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Q02880 (TOP2B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA topoisomerase 2-beta

EC=5.99.1.3
Alternative name(s):
DNA topoisomerase II, beta isozyme
Gene names
Name:TOP2B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1626 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks. Indirectly involved in vitamin D-coupled transcription regulation via its association with the WINAC complex, a chromatin-remodeling complex recruited by vitamin D receptor (VDR), which is required for the ligand-bound VDR-mediated transrepression of the CYP27B1 gene. Ref.8 Ref.10

Catalytic activity

ATP-dependent breakage, passage and rejoining of double-stranded DNA. Ref.8

Cofactor

Magnesium. Binds two Mg2+ per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn2+ and Ca2+. Ref.8 Ref.23

Subunit structure

Homodimer. Component of the WINAC complex, at least composed of SMARCA2, SMARCA4, SMARCB1, SMARCC1, SMARCC2, SMARCD1, SMARCE1, ACTL6A, BAZ1B/WSTF, ARID1A, SUPT16H, CHAF1A and TOP2B. Ref.10 Ref.23

Subcellular location

Cytoplasm. Nucleusnucleolus.

Miscellaneous

Eukaryotic topoisomerase I and II can relax both negative and positive supercoils, whereas prokaryotic enzymes relax only negative supercoils.

Sequence similarities

Belongs to the type II topoisomerase family.

Contains 1 Toprim domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   LigandATP-binding
DNA-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionIsomerase
Topoisomerase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.8. Source: GOC

DNA topological change

Inferred from direct assay Ref.8. Source: UniProtKB

DNA-dependent DNA replication

Inferred from Biological aspect of Ancestor. Source: RefGenome

axonogenesis

Inferred from electronic annotation. Source: Ensembl

chromosome segregation

Inferred from Biological aspect of Ancestor. Source: RefGenome

forebrain development

Inferred from electronic annotation. Source: Ensembl

mitotic recombination

Inferred from Biological aspect of Ancestor. Source: RefGenome

neuron migration

Inferred from electronic annotation. Source: Ensembl

resolution of meiotic recombination intermediates

Inferred from Biological aspect of Ancestor. Source: RefGenome

sister chromatid segregation

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentWINAC complex

Inferred from direct assay Ref.10. Source: BHF-UCL

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Inferred from direct assay PubMed 9049244. Source: UniProtKB

nucleoplasm

Inferred from direct assay PubMed 9049244. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 17567603PubMed 9049244. Source: UniProtKB

synaptonemal complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding, bending

Inferred from electronic annotation. Source: InterPro

DNA topoisomerase type II (ATP-hydrolyzing) activity

Inferred from direct assay Ref.8. Source: UniProtKB

chromatin binding

Inferred from direct assay PubMed 9049244. Source: UniProtKB

enzyme binding

Inferred from physical interaction PubMed 17567603. Source: UniProtKB

histone deacetylase binding

Inferred from physical interaction PubMed 11062478PubMed 11136718. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein C-terminus binding

Inferred from physical interaction PubMed 10666337. Source: UniProtKB

protein heterodimerization activity

Inferred from physical interaction PubMed 10473615. Source: UniProtKB

protein kinase C binding

Inferred from physical interaction PubMed 16611985. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Beta-2 (identifier: Q02880-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Beta-1 (identifier: Q02880-2)

The sequence of this isoform differs from the canonical sequence as follows:
     24-28: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 16261625DNA topoisomerase 2-beta
PRO_0000145369

Regions

Domain476 – 593118Toprim
Nucleotide binding169 – 1713ATP By similarity
Nucleotide binding182 – 1898ATP By similarity
Nucleotide binding397 – 3993ATP By similarity
Region363 – 3653Interaction with DNA By similarity
Region1011 – 102010Interaction with DNA
Motif1034 – 104411Nuclear export signal

Sites

Active site8261O-(5'-phospho-DNA)-tyrosine intermediate Ref.23
Metal binding4821Magnesium 1; catalytic By similarity
Metal binding5621Magnesium 1; catalytic By similarity
Metal binding5621Magnesium 2
Metal binding5641Magnesium 2
Binding site1121ATP By similarity
Binding site1411ATP By similarity
Site5101Interaction with DNA
Site5131Interaction with DNA
Site6821Interaction with DNA
Site6831Interaction with DNA
Site7441Interaction with DNA
Site7781Interaction with DNA By similarity
Site8251Transition state stabilizer
Site8771Important for DNA bending; intercalates between base pairs of target DNA
Site9521Interaction with DNA

