Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q02880

- TOP2B_HUMAN

UniProt

Q02880 - TOP2B_HUMAN

Protein

DNA topoisomerase 2-beta

Gene

TOP2B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 3 (31 Jan 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.2 Publications

    Catalytic activityi

    ATP-dependent breakage, passage and rejoining of double-stranded DNA.1 PublicationPROSITE-ProRule annotation

    Cofactori

    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+.2 PublicationsPROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei112 – 1121ATPBy similarity
    Binding sitei141 – 1411ATPBy similarity
    Metal bindingi482 – 4821Magnesium 1; catalyticPROSITE-ProRule annotation
    Sitei510 – 5101Interaction with DNA
    Sitei513 – 5131Interaction with DNA
    Metal bindingi562 – 5621Magnesium 1; catalyticPROSITE-ProRule annotation
    Metal bindingi562 – 5621Magnesium 21 PublicationPROSITE-ProRule annotation
    Metal bindingi564 – 5641Magnesium 21 PublicationPROSITE-ProRule annotation
    Sitei682 – 6821Interaction with DNA
    Sitei683 – 6831Interaction with DNA
    Sitei744 – 7441Interaction with DNA
    Sitei778 – 7781Interaction with DNAPROSITE-ProRule annotation
    Sitei825 – 8251Transition state stabilizer
    Active sitei826 – 8261O-(5'-phospho-DNA)-tyrosine intermediate1 Publication
    Sitei877 – 8771Important for DNA bending; intercalates between base pairs of target DNA
    Sitei952 – 9521Interaction with DNA

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi169 – 1713ATPBy similarity
    Nucleotide bindingi182 – 1898ATPBy similarity
    Nucleotide bindingi397 – 3993ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. chromatin binding Source: UniProtKB
    3. DNA binding, bending Source: InterPro
    4. DNA topoisomerase type II (ATP-hydrolyzing) activity Source: UniProtKB
    5. enzyme binding Source: UniProtKB
    6. histone deacetylase binding Source: UniProtKB
    7. metal ion binding Source: UniProtKB-KW
    8. protein C-terminus binding Source: UniProtKB
    9. protein heterodimerization activity Source: UniProtKB
    10. protein kinase C binding Source: UniProtKB

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. axonogenesis Source: Ensembl
    3. DNA topological change Source: UniProtKB
    4. DNA unwinding involved in DNA replication Source: RefGenome
    5. forebrain development Source: Ensembl
    6. mitotic DNA integrity checkpoint Source: RefGenome
    7. mitotic recombination Source: RefGenome
    8. neuron migration Source: Ensembl
    9. resolution of meiotic recombination intermediates Source: RefGenome
    10. sister chromatid segregation Source: RefGenome

