Tchem TOP2B DNA topoisomerase 2-beta

Protein Summary

Description

Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks. This gene encodes a DNA topoisomerase, an enzyme that controls and alters the topologic states of DNA during transcription. This nuclear enzyme is involved in processes such as chromosome condensation, chromatid separation, and the relief of torsional stress that occurs during DNA transcription and replication. It catalyzes the transient breaking and rejoining of two strands of duplex DNA which allows the strands to pass through one another, thus altering the topology of DNA. Two forms of this enzyme exist as likely products of a gene duplication event. The gene encoding this form, beta, is localized to chromosome 3 and the alpha form is localized to chromosome 17. The gene encoding this enzyme functions as the target for several anticancer agents and a variety of mutations in this gene have been associated with the development of drug resistance. Reduced activity of this enzyme may also play a role in ataxia-telangiectasia. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Aug 2016]

Uniprot Accession IDs

• Q02880
• Q13600
• Q9UMG8
• Q9UQP8

Gene Name

• TOP2B

Ensembl ID

• ENST00000264331
• ENSP00000264331
• ENSG00000077097
• ENST00000435706
• ENSP00000396704

Symbol

• TOPIIB
• top2beta

Knowledge Table

Most Knowledge About	Knowledge Value (0 to 1 scale)
molecular function	1
protein domain	1
drug perturbation	0.96
virus perturbation	0.95
hub protein	0.88

IDG Development Level Summary

Tdark

These are targets about which virtually nothing is known. They do not have known drug or small molecule activities
- AND - satisfy two or more of the following criteria:

Pubmed score: 110.28   (req: < 5)

Gene RIFs: 52   (req: <= 3)

Antibodies: 250   (req: <= 50)

Tbio

These targets do not have known drug or small molecule activities
- AND - satisfy two or more of the following criteria:

Pubmed score: 110.28   (req: >= 5)

Gene RIFs: 52   (req: > 3)

Antibodies: 250   (req: > 50)

- OR - satisfy the following criterion:

Gene Ontology Terms: 18

Tchem

Target has at least one ChEMBL compound with an activity cutoff of < 30 nM - AND - satisfies the preceding conditions

Active Ligand: 1

Tclin

Target has at least one approved drug - AND - satisfies the preceding conditions

Active Drugs: 2

Approved Drugs (2)

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1 – 2 of 2

amsacrine

TOP2BTchem Enzyme

EC50: 6.14

ciprofloxacin

TOP2BTchem Enzyme

EC50: 7.52

Active Ligands (1)

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1 – 1 of 1

CHEMBL130381

TOP2BTchem Enzyme

EC50: 6.03

Protein Data Bank (10)

1 – 5 of 10

PDB Structure Id	Ligand	Method	Resolution (Å)	M.W. (kDa)	Pub Year	Title

PDB Structure Id	M.W.	Resolution	Pub Year

Pathways (7)

Reactome (5)

KEGG (1)

PathwayCommons (1)

Metabolism of proteins (R-HSA-392499)

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Items per page:

5

1 – 5 of 5

Data Source	Name	Explore in Pharos	Explore in Source
Reactome	Metabolism of proteins	2050 targets	R-HSA-392499
Reactome	Post-translational protein modification	1450 targets	R-HSA-597592
Reactome	SUMO E3 ligases SUMOylate target proteins	170 targets	R-HSA-3108232
Reactome	SUMOylation	176 targets	R-HSA-2990846
Reactome	SUMOylation of DNA replication proteins	46 targets	R-HSA-4615885

Name	Explore in Pharos	Explore in Source
Metabolism of proteins	2050 targets	R-HSA-392499
Post-translational protein modification	1450 targets	R-HSA-597592
SUMO E3 ligases SUMOylate target proteins	170 targets	R-HSA-3108232
SUMOylation	176 targets	R-HSA-2990846
SUMOylation of DNA replication proteins	46 targets	R-HSA-4615885

Gene Ontology Terms (23)

Functions (10)

Components (5)

Processes (8)

Items per page:

10

1 – 10 of 10

GO Term	Evidence	Assigned by
chromatin binding	Inferred from Direct Assay (IDA)	UniProtKB
DNA topoisomerase type II (ATP-hydrolyzing) activity	Inferred from Direct Assay (IDA)	UniProtKB
enzyme binding	Inferred from Physical Interaction (IPI)	UniProtKB
histone deacetylase binding	Inferred from Physical Interaction (IPI)	UniProtKB
protein C-terminus binding	Inferred from Physical Interaction (IPI)	UniProtKB
protein heterodimerization activity	Inferred from Physical Interaction (IPI)	UniProtKB
protein kinase C binding	Inferred from Physical Interaction (IPI)	UniProtKB
ATP binding	Inferred from Electronic Annotation (IEA)	UniProtKB-KW
DNA binding	Inferred from Electronic Annotation (IEA)	UniProtKB-KW
metal ion binding	Inferred from Electronic Annotation (IEA)	UniProtKB-KW

Protein-Protein Interactions (198)

