| General information | | DisProt: | DP00044 | | Name: | Histone H5 | | Synonym(s): | H5_CHICK
| | First appeared in release: | Release 1.0 (08/01/2003) | | UniProt: | P02259 | | UniGene: | Gga.16744 | | SwissProt: | H5_CHICK | | TrEMBL: | | | NCBI (GI): | 122112 | | Source organism: | Gallus gallus (Chicken) | | Sequence length: | 189 | | Percent disordered: | 56% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
| | | | | |
TESLVLSPAP AKPKRVKASR RSASHPTYSE MIAAAIRAEK SRGGSSRQSI QKYIKSHYKV - 60
GHNADLQIKL SIRRLLAAGV LKQTKGVGAS GSFRLAKSDK AKRSPGKKKK AVRRSTSPKK - 120
AARPRKARSP AKKPKATARK ARKKSRASPK KAKKPKTVKA KSRKASKAKK VKRSKPRAKS - 180
GARKSPKKK
|
| Functional narrative |
H5 binds to the nucleosome and is essential for chromatin structure in avian erythrocytes. The linker histone consists of an ordered globular domain that spans residues 21-100. The N- terminal and C- terminal flank the central domain and are disordered.
|
| 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 - Extended | | Name: | | | Location: | 1 - 21 | | Length: | 21 | | Region sequence: |
TESLVLSPAPAKPKRVKASRR | | Modification type: | | | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (pH: 8.2; phosphate 2.2 M)
- Sensitivity to proteolysis
| References:
- Graziano, V.
Gerchman, S. E.
Wonacott, A. J.
Sweet, R. M.
Wells, J. R.
White, S. W.
Ramakrishnan, V. "Crystallization of the globular domain of histone H5." J Mol Biol. 1990; 212(2): 253-257. PubMed: 2181148
| Comments:
|
| Region 2 | | Type: | Disordered - Extended | | Name: | | | Location: | 101 - 185 | | Length: | 85 | | Region sequence: |
AKRSPGKKKKAVRRSTSPKKAARPRKARSPAKKPKATARKARKKSRASPKKAKKPKTVKA
KSRKASKAKKVKRSKPRAKSGARKS | | Modification type: | | | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-DNA binding
| Detection methods:
- X-ray crystallography (pH: 8.2; phosphate 2.2 M)
- Sensitivity to proteolysis
| References:
- Graziano, V.
Gerchman, S. E.
Wonacott, A. J.
Sweet, R. M.
Wells, J. R.
White, S. W.
Ramakrishnan, V. "Crystallization of the globular domain of histone H5." J Mol Biol. 1990; 212(2): 253-257. PubMed: 2181148
| Comments:
|
| Region 3 | | Type: | Ordered | | Name: | | | Location: | 21 - 100 | | Length: | 80 | | Region sequence: |
RSASHPTYSEMIAAAIRAEKSRGGSSRQSIQKYIKSHYKVGHNADLQIKLSIRRLLAAGV
LKQTKGVGASGSFRLAKSDK | | Modification type: | | | PDB: | | | Structural/functional type: | Function arises from the ordered state
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-DNA binding
| Detection methods:
| References:
- Graziano, V.
Gerchman, S. E.
Wonacott, A. J.
Sweet, R. M.
Wells, J. R.
White, S. W.
Ramakrishnan, V. "Crystallization of the globular domain of histone H5." J Mol Biol. 1990; 212(2): 253-257. PubMed: 2181148
| Comments:
|
| References |
- Ramakrishnan V, Finch JT, Graziano V, Lee PL, Sweet RM. "Crystal structure of globular domain of histone H5 and its implications for nucleosome binding." Nature. 1993; 362(6417): 219-223. PubMed: 8384699
|
| 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
|