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue31N6-acetyllysine By similarity
Modified residue12361Phosphoserine Ref.19 Ref.20
Modified residue12921Phosphothreonine Ref.19
Modified residue13361Phosphoserine Ref.11 Ref.17 Ref.20 Ref.22
Modified residue13401Phosphoserine Ref.11 Ref.17 Ref.20 Ref.22
Modified residue13421Phosphoserine Ref.17 Ref.19 Ref.20 Ref.22
Modified residue13441Phosphoserine Ref.17 Ref.19 Ref.20 Ref.22
Modified residue13581Phosphoserine Ref.22
Modified residue13751Phosphoserine Ref.17 Ref.19
Modified residue14001Phosphoserine Ref.11 Ref.15 Ref.17 Ref.19 Ref.20 Ref.22
Modified residue14031Phosphothreonine Ref.19
Modified residue14131Phosphoserine Ref.11 Ref.15 Ref.17 Ref.19 Ref.20 Ref.22
Modified residue14211Phosphotyrosine Ref.17
Modified residue14241Phosphoserine Ref.17 Ref.19 Ref.20 Ref.22
Modified residue14411Phosphoserine Ref.20 Ref.22
Modified residue14521Phosphoserine Ref.20
Modified residue14541Phosphoserine Ref.14 Ref.20 Ref.22
Modified residue14611Phosphoserine Ref.19
Modified residue14661Phosphoserine Ref.17 Ref.19 Ref.20 Ref.22
Modified residue14731Phosphoserine Ref.19
Modified residue14761Phosphoserine Ref.19 Ref.20
Modified residue15221Phosphoserine Ref.19 Ref.20 Ref.22
Modified residue15241Phosphoserine Ref.19 Ref.20 Ref.22
Modified residue15261Phosphoserine Ref.19 Ref.20
Modified residue15501Phosphoserine Ref.17 Ref.22
Modified residue15521Phosphoserine Ref.17
Modified residue15751Phosphothreonine Ref.19
Modified residue15811Phosphoserine Ref.15 Ref.17 Ref.19 Ref.22
Modified residue15921Phosphothreonine Ref.17
Modified residue15961Phosphoserine Ref.17
Modified residue16091Phosphotyrosine Ref.17
Modified residue16131Phosphoserine Ref.17 Ref.20 Ref.22

Natural variations

Alternative sequence24 – 285Missing in isoform Beta-1.
VSP_006532

Experimental info

Mutagenesis4821E → Q: Strongly reduced enzyme activity. Ref.8
Mutagenesis4851S → A: Slightly reduced enzyme activity. Ref.8
Mutagenesis5081R → E: Slightly reduced enzyme activity. Ref.8
Mutagenesis5101K → E: Strongly reduced enzyme activity. Ref.8
Mutagenesis5151R → Q: Slightly reduced enzyme activity. Ref.8
Sequence conflict14311T → S in CAA78821. Ref.4
Sequence conflict14311T → S in CAA09753. Ref.4
Sequence conflict16111A → T in CAA48197. Ref.1
Sequence conflict16211D → H in CAA09753. Ref.4

Secondary structure

.................................................................................................................. 1626
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Beta-2 [UniParc].

Last modified January 31, 2002. Version 3.
Checksum: E60E9262CC68B05D

FASTA1,626183,267
        10         20         30         40         50         60 
MAKSGGCGAG AGVGGGNGAL TWVTLFDQNN AAKKEESETA NKNDSSKKLS VERVYQKKTQ 

        70         80         90        100        110        120 
LEHILLRPDT YIGSVEPLTQ FMWVYDEDVG MNCREVTFVP GLYKIFDEIL VNAADNKQRD 

       130        140        150        160        170        180 
KNMTCIKVSI DPESNIISIW NNGKGIPVVE HKVEKVYVPA LIFGQLLTSS NYDDDEKKVT 

       190        200        210        220        230        240 
GGRNGYGAKL CNIFSTKFTV ETACKEYKHS FKQTWMNNMM KTSEAKIKHF DGEDYTCITF 

