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Details on Person UniProt:P11388 TOP2A
| Class:Id | ReferenceGeneProduct:69899 |
|---|---|
| _chainChangeLog | chain:1-1531 added on Sat February 7 2015 |
| _displayName | UniProt:P11388 TOP2A |
| _timestamp | 2026-02-20 23:12:26 |
| chain | chain:1-1531 |
| checksum | 3DF40BC9E84789DC |
| comment | 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 (PubMed:17567603, PubMed:18790802, PubMed:22013166, PubMed:22323612, PubMed:27754753). May play a role in regulating the period length of BMAL1 transcriptional oscillation (By similarity).CATALYTIC ACTIVITY ATP-dependent breakage, passage and rejoining of double-stranded DNA.COFACTOR 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+).ACTIVITY REGULATION Specifically inhibited by the intercalating agent amsacrine.SUBUNIT Homodimer. Interacts with COPS5. Interacts with RECQL5; this stimulates DNA decatenation. Interacts with SETMAR; stimulates the topoisomerase activity (PubMed:18790802, PubMed:20457750). Interacts with DHX9; this interaction occurs in a E2 enzyme UBE2I- and RNA-dependent manner, negatively regulates DHX9-mediated double-stranded DNA and RNA duplex helicase activity and stimulates TOP2A-mediated supercoiled DNA relaxation activity (PubMed:12711669). Interacts with HNRNPU (via C-terminus); this interaction protects the topoisomerase TOP2A from degradation and positively regulates the relaxation of supercoiled DNA in a RNA-dependent manner (By similarity). Interacts with MCM3AP isoform GANP (PubMed:23652018). Interacts with ERCC6 (PubMed:26030138). Interacts with PLSCR1 (PubMed:17567603). Interacts with GCNA; this interaction allows the resolution of topoisomerase II (TOP2A) DNA-protein cross-links (By similarity). Interacts with POL1RA/RPA1 (via dock II) and UBTF in the context of Pol I complex; may assist Pol I transcription initiation by releasing supercoils occurring during DNA unwinding. Interacts with TPRN; TPRN interacts with a number of DNA damage response proteins, is recruited to sites of DNA damage and may play a role in DNA damage repair (PubMed:23213405). Interacts with FBXO28; this interaction leads to TOP2A proteasomal degradation (PubMed:27754753).INTERACTION Expressed in the tonsil, spleen, lymph node, thymus, skin, pancreas, testis, colon, kidney, liver, brain and lung (PubMed:9155056). Also found in high-grade lymphomas, squamous cell lung tumors and seminomas (PubMed:9155056).DOMAIN The N-terminus has several structural domains; the ATPase domain (about residues 1-265), the transducer domain (about 266-428) and the toprim domain (455-572) (PubMed:25202966). Comparing different structures shows ATP hydrolysis induces domain shifts in the N-terminus that are probably part of the mechanism of DNA cleavage and rejoining (PubMed:25202966).PTM Phosphorylation has no effect on catalytic activity. However, phosphorylation at Ser-1106 by CSNK1D/CK1 promotes DNA cleavable complex formation.PTM (Microbial infection) Deubiquitinated by Epstein-Barr virus BPLF1; leading to stabilized SUMOylated TOP2A trapped in cleavage complexes, which halts the DNA damage response to TOP2A-induced double-strand DNA breaks.PTM SUMOylated.PTM Ubiquitinated in a FBXO28-dependent manner; leading to TOP2A proteasomal degradation.MISCELLANEOUS Eukaryotic topoisomerase I and II can relax both negative and positive supercoils, whereas prokaryotic enzymes relax only negative supercoils.SIMILARITY Belongs to the type II topoisomerase family. |
| description | recommendedName: DNA topoisomerase 2-alpha ecNumber evidence="5 18 19"5.6.2.2 alternativeName: DNA topoisomerase II, alpha isozyme |
| geneName | TOP2A TOP2 |
| identifier | P11388 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Acetylation Alternative splicing ATP-binding Biological rhythms Cytoplasm Direct protein sequencing DNA-binding Isomerase Isopeptide bond Magnesium Metal-binding Nucleotide-binding Nucleus Phosphoprotein Proteomics identification Reference proteome Topoisomerase Ubl conjugation |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9841277] Weiser, Joel [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9862192] Weiser, Joel, 2024-02-26 [InstanceEdit:9909836] Weiser, Joel, 2024-05-14 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9983091] Weiser, Joel, 2026-02-20 |
| name | TOP2A |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:8962257] ENSEMBL:ENSG00000131747 TOP2A [Homo sapiens] |
| secondaryIdentifier | TOP2A_HUMAN B2RTS1 Q71UN1 Q71UQ5 Q9HB24 Q9HB25 Q9HB26 Q9UP44 Q9UQP9 |
| sequenceLength | 1531 |
| species | [Species:48887] Homo sapiens |
| (isoformParent) | [ReferenceIsoform:155047] UniProt:P11388-2 TOP2A [Homo sapiens] [ReferenceIsoform:155048] UniProt:P11388-3 TOP2A [Homo sapiens] [ReferenceIsoform:155049] UniProt:P11388-4 TOP2A [Homo sapiens] [ReferenceIsoform:402794] UniProt:P11388-1 TOP2A [Homo sapiens] |
| (referenceEntity) | [EntityWithAccessionedSequence:1362276] TOP2A [nucleoplasm] [Homo sapiens] [EntityWithAccessionedSequence:4641298] polySUMO2,3-TOP2A [nucleoplasm] [Homo sapiens] [EntityWithAccessionedSequence:4641367] monoSUMO1-K-TOP2A [nucleoplasm] [Homo sapiens] |
| (referenceSequence) | [GroupModifiedResidue:4641309] sumoylated lysine (monoSUMO1 [nucleoplasm]) at unknown position [GroupModifiedResidue:4641352] sumoylated lysine (polySUMO2,3 [nucleoplasm]) at unknown position |
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No pathways have been reviewed or authored by UniProt:P11388 TOP2A (69899)
