Q7YR26 (TOP1_CHLAE) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 56.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: DNA topoisomerase 1 EC=5.99.1.2 Alternative name(s): DNA topoisomerase I | ||
| Gene names |
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| Organism | Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops) | ||
| Taxonomic identifier | 9534 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Cercopithecinae › Chlorocebus |
Protein attributes
| Sequence length | 767 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | 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-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand than undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells By similarity. |
| Catalytic activity | ATP-independent breakage of single-stranded DNA, followed by passage and rejoining. |
| Enzyme regulation | Specifically inhibited by camptothecin (CPT), a plant alkaloid with antitumor activity. |
| Subunit structure | Monomer By similarity. |
| Subcellular location | Nucleus › nucleolus. Nucleus › nucleoplasm. Note: Diffuse nuclear localization with some enrichment in nucleoli. On CPT treatment, cleared from nucleoli into nucleoplasm. Sumolyated forms found in both nucleoplasm and nucleoli By similarity. |
| Post-translational modification | Sumoylated. Lys-119 is the main site of sumoylation. Sumoylation plays a role in partitioning TOP1 between nucleoli and nucleoplasm. Levels are dramatically increased on camptothecin (CPT) treatment By similarity. |
| Miscellaneous | Eukaryotic topoisomerase I and II can relax both negative and positive supercoils, whereas prokaryotic enzymes relax only negative supercoils. |
| Sequence similarities | Belongs to the type IB topoisomerase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Nucleus |
| Ligand | ATP-binding DNA-binding Nucleotide-binding |
| Molecular function | Isomerase Topoisomerase |
| PTM | Acetylation Isopeptide bond Phosphoprotein Ubl conjugation |
| Gene Ontology (GO) | |
| Biological process | DNA topological change Inferred from electronic annotation. Source: InterPro |
| Cellular component | chromosome Inferred from electronic annotation. Source: InterPro nucleolusInferred from sequence or structural similarity. Source: UniProtKB nucleoplasmInferred from sequence or structural similarity. Source: UniProtKB |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA topoisomerase (ATP-hydrolyzing) activityInferred from electronic annotation. Source: InterPro DNA topoisomerase type I activityInferred from sequence or structural similarity. Source: UniProtKB chromatin bindingInferred from sequence or structural similarity. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 767 | 766 | DNA topoisomerase 1 | PRO_0000145199 | |||||
Regions | |||||||||
| Compositional bias | 23 – 206 | 184 | Lys-rich | ||||||
Sites | |||||||||
| Active site | 725 | 1 | O-(3'-phospho-DNA)-tyrosine intermediate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylserine By similarity | ||||||
| Modified residue | 114 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 282 | 1 | N6-acetyllysine By similarity | ||||||
| Cross-link | 105 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Probable | |||||||
| Cross-link | 119 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity | |||||||
| Cross-link | 155 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Probable | |||||||
Sequences
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References
| [1] | "Human topoisomerase I promotes HIV-1 proviral DNA synthesis: Implications for the species specificity and cellular tropism of HIV-1 infection." Shoya Y., Tokunaga K., Sawa H., Maeda M., Ueno T., Yoshikawa T., Hasegawa H., Sata T., Kurata T., Hall W.W., Cullen B.R., Takahashi H. Proc. Natl. Acad. Sci. U.S.A. 100:8442-8447(2003) [PubMed: 12829794] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB089321 mRNA. Translation: BAC78678.1. |
3D structure databases | |
| ProteinModelPortal | Q7YR26. |
| SMR | Q7YR26. Positions 201-767. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | Q7YR26. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| HOVERGEN | HBG007988. |
Family and domain databases | |
| InterPro | IPR011010. DNA_brk_join_enz. IPR013034. DNA_topo_domain1. IPR018521. TopoI_AS. IPR001631. TopoI_C. IPR013499. TopoI_C_euk. IPR014711. TopoI_cat_a-hlx-sub_euk. IPR014727. TopoI_cat_a/b-sub_euk. IPR013500. TopoI_cat_euk. IPR008336. TopoI_DNA-bd_euk. IPR013030. TopoI_DNA-bd_mixed-a/b_euk. IPR009054. TopoI_insert_euk. [Graphical view] |
| Gene3D | G3DSA:3.90.15.10. TopoI_cat_a-hlx-sub_euk. 1 hit. G3DSA:1.10.132.10. TopoI_cat_a/b-sub_euk. 1 hit. G3DSA:1.10.10.41. TopoI_DNA-bd_a-hlx_euk. 1 hit. G3DSA:2.170.11.10. TopoI_DNA-bd_mixed-a/b_euk. 2 hits. |
| Pfam | PF01028. Topoisom_I. 1 hit. PF02919. Topoisom_I_N. 1 hit. [Graphical view] |
| PRINTS | PR00416. EUTPISMRASEI. |
| SMART | SM00435. TOPEUc. 1 hit. [Graphical view] |
| SUPFAM | SSF56349. DNA_brk_join_enz. 1 hit. SSF46596. Topismrse_insert. 1 hit. SSF56741. TopoI_DNA_bd_euk. 1 hit. |
| PROSITE | PS00176. TOPOISOMERASE_I_EUK. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | TOP1_CHLAE | ||||||||
| Accession | Primary (citable) accession number: Q7YR26 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with