       250        260        270        280        290        300 
QPDLSKFKME KLDKDIVALM TRRAYDLAGS CRGVKVMFNG KKLPVNGFRS YVDLYVKDKL 

       310        320        330        340        350        360 
DETGVALKVI HELANERWDV CLTLSEKGFQ QISFVNSIAT TKGGRHVDYV VDQVVGKLIE 

       370        380        390        400        410        420 
VVKKKNKAGV SVKPFQVKNH IWVFINCLIE NPTFDSQTKE NMTLQPKSFG SKCQLSEKFF 

       430        440        450        460        470        480 
KAASNCGIVE SILNWVKFKA QTQLNKKCSS VKYSKIKGIP KLDDANDAGG KHSLECTLIL 

       490        500        510        520        530        540 
TEGDSAKSLA VSGLGVIGRD RYGVFPLRGK ILNVREASHK QIMENAEINN IIKIVGLQYK 

       550        560        570        580        590        600 
KSYDDAESLK TLRYGKIMIM TDQDQDGSHI KGLLINFIHH NWPSLLKHGF LEEFITPIVK 

       610        620        630        640        650        660 
ASKNKQELSF YSIPEFDEWK KHIENQKAWK IKYYKGLGTS TAKEAKEYFA DMERHRILFR 

       670        680        690        700        710        720 
YAGPEDDAAI TLAFSKKKID DRKEWLTNFM EDRRQRRLHG LPEQFLYGTA TKHLTYNDFI 

       730        740        750        760        770        780 
NKELILFSNS DNERSIPSLV DGFKPGQRKV LFTCFKRNDK REVKVAQLAG SVAEMSAYHH 

       790        800        810        820        830        840 
GEQALMMTIV NLAQNFVGSN NINLLQPIGQ FGTRLHGGKD AASPRYIFTM LSTLARLLFP 

       850        860        870        880        890        900 
AVDDNLLKFL YDDNQRVEPE WYIPIIPMVL INGAEGIGTG WACKLPNYDA REIVNNVRRM 

       910        920        930        940        950        960 
LDGLDPHPML PNYKNFKGTI QELGQNQYAV SGEIFVVDRN TVEITELPVR TWTQVYKEQV 

       970        980        990       1000       1010       1020 
LEPMLNGTDK TPALISDYKE YHTDTTVKFV VKMTEEKLAQ AEAAGLHKVF KLQTTLTCNS 

      1030       1040       1050       1060       1070       1080 
MVLFDHMGCL KKYETVQDIL KEFFDLRLSY YGLRKEWLVG MLGAESTKLN NQARFILEKI 

      1090       1100       1110       1120       1130       1140 
QGKITIENRS KKDLIQMLVQ RGYESDPVKA WKEAQEKAAE EDETQNQHDD SSSDSGTPSG 

      1150       1160       1170       1180       1190       1200 
PDFNYILNMS LWSLTKEKVE ELIKQRDAKG REVNDLKRKS PSDLWKEDLA AFVEELDKVE 

      1210       1220       1230       1240       1250       1260 
SQEREDVLAG MSGKAIKGKV GKPKVKKLQL EETMPSPYGR RIIPEITAMK ADASKKLLKK 

      1270       1280       1290       1300       1310       1320 
KKGDLDTAAV KVEFDEEFSG APVEGAGEEA LTPSVPINKG PKPKREKKEP GTRVRKTPTS 

      1330       1340       1350       1360       1370       1380 
SGKPSAKKVK KRNPWSDDES KSESDLEETE PVVIPRDSLL RRAAAERPKY TFDFSEEEDD 

      1390       1400       1410       1420       1430       1440 
DADDDDDDNN DLEELKVKAS PITNDGEDEF VPSDGLDKDE YTFSPGKSKA TPEKSLHDKK 

      1450       1460       1470       1480       1490       1500 
SQDFGNLFSF PSYSQKSEDD SAKFDSNEED SASVFSPSFG LKQTDKVPSK TVAAKKGKPS 

      1510       1520       1530       1540       1550       1560 
SDTVPKPKRA PKQKKVVEAV NSDSDSEFGI PKKTTTPKGK GRGAKKRKAS GSENEGDYNP 

      1570       1580       1590       1600       1610       1620 
GRKTSKTTSK KPKKTSFDQD SDVDIFPSDF PTEPPSLPRT GRARKEVKYF AESDEEEDDV 


DFAMFN 

« Hide

Isoform Beta-1 [UniParc].

