| General information | | DisProt: | DP00084_A002 | | Name: | Protein max [Isoform 2] | | Synonym(s): | MAX_HUMAN
Myc-associated factor X
p21 Max
| | First appeared in release: | Release 3.0 (02/17/2006) | | UniProt: | P61244-2 | | UniGene: | Hs.285354 | | SwissProt: | MAX_HUMAN | | TrEMBL: | | | NCBI (GI): | 47117704 | | Source organism: | Homo sapiens (Human) | | Sequence length: | 151 | | Percent disordered: | 46% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MSDNDDIEVE SDADKRAHHN ALERKRRDHI KDSFHSLRDS VPSLQGEKAS RAQILDKATE - 60
YIQYMRRKNH THQQDIDDLK RQNALLEQQV RALEKARSSA QLQTNYPSSD NSLYTNAKGS - 120
TISAFDGGSD SSSESEPEEP QSRKKLRMEA S
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| 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.
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| 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.
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| Region 1 | | Type: | Disordered | | Name: | N-terminal | | Location: | 1 - 12 | | Length: | 12 | | Region sequence: |
MSDNDDIEVESD | | Modification type: | Engineered
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- Nuclear magnetic resonance (NMR) (308 K; pH: 6.8; D2O 10 %; DSS; KCl 100 mM; NaN3 50 mM; Phosphate 50 mM)
- Circular dichroism (CD) spectroscopy, far-UV (293 K; pH: 6.8; KCl 100 mM; Sodium Phosphate 50 mM)
| References:
- Naud JF, McDuff FO, Sauve S, Montagne M, Webb BA, Smith SP, Chabot B, Lavigne P. "Structural and Thermodynamical Characterization of the Complete p21 Gene Product of Max." Biochemistry. 2005; 44(38): 12746-12758. PubMed: 16171389
| Comments:
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| Region 2 | | Type: | Disordered | | Name: | C-terminal | | Location: | 95 - 151 | | Length: | 57 | | Region sequence: |
KARSSAQLQTNYPSSDNSLYTNAKGSTISAFDGGSDSSSESEPEEPQSRKKLRMEAS | | Modification type: | Engineered
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- Nuclear magnetic resonance (NMR) (308 K; pH: 6.8; D2O 10 %; DSS; KCl 100 mM; NaN3 50 mM; Phosphate 50 mM)
- Circular dichroism (CD) spectroscopy, far-UV (293 K; pH: 6.8; KCl 100 mM; Sodium Phosphate 50 mM)
| References:
- Naud JF, McDuff FO, Sauve S, Montagne M, Webb BA, Smith SP, Chabot B, Lavigne P. "Structural and Thermodynamical Characterization of the Complete p21 Gene Product of Max." Biochemistry. 2005; 44(38): 12746-12758. PubMed: 16171389
| Comments:
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| 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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