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IID00458
 UniprotP58340
ProteinMyeloid leukemia factor 1
GeneMLF1
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
 Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
268
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 29-42 Hetero tetramer : IID00512Complex
 Evidence X-RAY 3ubw P Reference
       Region 3ubw P 29-30 disorder
       Region 3ubw P 31-37 order
       Region 3ubw P 38-42 disorder
 Evidence X-RAY 3ual P Reference
       Region 3ual P 29-30 disorder
       Region 3ual P 31-38 order
       Region 3ual P 39-42 disorder
SeqProS possible 31-38 14-3-3 binding motif Hetero tetramer : IID00512Complex
       Region 3ual P 31-38 order
       Region 3ubw P 31-37 order
Seqphosphorylation
    8-8 Phosphoserine
    32-32 Phosphoserine
    34-34 Phosphoserine
 
Prediction
NeProc
Disorder 1-120,145-149,173-176,183-186,196-268
Order 121-144,150-172,177-182,187-195
ProS 1-23,35-39,65-71,85-120,145-149,173-176,183-186,196-215,250-265
AlphaFold
Disorder 1-11,29-30,32-76,90-90,94-100,207-268
Order 12-28,31-31,77-89,91-93,101-206
SEG 7-18 ,46-60
Function
Function in SwissProt
Involved in lineage commitment of primary hemopoietic progenitors by restricting erythroid formation and enhancing myeloid formation. Interferes with erythropoietin-induced erythroid terminal differentiation by preventing cells from exiting the cell cycle through suppression of CDKN1B/p27Kip1 levels. Suppresses COP1 activity via CSN3 which activates p53 and induces cell cycle arrest. Binds DNA and affects the expression of a number of genes so may function as a transcription factor in the nucleus.
Biological Process
Diagram with PDB data
MLF1/YWHAECrystal structure of 14-3-3 epsilon with Mlf1 peptide