Checksum: B1C091BF539F2391
Show »

FASTA1,621182,663

References

« Hide 'large scale' references
[1]"Isolation of cDNA clones encoding the beta isozyme of human DNA topoisomerase II and localisation of the gene to chromosome 3p24."
Jenkins J.R., Ayton P., Jones T., Davies S.L., Simmons D.L., Harris A.L., Sheer D., Hickson I.D.
Nucleic Acids Res. 20:5587-5592(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Novel HeLa topoisomerase II is the II beta isoform: complete coding sequence and homology with other type II topoisomerases."
Austin C.A., Sng J.H., Patel S., Fisher L.M.
Biochim. Biophys. Acta 1172:283-291(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Characterization and immunological identification of cDNA clones encoding two human DNA topoisomerase II isozymes."
Chung T.D., Drake F.H., Tan K.B., Per S.R., Crooke S.T., Mirabelli C.K.
Proc. Natl. Acad. Sci. U.S.A. 86:9431-9435(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 149-1034.
[4]"Molecular cloning and characterization of the human topoisomerase IIalpha and IIbeta genes: evidence for isoform evolution through gene duplication."
Sng J.H., Heaton V.J., Bell M., Mani P., Austin C.A., Fisher L.M.
Biochim. Biophys. Acta 1444:395-406(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 910-1626.
[5]"Isolation and characterization of a human cDNA clone encoding a novel DNA topoisomerase II homologue from HeLa cells."
Austin C.A., Fisher L.M.
FEBS Lett. 266:115-117(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 1038-1271.
[6]"Binding of wild-type p53 by topoisomerase II and overexpression of topoisomerase II in human hepatocellular carcinoma."
Yuwen H., Hsia C.C., Nakashima Y., Evangelista A., Tabor E.
Biochem. Biophys. Res. Commun. 234:194-197(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 1277-1626.
[7]"Human cells express two differentially spliced forms of topoisomerase II beta mRNA."
Davies S.L., Jenkins J.R., Hickson I.D.
Nucleic Acids Res. 21:3719-3723(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING.
[8]"Mutagenesis of E477 or K505 in the B' domain of human topoisomerase II beta increases the requirement for magnesium ions during strand passage."
West K.L., Meczes E.L., Thorn R., Turnbull R.M., Marshall R., Austin C.A.
Biochemistry 39:1223-1233(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: COFACTOR, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-482; SER-485; ARG-508; LYS-510 AND ARG-515.
[9]"Identification of functional nuclear export sequences in human topoisomerase IIalpha and beta."
Mirski S.E., Bielawski J.C., Cole S.P.
Biochem. Biophys. Res. Commun. 306:905-911(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEAR EXPORT SIGNAL.
[10]"The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome."
Kitagawa H., Fujiki R., Yoshimura K., Mezaki Y., Uematsu Y., Matsui D., Ogawa S., Unno K., Okubo M., Tokita A., Nakagawa T., Ito T., Ishimi Y., Nagasawa H., Matsumoto T., Yanagisawa J., Kato S.
Cell 113:905-917(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE WINAC COMPLEX, FUNCTION.
[11]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1336; SER-1340; SER-1400 AND SER-1413, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Prostate cancer.
[14]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
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.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1454, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[15]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1400; SER-1413 AND SER-1581, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[17]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: 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; SER-1526; THR-1575 AND SER-1581, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[20]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Structural basis of type II topoisomerase inhibition by the anticancer drug etoposide."
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.
Science 333:459-462(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) OF 450-1206 IN COMPLEX WITH DNA; MAGNESIUM AND ETOPOSIDE, ACTIVE SITE, COFACTOR, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X68060 mRNA. Translation: CAA48197.1.
X71911 Genomic DNA. No translation available.
Z15111 mRNA. Translation: CAA78815.1.
Z15115 mRNA. Translation: CAA78821.1.
M27504 mRNA. Translation: AAA61210.1.
AJ011721 expand/collapse EMBL AC list , AJ011722, AJ011723, AJ011724, AJ011725, AJ011726, AJ011727, AJ011728, AJ011729, AJ011730, AJ011731, AJ011732 Genomic DNA. Translation: CAA09753.1.
X53662 mRNA. Translation: CAA37706.1.
U54831 mRNA. Translation: AAB01982.1.
PIRA39242. S26730.
RefSeqNP_001059.2. NM_001068.3.
XP_005265484.1. XM_005265427.1.
UniGeneHs.475733.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3QX3X-ray2.16A/B450-1206[»]
4G0UX-ray2.70A/B450-1206[»]
4G0VX-ray2.55A/B450-1206[»]
4G0WX-ray2.70A/B450-1206[»]
4J3NX-ray2.30A/B450-1206[»]
ProteinModelPortalQ02880.
SMRQ02880. Positions 50-1206.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113008. 43 interactions.
IntActQ02880. 4 interactions.
MINTMINT-155585.
STRING9606.ENSP00000396704.