    Keywords - Molecular functioni

    Isomerase, Topoisomerase

    Keywords - Ligandi

    ATP-binding, DNA-binding, Magnesium, Metal-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA topoisomerase 2-beta (EC:5.99.1.3)
    Alternative name(s):
    DNA topoisomerase II, beta isozyme
    Gene namesi
    Name:TOP2B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:11990. TOP2B.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: UniProtKB
    3. DNA topoisomerase complex (ATP-hydrolyzing) Source: RefGenome
    4. nucleoplasm Source: UniProtKB
    5. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi482 – 4821E → Q: Strongly reduced enzyme activity. 1 Publication
    Mutagenesisi485 – 4851S → A: Slightly reduced enzyme activity. 1 Publication
    Mutagenesisi508 – 5081R → E: Slightly reduced enzyme activity. 1 Publication
    Mutagenesisi510 – 5101K → E: Strongly reduced enzyme activity. 1 Publication
    Mutagenesisi515 – 5151R → Q: Slightly reduced enzyme activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA36672.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 16261625DNA topoisomerase 2-betaPRO_0000145369Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei3 – 31N6-acetyllysineBy similarity
    Modified residuei1236 – 12361Phosphoserine2 Publications
    Modified residuei1292 – 12921Phosphothreonine1 Publication
    Modified residuei1336 – 13361Phosphoserine4 Publications
    Modified residuei1340 – 13401Phosphoserine4 Publications
    Modified residuei1342 – 13421Phosphoserine4 Publications
    Modified residuei1344 – 13441Phosphoserine4 Publications
    Modified residuei1358 – 13581Phosphoserine1 Publication
    Modified residuei1375 – 13751Phosphoserine2 Publications
    Modified residuei1400 – 14001Phosphoserine6 Publications
    Modified residuei1403 – 14031Phosphothreonine1 Publication
    Modified residuei1413 – 14131Phosphoserine6 Publications
    Modified residuei1421 – 14211Phosphotyrosine1 Publication
    Modified residuei1424 – 14241Phosphoserine4 Publications
    Modified residuei1441 – 14411Phosphoserine2 Publications
    Modified residuei1452 – 14521Phosphoserine1 Publication
    Modified residuei1454 – 14541Phosphoserine3 Publications
    Modified residuei1461 – 14611Phosphoserine1 Publication
    Modified residuei1466 – 14661Phosphoserine4 Publications
    Modified residuei1473 – 14731Phosphoserine1 Publication
    Modified residuei1476 – 14761Phosphoserine2 Publications
    Modified residuei1522 – 15221Phosphoserine3 Publications
    Modified residuei1524 – 15241Phosphoserine3 Publications
    Modified residuei1526 – 15261Phosphoserine2 Publications
    Modified residuei1550 – 15501Phosphoserine2 Publications
    Modified residuei1552 – 15521Phosphoserine1 Publication
    Modified residuei1575 – 15751Phosphothreonine1 Publication
    Modified residuei1581 – 15811Phosphoserine4 Publications
    Modified residuei1592 – 15921Phosphothreonine1 Publication
    Modified residuei1596 – 15961Phosphoserine1 Publication
    Modified residuei1609 – 16091Phosphotyrosine1 Publication
    Modified residuei1613 – 16131Phosphoserine3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ02880.
    PaxDbiQ02880.
    PRIDEiQ02880.

    PTM databases

    PhosphoSiteiQ02880.

    Expressioni

    Gene expression databases

    ArrayExpressiQ02880.
    BgeeiQ02880.
    CleanExiHS_TOP2B.
    GenevestigatoriQ02880.

    Organism-specific databases

    HPAiCAB004601.
    HPA024120.
    HPA050441.

    Interactioni

    Subunit structurei

    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.2 Publications

    Protein-protein interaction databases

    BioGridi113008. 48 interactions.
    IntActiQ02880. 4 interactions.
    MINTiMINT-155585.
    STRINGi9606.ENSP00000396704.

    Structurei

    Secondary structure

    1
    1626
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni466 – 4694
    Beta strandi470 – 4723
    Helixi473 – 4753
    Beta strandi477 – 4826
    Helixi483 – 4919
    Helixi497 – 4993
    Beta strandi502 – 5076
    Helixi514 – 5163
    Helixi519 – 5246
    Helixi526 – 53510
    Beta strandi545 – 5473
    Helixi548 – 5514
    Beta strandi555 – 5606
    Helixi565 – 58117
    Helixi583 – 5875
    Beta strandi591 – 5944
    Helixi644 – 6507
    Helixi652 – 6554
    Beta strandi656 – 6605
    Helixi664 – 67411
    Helixi676 – 6783
    Helixi679 – 69820
    Beta strandi713 – 7153
    Helixi716 – 7227
    Helixi724 – 73512
    Turni739 – 7413
    Helixi745 – 75713
    Helixi765 – 77612
    Helixi782 – 79312
    Turni814 – 8207
    Helixi824 – 8263
    Helixi835 – 8384
    Helixi841 – 8444
    Beta strandi849 – 8524
    Beta strandi855 – 8606
    Helixi868 – 8714
    Beta strandi875 – 8773
    Beta strandi882 – 8843
    Helixi890 – 90112
    Beta strandi918 – 9247
    Beta strandi927 – 9315
    Beta strandi933 – 9386
    Beta strandi941 – 9466
    Helixi953 – 9597
    Helixi961 – 9666
    Beta strandi969 – 9713
    Beta strandi976 – 9805
    Beta strandi989 – 9924
    Helixi995 – 100410
    Helixi1006 – 10094
    Beta strandi1013 – 10175
    Beta strandi1021 – 10244
    Beta strandi1030 – 10345
    Helixi1036 – 108045
    Helixi1091 – 110010
    Helixi1107 – 11148
    Helixi1144 – 11474
    Helixi1151 – 11544
    Helixi1156 – 117722
    Helixi1181 – 120525

