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Q64511

- TOP2B_MOUSE

UniProt

Q64511 - TOP2B_MOUSE

Protein

DNA topoisomerase 2-beta

Gene

Top2b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 2 (27 Sep 2005)
      Previous versions | rss
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    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 By similarity.By similarity

    Catalytic activityi

    ATP-dependent breakage, passage and rejoining of double-stranded DNA.PROSITE-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+.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei100 – 1001ATPBy similarity
    Binding sitei129 – 1291ATPBy similarity
    Metal bindingi470 – 4701Magnesium 1; catalyticPROSITE-ProRule annotation
    Sitei498 – 4981Interaction with DNAPROSITE-ProRule annotation
    Sitei501 – 5011Interaction with DNAPROSITE-ProRule annotation
    Metal bindingi550 – 5501Magnesium 1; catalyticPROSITE-ProRule annotation
    Metal bindingi550 – 5501Magnesium 2PROSITE-ProRule annotation
    Metal bindingi552 – 5521Magnesium 2PROSITE-ProRule annotation
    Sitei670 – 6701Interaction with DNAPROSITE-ProRule annotation
    Sitei671 – 6711Interaction with DNAPROSITE-ProRule annotation
    Sitei732 – 7321Interaction with DNAPROSITE-ProRule annotation
    Sitei766 – 7661Interaction with DNAPROSITE-ProRule annotation
    Sitei813 – 8131Transition state stabilizerBy similarity
    Active sitei814 – 8141O-(5'-phospho-DNA)-tyrosine intermediateBy similarity
    Sitei865 – 8651Important for DNA bending; intercalates between base pairs of target DNABy similarity
    Sitei940 – 9401Interaction with DNAPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi157 – 1593ATPBy similarity
    Nucleotide bindingi170 – 1778ATPBy similarity
    Nucleotide bindingi385 – 3873ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. chromatin binding Source: Ensembl
    3. DNA binding, bending Source: InterPro
    4. DNA topoisomerase type II (ATP-hydrolyzing) activity Source: UniProtKB
    5. metal ion binding Source: UniProtKB-KW
    6. protein binding Source: IntAct

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. axonogenesis Source: MGI
    3. DNA topological change Source: UniProtKB
    4. DNA unwinding involved in DNA replication Source: RefGenome
    5. forebrain development Source: MGI
    6. mitotic DNA integrity checkpoint Source: RefGenome
    7. mitotic recombination Source: RefGenome
    8. neuron migration Source: MGI
    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 14

    Organism-specific databases

    MGIiMGI:98791. Top2b.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Ensembl
    2. DNA topoisomerase complex (ATP-hydrolyzing) Source: RefGenome
    3. nucleolus Source: UniProtKB-SubCell
    4. nucleoplasm Source: Ensembl
    5. nucleus Source: MGI

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 16121611DNA topoisomerase 2-betaPRO_0000145370Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei3 – 31N6-acetyllysine1 Publication
    Modified residuei1224 – 12241PhosphoserineBy similarity
    Modified residuei1280 – 12801PhosphothreonineBy similarity
    Modified residuei1324 – 13241PhosphoserineBy similarity
    Modified residuei1328 – 13281PhosphoserineBy similarity
    Modified residuei1330 – 13301PhosphoserineBy similarity
    Modified residuei1332 – 13321PhosphoserineBy similarity
    Modified residuei1346 – 13461PhosphoserineBy similarity
    Modified residuei1363 – 13631PhosphoserineBy similarity
    Modified residuei1387 – 13871Phosphoserine1 Publication
    Modified residuei1390 – 13901PhosphothreonineBy similarity
    Modified residuei1400 – 14001Phosphoserine1 Publication
    Modified residuei1408 – 14081PhosphotyrosineBy similarity
    Modified residuei1411 – 14111PhosphoserineBy similarity
    Modified residuei1428 – 14281PhosphoserineBy similarity
    Modified residuei1439 – 14391PhosphoserineBy similarity
    Modified residuei1441 – 14411PhosphoserineBy similarity
    Modified residuei1448 – 14481PhosphoserineBy similarity
    Modified residuei1453 – 14531PhosphoserineBy similarity
    Modified residuei1460 – 14601PhosphoserineBy similarity
    Modified residuei1509 – 15091Phosphoserine3 Publications
    Modified residuei1511 – 15111Phosphoserine3 Publications
    Modified residuei1513 – 15131Phosphoserine1 Publication
    Modified residuei1537 – 15371Phosphoserine1 Publication
    Modified residuei1539 – 15391Phosphoserine1 Publication
    Modified residuei1562 – 15621PhosphothreonineBy similarity
    Modified residuei1568 – 15681PhosphoserineBy similarity
    Modified residuei1596 – 15961PhosphotyrosineBy similarity
    Modified residuei1600 – 16001PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ64511.
    PaxDbiQ64511.
    PRIDEiQ64511.

