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TOP3A (DNA topoisomerase 3-alpha) is an enzyme. In the public catalogues the evidence so far is association rather than a proven role.
Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand.
Open Targets scores its association with cancer at 0.55 (direct and indirect evidence; datatypes literature 0.83, affected pathway 0.87, genetic association 0.00).
In plain words · TOP3A (DNA topoisomerase 3-alpha) is an enzyme. In the public catalogues the evidence so far is association rather than a proven role.
TOP3A (DNA topoisomerase 3-alpha) is an enzyme. In the public catalogues the evidence so far is association rather than a proven role.
Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex.
No product in this corpus aims at TOP3A yet. Inhibitors are shaped to fit the enzyme's active site so the reaction the cancer relies on stops.
First described 1996. Earliest sequence paper UniProt cites for the protein: Hanai et al, Proc. Natl. Acad. Sci. U.S.A, 1996, "Human TOP3: a single-copy gene encoding DNA topoisomerase III". Source.
Sources: HGNC HGNC:11992 (approved symbol, name, aliases, locus and cross-references (hgnc_complete_set.txt)); UniProt Q13472 (protein name, function text, keywords and locations (REST API)); Open Targets ENSG00000177302 (association with cancer (MONDO_0004992) 0.55; (GraphQL API, CC0))
Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone. As an essential component of the RMI complex it is involved in chromosome separation and the processing of homologous recombination intermediates to limit DNA crossover formation in cells. Location: Mitochondrion matrix (UniProt). Locus 17p11.2 (HGNC).
Query for this target: (TITLE:"TOP3A" OR ABSTRACT:"TOP3A" OR TITLE:"DNA topoisomerase III alpha" OR ABSTRACT:"DNA topoisomerase III alpha" OR TITLE:"DNA topoisomerase 3-alpha" OR ABSTRACT:"DNA topoisomerase 3-alpha" OR TITLE:"ZGRF7" OR ABSTRACT:"ZGRF7" OR TITLE:"TOP3" OR ABSTRACT:"TOP3") AND (cancer OR tumor OR tumour OR oncology OR carcinoma OR lymphoma OR leukemia OR leukaemia OR myeloma OR sarcoma OR melanoma OR glioma). Results are unfiltered search hits about TOP3A, not a curated reading list.