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliQ02880.
    SMRiQ02880. Positions 50-1206.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini476 – 593118ToprimPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni363 – 3653Interaction with DNABy similarity
    Regioni1011 – 102010Interaction with DNA

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1034 – 104411Nuclear export signalAdd
    BLAST

    Sequence similaritiesi

    Belongs to the type II topoisomerase family.Curated
    Contains 1 Toprim domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0187.
    HOGENOMiHOG000216693.
    HOVERGENiHBG052998.
    InParanoidiQ02880.
    KOiK03164.
    OMAiEPLTQFM.
    OrthoDBiEOG73JKTM.
    PhylomeDBiQ02880.
    TreeFamiTF105282.

    Family and domain databases

    Gene3Di1.10.268.10. 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.
    InterProiIPR024946. 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]
    PANTHERiPTHR10169:SF36. PTHR10169:SF36. 1 hit.
    PfamiPF00204. DNA_gyraseB. 1 hit.
    PF00521. DNA_topoisoIV. 1 hit.
    PF08070. DTHCT. 1 hit.
    PF02518. HATPase_c. 1 hit.
    PF01751. Toprim. 1 hit.
    [Graphical view]
    PRINTSiPR00418. TPI2FAMILY.
    SMARTiSM00387. HATPase_c. 1 hit.
    SM00433. TOP2c. 1 hit.
    SM00434. TOP4c. 1 hit.
    [Graphical view]
    SUPFAMiSSF54211. SSF54211. 1 hit.
    SSF55874. SSF55874. 1 hit.
    SSF56719. SSF56719. 1 hit.
    PROSITEiPS00177. TOPOISOMERASE_II. 1 hit.
    PS50880. TOPRIM. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Beta-2 (identifier: Q02880-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MAKSGGCGAG AGVGGGNGAL TWVTLFDQNN AAKKEESETA NKNDSSKKLS     50
    VERVYQKKTQ LEHILLRPDT YIGSVEPLTQ FMWVYDEDVG MNCREVTFVP 100
    GLYKIFDEIL VNAADNKQRD KNMTCIKVSI DPESNIISIW NNGKGIPVVE 150
    HKVEKVYVPA LIFGQLLTSS NYDDDEKKVT GGRNGYGAKL CNIFSTKFTV 200
    ETACKEYKHS FKQTWMNNMM KTSEAKIKHF DGEDYTCITF QPDLSKFKME 250
    KLDKDIVALM TRRAYDLAGS CRGVKVMFNG KKLPVNGFRS YVDLYVKDKL 300
    DETGVALKVI HELANERWDV CLTLSEKGFQ QISFVNSIAT TKGGRHVDYV 350
    VDQVVGKLIE VVKKKNKAGV SVKPFQVKNH IWVFINCLIE NPTFDSQTKE 400
    NMTLQPKSFG SKCQLSEKFF KAASNCGIVE SILNWVKFKA QTQLNKKCSS 450
    VKYSKIKGIP KLDDANDAGG KHSLECTLIL TEGDSAKSLA VSGLGVIGRD 500
    RYGVFPLRGK ILNVREASHK QIMENAEINN IIKIVGLQYK KSYDDAESLK 550
    TLRYGKIMIM TDQDQDGSHI KGLLINFIHH NWPSLLKHGF LEEFITPIVK 600
