Annotation for this protein is in progress - please check future releases for more complete information


DP00260: Myc proto-oncogene protein [Isoform 1]FASTA viewXML view

General information
DisProt:DP00260
Name:Myc proto-oncogene protein [Isoform 1]
Synonym(s):MYC_HUMAN
c-Myc
Transcription factor p64
First appeared in release:Release 1.0 (08/01/2003)
UniProt:P01106
UniGene:Hs.202453
SwissProt: MYC_HUMAN
TrEMBL:  
NCBI (GI): 127619
Source organism:Homo sapiens (Human)
Sequence length:439
Percent disordered:45%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MPLNVSFTNR NYDLDYDSVQ PYFYCDEEEN FYQQQQQSEL QPPAPSEDIW KKFELLPTPP - 60
LSPSRRSGLC SPSYVAVTPF SLRGDNDGGG GSFSTADQLE MVTELLGGDM VNQSFICDPD - 120
DETFIKNIII QDCMWSGFSA AAKLVSEKLA SYQAARKDSG SPNPARGHSV CSTSSLYLQD - 180
LSAAASECID PSVVFPYPLN DSSSPKSCAS QDSSAFSPSS DSLLSSTESS PQGSPEPLVL - 240
HEETPPTTSS DSEEEQEDEE EIDVVSVEKR QAPGKRSESG SPSAGGHSKP PHSPLVLKRC - 300
HVSTHQHNYA APPSTRKDYP AAKRVKLDSV RVLRQISNNR KCTSPRSSDT EENVKRRTHN - 360
VLERQRRNEL KRSFFALRDQ IPELENNEKA PKVVILKKAT AYILSVQAEE QKLISEEDLL - 420
RKRREQLKHK LEQLRNSCA

Region 1: 1-88 Region 3: 1-143 Region 2: 1-167 Region 4: 406-434

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: 
Location:1 - 88
Length:88
Region sequence:

MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPP
LSPSRRSGLCSPSYVAVTPFSLRGDNDG

Modification type: Fragment
PDB:  
Structural/functional type:  
Functional classes:  
Functional subclasses: Transactivation (transcriptional activation)
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (278 K; )

  2. Circular dichroism (CD) spectroscopy, far-UV (298 K; )

  3. Circular dichroism (CD) spectroscopy, far-UV (343 K; )

  4. Fluorescence resonance energy transfer (FRET) (298 K; pH: 8; ANS 20 uM; GuHCl 6 M; NaCl 100 mM; NaH2PO4 20 mM)

  5. Fluorescence resonance energy transfer (FRET) (298 K; pH: 8; ANS 20 uM; NaCl 100 mM; NaH2PO4 20 mM)

  6. Sensitivity to proteolysis (298 K; 2-mercaptoethanol 0.02 M; bromophenol blue (w/v) 0.002 %; glycerol (v/v) 35 %; SDS (w/v) 3 %; Tris-HCl (pH 6.8) 80 uM)
References:
  1. Fladvad M, Zhou K, Moshref A, Pursglove S, Safsten P, Sunnerhagen M. "N and C-terminal sub-regions in the c-Myc transactivation region and their joint role in creating versatility in folding and binding." J Mol Biol. 2005; 346(1): 175-89. PubMed: 15663936
Comments:
 



Region 2
Type:Disordered - Molten Globule
Name: 
Location:1 - 167
Length:167
Region sequence:

MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPP
LSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPD
DETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARG

Modification type: Fragment
PDB:  
Structural/functional type: Function arises from the molten globule state
Functional classes:  
Functional subclasses: Transactivation (transcriptional activation)
Protein-protein binding
Detection methods:
  1. Stability at thermal extremes

  2. Circular dichroism (CD) spectroscopy, far-UV (278 K; )

  3. Circular dichroism (CD) spectroscopy, far-UV (298 K; )

  4. Circular dichroism (CD) spectroscopy, far-UV (343 K; )

  5. Fluorescence resonance energy transfer (FRET) (298 K; pH: 8; ANS 20 uM; GuHCl 6 M; NaCl 100 mM; NaH2PO4 20 mM)

  6. Fluorescence resonance energy transfer (FRET) (298 K; pH: 8; ANS 20 uM; NaCl 100 mM; NaH2PO4 20 mM)

  7. Sensitivity to proteolysis (298 K; 2-mercaptoethanol 0.02 M; bromophenol blue (w/v) 0.002 %; glycerol (v/v) 35 %; SDS (w/v) 3 %; Tris-HCl (pH 6.8) 80 uM)
References:
  1. Fladvad M, Zhou K, Moshref A, Pursglove S, Safsten P, Sunnerhagen M. "N and C-terminal sub-regions in the c-Myc transactivation region and their joint role in creating versatility in folding and binding." J Mol Biol. 2005; 346(1): 175-89. PubMed: 15663936
Comments:
 



Region 3
Type:Disordered
Name:transactivation domain (TAD)
Location:1 - 143
Length:143
Region sequence:

MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPP
LSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPD
DETFIKNIIIQDCMWSGFSAAAK

Modification type: Engineered
Fragment
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Modification site
Molecular assembly
Functional subclasses: Transactivation (transcriptional activation)
Protein-protein binding
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (phosphate (buffer) 3 mM)

  2. Circular dichroism (CD) spectroscopy, far-UV (phosphate (buffer) 10 mM)
References:
  1. Fladvad M, Zhou K, Moshref A, Pursglove S, Safsten P, Sunnerhagen M. "N and C-terminal sub-regions in the c-Myc transactivation region and their joint role in creating versatility in folding and binding." J Mol Biol. 2005; 346(1): 175-89. PubMed: 15663936

  2. McEwan IJ, Dahlman-Wright K, Ford J, Wright AP. "Functional interaction of the c-Myc transactivation domain with the TATA binding protein: evidence for an induced fit model of transactivation domain folding." Biochemistry. 1996; 35(29): 9584-93. PubMed: 8755740
Comments:
 



Region 4
Type:Disordered - Extended
Name:C-terminal
Location:406 - 434
Length:29
Region sequence:

VQAEEQKLISEEDLLRKRREQLKHKLEQL

Modification type:  
PDB:  
Structural/functional type:  
Functional classes:  
Functional subclasses:  
Detection methods:
 
References:
  1. McEwan IJ, Dahlman-Wright K, Ford J, Wright AP. "Functional interaction of the c-Myc transactivation domain with the TATA binding protein: evidence for an induced fit model of transactivation domain folding." Biochemistry. 1996; 35(29): 9584-93. PubMed: 8755740
Comments:
 


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