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1 – 10 of 198

• See Interactions on String-DB

CUL5

Tbio

Novelty: 0.01021591

p_int: 0.999999938

p_ni: 2.2e-8

p_wrong: 4e-8

Score: 0.32

Data Source: BioPlex,STRINGDB

ASB3

Tdark

Novelty: 0.29666183

p_int: 0.999999925

p_ni: 5.1e-8

p_wrong: 2.4e-8

Score: 0.695

Data Source: BioPlex,STRINGDB

HSD3B2

Tclin

Family: Enzyme

Novelty: 0.00875526

p_int: 0.999977552

p_ni: 0.000022381

p_wrong: 6.7e-8

Score: 0.195

Data Source: BioPlex,STRINGDB

PLAUR

Tchem

Family: Enzyme

Novelty: 0.00096649

p_int: 0.994778883

p_ni: 0.001392415

p_wrong: 0.003828702

Data Source: BioPlex

GPATCH4

Tdark

Novelty: 2.35294118

p_int: 0.919926828

p_ni: 0.00020309

p_wrong: 0.079870083

Data Source: BioPlex

SMARCA4

Tchem

Family: Epigenetic

Novelty: 0.00120535

Score: 0.99

Data Source: STRINGDB

SUPT16H

Tbio

Family: Enzyme

Novelty: 0.01332412

Score: 0.989

Data Source: STRINGDB

BAZ1B

Tbio

Family: Epigenetic

Novelty: 0.03400267

Score: 0.984

Data Source: STRINGDB

SMARCE1

Tbio

Family: TF

Novelty: 0.02547452

Score: 0.983

Data Source: STRINGDB

SMARCC1

Tbio

Family: TF; Epigenetic

Novelty: 0.01474339

Score: 0.983

Data Source: STRINGDB

Publication Statistics

PubMed Score  110.28

PubMed score by year

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PubTator Score  224.13

PubTator score by year

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Amino Acid Sequence

Residue Counts

Sequence

MAKSGGCGAGAGVGGGNGALTWVTLFDQNNAAKKEESETANKNDSSKKLSVERVYQKKTQLEHILLRPDT

1-70

YIGSVEPLTQFMWVYDEDVGMNCREVTFVPGLYKIFDEILVNAADNKQRDKNMTCIKVSIDPESNIISIW

70-140

NNGKGIPVVEHKVEKVYVPALIFGQLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTKFTVETACKEYKHS

140-210

FKQTWMNNMMKTSEAKIKHFDGEDYTCITFQPDLSKFKMEKLDKDIVALMTRRAYDLAGSCRGVKVMFNG

210-280

KKLPVNGFRSYVDLYVKDKLDETGVALKVIHELANERWDVCLTLSEKGFQQISFVNSIATTKGGRHVDYV

280-350

VDQVVGKLIEVVKKKNKAGVSVKPFQVKNHIWVFINCLIENPTFDSQTKENMTLQPKSFGSKCQLSEKFF

350-420

KAASNCGIVESILNWVKFKAQTQLNKKCSSVKYSKIKGIPKLDDANDAGGKHSLECTLILTEGDSAKSLA

420-490

VSGLGVIGRDRYGVFPLRGKILNVREASHKQIMENAEINNIIKIVGLQYKKSYDDAESLKTLRYGKIMIM

490-560

TDQDQDGSHIKGLLINFIHHNWPSLLKHGFLEEFITPIVKASKNKQELSFYSIPEFDEWKKHIENQKAWK

560-630

IKYYKGLGTSTAKEAKEYFADMERHRILFRYAGPEDDAAITLAFSKKKIDDRKEWLTNFMEDRRQRRLHG

630-700

LPEQFLYGTATKHLTYNDFINKELILFSNSDNERSIPSLVDGFKPGQRKVLFTCFKRNDKREVKVAQLAG

700-770

SVAEMSAYHHGEQALMMTIVNLAQNFVGSNNINLLQPIGQFGTRLHGGKDAASPRYIFTMLSTLARLLFP

770-840

AVDDNLLKFLYDDNQRVEPEWYIPIIPMVLINGAEGIGTGWACKLPNYDAREIVNNVRRMLDGLDPHPML

840-910

PNYKNFKGTIQELGQNQYAVSGEIFVVDRNTVEITELPVRTWTQVYKEQVLEPMLNGTDKTPALISDYKE

910-980

