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Open data
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Basic information
Entry | ![]() |
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![]() | Basic domain of telomeric repeat-binding factor 2 (TRF2)
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Function / homology | ![]() axonal transport of messenger ribonucleoprotein complex / negative regulation of beta-galactosidase activity / negative regulation of telomere single strand break repair / negative regulation of telomere maintenance via recombination / telomeric loop formation / negative regulation of telomere maintenance via semi-conservative replication / : / negative regulation of telomeric D-loop disassembly / negative regulation of telomere capping / protection from non-homologous end joining at telomere ...axonal transport of messenger ribonucleoprotein complex / negative regulation of beta-galactosidase activity / negative regulation of telomere single strand break repair / negative regulation of telomere maintenance via recombination / telomeric loop formation / negative regulation of telomere maintenance via semi-conservative replication / : / negative regulation of telomeric D-loop disassembly / negative regulation of telomere capping / protection from non-homologous end joining at telomere / RNA-templated DNA biosynthetic process / negative regulation of t-circle formation / negative regulation of telomere maintenance / telomeric D-loop disassembly / shelterin complex / Telomere C-strand synthesis initiation / regulation of telomere maintenance via telomerase / double-stranded telomeric DNA binding / Telomere C-strand (Lagging Strand) Synthesis / nuclear telomere cap complex / G-rich strand telomeric DNA binding / telomere capping / Processive synthesis on the C-strand of the telomere / Polymerase switching on the C-strand of the telomere / Removal of the Flap Intermediate from the C-strand / regulation of telomere maintenance / negative regulation of telomere maintenance via telomere lengthening / protein localization to chromosome, telomeric region / telomeric DNA binding / negative regulation of telomere maintenance via telomerase / positive regulation of telomere maintenance / negative regulation of cellular senescence / Telomere Extension By Telomerase / Packaging Of Telomere Ends / Recognition and association of DNA glycosylase with site containing an affected purine / Cleavage of the damaged purine / Recognition and association of DNA glycosylase with site containing an affected pyrimidine / Cleavage of the damaged pyrimidine / Inhibition of DNA recombination at telomere / Meiotic synapsis / telomere maintenance / positive regulation of nitric-oxide synthase activity / male germ cell nucleus / DNA Damage/Telomere Stress Induced Senescence / cellular senescence / in utero embryonic development / chromosome, telomeric region / nuclear body / axon / negative regulation of gene expression / positive regulation of gene expression / protein-containing complex binding / enzyme binding / protein homodimerization activity / nucleoplasm / nucleus Similarity search - Function |
Biological species | ![]() |
![]() | ![]() Title: Basic domain of telomere guardian TRF2 reduces D-loop unwinding whereas Rap1 restores it Authors: Nečasová I / Janoušková E / Klumpler T |
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Structure visualization
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Downloads & links
-Data source
SASBDB page | ![]() |
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-Related structure data
Related structure data | C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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External links
Related items in Molecule of the Month |
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-Models
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Sample
![]() | Name: Basic domain of telomeric repeat-binding factor 2 (TRF2) Specimen concentration: 1.2 mg/ml |
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Buffer | Name: 50 mM NaPi, 50 mM NaCl / pH: 7 |
Entity #569 | Name: TRF2 / Type: protein Description: Basic domain of telomeric repeat-binding factor 2 Formula weight: 4.587 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: Q15554 Sequence: GPPGSMAGGG GSSDGSGRAA GRRASRSSGR ARRGRHEPGL GGPAERGAG |
-Experimental information
Beam | Instrument name: CEITEC Rigaku BioSAXS-1000 / City: Brno / 国: Czech Republic ![]() | |||||||||||||||||||||||||||||||||
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Detector | Name: Pilatus 100K / Pixsize x: 172 mm | |||||||||||||||||||||||||||||||||
Scan | Measurement date: Mar 5, 2015 / Storage temperature: 4 °C / Cell temperature: 4 °C / Exposure time: 3600 sec. / Number of frames: 6 / Unit: 1/A /
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Distance distribution function P(R) |
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Result |
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