DP00084: Protein max [Isoform 1]FASTA viewXML view

General information
DisProt:DP00084
Name:Protein max [Isoform 1]
Synonym(s):MAX_HUMAN
Myc-associated factor X
p21 Max
First appeared in release:Release 1.0 (08/01/2003)
UniProt:P61244
UniGene:Hs.285354
SwissProt: MAX_HUMAN
TrEMBL:  
NCBI (GI): 47117704
Source organism:Homo sapiens (Human)
Sequence length:160
Percent disordered:69%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MSDNDDIEVE SDEEQPRFQS AADKRAHHNA LERKRRDHIK DSFHSLRDSV PSLQGEKASR - 60
AQILDKATEY IQYMRRKNHT HQQDIDDLKR QNALLEQQVR ALEKARSSAQ LQTNYPSSDN - 120
SLYTNAKGST ISAFDGGSDS SSESEPEEPQ SRKKLRMEAS



Functional narrative    

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.

Region 1: 1-110

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered
Name:N terminal to b/HLH/Z region
Location:1 - 110
Length:110
Region sequence:

MSDNDDIEVESDEEQPRFQSAADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASR
AQILDKATEYIQYMRRKNHTHQQDIDDLKRQNALLEQQVRALEKARSSAQ

Modification type: Fragment
PDB:  
Structural/functional type:  
Functional classes:  
Functional subclasses: Protein-DNA binding
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (310 K; pH: 6.8; Jasco J-720 (spectropolarimeter); MgCl2 10 mM; NaCl 150 mM; sodium phosphate (buffer) 20 mM)

  2. Analytical ultracentrifugation (310 K; pH: 6.8; Beckman Optima XL-A (analytical ultracentrifuge); MgCl2 10 mM; NaCl 150 mM; sodium phosphate (buffer) 20 mM; speed 18000 rpm)

References:
  1. Horiuchi M, Kurihara Y, Katahira M, Maeda T, Saito T, Uesugi S. "Dimerization and DNA binding facilitate alpha-helix formation of Max in solution." J Biochem (Tokyo). 1997; 122(4): 711-6. PubMed: 9399572

Comments:
The experimental sequence consisted of the first 110 residues of Max.




References

  1. Ferre-D'Amare AR, Pognonec P, Roeder RG, Burley SK. "Structure and function of the b/HLH/Z domain of USF." Embo J. 1994; 13(1): 180-9. PubMed: 8306960

  2. Pursglove SE, Fladvad M, Bellanda M, Moshref A, Henriksson M, Carey J, Sunnerhagen M. "Biophysical properties of regions flanking the bHLH-Zip motif in the p22 Max protein." Biochem Biophys Res Commun. 2004; 323(3): 750-9. PubMed: 15381064

  3. Sauve S, Tremblay L, Lavigne P. "The NMR solution structure of a mutant of the Max b/HLH/LZ free of DNA: insights into the specific and reversible DNA binding mechanism of dimeric transcription factors." J Mol Biol. 2004; 342(3): 813-32. PubMed: 15342239



Comments


Additional UniGene ID: Hs.712926



Previous entry DP00084 has been split into canonical isoform 1 DP00084 and isoform 2 DP00084_A002, which have separate characterizations of disorder.


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