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
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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 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:
- 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)
- 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:
- 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.
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References |
- 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
- 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
- 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
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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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