    ASKNKQELSF YSIPEFDEWK KHIENQKAWK IKYYKGLGTS TAKEAKEYFA 650
    DMERHRILFR YAGPEDDAAI TLAFSKKKID DRKEWLTNFM EDRRQRRLHG 700
    LPEQFLYGTA TKHLTYNDFI NKELILFSNS DNERSIPSLV DGFKPGQRKV 750
    LFTCFKRNDK REVKVAQLAG SVAEMSAYHH GEQALMMTIV NLAQNFVGSN 800
    NINLLQPIGQ FGTRLHGGKD AASPRYIFTM LSTLARLLFP AVDDNLLKFL 850
    YDDNQRVEPE WYIPIIPMVL INGAEGIGTG WACKLPNYDA REIVNNVRRM 900
    LDGLDPHPML PNYKNFKGTI QELGQNQYAV SGEIFVVDRN TVEITELPVR 950
    TWTQVYKEQV LEPMLNGTDK TPALISDYKE YHTDTTVKFV VKMTEEKLAQ 1000
    AEAAGLHKVF KLQTTLTCNS MVLFDHMGCL KKYETVQDIL KEFFDLRLSY 1050
    YGLRKEWLVG MLGAESTKLN NQARFILEKI QGKITIENRS KKDLIQMLVQ 1100
    RGYESDPVKA WKEAQEKAAE EDETQNQHDD SSSDSGTPSG PDFNYILNMS 1150
    LWSLTKEKVE ELIKQRDAKG REVNDLKRKS PSDLWKEDLA AFVEELDKVE 1200
    SQEREDVLAG MSGKAIKGKV GKPKVKKLQL EETMPSPYGR RIIPEITAMK 1250
    ADASKKLLKK KKGDLDTAAV KVEFDEEFSG APVEGAGEEA LTPSVPINKG 1300
    PKPKREKKEP GTRVRKTPTS SGKPSAKKVK KRNPWSDDES KSESDLEETE 1350
    PVVIPRDSLL RRAAAERPKY TFDFSEEEDD DADDDDDDNN DLEELKVKAS 1400
    PITNDGEDEF VPSDGLDKDE YTFSPGKSKA TPEKSLHDKK SQDFGNLFSF 1450
    PSYSQKSEDD SAKFDSNEED SASVFSPSFG LKQTDKVPSK TVAAKKGKPS 1500
    SDTVPKPKRA PKQKKVVEAV NSDSDSEFGI PKKTTTPKGK GRGAKKRKAS 1550
    GSENEGDYNP GRKTSKTTSK KPKKTSFDQD SDVDIFPSDF PTEPPSLPRT 1600
    GRARKEVKYF AESDEEEDDV DFAMFN 1626
    Length:1,626
    Mass (Da):183,267
    Last modified:January 31, 2002 - v3
    Checksum:iE60E9262CC68B05D
    GO
    Isoform Beta-1 (identifier: Q02880-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:1,621
    Mass (Da):182,663
    Checksum:iB1C091BF539F2391
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1431 – 14311T → S in CAA78821. (PubMed:10095062)Curated
    Sequence conflicti1431 – 14311T → S in CAA09753. (PubMed:10095062)Curated
    Sequence conflicti1611 – 16111A → T in CAA48197. (PubMed:1333583)Curated
    Sequence conflicti1621 – 16211D → H in CAA09753. (PubMed:10095062)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei24 – 285Missing in isoform Beta-1. CuratedVSP_006532

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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
    , 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.
    CCDSiCCDS46776.1. [Q02880-2]
    PIRiS26730. A39242.
    RefSeqiNP_001059.2. NM_001068.3. [Q02880-2]
    XP_005265484.1. XM_005265427.1. [Q02880-1]
    UniGeneiHs.475733.

