Reviewed,
UniProtKB/Swiss-Prot Q02880 (TOP2B_HUMAN)
Last modified
June 16, 2009.
Version 107.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: DNA topoisomerase 2-beta EC=5.99.1.3 Alternative name(s): DNA topoisomerase II, beta isozyme | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 1626 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence 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 ivolved 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. |
| Catalytic activity | ATP-dependent breakage, passage and rejoining of double-stranded DNA. |
| 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. |
| Subcellular location | |
| Post-translational modification | Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 |
| 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. |
Ontologies
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 key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1626 | 1626 | DNA topoisomerase 2-beta | PRO_0000145369 | |||||
Regions | |||||||||
| Nucleotide binding | 182 – 187 | 6 | ATP Potential | ||||||
| Motif | 1034 – 1044 | 11 | Nuclear export signal | ||||||
Sites | |||||||||
| Active site | 826 | 1 | O-(5'-phospho-DNA)-tyrosine intermediate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 431 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 639 | 1 | Phosphothreonine Ref.11 | ||||||
| Modified residue | 640 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 1236 | 1 | Phosphoserine Ref.14 Ref.17 | ||||||
| Modified residue | 1336 | 1 | Phosphoserine Ref.11 Ref.17 | ||||||
| Modified residue | 1340 | 1 | Phosphoserine Ref.11 Ref.17 | ||||||
| Modified residue | 1342 | 1 | Phosphoserine Ref.11 Ref.17 | ||||||
| Modified residue | 1344 | 1 | Phosphoserine Ref.11 Ref.17 | ||||||
| Modified residue | 1375 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 1400 | 1 | Phosphoserine Ref.11 Ref.16 Ref.17 | ||||||
| Modified residue | 1413 | 1 | Phosphoserine Ref.11 Ref.16 Ref.17 | ||||||
| Modified residue | 1421 | 1 | Phosphotyrosine Ref.17 | ||||||
| Modified residue | 1424 | 1 | Phosphoserine Ref.16 Ref.17 | ||||||
| Modified residue | 1454 | 1 | Phosphoserine Ref.15 | ||||||
| Modified residue | 1466 | 1 | Phosphoserine Ref.10 Ref.17 | ||||||
| Modified residue | 1471 | 1 | Phosphoserine Ref.12 | ||||||
| Modified residue | 1522 | 1 | Phosphoserine Ref.10 Ref.11 Ref.12 Ref.13 Ref.17 | ||||||
| Modified residue | 1524 | 1 | Phosphoserine Ref.11 Ref.12 Ref.13 Ref.17 | ||||||
| Modified residue | 1526 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 1550 | 1 | Phosphoserine Ref.11 Ref.17 | ||||||
| Modified residue | 1552 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 1575 | 1 | Phosphothreonine Ref.16 | ||||||
| Modified residue | 1576 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 1581 | 1 | Phosphoserine Ref.16 Ref.17 | ||||||
| Modified residue | 1592 | 1 | Phosphothreonine Ref.17 | ||||||
| Modified residue | 1596 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 1609 | 1 | Phosphotyrosine Ref.17 | ||||||
| Modified residue | 1613 | 1 | Phosphoserine Ref.17 | ||||||
Natural variations | |||||||||
| Alternative sequence | 24 – 28 | 5 | Missing in isoform Beta-1. | VSP_006532 | |||||
Experimental info | |||||||||
| Sequence conflict | 1431 | 1 | T → S in CAA78821. Ref.4 | ||||||
| Sequence conflict | 1431 | 1 | T → S in CAA09753. Ref.4 | ||||||
| Sequence conflict | 1611 | 1 | A → T in CAA48197. Ref.1 | ||||||
| Sequence conflict | 1621 | 1 | D → H in CAA09753. Ref.4 | ||||||
Sequences
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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: 1333583] [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: 8383537] [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: 2556712] [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: 10095062] [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: 2163884] [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: 9168988] [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: 8396237] [Abstract] Cited for: ALTERNATIVE SPLICING. |
| [8] | "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: 12821127] [Abstract] Cited for: NUCLEAR EXPORT SIGNAL. |
