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Q02880

- TOP2B_HUMAN

UniProt

Q02880 - TOP2B_HUMAN

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Protein

DNA topoisomerase 2-beta

Gene

TOP2B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

Mg2+2 PublicationsPROSITE-ProRule annotation, Mn2+2 PublicationsPROSITE-ProRule annotation, Ca2+2 PublicationsPROSITE-ProRule annotationNote: Binds two Mg(2+) per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca(2+).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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ02880.
CleanExiHS_TOP2B.
ExpressionAtlasiQ02880. baseline and differential.
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. 49 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 – 4694Combined sources
Beta strandi470 – 4723Combined sources
Helixi473 – 4753Combined sources
Beta strandi477 – 4826Combined sources
Helixi483 – 4919Combined sources
Helixi497 – 4993Combined sources
Beta strandi502 – 5076Combined sources
Helixi514 – 5163Combined sources
Helixi519 – 5246Combined sources
Helixi526 – 53510Combined sources
Beta strandi545 – 5473Combined sources
Helixi548 – 5514Combined sources
Beta strandi555 – 5606Combined sources
Helixi565 – 58117Combined sources
Helixi583 – 5875Combined sources
Beta strandi591 – 5944Combined sources
Helixi644 – 6507Combined sources
Helixi652 – 6554Combined sources
Beta strandi656 – 6605Combined sources
Helixi664 – 67411Combined sources
Helixi676 – 6783Combined sources
Helixi679 – 69820Combined sources
Beta strandi713 – 7153Combined sources
Helixi716 – 7227Combined sources
Helixi724 – 73512Combined sources
Turni739 – 7413Combined sources
Helixi745 – 75713Combined sources
Helixi765 – 77612Combined sources
Helixi782 – 79312Combined sources
Turni814 – 8207Combined sources
Helixi824 – 8263Combined sources
Helixi835 – 8384Combined sources
Helixi841 – 8444Combined sources
Beta strandi849 – 8524Combined sources
Beta strandi855 – 8606Combined sources
Helixi868 – 8714Combined sources
Beta strandi875 – 8773Combined sources
Beta strandi882 – 8843Combined sources
Helixi890 – 90112Combined sources
Beta strandi918 – 9247Combined sources
Beta strandi927 – 9315Combined sources
Beta strandi933 – 9386Combined sources
Beta strandi941 – 9466Combined sources
Helixi953 – 9597Combined sources
Helixi961 – 9666Combined sources
Beta strandi969 – 9713Combined sources
Beta strandi976 – 9805Combined sources
Beta strandi989 – 9924Combined sources
Helixi995 – 100410Combined sources
Helixi1006 – 10094Combined sources
Beta strandi1013 – 10175Combined sources
Beta strandi1021 – 10244Combined sources
Beta strandi1030 – 10345Combined sources
Helixi1036 – 108045Combined sources
Helixi1091 – 110010Combined sources
Helixi1107 – 11148Combined sources
Helixi1144 – 11474Combined sources
Helixi1151 – 11544Combined sources
Helixi1156 – 117722Combined sources
Helixi1181 – 120525Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000016222.
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_C.
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