    PTM databases

    PhosphoSiteiQ64511.

    Expressioni

    Gene expression databases

    ArrayExpressiQ64511.
    BgeeiQ64511.
    CleanExiMM_TOP2B.
    GenevestigatoriQ64511.

    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 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AicdaQ9WVE03EBI-2325586,EBI-3835567

    Protein-protein interaction databases

    BioGridi204277. 5 interactions.
    IntActiQ64511. 6 interactions.
    MINTiMINT-4138251.
    STRINGi10090.ENSMUSP00000017629.

    Structurei

    3D structure databases

    ProteinModelPortaliQ64511.
    SMRiQ64511. Positions 38-1194.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini464 – 581118ToprimPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni351 – 3533Interaction with DNABy similarity
    Regioni999 – 100810Interaction with DNABy similarity

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0187.
    GeneTreeiENSGT00390000016222.
    HOGENOMiHOG000216693.
    HOVERGENiHBG052998.
    InParanoidiQ64511.
    KOiK03164.
    OMAiEPLTQFM.
    OrthoDBiEOG73JKTM.
    PhylomeDBiQ64511.
    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]

    Sequencei

    Sequence statusi: Complete.

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

    Q64511-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKSSLAGSD GALTWVNNAT KKEELETANK NDSTKKLSVE RVYQKKTQLE     50
    HILLRPDTYI GSVEPLTQLM WVYDEDVGMN CREVTFVPGL YKIFDEILVN 100
    AADNKQRDKN MTCIKVSIDP ESNIISIWNN GKGIPVVEHK VEKVYVPALI 150
    FGQLLTSSNY DDDEKKVTGG RNGYGAKLCN IFSTKFTVET ACKEYKHSFK 200
    QTWMNNMMKT SEAKIKHFDG EDYTCITFQP DLSKFKMEKL DKDIVALMTR 250
    RAYDLAGSCK GVKVMFNGKK LPVNGFRSYV DLYVKDKLDE TGVALKVIHE 300
    LANERWDVCL TLSEKGFQQI SFVNSIATTK GGRHVDYVVD QVVSKLIEVV 350
    KKKNKAGVSV KPFQVKNHIW VFINCLIENP TFDSQTKENM TLQPKSFGSK 400
    CQLSEKFFKA ASNCGIVESI LNWVKFKAQT QLNKKCSSVK YSKIKGIPKL 450
    DDANDAGGKH SLECTLILTE GDSAKSLAVS GLGVIGRDRY GVFPLRGKIL 500
    NVREASHKQI MENAEINNII KIVGLQYKKS YDDAESLKTL RYGKIMIMTD 550
    QDQDGSHIKG LLINFIHHNW PSLLKHGFLE EFITPIVKAS KNKQELSFYS 600
    IPEFDEWKKH IENQKAWKIK YYKGLGTSTA KEAKEYFADM ERHRILFRYA 650
    GPEDDAAITL AFSKKKIDDR KEWLTNFMED RRQRRLHGLP EQFLYGTATK 700
    HLTYNDFINK ELILFSNSDN ERSIPSLVDG FKPGQRKVLF TCFKRNDKRE 750
    VKVAQLAGSV AEMSAYHHGE QALMMTIVNL AQNFVGSNNI NLLQPIGQFG 800
    TRLHGGKDAA SPRYIFTMLS SLARLLFPAV DDNLLKFLYD DNQRVEPEWY 850
    IPIIPMVLIN GAEGIGTGWA CKLPNYDARE IVNNVRRMLE GLDPHPMLPN 900
    YKNFKGTIQE LGQNQYAVSG EIFVVDRNTV EITELPVRTW TQVYKEQVLE 950
    PMLNGTDKTP ALISDYKEYH TDTTVKFVVK MTEEKLAQAE AAGLHKVFKL 1000
    QTTLTCNSMV LFDHMGCLKK YETVQDILKE FFDLRLSYYG LRKEWLVGML 1050
    GAESTKLNNQ ARFILEKIQG KITIENRSKK DLIQMLVQRG YESDPVKAWK 1100
    EAQEKAAEEE DSQNQHDDSS SDSGTPSGPD FNYILNMSLW SLTKEKVEEL 1150
    IKQRDTKGRE VNDLKRKSPS DLWKEDLAAF VEELDKVEAQ EREDILAGMS 1200
    GKAIKGKVGK PKVKKLQLEE TMPSPYGRRI VPEITAMKAD ASRKLLKKKK 1250
    GDPDTTVVKV EFDEEFSGTP AEGTGEETLT PSAPVNKGPK PKREKKEPGT 1300
    RVRKTPTSTG KTNAKKVKKR NPWSDDESKS ESDLEEAEPV VIPRDSLLRR 1350
    AAAERPKYTF DFSEEEDDDA AAADDSNDLE ELKVKASPIT NDGEDEFVPS 1400
    DGLDKDEYAF SSGKSKATPE KSSNDKKSQD FGNLFSFPSY SQKSEDDSAK 1450
    FDSNEEDTAS VFAPSFGLKQ TDKLPSKTVA AKKGKPPSDT APKAKRAPKQ 1500
    KKIVETINSD SDSEFGIPKK TTTPKGKGRG AKKRKASGSE NEGDYNPGRK 1550
    PSKTASKKPK KTSFDQDSDV DIFPSDFTSE PPALPRTGRA RKEVKYFAES 1600
    DEEEDVDFAM FN 1612
    Length:1,612
    Mass (Da):181,909
    Last modified:September 27, 2005 - v2
    Checksum:i974D9D5DAD0DB96A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti16 – 161V → A in BAA07236. 1 PublicationCurated
    Sequence conflicti1434 – 14341L → P in BAA07236. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D38046 mRNA. Translation: BAA07236.1.
    BC041106 mRNA. Translation: AAH41106.1.
    BC054541 mRNA. Translation: AAH54541.1.
    CCDSiCCDS26833.1.
    RefSeqiNP_033435.2. NM_009409.2.
    UniGeneiMm.130362.

