Annotations for this protein have been verified by the authors of the corresponding papers



DP00097: Histone H1.0FASTA viewXML view

General information
DisProt:DP00097
Name:Histone H1.0
Synonym(s):H10_MOUSE
Histone H1(0)
Histone H1'
MyD196
H1 histone family, member 0
First appeared in release:Release 3.0 (02/17/2006)
UniProt:P10922
UniGene:Mm.24350
SwissProt: H10_MOUSE
TrEMBL:  
NCBI (GI): 1346247
Source organism:Mus musculus (Mouse)
Sequence length:193
Percent disordered:66%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
TENSTSAPAA KPKRAKASKK STDHPKYSDM IVAAIQAEKN RAGSSRQSIQ KYIKSHYKVG - 60
ENADSQIKLS IKRLVTTGVL KQTKGVGASG SFRLAKGDEP KRSVAFKKTK KEVKKVATPK - 120
KAAKPKKAAS KAPSKKPKAT PVKKAKKKPA ATPKKAKKPK VVKVKPVKAS KPKKAKTVKP - 180
KAKSSAKRAS KKK

Region 1: 1-20 Region 2: 8-30 Region 4: 99-121 Region 3: 96-193

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 - 20
Length:20
Region sequence:

TENSTSAPAAKPKRAKASKK

Modification type: Fragment
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes:  
Functional subclasses: Protein-DNA binding
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (293 K; pH: 3.5; Water; NaCl 10 mM; Sodium phosphate buffer 5 mM)

  2. Circular dichroism (CD) spectroscopy, far-UV (293 K; pH: 3.5; Water (10%); NaCl 10 mM; Sodium phosphate buffer 5 mM; TFE (90%))

  3. Nuclear magnetic resonance (NMR) (298 K; pH: 3.5; Deuterated TFE (90%); H2O (10%); NaCl 10 mM; Peptide 2.7 mM; Phosphate buffer 5 mM)

  4. Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) (D2O; HEPES (pH 7.0) 10 mM; NaCl (10 mM or 70 mM); peptide 4.6 mg/ml)

  5. Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) (HEPES (pH 7.0) 10 mM; Murine DNA 6.7 mg/ml; NaCl (10 mM or 70 mM); TFE)

References:
  1. Vila R, Ponte I, Collado M, Arrondo JL, Jimenez MA, Rico M, Suau P. "DNA-induced alpha-helical structure in the NH2-terminal domain of histone H1." J Biol Chem. 2001; 276(49): 46429-35. PubMed: 11584004

Comments:
The fragment used consisted of residues 1-20.




Region 2
Type:Disordered
Name: 
Location:8 - 30
Length:23
Region sequence:

PAAKPKRAKASKKSTDHPKYSDM

Modification type: Fragment
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes:  
Functional subclasses: Protein-DNA binding
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (293 K; pH: 3.5; H2O; NaCl 10 mM; Sodium phosphate buffer 5 mM)

  2. Circular dichroism (CD) spectroscopy, far-UV (293 K; pH: 3.5; H2O (10%); NaCl 10 mM; Sodium phosphate buffer 5 mM; TFE (90%))

  3. Nuclear magnetic resonance (NMR) (298 K; pH: 3.5; deuterated TFE (90%); H2O (10%); NaCl 10 mM; peptide 2.7 mM; Phosphate buffer 5 mM)

  4. Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) (D2O; HEPES (pH 7.0) 10 mM; NaCl (10 mM or 70 mM); peptide 4.6 mg/ml)

  5. Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) (HEPES (pH 7.0) 10 mM; Murine DNA 6.7 mg/ml; NaCl (10 mM or 70 mM); TFE)

References:
  1. Vila R, Ponte I, Collado M, Arrondo JL, Jimenez MA, Rico M, Suau P. "DNA-induced alpha-helical structure in the NH2-terminal domain of histone H1." J Biol Chem. 2001; 276(49): 46429-35. PubMed: 11584004

Comments:
The fragment used consisted of residues 8-30.




Region 3
Type:Disordered
Name: 
Location:96 - 193
Length:98
Region sequence:

KGDEPKRSVAFKKTKKEVKKVATPKKAAKPKKAASKAPSKKPKATPVKKAKKKPAATPKK
AKKPKVVKVKPVKASKPKKAKTVKPKAKSSAKRASKKK

Modification type: Fragment
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes:  
Functional subclasses: Protein-DNA binding
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (293 K; Phosphate buffer (pH 7.0) 10 mM)

  2. Circular dichroism (CD) spectroscopy, far-UV (293 K; Phosphate buffer (pH 7.0) 10 mM; TFE (60% (v/v)))

  3. Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) (295 K; HEPES 10 mM; NaCl (10 mM or 140 mM); peptide 5 mg/ml)

  4. Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) (295 K; HEPES 10 mM; Murine DNA 7 mg/ml; NaCl (10 mM or 140 mM); peptide 5 mg/ml)

References:
  1. Roque A, Iloro I, Ponte I, Arrondo JL, Suau P. "DNA-induced secondary structure of the carboxyl-terminal domain of histone H1." J Biol Chem. 2005; 280(37): 32141-7. PubMed: 16006555

Comments:
The fragment used consisted of residues 96-193.




Region 4
Type:Disordered
Name: 
Location:99 - 121
Length:23
Region sequence:

EPKRSVAFKKTKKEVKKVATPKK

Modification type: Fragment
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes:  
Functional subclasses: Protein-DNA binding
Detection methods:
  1. Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) (295 K; HEPES (pD 7.0) 10 mM; NaCl (10 mM or 70 mM); peptide 4.6 mg/ml)

  2. Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) (295 K; HEPES (pD 7.0) 10 mM; Murine DNA 6.7 mg/ml; NaCl (10 mM or 70 mM))

  3. Circular dichroism (CD) spectroscopy, far-UV (278 K; pH: 3.5; Phosphate buffer 5 mM; Water)

  4. Circular dichroism (CD) spectroscopy, far-UV (278 K; pH: 3.5; Phosphate buffer 5 mM; TFE (50%); Water (50%))

  5. Circular dichroism (CD) spectroscopy, far-UV (278 K; pH: 3.5; H2O (10%); Phosphate buffer 5 mM; TFE (90%))

  6. Nuclear magnetic resonance (NMR) (298 K; pH: 3.5; TFE (50%))

  7. Nuclear magnetic resonance (NMR) (298 K; pH: 3.5; TFE (90%))

References:
  1. Vila R, Ponte I, Collado M, Arrondo JL, Suau P. "Induction of secondary structure in a COOH-terminal peptide of histone H1 by interaction with the DNA: an infrared spectroscopy study." J Biol Chem. 2001; 276(33): 30898-903. PubMed: 11413144

  2. Vila R, Ponte I, Jimenez MA, Rico M, Suau P. "A helix-turn motif in the C-terminal domain of histone H1." Protein Sci. 2000; 9(4): 627-36. PubMed: 10794405

Comments:
The fragment used consisted of residues 99-121.



If you have any comments or wish to provide additional references to this protein or its disordered region(s), please click here to e-mail us.


Disprot-footer
Contact us