        10         20         30         40         50
MAKSGGCGAG AGVGGGNGAL TWVTLFDQNN AAKKEESETA NKNDSSKKLS
60 70 80 90 100
VERVYQKKTQ LEHILLRPDT YIGSVEPLTQ FMWVYDEDVG MNCREVTFVP
110 120 130 140 150
GLYKIFDEIL VNAADNKQRD KNMTCIKVSI DPESNIISIW NNGKGIPVVE
160 170 180 190 200
HKVEKVYVPA LIFGQLLTSS NYDDDEKKVT GGRNGYGAKL CNIFSTKFTV
210 220 230 240 250
ETACKEYKHS FKQTWMNNMM KTSEAKIKHF DGEDYTCITF QPDLSKFKME
260 270 280 290 300
KLDKDIVALM TRRAYDLAGS CRGVKVMFNG KKLPVNGFRS YVDLYVKDKL
310 320 330 340 350
DETGVALKVI HELANERWDV CLTLSEKGFQ QISFVNSIAT TKGGRHVDYV
360 370 380 390 400
VDQVVGKLIE VVKKKNKAGV SVKPFQVKNH IWVFINCLIE NPTFDSQTKE
410 420 430 440 450
NMTLQPKSFG SKCQLSEKFF KAASNCGIVE SILNWVKFKA QTQLNKKCSS
460 470 480 490 500
VKYSKIKGIP KLDDANDAGG KHSLECTLIL TEGDSAKSLA VSGLGVIGRD
510 520 530 540 550
RYGVFPLRGK ILNVREASHK QIMENAEINN IIKIVGLQYK KSYDDAESLK
560 570 580 590 600
TLRYGKIMIM TDQDQDGSHI KGLLINFIHH NWPSLLKHGF LEEFITPIVK
610 620 630 640 650
ASKNKQELSF YSIPEFDEWK KHIENQKAWK IKYYKGLGTS TAKEAKEYFA
660 670 680 690 700
DMERHRILFR YAGPEDDAAI TLAFSKKKID DRKEWLTNFM EDRRQRRLHG
710 720 730 740 750
LPEQFLYGTA TKHLTYNDFI NKELILFSNS DNERSIPSLV DGFKPGQRKV
760 770 780 790 800
LFTCFKRNDK REVKVAQLAG SVAEMSAYHH GEQALMMTIV NLAQNFVGSN
810 820 830 840 850
NINLLQPIGQ FGTRLHGGKD AASPRYIFTM LSTLARLLFP AVDDNLLKFL
860 870 880 890 900
YDDNQRVEPE WYIPIIPMVL INGAEGIGTG WACKLPNYDA REIVNNVRRM
910 920 930 940 950
LDGLDPHPML PNYKNFKGTI QELGQNQYAV SGEIFVVDRN TVEITELPVR
960 970 980 990 1000
TWTQVYKEQV LEPMLNGTDK TPALISDYKE YHTDTTVKFV VKMTEEKLAQ
1010 1020 1030 1040 1050
AEAAGLHKVF KLQTTLTCNS MVLFDHMGCL KKYETVQDIL KEFFDLRLSY
1060 1070 1080 1090 1100
YGLRKEWLVG MLGAESTKLN NQARFILEKI QGKITIENRS KKDLIQMLVQ
1110 1120 1130 1140 1150
RGYESDPVKA WKEAQEKAAE EDETQNQHDD SSSDSGTPSG PDFNYILNMS
1160 1170 1180 1190 1200
LWSLTKEKVE ELIKQRDAKG REVNDLKRKS PSDLWKEDLA AFVEELDKVE
1210 1220 1230 1240 1250
SQEREDVLAG MSGKAIKGKV GKPKVKKLQL EETMPSPYGR RIIPEITAMK
1260 1270 1280 1290 1300
ADASKKLLKK KKGDLDTAAV KVEFDEEFSG APVEGAGEEA LTPSVPINKG
1310 1320 1330 1340 1350
PKPKREKKEP GTRVRKTPTS SGKPSAKKVK KRNPWSDDES KSESDLEETE
1360 1370 1380 1390 1400
PVVIPRDSLL RRAAAERPKY TFDFSEEEDD DADDDDDDNN DLEELKVKAS
1410 1420 1430 1440 1450
PITNDGEDEF VPSDGLDKDE YTFSPGKSKA TPEKSLHDKK SQDFGNLFSF
1460 1470 1480 1490 1500
PSYSQKSEDD SAKFDSNEED SASVFSPSFG LKQTDKVPSK TVAAKKGKPS
1510 1520 1530 1540 1550
SDTVPKPKRA PKQKKVVEAV NSDSDSEFGI PKKTTTPKGK GRGAKKRKAS
1560 1570 1580 1590 1600
GSENEGDYNP GRKTSKTTSK KPKKTSFDQD SDVDIFPSDF PTEPPSLPRT
1610 1620
GRARKEVKYF AESDEEEDDV DFAMFN
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 49 interactions.
IntActi Q02880. 4 interactions.
MINTi MINT-155585.
STRINGi 9606.ENSP00000396704.

Chemistry

BindingDBi Q02880.
ChEMBLi CHEMBL3396.
DrugBanki DB00970. Dactinomycin.
DB00694. Daunorubicin.
DB00380. Dexrazoxane.
DB00773. Etoposide.

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.
GeneTreei ENSGT00390000016222.
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

Bgeei Q02880.
CleanExi HS_TOP2B.
ExpressionAtlasi Q02880. baseline and differential.
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_C.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 166 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