Q64399 · TOP2B_CRILO
- ProteinDNA topoisomerase 2-beta
- GeneTOP2B
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1612 (go to sequence)
- Protein existenceEvidence at transcript 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.
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
Aspect | Term | |
---|---|---|
Cellular Component | nucleolus | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | ATP binding | |
Molecular Function | DNA binding | |
Molecular Function | DNA topoisomerase activity | |
Molecular Function | DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity | |
Molecular Function | metal ion binding | |
Molecular Function | ribonucleoprotein complex binding | |
Biological Process | DNA topological change | |
Biological Process | resolution of meiotic recombination intermediates | |
Biological Process | sister chromatid segregation |
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
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Cricetidae > Cricetinae > Cricetulus
Accessions
- Primary accessionQ64399
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
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_0000145368 | 2-1612 | DNA topoisomerase 2-beta | |||
Sequence: AKSSLAGADGALTWVNNAAKKEELETSNKNDSSKKLSVERVYQKKTQLEHILLRPDTYIGSVEPLTQLMWVYDEDVGMNCREVTFVPGLYKIFDEILVNAADNKQRDKNMTCIKVSIDPESNIISIWNNGKGIPVVEHKVEKVYVPALIFGQLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTKFTVETACKEYKHSFKQTWMNNMMKTSEAKIKHFDGEDYTCITFQPDLAKFKMEKLDKDIVALMTRRAYDLAGSCKGVKVMFNGKKLPVNGFRSYVDLYVKDKLDETGVALKVIHELANERWDVCLTLSEKGFQQISFVNSIATTKGGRHVDYVVDQVVGKLIEVVKKKNKAGVSVKPFQVKNHIWVFINCLIENPTFDSQTKENMTLQPKSFGSKCQLSEKFFKAASNCGIVESILNWVKFKAQTQLNKKCSSVKYSKIKGIPKLDDANDAGGKHSLECTLILTEGDSAKSLAVSGLGVIGRDRYGVFPLRGKILNVREASHKQIMENAEINNIIKIVGLQYKKSYDDAESLKTLRYGKIMIMTDQDQDGSHIKGLLINFIHHNWPSLLKHGFLEEFITPIVKASKNKQELSFYSIPEFDEWKKHIENQKAWKIKYYKGLGTSTAKEAKEYFADMERHRILFRYAGPEDDAAITLAFSKKKIDDRKEWLTNFMEDRRQRRLHGLPEQFLYGTATKHLTYNDFINKELILFSNSDNERSIPSLVDGFKPGQRKVLFTCFKRNDKREVKVAQLAGSVAEMSAYHHGEQALMMTIVNLAQNFVGSNNINLLQPIGQFGTRLHGGKDAASPRYIFTMLSSLARLLFPAVDDNLLKFLYDDNQRVEPEWYIPIIPMVLINGAEGIGTGWACKLPNYDAREIVNNVRRMLDGLDPHPMLPNYKNFKGTIQELGQNQYAVSGEIFVVDRNTVEITELPVRTWTQVYKEQVLEPMLNGTDKTPALISDYKEYHTDTTVKFVVKMTEEKLAQAEAAGLHKVFKLQTTLTCNSMVLFDHMGCLKKYETVQDILKEFFDLRLSYYGLRKEWLVGMLGAESTKLNNQARFILEKIQGKITIENRSKKDLIQMLVQRGYESDPVRAWKEAQEKAAEEEDTQNQHDDSSSDSGTPSGPDFNYILNMSLWSLTKEKVEELIKQRDTKGREVNDLKRKSPSDLWKEDLAAFVEELDKVEAQEREDILAGMSGKAIKGKVGKPKVKKLQLEETMPSPYGRRIVPEITAMKADASRKLLKKKKGDPDTPVVKVEFDEEFSGTPVEGTGEETLTPSAPVNKGPKPKREKKEPGTRVRKTPTSAGKPNAKKVKKRNPWSDDESKSESDLEETEPVVIPRDSLLRRAAAERPKYTFDFSEEEEEDADDDDDNNDLEELKVKASPITNDGEDEFVPSDGLDKDEYAFSPGKSKATPEKSSHDKKSQDFGNLFSFPSYSQKSEDDSAKFDSNEEDTASVFTPSFGLKQTDKVPSKTVAAKKGKPPSDTAPKAKRAPKQKKVVETVNSDSDSEFGIPKKTTTPKGKGRGAKKRKASGSENEGDYNPGRKPSKTASKKPKKTSFDQDSDVDIFPSDFTSEPPALPRTGRARKEVKYFAESDEEEDVDFAMFN | ||||||
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 | ||||||
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
Interaction
Subunit
Homodimer (By similarity).
Interacts with PLSCR1 and KIAA1210 (By similarity).
Interacts with PLSCR1 and KIAA1210 (By similarity).