| [9] | "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: 12837248] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE WINAC COMPLEX, FUNCTION. |
| [10] | "Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1466 AND SER-1522, MASS SPECTROMETRY. Tissue: Epithelium. |
| [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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-639; SER-640; SER-1336; SER-1340; SER-1342; SER-1344; SER-1400; SER-1413; SER-1522; SER-1524 AND SER-1550, MASS SPECTROMETRY. Tissue: Epithelium. |
| [12] | "Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1471; SER-1522 AND SER-1524, MASS SPECTROMETRY. Tissue: Epithelium. |
| [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: 17487921] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1522 AND SER-1524, MASS SPECTROMETRY. |
| [14] | "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1236, MASS SPECTROMETRY. Tissue: Epithelium. |
| [15] | "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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1454, MASS SPECTROMETRY. |
| [16] | "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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1400; SER-1413; SER-1424; THR-1575 AND SER-1581, MASS SPECTROMETRY. |
| [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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1236; SER-1336; SER-1340; SER-1342; SER-1344; SER-1375; SER-1400; SER-1413; TYR-1421; SER-1424; SER-1466; SER-1522; SER-1524; SER-1526; SER-1550; SER-1552; SER-1576; SER-1581; THR-1592; SER-1596; TYR-1609 AND SER-1613, MASS SPECTROMETRY. |
| [18] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| 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 AJ011732 Genomic DNA. Translation: CAA09753.1. X53662 mRNA. Translation: CAA37706.1. U54831 mRNA. Translation: AAB01982.1. | |
| IPI | IPI00027280. IPI00217709. |
| PIR | A39242. S26730. |
| RefSeq | NP_001059.2. |
| UniGene | Hs.475733 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1BJT based on UniProtKB P06786. |
| SMR | Q02880. Positions 50-426. |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | Q02880. |
Proteomic databases | |
| PRIDE | Q02880. |
Genome annotation databases | |
| Ensembl | ENSG00000077097. Homo sapiens. [Contig view] |
| GeneID | 7155. |
| KEGG | hsa:7155. |
| NMPDR | fig|9606.3.peg.22225. |
Organism-specific databases | |
| GeneCards | GC03M025614. |
| H-InvDB | HIX0030807. |
| HGNC | HGNC:11990. TOP2B. |
| HPA | CAB004601. |
| MIM | 126431. gene. |
| PharmGKB | PA36672. |
| GenAtlas | Search... |
Phylogenomic databases | |
| HOGENOM | Q02880. |
| HOVERGEN | Q02880. |
| OMA | Q02880. GAESTKL. |
Enzyme and pathway databases | |
| BRENDA | 5.99.1.3. 247. |
Gene expression databases | |
| ArrayExpress | Q02880. |
| Bgee | Q02880. |
| CleanEx | HS_TOP2B. |
| GermOnline | ENSG00000077097. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR003594. ATP_bd_ATPase. IPR012542. DTHCT. IPR002205. Topo_IIA_A/C. IPR013758. Topo_IIA_A/C_ab. IPR013757. Topo_IIA_A_a. IPR001241. Topo_IIA_B/N. IPR013759. Topo_IIA_B/N_ab. IPR013506. Topo_IIA_B_2. IPR018522. TopoIIA_CS. [Graphical view] |
| Gene3D | G3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit. G3DSA:3.90.199.10. Topo_IIA_A/C_ab. 1 hit. G3DSA:1.10.268.10. Topo_IIA_A_a. 1 hit. G3DSA:3.40.50.670. Topo_IIA_B/N_ab. 1 hit. |
| Pfam | PF00204. DNA_gyraseB. 1 hit. PF00521. DNA_topoisoIV. 1 hit. PF08070. DTHCT. 1 hit. PF02518. HATPase_c. 1 hit. [Graphical view] |
| PRINTS | PR00418. TPI2FAMILY. |
| ProDom | PD149633. DNA_gyrase_B. 1 hit. PD000742. DNA_topoisoIV. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| SMART | SM00387. HATPase_c. 1 hit. SM00433. TOP2c. 1 hit. SM00434. TOP4c. 1 hit. [Graphical view] |
| PROSITE | PS00177. TOPOISOMERASE_II. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 27998. |
| SOURCE | Search... |
Entry information
| Entry name | TOP2B_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q02880 Secondary accession number(s): Q13600, Q9UMG8, Q9UQP8 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 3 Human chromosome 3: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