    Genome annotation databases

    EnsembliENSMUST00000017629; ENSMUSP00000017629; ENSMUSG00000017485.
    GeneIDi21974.
    KEGGimmu:21974.
    UCSCiuc007shc.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D38046 mRNA. Translation: BAA07236.1 .
    BC041106 mRNA. Translation: AAH41106.1 .
    BC054541 mRNA. Translation: AAH54541.1 .
    CCDSi CCDS26833.1.
    RefSeqi NP_033435.2. NM_009409.2.
    UniGenei Mm.130362.

    3D structure databases

    ProteinModelPortali Q64511.
    SMRi Q64511. Positions 38-1194.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204277. 5 interactions.
    IntActi Q64511. 6 interactions.
    MINTi MINT-4138251.
    STRINGi 10090.ENSMUSP00000017629.

    Chemistry

    BindingDBi Q64511.
    ChEMBLi CHEMBL5564.

    PTM databases

    PhosphoSitei Q64511.

    Proteomic databases

    MaxQBi Q64511.
    PaxDbi Q64511.
    PRIDEi Q64511.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000017629 ; ENSMUSP00000017629 ; ENSMUSG00000017485 .
    GeneIDi 21974.
    KEGGi mmu:21974.
    UCSCi uc007shc.1. mouse.

    Organism-specific databases

    CTDi 7155.
    MGIi MGI:98791. Top2b.

    Phylogenomic databases

    eggNOGi COG0187.
    GeneTreei ENSGT00390000016222.
    HOGENOMi HOG000216693.
    HOVERGENi HBG052998.
    InParanoidi Q64511.
    KOi K03164.
    OMAi EPLTQFM.
    OrthoDBi EOG73JKTM.
    PhylomeDBi Q64511.
    TreeFami TF105282.

    Miscellaneous databases

    NextBioi 301674.
    PROi Q64511.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q64511.
    Bgeei Q64511.
    CleanExi MM_TOP2B.
    Genevestigatori Q64511.

    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. Miyaike M., Adachi N., Kikuchi A.
      Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Brain.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6.
      Tissue: Brain and Eye.
    3. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
      Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
      Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1387; SER-1509; SER-1511; SER-1513; SER-1537 AND SER-1539, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    5. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1400; SER-1509 AND SER-1511, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1509 AND SER-1511, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    7. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 AND LYS-3, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiTOP2B_MOUSE
    AccessioniPrimary (citable) accession number: Q64511
    Secondary accession number(s): Q7TQG4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: September 27, 2005
    Last modified: October 1, 2014
    This is version 137 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3