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: IPSLVDGFKPGQRKVLFTCFKRNDKREVKVAQLAGSVAEMSAYHHGEQALMMTIVNLAQNFVGSNNINLLQPIGQFGTRLHGGKDAASPRYIFTMLSSLARLLFPAVDDNLLKFLYDDNQRVEPEWYIPIIPMVLINGAEGIGTGWACKLPNYDAREIVNNVRRMLDGLDPHPMLPNYKNFKGTIQELGQNQYAVSGEIFVVDRNTVEITELPVRTWTQVYKEQVLEPMLNGTDKTPALISDYKEYHTDTTVKFVVKMTEEKLAQAEAAGLHKVFKLQTTLTCNSMVLFDHMGCLKKYETVQDILKEFFDLRLSYYGLRKEWLVGMLGAESTKLNNQARFILEKIQGKITIENRSKKDLIQMLVQRGYESDPVRAWKEAQEKAAEEEDTQNQHDDSSSDSGTPSGPDFNYILNMSLWSLTKEKVEELIKQRDTKGREVNDLKRKSPSDLWKEDL | ||||||
Region | 999-1008 | Interaction with DNA | ||||
Sequence: KLQTTLTCNS | ||||||
Compositional bias | 1098-1117 | Basic and acidic residues | ||||
Sequence: AWKEAQEKAAEEEDTQNQHD | ||||||
Region | 1098-1128 | Disordered | ||||
Sequence: AWKEAQEKAAEEEDTQNQHDDSSSDSGTPSG | ||||||
Compositional bias | 1245-1261 | Basic and acidic residues | ||||
Sequence: LLKKKKGDPDTPVVKVE | ||||||
Region | 1245-1586 | Disordered | ||||
Sequence: LLKKKKGDPDTPVVKVEFDEEFSGTPVEGTGEETLTPSAPVNKGPKPKREKKEPGTRVRKTPTSAGKPNAKKVKKRNPWSDDESKSESDLEETEPVVIPRDSLLRRAAAERPKYTFDFSEEEEEDADDDDDNNDLEELKVKASPITNDGEDEFVPSDGLDKDEYAFSPGKSKATPEKSSHDKKSQDFGNLFSFPSYSQKSEDDSAKFDSNEEDTASVFTPSFGLKQTDKVPSKTVAAKKGKPPSDTAPKAKRAPKQKKVVETVNSDSDSEFGIPKKTTTPKGKGRGAKKRKASGSENEGDYNPGRKPSKTASKKPKKTSFDQDSDVDIFPSDFTSEPPALPR | ||||||
Compositional bias | 1288-1302 | Basic and acidic residues | ||||
Sequence: GPKPKREKKEPGTRV | ||||||
Compositional bias | 1318-1362 | Basic and acidic residues | ||||
Sequence: KKRNPWSDDESKSESDLEETEPVVIPRDSLLRRAAAERPKYTFDF | ||||||
Compositional bias | 1363-1378 | Acidic residues | ||||
Sequence: SEEEEEDADDDDDNND | ||||||
Compositional bias | 1429-1444 | Polar residues | ||||
Sequence: QDFGNLFSFPSYSQKS | ||||||
Compositional bias | 1455-1472 | Polar residues | ||||
Sequence: EEDTASVFTPSFGLKQTD | ||||||
Compositional bias | 1488-1508 | Basic and acidic residues | ||||
Sequence: SDTAPKAKRAPKQKKVVETVN | ||||||
Region | 1493-1499 | Interaction with PLSCR1 | ||||
Sequence: KAKRAPK |
Sequence similarities
Belongs to the type II topoisomerase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,612
- Mass (Da)182,075
- Last updated1996-11-01 v1
- ChecksumC01D6FC40620FC68
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1098-1117 | Basic and acidic residues | ||||
Sequence: AWKEAQEKAAEEEDTQNQHD | ||||||
Compositional bias | 1245-1261 | Basic and acidic residues | ||||
Sequence: LLKKKKGDPDTPVVKVE | ||||||
Compositional bias | 1288-1302 | Basic and acidic residues | ||||
Sequence: GPKPKREKKEPGTRV | ||||||
Compositional bias | 1318-1362 | Basic and acidic residues | ||||
Sequence: KKRNPWSDDESKSESDLEETEPVVIPRDSLLRRAAAERPKYTFDF | ||||||
Compositional bias | 1363-1378 | Acidic residues | ||||
Sequence: SEEEEEDADDDDDNND | ||||||
Compositional bias | 1429-1444 | Polar residues | ||||
Sequence: QDFGNLFSFPSYSQKS | ||||||
Compositional bias | 1455-1472 | Polar residues | ||||
Sequence: EEDTASVFTPSFGLKQTD | ||||||
Compositional bias | 1488-1508 | Basic and acidic residues | ||||
Sequence: SDTAPKAKRAPKQKKVVETVN |