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IID50243
 UniprotP28574
ProteinProtein max
GeneMax
OrganismMus musculus
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
 Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
160
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 22-36 Homo dimer : IID00541Complex
 Evidence X-RAY 3u5v A Reference
       Region 3u5v A 22-27 disorder
       Region 3u5v A 28-36 order
Seq 74-102 Hetero dimer : IID00012Complex
 Evidence NMR 2a93 B Reference
       Region 2a93 B 74-102 order
 Evidence NMR 1a93 B Reference
       Region 1a93 B 74-102 order
Seqphosphorylation
    11-11 Phosphoserine
    2-2 Phosphoserine
    107-107 Phosphoserine
Seqacetylation
    2-2 N-acetylserine
    66-66 N6-acetyllysine
    154-154 N6-acetyllysine
    153-153 N6-acetyllysine
 
Prediction
NeProc
Disorder 1-26,113-160
Order 27-112
ProS 21-26,133-136
AlphaFold
Disorder 1-3,5-6,8-16,111-125,128-160
Order 4-4,7-7,17-110,126-127
Pfam Hmmer
PF00010 24-75 2.6e-21
SEG 135-149
Function
Function in SwissProt
Transcription regulator. Forms a sequence-specific DNA-binding protein complex with MYC or MAD which recognizes the core sequence 5'-CAC[GA]TG-3'. The MYC:MAX complex is a transcriptional activator, whereas the MAD:MAX complex is a repressor. CpG methylation of the recognition site greatly inhibits DNA binding, suggesting that DNA methylation may regulate the MYC:MAX complex in vivo. May repress transcription via the recruitment of a chromatin remodeling complex containing H3 'Lys-9' histone methyltransferase activity. Represses MYC transcriptional activity from E-box elements (By similarity).