Q64511 · TOP2B_MOUSE
- ProteinDNA topoisomerase 2-beta
- GeneTop2b
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1612 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Key decatenating enzyme that alters DNA topology by binding to two double-stranded DNA molecules, generating a double-stranded break in one of the strands, passing the intact strand through the broken strand, and religating the broken strand. Plays a role in B-cell differentiation.
Miscellaneous
Eukaryotic topoisomerase I and II can relax both negative and positive supercoils, whereas prokaryotic enzymes relax only negative supercoils.
Catalytic activity
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Ca2+ (UniProtKB | Rhea| CHEBI:29108 )
Note: 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+ or Ca2+.
Features
Showing features for binding site, site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 100 | ATP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 129 | ATP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 157-159 | ATP (UniProtKB | ChEBI) | ||||
Sequence: SSN | ||||||
Binding site | 170-177 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GRNGYGAK | ||||||
Binding site | 385-387 | ATP (UniProtKB | ChEBI) | ||||
Sequence: QTK | ||||||
Binding site | 470 | Mg2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Site | 498 | Interaction with DNA | ||||
Sequence: K | ||||||
Site | 501 | Interaction with DNA | ||||
Sequence: N | ||||||
Binding site | 550 | Mg2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 550 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 552 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Site | 670 | Interaction with DNA | ||||
Sequence: R | ||||||
Site | 671 | Interaction with DNA | ||||
Sequence: K | ||||||
Site | 732 | Interaction with DNA | ||||
Sequence: K | ||||||
Site | 766 | Interaction with DNA | ||||
Sequence: Y | ||||||
Site | 813 | Transition state stabilizer | ||||
Sequence: R | ||||||
Active site | 814 | O-(5'-phospho-DNA)-tyrosine intermediate | ||||
Sequence: Y | ||||||
Site | 865 | Important for DNA bending; intercalates between base pairs of target DNA | ||||
Sequence: I | ||||||
Site | 940 | Interaction with DNA | ||||
Sequence: W |
GO annotations
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDNA topoisomerase 2-beta
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ64511
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Knockout animals have B-cell developmental defects affecting multiple stages of development likely due to transcriptional defects. These mutant mice have altered splenic follicle structure with reduce marginal zone and follicular B-cell zones; immunophenotyping show decreased B- cells at all stages of development. Mutant mice fail to mount an antibody response to vaccination and B-cells fail to proliferate in response to stimulation, indicating deficits in B-cell function.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 581 | Impairs B-cell development. | ||||
Sequence: Missing |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 45 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000145370 | 2-1612 | DNA topoisomerase 2-beta | |||
Sequence: AKSSLAGSDGALTWVNNATKKEELETANKNDSTKKLSVERVYQKKTQLEHILLRPDTYIGSVEPLTQLMWVYDEDVGMNCREVTFVPGLYKIFDEILVNAADNKQRDKNMTCIKVSIDPESNIISIWNNGKGIPVVEHKVEKVYVPALIFGQLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTKFTVETACKEYKHSFKQTWMNNMMKTSEAKIKHFDGEDYTCITFQPDLSKFKMEKLDKDIVALMTRRAYDLAGSCKGVKVMFNGKKLPVNGFRSYVDLYVKDKLDETGVALKVIHELANERWDVCLTLSEKGFQQISFVNSIATTKGGRHVDYVVDQVVSKLIEVVKKKNKAGVSVKPFQVKNHIWVFINCLIENPTFDSQTKENMTLQPKSFGSKCQLSEKFFKAASNCGIVESILNWVKFKAQTQLNKKCSSVKYSKIKGIPKLDDANDAGGKHSLECTLILTEGDSAKSLAVSGLGVIGRDRYGVFPLRGKILNVREASHKQIMENAEINNIIKIVGLQYKKSYDDAESLKTLRYGKIMIMTDQDQDGSHIKGLLINFIHHNWPSLLKHGFLEEFITPIVKASKNKQELSFYSIPEFDEWKKHIENQKAWKIKYYKGLGTSTAKEAKEYFADMERHRILFRYAGPEDDAAITLAFSKKKIDDRKEWLTNFMEDRRQRRLHGLPEQFLYGTATKHLTYNDFINKELILFSNSDNERSIPSLVDGFKPGQRKVLFTCFKRNDKREVKVAQLAGSVAEMSAYHHGEQALMMTIVNLAQNFVGSNNINLLQPIGQFGTRLHGGKDAASPRYIFTMLSSLARLLFPAVDDNLLKFLYDDNQRVEPEWYIPIIPMVLINGAEGIGTGWACKLPNYDAREIVNNVRRMLEGLDPHPMLPNYKNFKGTIQELGQNQYAVSGEIFVVDRNTVEITELPVRTWTQVYKEQVLEPMLNGTDKTPALISDYKEYHTDTTVKFVVKMTEEKLAQAEAAGLHKVFKLQTTLTCNSMVLFDHMGCLKKYETVQDILKEFFDLRLSYYGLRKEWLVGMLGAESTKLNNQARFILEKIQGKITIENRSKKDLIQMLVQRGYESDPVKAWKEAQEKAAEEEDSQNQHDDSSSDSGTPSGPDFNYILNMSLWSLTKEKVEELIKQRDTKGREVNDLKRKSPSDLWKEDLAAFVEELDKVEAQEREDILAGMSGKAIKGKVGKPKVKKLQLEETMPSPYGRRIVPEITAMKADASRKLLKKKKGDPDTTVVKVEFDEEFSGTPAEGTGEETLTPSAPVNKGPKPKREKKEPGTRVRKTPTSTGKTNAKKVKKRNPWSDDESKSESDLEEAEPVVIPRDSLLRRAAAERPKYTFDFSEEEDDDAAAADDSNDLEELKVKASPITNDGEDEFVPSDGLDKDEYAFSSGKSKATPEKSSNDKKSQDFGNLFSFPSYSQKSEDDSAKFDSNEEDTASVFAPSFGLKQTDKLPSKTVAAKKGKPPSDTAPKAKRAPKQKKIVETINSDSDSEFGIPKKTTTPKGKGRGAKKRKASGSENEGDYNPGRKPSKTASKKPKKTSFDQDSDVDIFPSDFTSEPPALPRTGRARKEVKYFAESDEEEDVDFAMFN | ||||||
Modified residue | 3 | N6-acetyllysine | ||||
Sequence: K | ||||||
Cross-link | 21 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 22 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 165 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 166 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 216 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 287 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 355 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 361 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 425 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 427 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 434 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 588 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 593 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 623 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 631 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 634 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 664 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 700 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 1080 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 1202 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 1205 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 1214 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 1215 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 1224 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 1238 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 1250 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 1259 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 1280 | Phosphothreonine | ||||
Sequence: T | ||||||
Cross-link | 1311 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 1315 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 1324 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1328 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1330 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1332 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1346 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1358 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 1363 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1376 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 1385 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 1387 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1390 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1400 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1408 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 1411 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 1427 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 1428 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1439 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1441 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 1443 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 1448 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1453 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1460 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 1477 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 1509 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1511 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1513 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1537 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1539 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1562 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1563 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1568 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1596 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 1600 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Homodimer (By similarity).