YHTDTTVKFVVKMTEEKLAQAEAAGLHKVFKLQTTLTCNSMVLFDHMGCLKKYETVQDILKEFFDLRLSY

980-1050

YGLRKEWLVGMLGAESTKLNNQARFILEKIQGKITIENRSKKDLIQMLVQRGYESDPVKAWKEAQEKAAE

1050-1120

EDETQNQHDDSSSDSGTPSGPDFNYILNMSLWSLTKEKVEELIKQRDAKGREVNDLKRKSPSDLWKEDLA

1120-1190

AFVEELDKVESQEREDVLAGMSGKAIKGKVGKPKVKKLQLEETMPSPYGRRIIPEITAMKADASKKLLKK

1190-1260

KKGDLDTAAVKVEFDEEFSGAPVEGAGEEALTPSVPINKGPKPKREKKEPGTRVRKTPTSSGKPSAKKVK

1260-1330

KRNPWSDDESKSESDLEETEPVVIPRDSLLRRAAAERPKYTFDFSEEEDDDADDDDDDNNDLEELKVKAS

1330-1400

PITNDGEDEFVPSDGLDKDEYTFSPGKSKATPEKSLHDKKSQDFGNLFSFPSYSQKSEDDSAKFDSNEED

1400-1470

SASVFSPSFGLKQTDKVPSKTVAAKKGKPSSDTVPKPKRAPKQKKVVEAVNSDSDSEFGIPKKTTTPKGK

1470-1540

GRGAKKRKASGSENEGDYNPGRKTSKTTSKKPKKTSFDQDSDVDIFPSDFPTEPPSLPRTGRARKEVKYF

1540-1610

AESDEEEDDVDFAMFN

1610-1626

MAKSGGCGAGAGVGGGNGALTWVTLFDQNNAAKKEESETANKNDSSKKLSVERVYQKKTQLEHILLRPDTYIGSVEPLTQFMWVYDEDVGMNCREVTFVPGLYKIFDEILVNAADNKQRDKNMTCIKVSIDPESNIISIWNNGKGIPVVEHKVEKVYVPALIFGQLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTKFTVETACKEYKHSFKQTWMNNMMKTSEAKIKHFDGEDYTCITFQPDLSKFKMEKLDKDIVALMTRRAYDLAGSCRGVKVMFNGKKLPVNGFRSYVDLYVKDKLDETGVALKVIHELANERWDVCLTLSEKGFQQISFVNSIATTKGGRHVDYVVDQVVGKLIEVVKKKNKAGVSVKPFQVKNHIWVFINCLIENPTFDSQTKENMTLQPKSFGSKCQLSEKFFKAASNCGIVESILNWVKFKAQTQLNKKCSSVKYSKIKGIPKLDDANDAGGKHSLECTLILTEGDSAKSLAVSGLGVIGRDRYGVFPLRGKILNVREASHKQIMENAEINNIIKIVGLQYKKSYDDAESLKTLRYGKIMIMTDQDQDGSHIKGLLINFIHHNWPSLLKHGFLEEFITPIVKASKNKQELSFYSIPEFDEWKKHIENQKAWKIKYYKGLGTSTAKEAKEYFADMERHRILFRYAGPEDDAAITLAFSKKKIDDRKEWLTNFMEDRRQRRLHGLPEQFLYGTATKHLTYNDFINKELILFSNSDNERSIPSLVDGFKPGQRKVLFTCFKRNDKREVKVAQLAGSVAEMSAYHHGEQALMMTIVNLAQNFVGSNNINLLQPIGQFGTRLHGGKDAASPRYIFTMLSTLARLLFPAVDDNLLKFLYDDNQRVEPEWYIPIIPMVLINGAEGIGTGWACKLPNYDAREIVNNVRRMLDGLDPHPMLPNYKNFKGTIQELGQNQYAVSGEIFVVDRNTVEITELPVRTWTQVYKEQVLEPMLNGTDKTPALISDYKEYHTDTTVKFVVKMTEEKLAQAEAAGLHKVFKLQTTLTCNSMVLFDHMGCLKKYETVQDILKEFFDLRLSYYGLRKEWLVGMLGAESTKLNNQARFILEKIQGKITIENRSKKDLIQMLVQRGYESDPVKAWKEAQEKAAEEDETQNQHDDSSSDSGTPSGPDFNYILNMSLWSLTKEKVEELIKQRDAKGREVNDLKRKSPSDLWKEDLAAFVEELDKVESQEREDVLAGMSGKAIKGKVGKPKVKKLQLEETMPSPYGRRIIPEITAMKADASKKLLKKKKGDLDTAAVKVEFDEEFSGAPVEGAGEEALTPSVPINKGPKPKREKKEPGTRVRKTPTSSGKPSAKKVKKRNPWSDDESKSESDLEETEPVVIPRDSLLRRAAAERPKYTFDFSEEEDDDADDDDDDNNDLEELKVKASPITNDGEDEFVPSDGLDKDEYTFSPGKSKATPEKSLHDKKSQDFGNLFSFPSYSQKSEDDSAKFDSNEEDSASVFSPSFGLKQTDKVPSKTVAAKKGKPSSDTVPKPKRAPKQKKVVEAVNSDSDSEFGIPKKTTTPKGKGRGAKKRKASGSENEGDYNPGRKTSKTTSKKPKKTSFDQDSDVDIFPSDFPTEPPSLPRTGRARKEVKYFAESDEEEDDVDFAMFN

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Uniprot Keyword

3D-structure
Acetylation
Alternative splicing
ATP-binding
Autism spectrum disorder
Complete proteome
Cytoplasm
Disease mutation
DNA-binding
Isomerase