Serine 298 Phosphorylation in Linker 2 of UHRF1 Regulates Ligand-Binding Property of its Tandem Tudor Domain

Kori S, Jimenji T, Ekimoto T, Sato M, Kusano F, Oda T, Unoki M, Ikeguchi M, Arita K Journal of Molecular Biology (2020) DOI

SASDJ73 – Ubiquitin-like UHRF1 with PHD and RING finger domains (TTD-L2 (123-301))

E3 ubiquitin-protein ligase UHRF1
MWexperimental 20 kDa
MWexpected 21 kDa
VPorod 26 nm3
log I(s) 2.18×10-2 2.18×10-3 2.18×10-4 2.18×10-5
E3 ubiquitin-protein ligase UHRF1 small angle scattering data  s, nm-1
ln I(s)
E3 ubiquitin-protein ligase UHRF1 Guinier plot ln 2.19×10-2 Rg: 2.0 nm 0 (2.0 nm)-2 s2
(sRg)2I(s)/I(0)
E3 ubiquitin-protein ligase UHRF1 Kratky plot 1.104 0 3 sRg
p(r)
E3 ubiquitin-protein ligase UHRF1 pair distance distribution function Rg: 2.0 nm 0 Dmax: 6.6 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of UHRF1 PHD and RING finger domains (TTD-L2 (123-301)) were collected on the BL-10C beam line at the Photon Factory (PF), High Energy Accelerator Research Organization (KEK; Tsukuba, Japan) using a Pilatus3 2M detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.15 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 50.00 μl sample at 6 mg/ml was injected at a 0.02 ml/min flow rate onto a GE Superdex 200 Increase 5/150 column at 20°C. 79 successive 20 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

CAUTION! Buffer composition unknown.

E3 ubiquitin-protein ligase UHRF1 (UHRF1)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   20.8 kDa
 
UniProt   Q96T88 (123-301)
Sequence   FASTA