Interacts with KIAA1210 (PubMed:28203736).
Interacts with PLSCR1 (By similarity).
Interacts with KIAA1210 (PubMed:28203736).
Interacts with PLSCR1 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q64511 | Aicda Q9WVE0 | 3 | EBI-2325586, EBI-3835567 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 351-353 | Interaction with DNA | ||||
Sequence: KKK | ||||||
Domain | 464-581 | Toprim | ||||
Sequence: CTLILTEGDSAKSLAVSGLGVIGRDRYGVFPLRGKILNVREASHKQIMENAEINNIIKIVGLQYKKSYDDAESLKTLRYGKIMIMTDQDQDGSHIKGLLINFIHHNWPSLLKHGFLEE | ||||||
Domain | 724-1177 | Topo IIA-type catalytic | ||||
Sequence: IPSLVDGFKPGQRKVLFTCFKRNDKREVKVAQLAGSVAEMSAYHHGEQALMMTIVNLAQNFVGSNNINLLQPIGQFGTRLHGGKDAASPRYIFTMLSSLARLLFPAVDDNLLKFLYDDNQRVEPEWYIPIIPMVLINGAEGIGTGWACKLPNYDAREIVNNVRRMLEGLDPHPMLPNYKNFKGTIQELGQNQYAVSGEIFVVDRNTVEITELPVRTWTQVYKEQVLEPMLNGTDKTPALISDYKEYHTDTTVKFVVKMTEEKLAQAEAAGLHKVFKLQTTLTCNSMVLFDHMGCLKKYETVQDILKEFFDLRLSYYGLRKEWLVGMLGAESTKLNNQARFILEKIQGKITIENRSKKDLIQMLVQRGYESDPVKAWKEAQEKAAEEEDSQNQHDDSSSDSGTPSGPDFNYILNMSLWSLTKEKVEELIKQRDTKGREVNDLKRKSPSDLWKEDL | ||||||
Region | 999-1008 | Interaction with DNA | ||||
Sequence: KLQTTLTCNS | ||||||
Compositional bias | 1098-1117 | Basic and acidic residues | ||||
Sequence: AWKEAQEKAAEEEDSQNQHD | ||||||
Region | 1098-1128 | Disordered | ||||
Sequence: AWKEAQEKAAEEEDSQNQHDDSSSDSGTPSG | ||||||
Compositional bias | 1245-1261 | Basic and acidic residues | ||||
Sequence: LLKKKKGDPDTTVVKVE | ||||||
Region | 1245-1586 | Disordered | ||||
Sequence: LLKKKKGDPDTTVVKVEFDEEFSGTPAEGTGEETLTPSAPVNKGPKPKREKKEPGTRVRKTPTSTGKTNAKKVKKRNPWSDDESKSESDLEEAEPVVIPRDSLLRRAAAERPKYTFDFSEEEDDDAAAADDSNDLEELKVKASPITNDGEDEFVPSDGLDKDEYAFSSGKSKATPEKSSNDKKSQDFGNLFSFPSYSQKSEDDSAKFDSNEEDTASVFAPSFGLKQTDKLPSKTVAAKKGKPPSDTAPKAKRAPKQKKIVETINSDSDSEFGIPKKTTTPKGKGRGAKKRKASGSENEGDYNPGRKPSKTASKKPKKTSFDQDSDVDIFPSDFTSEPPALPR | ||||||
Compositional bias | 1288-1302 | Basic and acidic residues | ||||
Sequence: GPKPKREKKEPGTRV | ||||||
Compositional bias | 1318-1362 | Basic and acidic residues | ||||
Sequence: KKRNPWSDDESKSESDLEEAEPVVIPRDSLLRRAAAERPKYTFDF | ||||||
Compositional bias | 1376-1390 | Basic and acidic residues | ||||
Sequence: SNDLEELKVKASPIT | ||||||
Compositional bias | 1428-1444 | Polar residues | ||||
Sequence: SQDFGNLFSFPSYSQKS | ||||||
Compositional bias | 1488-1508 | Basic and acidic residues | ||||
Sequence: SDTAPKAKRAPKQKKIVETIN | ||||||
Region | 1493-1499 | Interaction with PLSCR1 | ||||
Sequence: KAKRAPK |
Sequence similarities
Belongs to the type II topoisomerase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,612
- Mass (Da)181,909
- Last updated2005-09-27 v2
- Checksum974D9D5DAD0DB96A
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 16 | in Ref. 1; BAA07236 | ||||
Sequence: V → A | ||||||
Compositional bias | 1098-1117 | Basic and acidic residues | ||||
Sequence: AWKEAQEKAAEEEDSQNQHD | ||||||
Compositional bias | 1245-1261 | Basic and acidic residues | ||||
Sequence: LLKKKKGDPDTTVVKVE | ||||||
Compositional bias | 1288-1302 | Basic and acidic residues | ||||
Sequence: GPKPKREKKEPGTRV | ||||||
Compositional bias | 1318-1362 | Basic and acidic residues | ||||
Sequence: KKRNPWSDDESKSESDLEEAEPVVIPRDSLLRRAAAERPKYTFDF | ||||||
Compositional bias | 1376-1390 | Basic and acidic residues | ||||
Sequence: SNDLEELKVKASPIT | ||||||
Compositional bias | 1428-1444 | Polar residues | ||||
Sequence: SQDFGNLFSFPSYSQKS | ||||||
Sequence conflict | 1434 | in Ref. 1; BAA07236 | ||||
Sequence: L → P | ||||||
Compositional bias | 1488-1508 | Basic and acidic residues | ||||
Sequence: SDTAPKAKRAPKQKKIVETIN |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D38046 EMBL· GenBank· DDBJ | BAA07236.1 EMBL· GenBank· DDBJ | mRNA | ||
BC041106 EMBL· GenBank· DDBJ | AAH41106.1 EMBL· GenBank· DDBJ | mRNA | ||
BC054541 EMBL· GenBank· DDBJ | AAH54541.1 EMBL· GenBank· DDBJ | mRNA |