Chemistry

BindingDBQ02880.
ChEMBLCHEMBL3396.

PTM databases

PhosphoSiteQ02880.

Polymorphism databases

DMDM20141946.

Proteomic databases

PaxDbQ02880.
PRIDEQ02880.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264331; ENSP00000264331; ENSG00000077097. [Q02880-1]
ENST00000435706; ENSP00000396704; ENSG00000077097. [Q02880-2]
GeneID7155.
KEGGhsa:7155.
UCSCuc003cdj.3. human. [Q02880-2]
uc011awn.1. human. [Q02880-1]

Organism-specific databases

CTD7155.
GeneCardsGC03M025639.
H-InvDBHIX0030807.
HGNCHGNC:11990. TOP2B.
HPACAB004601.
HPA024120.
HPA050441.
MIM126431. gene.
neXtProtNX_Q02880.
PharmGKBPA36672.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0187.
HOGENOMHOG000216693.
HOVERGENHBG052998.
InParanoidQ02880.
KOK03164.
OMARHIDYVV.
OrthoDBEOG73JKTM.
PhylomeDBQ02880.
TreeFamTF105282.

Gene expression databases

ArrayExpressQ02880.
BgeeQ02880.
CleanExHS_TOP2B.
GenevestigatorQ02880.

Family and domain databases

Gene3D1.10.268.10. 1 hit.
3.30.1360.40. 1 hit.
3.30.230.10. 1 hit.
3.30.565.10. 1 hit.
3.40.50.670. 1 hit.
3.90.199.10. 1 hit.
InterProIPR024946. Arg_repress_C-like.
IPR012542. DTHCT.
IPR003594. HATPase_ATP-bd.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR028467. Top2b.
IPR001241. Topo_IIA.
IPR002205. Topo_IIA_A/C.
IPR013758. Topo_IIA_A/C_ab.
IPR013757. Topo_IIA_A_a.
IPR013506. Topo_IIA_bsu_dom2.
IPR013759. Topo_IIA_cen_dom.
IPR013760. Topo_IIA_like_dom.
IPR018522. TopoIIA_CS.
IPR006171. Toprim_domain.
[Graphical view]
PANTHERPTHR10169:SF18. PTHR10169:SF18. 1 hit.
PfamPF00204. DNA_gyraseB. 1 hit.
PF00521. DNA_topoisoIV. 1 hit.
PF08070. DTHCT. 1 hit.
PF02518. HATPase_c. 1 hit.
PF01751. Toprim. 1 hit.
[Graphical view]
PRINTSPR00418. TPI2FAMILY.
SMARTSM00387. HATPase_c. 1 hit.
SM00433. TOP2c. 1 hit.
SM00434. TOP4c. 1 hit.
[Graphical view]
SUPFAMSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
SSF56719. SSF56719. 1 hit.
PROSITEPS00177. TOPOISOMERASE_II. 1 hit.
PS50880. TOPRIM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTOP2B. human.
GeneWikiTOP2B.
GenomeRNAi7155.
NextBio27998.
PROQ02880.
SOURCESearch...

Entry information

Entry nameTOP2B_HUMAN
AccessionPrimary (citable) accession number: Q02880
Secondary accession number(s): Q13600, Q9UMG8, Q9UQP8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 31, 2002
Last modified: April 16, 2014
This is version 159 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM