Details for: TOP1
Associated with
Other Information
Genular Protein ID: 1492285734
Symbol: TOP1_HUMAN
Name: DNA topoisomerase 1
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 2833744
Title: cDNA cloning of human DNA topoisomerase I: catalytic activity of a 67.7-kDa carboxyl-terminal fragment.
PubMed ID: 2833744
PubMed ID: 1851751
Title: Structure of the human type I DNA topoisomerase gene.
PubMed ID: 1851751
PubMed ID: 14702039
Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.
PubMed ID: 14702039
DOI: 10.1038/ng1285
PubMed ID: 11780052
Title: The DNA sequence and comparative analysis of human chromosome 20.
PubMed ID: 11780052
DOI: 10.1038/414865a
PubMed ID: 2176592
Title: Structural characterisation of the human DNA topoisomerase I gene promoter.
PubMed ID: 2176592
PubMed ID: 7882333
Title: Mutation at the catalytic site of topoisomerase I in CEM/C2, a human leukemia cell line resistant to camptothecin.
PubMed ID: 7882333
PubMed ID: 2461859
Title: Monoclonal antibodies neutralizing mammalian DNA topoisomerase I activity.
PubMed ID: 2461859
PubMed ID: 2544263
Title: Characterization of the 3' region of the human DNA topoisomerase I gene.
PubMed ID: 2544263
PubMed ID: 2479024
Title: Determination of an epitope of the diffuse systemic sclerosis marker antigen DNA topoisomerase I: sequence similarity with retroviral p30gag protein suggests a possible cause for autoimmunity in systemic sclerosis.
PubMed ID: 2479024
PubMed ID: 10556215
Title: The t(11;20)(p15;q11) chromosomal translocation associated with therapy-related myelodysplastic syndrome results in an NUP98-TOP1 fusion.
PubMed ID: 10556215
PubMed ID: 12149243
Title: Sumoylation of topoisomerase I is involved in its partitioning between nucleoli and nucleoplasm and its clearing from nucleoli in response to camptothecin.
PubMed ID: 12149243
PubMed ID: 17081983
Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
PubMed ID: 17081983
PubMed ID: 18003733
Title: Simian virus 40 DNA replication is dependent on an interaction between topoisomerase I and the C-terminal end of T antigen.
PubMed ID: 18003733
DOI: 10.1128/jvi.01314-07
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
PubMed ID: 19413330
Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
PubMed ID: 19413330
DOI: 10.1021/ac9004309
PubMed ID: 19168442
Title: Cdc2-like kinases and DNA topoisomerase I regulate alternative splicing of tissue factor in human endothelial cells.
PubMed ID: 19168442
PubMed ID: 19608861
Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.
PubMed ID: 19608861
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 21406692
Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
PubMed ID: 21406692
PubMed ID: 22904072
Title: Rhythmic binding of Topoisomerase I impacts on the transcription of Bmal1 and circadian period.
PubMed ID: 22904072
DOI: 10.1093/nar/gks779
PubMed ID: 23185622
Title: CK2-mediated hyperphosphorylation of topoisomerase I targets serine 506, enhances topoisomerase I-DNA Binding, and increases cellular camptothecin sensitivity.
PubMed ID: 23185622
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
DOI: 10.1021/pr300630k
PubMed ID: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
PubMed ID: 24275569
PubMed ID: 25218447
Title: Uncovering global SUMOylation signaling networks in a site-specific manner.
PubMed ID: 25218447
DOI: 10.1038/nsmb.2890
PubMed ID: 25114211
Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.
PubMed ID: 25114211
PubMed ID: 25772364
Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.
PubMed ID: 25772364
PubMed ID: 25755297
Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.
PubMed ID: 25755297
PubMed ID: 26030138
Title: Identification of Novel Proteins Co-Purifying with Cockayne Syndrome Group B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and Chromatin Dynamics.
PubMed ID: 26030138
PubMed ID: 28112733
Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.
PubMed ID: 28112733
DOI: 10.1038/nsmb.3366
PubMed ID: 9488644
Title: Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA.
PubMed ID: 9488644
PubMed ID: 9488652
Title: A model for the mechanism of human topoisomerase I.
PubMed ID: 9488652
PubMed ID: 10841763
Title: Novel insights into catalytic mechanism from a crystal structure of human topoisomerase I in complex with DNA.
PubMed ID: 10841763
DOI: 10.1021/bi992690t
PubMed ID: 12209008
Title: 8-Oxoguanine rearranges the active site of human topoisomerase I.
PubMed ID: 12209008
PubMed ID: 12426403
Title: The mechanism of topoisomerase I poisoning by a camptothecin analog.
PubMed ID: 12426403
PubMed ID: 12533542
Title: Structural impact of the leukemia drug 1-beta-D-arabinofuranosylcytosine (Ara-C) on the covalent human topoisomerase I-DNA complex.
PubMed ID: 12533542
PubMed ID: 14594810
Title: The role of lysine 532 in the catalytic mechanism of human topoisomerase I.
PubMed ID: 14594810
PubMed ID: 15165849
Title: Mechanisms of camptothecin resistance by human topoisomerase I mutations.
PubMed ID: 15165849
PubMed ID: 15801827
Title: Structures of three classes of anticancer agents bound to the human topoisomerase I-DNA covalent complex.
PubMed ID: 15801827
DOI: 10.1021/jm049146p
PubMed ID: 16033260
Title: Synthesis and mechanism of action studies of a series of norindenoisoquinoline topoisomerase I poisons reveal an inhibitor with a flipped orientation in the ternary DNA-enzyme-inhibitor complex as determined by X-ray crystallographic analysis.
PubMed ID: 16033260
DOI: 10.1021/jm050076b
PubMed ID: 1849260
Title: Molecular cloning of a cDNA of a camptothecin-resistant human DNA topoisomerase I and identification of mutation sites.
PubMed ID: 1849260
DOI: 10.1093/nar/19.1.69
PubMed ID: 1332703
Title: Detection of topoisomerase I gene point mutation in CPT-11 resistant lung cancer cell line.
PubMed ID: 1332703
PubMed ID: 16959974
Title: The consensus coding sequences of human breast and colorectal cancers.
PubMed ID: 16959974
Sequence Information:
- Length: 765
- Mass: 90726
- Checksum: 6FBED540BCF7BE28
- Sequence:
MSGDHLHNDS QIEADFRLND SHKHKDKHKD REHRHKEHKK EKDREKSKHS NSEHKDSEKK HKEKEKTKHK DGSSEKHKDK HKDRDKEKRK EEKVRASGDA KIKKEKENGF SSPPQIKDEP EDDGYFVPPK EDIKPLKRPR DEDDADYKPK KIKTEDTKKE KKRKLEEEED GKLKKPKNKD KDKKVPEPDN KKKKPKKEEE QKWKWWEEER YPEGIKWKFL EHKGPVFAPP YEPLPENVKF YYDGKVMKLS PKAEEVATFF AKMLDHEYTT KEIFRKNFFK DWRKEMTNEE KNIITNLSKC DFTQMSQYFK AQTEARKQMS KEEKLKIKEE NEKLLKEYGF CIMDNHKERI ANFKIEPPGL FRGRGNHPKM GMLKRRIMPE DIIINCSKDA KVPSPPPGHK WKEVRHDNKV TWLVSWTENI QGSIKYIMLN PSSRIKGEKD WQKYETARRL KKCVDKIRNQ YREDWKSKEM KVRQRAVALY FIDKLALRAG NEKEEGETAD TVGCCSLRVE HINLHPELDG QEYVVEFDFL GKDSIRYYNK VPVEKRVFKN LQLFMENKQP EDDLFDRLNT GILNKHLQDL MEGLTAKVFR TYNASITLQQ QLKELTAPDE NIPAKILSYN RANRAVAILC NHQRAPPKTF EKSMMNLQTK IDAKKEQLAD ARRDLKSAKA DAKVMKDAKT KKVVESKKKA VQRLEEQLMK LEVQATDREE NKQIALGTSK LNYLDPRITV AWCKKWGVPI EKIYNKTQRE KFAWAIDMAD EDYEF
Genular Protein ID: 1814073333
Symbol: Q9BVT2_HUMAN
Name: N/A
UniProtKB Accession Codes:
Database IDs:
Sequence Information:
- Length: 176
- Mass: 20342
- Checksum: 2D922F02D032E4CD
- Sequence:
RTYNASITLQ QQLKELTAPD ENIPAKILSY NRANRAVAIL CNHQRAPPKT FEKSMMNLQT KIDAKKEQLA DARRDLKSAK ADAKVMKDAK TKKVVESKKK AVQRLEEQLM KLEVQATDRE ENKQIALGTS KLNYLDPRIT VAWCKKWGVP IEKIYNKTQR EKFAWAIDMA DEDYEF
Database document:
This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.