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IID00814
UniprotP61244
ProteinProtein max
GeneMAX
OrganismHomo sapiens
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 4-12,22-107 Homo dimer :
 Evidence X-RAY 1an2 A Reference
       Region 1an2 A 22-107 order
 Evidence X-RAY 5eyo A Reference
       Region 5eyo A 22-106 order
       Region 5eyo A 107-107 disorder
 Evidence X-RAY 5eyo C Reference
       Region 5eyo C 22-107 order
 Evidence X-RAY 1hlo A Reference
       Region 1hlo A 4-12 order
       Region 1hlo A 22-92 order
 Evidence X-RAY 1hlo B Reference
       Region 1hlo B 4-10 disorder
       Region 1hlo B 11-12 order
       Region 1hlo B 22-92 order
 Evidence NMR 1r05 A Reference
       Region 1r05 A 22-103 order
       Region 1r05 A 22-32 high_rmsd
       Region 1r05 A 54-54 high_rmsd
 Evidence NMR 1r05 B Reference
       Region 1r05 B 22-103 order
       Region 1r05 B 22-32 high_rmsd
       Region 1r05 B 54-54 high_rmsd
Seqdisorder 22-34
 Evidence NMR Reference
       Region 22-34 disorder
Seq 22-103 Hetero octamer : IID00012Complex
 Evidence X-RAY 6g6l H Reference
       Region 6g6l H 22-35 disorder
       Region 6g6l H 36-102 order
       Region 6g6l H 103-103 disorder
 Evidence X-RAY 6g6l F Reference
       Region 6g6l F 22-31 disorder
       Region 6g6l F 32-102 order
       Region 6g6l F 103-103 disorder
 Evidence X-RAY 6g6l D Reference
       Region 6g6l D 22-31 disorder
       Region 6g6l D 32-102 order
       Region 6g6l D 103-103 disorder
 Evidence X-RAY 6g6l B Reference
       Region 6g6l B 22-34 disorder
       Region 6g6l B 35-102 order
       Region 6g6l B 103-103 disorder
Seq 22-103 Hetero tetramer : IID00012Complex
 Evidence X-RAY 6g6j D Reference
       Region 6g6j D 22-32 disorder
       Region 6g6j D 33-102 order
       Region 6g6j D 103-103 disorder
 Evidence X-RAY 6g6j B Reference
       Region 6g6j B 22-29 disorder
       Region 6g6j B 30-102 order
       Region 6g6j B 103-103 disorder
Seq 22-103 Hetero tetramer : IID00012Complex
 Evidence X-RAY 6g6k D Reference
       Region 6g6k D 22-25 disorder
       Region 6g6k D 26-101 order
       Region 6g6k D 102-103 disorder
 Evidence X-RAY 6g6k B Reference
       Region 6g6k B 22-25 disorder
       Region 6g6k B 26-101 order
       Region 6g6k B 102-103 disorder
Seq 23-102 Hetero dimer : IID00012Complex
 Evidence X-RAY 1nkp E Reference
       Region 1nkp E 23-24 disorder
       Region 1nkp E 25-102 order
 Evidence X-RAY 1nkp B Reference
       Region 1nkp B 23-102 order
Seq 24-99 Hetero dimer : IID00165Complex
 Evidence X-RAY 1nlw E Reference
       Region 1nlw E 24-25 disorder
       Region 1nlw E 26-99 order
 Evidence X-RAY 1nlw B Reference
       Region 1nlw B 24-99 order
Seqdisorder 103-160
 Evidence X-RAY The C-terminal domain comprising residues 93-150 is disordered in the study using the isoform 2 of Max (PubMed=9115440, P61244-2), which corresponds to the residues 103-160 in the isoform 1 (P61244-1). Reference
       Region 103-160 disorder
SeqProS verified 22-34 The basic region of bHLH adapts a helical structure when the homo/hetero-dimer binds DNA. Hetero dimer : IID00165Complex
       Region 1nlw B 24-99 order
       Region 1nlw E 26-99 order
       Region 22-34 disorder
SeqProS verified 22-34 The basic region of bHLH adapts a helical structure when the homo/hetero-dimer binds DNA. Homo dimer :
       Region 1an2 A 22-107 order
       Region 1hlo A 22-92 order
       Region 1hlo B 22-92 order
       Region 5eyo A 22-106 order
       Region 5eyo C 22-107 order
       Region 22-34 disorder
SeqProS verified 22-34 The basic region of bHLH adapts a helical structure when the homo/hetero-dimer binds DNA. Hetero dimer : IID00012Complex
       Region 1nkp B 23-102 order
       Region 1nkp E 25-102 order
       Region 22-34 disorder
Seqphosphorylation
    11-11 Phosphoserine
    2-2 Phosphoserine
    2-2 Phosphoserine
    11-11 Phosphoserine
    107-107 Phosphoserine
Seqacetylation
    2-2 N-acetylserine
    2-2 N-acetylserine
    66-66 N6-acetyllysine
    153-153 N6-acetyllysine
    154-154 N6-acetyllysine
 
Prediction
NeProc
Disorder 1-27,113-160
Order 28-112
ProS 22-27
AlphaFold
Disorder 1-3,5-5,8-16,111-125,128-128,130-160
Order 4-4,6-7,17-110,126-127,129-129
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. 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.
Biological Process
Diagram with PDB data
MAX/MYC/DNACrystal structure of Myc-Max recognizing DNA
See also
Diagram with PDB data
MYC/WDR5Crystal structure of WDR5 in complex with MYC MbIIIb peptide
MXD1/Sin3bStructure of the complex of the Mad1-Sin3B interaction domains