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IID00596
UniprotP13498
ProteinCytochrome b-245 light chain
GeneCYBA
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
195
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 149-168 Hetero dimer : IID00597Complex
 Evidence NMR 1wlp A The residues from Lys149 to Arg164 of p22phox-(149-168) form a relatively well defined structure, although the C-terminal four residues (165-168) are disordered (PMID: 16326715). Reference
       Region 1wlp A 149-168 order
Seq 151-168 Hetero dimer : IID00597Complex
 Evidence X-RAY 7yxw D Reference
       Region 7yxw D 151-161 order
       Region 7yxw D 162-168 disorder
SeqProS predicted 149-164 This region is predicted to be disordered by AlphaFold and NeProc; The residues from Lys149 to Arg164 of p22phox-(149-168) form a relatively well defined structure, although the C-terminal four residues (165-168) are disordered (PMID: 16326715). Hetero dimer : IID00597Complex
       Region 1wlp A 149-168 order
SeqProS predicted 151-161 This region is predicted to be disordered by AlphaFold and NeProc. Hetero dimer : IID00597Complex
       Region 7yxw D 151-161 order
Seqphosphorylation
    147-147 Phosphothreonine
    168-168 Phosphoserine
 
Prediction
NeProc
Disorder 135-195
Order 1-134
ProS 145-150,182-195
AlphaFold
Disorder 1-2,60-61,135-154,159-195
Order 3-59,62-134,155-158
Pfam Hmmer
PF05038 2-195 1.9e-159
SEG 151-183
Function
Function in SwissProt
Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. Associates with NOX3 to form a functional NADPH oxidase constitutively generating superoxide.
Biological Process
Diagram with PDB data
CYBA/NCF1Solution Structure Of The P22Phox-P47Phox Complex