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