ECO:0000244|PDB:4G0V}.
HELIX 519 524 {ECO:0000244|PDB:3QX3}.
HELIX 526 535 {ECO:0000244|PDB:3QX3}.
STRAND 545 547 {ECO:0000244|PDB:4G0V}.
HELIX 548 551 {ECO:0000244|PDB:3QX3}.
STRAND 555 560 {ECO:0000244|PDB:3QX3}.
HELIX 565 581 {ECO:0000244|PDB:3QX3}.
HELIX 583 587 {ECO:0000244|PDB:3QX3}.
STRAND 591 594 {ECO:0000244|PDB:3QX3}.
HELIX 644 650 {ECO:0000244|PDB:3QX3}.
HELIX 652 655 {ECO:0000244|PDB:3QX3}.
STRAND 656 660 {ECO:0000244|PDB:3QX3}.
HELIX 664 674 {ECO:0000244|PDB:3QX3}.
HELIX 676 678 {ECO:0000244|PDB:3QX3}.
HELIX 679 698 {ECO:0000244|PDB:3QX3}.
STRAND 713 715 {ECO:0000244|PDB:3QX3}.
HELIX 716 722 {ECO:0000244|PDB:3QX3}.
HELIX 724 735 {ECO:0000244|PDB:3QX3}.
TURN 739 741 {ECO:0000244|PDB:3QX3}.
HELIX 745 757 {ECO:0000244|PDB:3QX3}.
HELIX 765 776 {ECO:0000244|PDB:3QX3}.
HELIX 782 793 {ECO:0000244|PDB:3QX3}.
TURN 814 820 {ECO:0000244|PDB:3QX3}.
HELIX 824 826 {ECO:0000244|PDB:4J3N}.
HELIX 835 838 {ECO:0000244|PDB:3QX3}.
HELIX 841 844 {ECO:0000244|PDB:3QX3}.
STRAND 849 852 {ECO:0000244|PDB:3QX3}.
STRAND 855 860 {ECO:0000244|PDB:3QX3}.
HELIX 868 871 {ECO:0000244|PDB:3QX3}.
STRAND 875 877 {ECO:0000244|PDB:3QX3}.
STRAND 882 884 {ECO:0000244|PDB:3QX3}.
HELIX 890 901 {ECO:0000244|PDB:3QX3}.
STRAND 918 924 {ECO:0000244|PDB:3QX3}.
STRAND 927 931 {ECO:0000244|PDB:3QX3}.
STRAND 933 938 {ECO:0000244|PDB:3QX3}.
STRAND 941 946 {ECO:0000244|PDB:3QX3}.
HELIX 953 959 {ECO:0000244|PDB:3QX3}.
HELIX 961 966 {ECO:0000244|PDB:3QX3}.
STRAND 969 971 {ECO:0000244|PDB:3QX3}.
STRAND 976 980 {ECO:0000244|PDB:3QX3}.
STRAND 989 992 {ECO:0000244|PDB:3QX3}.
HELIX 995 1004 {ECO:0000244|PDB:3QX3}.
HELIX 1006 1009 {ECO:0000244|PDB:3QX3}.
STRAND 1013 1017 {ECO:0000244|PDB:3QX3}.
STRAND 1021 1024 {ECO:0000244|PDB:3QX3}.
STRAND 1030 1034 {ECO:0000244|PDB:3QX3}.
HELIX 1036 1080 {ECO:0000244|PDB:3QX3}.
HELIX 1091 1100 {ECO:0000244|PDB:3QX3}.
HELIX 1107 1114 {ECO:0000244|PDB:3QX3}.
HELIX 1144 1147 {ECO:0000244|PDB:3QX3}.
HELIX 1151 1154 {ECO:0000244|PDB:3QX3}.
HELIX 1156 1177 {ECO:0000244|PDB:3QX3}.
HELIX 1181 1205 {ECO:0000244|PDB:3QX3}.
SEQUENCE 1626 AA; 183267 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


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