› 2kqs

Solution NMR

Phosphorylation of SUMO-interacting motif by CK2 enhances Daxx SUMO binding activity

Released:
DOI: 10.2210/pdb2kqs/pdb
PDB entry 2kqs coloured by chain, ensemble of 20 models, front view.
PDB entry 2kqs coloured by chain, ensemble of 20 models, side view.
PDB entry 2kqs coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Structural and functional roles of Daxx SIM phosphorylation in SUMO paralog-selective binding and apoptosis modulation.
Chang CC, Naik MT, Huang YS, Jeng JC, Liao PH, Kuo HY, Ho CC, Hsieh YL, Lin CH, Huang NJ, Naik NM, Kung CC, Lin SY, Chen RH, Chang KS, Huang TH, Shih HM
Mol Cell 42 62-74 (2011)
PMID: 21474068

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159022 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Small ubiquitin-related modifier 1 Chain: A
Molecule details ›
Chain: A
Length: 99 amino acids
Theoretical weight: 11.29 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P63165 (Residues: 1-97; Coverage: 96%)
Gene names: OK/SW-cl.43, SMT3C, SMT3H3, SUMO1, UBL1
Sequence domains: Ubiquitin-2 like Rad60 SUMO-like
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Death domain-associated protein 6 Chain: B
Molecule details ›
Chain: B
Length: 22 amino acids
Theoretical weight: 2.3 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q9UER7 (Residues: 721-740; Coverage: 3%)
Gene names: BING2, DAP6, DAXX

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

26 review citations

Sumoylation: a regulatory protein modification in health and disease.
Flotho et al. (2013)
25 more

2 mentions without citation

Characterizing the N- and C-terminal Small ubiquitin-like modifier (SUMO)-interacting motifs of the scaffold protein DAXX.
Escobar-Cabrera et al. (2011)
1 more