    Genome annotation databases

    EnsembliENST00000264331; ENSP00000264331; ENSG00000077097. [Q02880-1]
    ENST00000435706; ENSP00000396704; ENSG00000077097. [Q02880-2]
    GeneIDi7155.
    KEGGihsa:7155.
    UCSCiuc003cdj.3. human. [Q02880-2]
    uc011awn.1. human. [Q02880-1]

    Polymorphism databases

    DMDMi20141946.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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
    , 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 .
    CCDSi CCDS46776.1. [Q02880-2 ]
    PIRi S26730. A39242.
    RefSeqi NP_001059.2. NM_001068.3. [Q02880-2 ]
    XP_005265484.1. XM_005265427.1. [Q02880-1 ]
    UniGenei Hs.475733.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3QX3 X-ray 2.16 A/B 450-1206 [» ]
    4G0U X-ray 2.70 A/B 450-1206 [» ]
    4G0V X-ray 2.55 A/B 450-1206 [» ]
    4G0W X-ray 2.70 A/B 450-1206 [» ]
    4J3N X-ray 2.30 A/B 450-1206 [» ]
    ProteinModelPortali Q02880.
    SMRi Q02880. Positions 50-1206.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113008. 48 interactions.
    IntActi Q02880. 4 interactions.
    MINTi MINT-155585.
    STRINGi 9606.ENSP00000396704.

    Chemistry

    BindingDBi Q02880.
    ChEMBLi CHEMBL3396.

    PTM databases

    PhosphoSitei Q02880.

    Polymorphism databases

    DMDMi 20141946.

    Proteomic databases

    MaxQBi Q02880.
    PaxDbi Q02880.
    PRIDEi Q02880.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264331 ; ENSP00000264331 ; ENSG00000077097 . [Q02880-1 ]
    ENST00000435706 ; ENSP00000396704 ; ENSG00000077097 . [Q02880-2 ]
    GeneIDi 7155.
    KEGGi hsa:7155.
    UCSCi uc003cdj.3. human. [Q02880-2 ]
    uc011awn.1. human. [Q02880-1 ]

    Organism-specific databases

    CTDi 7155.
    GeneCardsi GC03M025639.
    H-InvDB HIX0030807.
    HGNCi HGNC:11990. TOP2B.
    HPAi CAB004601.
    HPA024120.
    HPA050441.
    MIMi 126431. gene.
    neXtProti NX_Q02880.
    PharmGKBi PA36672.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0187.
    HOGENOMi HOG000216693.
    HOVERGENi HBG052998.
    InParanoidi Q02880.
    KOi K03164.
    OMAi EPLTQFM.
    OrthoDBi EOG73JKTM.
    PhylomeDBi Q02880.
    TreeFami TF105282.

    Miscellaneous databases

    ChiTaRSi TOP2B. human.
    GeneWikii TOP2B.
    GenomeRNAii 7155.
    NextBioi 27998.
    PROi Q02880.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q02880.
    Bgeei Q02880.
    CleanExi HS_TOP2B.
    Genevestigatori Q02880.

    Family and domain databases

    Gene3Di 1.10.268.10. 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.
    InterProi IPR024946. 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 ]
    PANTHERi PTHR10169:SF36. PTHR10169:SF36. 1 hit.
    Pfami PF00204. DNA_gyraseB. 1 hit.
    PF00521. DNA_topoisoIV. 1 hit.
    PF08070. DTHCT. 1 hit.
    PF02518. HATPase_c. 1 hit.
    PF01751. Toprim. 1 hit.
    [Graphical view ]
    PRINTSi PR00418. TPI2FAMILY.
    SMARTi SM00387. HATPase_c. 1 hit.
    SM00433. TOP2c. 1 hit.
    SM00434. TOP4c. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54211. SSF54211. 1 hit.
    SSF55874. SSF55874. 1 hit.
    SSF56719. SSF56719. 1 hit.
    PROSITEi PS00177. TOPOISOMERASE_II. 1 hit.
    PS50880. TOPRIM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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. 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.

    Entry informationi

    Entry nameiTOP2B_HUMAN
    AccessioniPrimary (citable) accession number: Q02880
    Secondary accession number(s): Q13600, Q9UMG8, Q9UQP8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: January 31, 2002
    Last modified: October 1, 2014
    This is version 164 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Miscellaneous

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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3