| General Information |
| MoonProt ID | 471 |
| First appeared in release | 3.0 |
| Name(s) | H4 histone |
| UniProt ID | P62799 (H4_XENLA) |
| GO terms | GO:0000786 nucleosome
GO:0005694 chromosome
GO:0003677 DNA binding
GO:0005634 nucleus |
| Organisms for which functions have been demonstrated | Xenopus laevis (African clawed frog, an amphibian) |
| Sequence length | 103 amino acids |
| FASTA sequence | >sp|P62799|H4_XENLA Histone H4 OS=Xenopus laevis OX=8355 PE=1 SV=2
MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG |
| Structure Information |
| PDB ID | 1AOI |
| Quaternary structure | The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. |
| SCOP | Histone-fold |
| CATH | 1.10.20.10 |
| TM Helix Prediction | no TM helices
# sp|P62799|H4_XENLA Number of predicted TMHs: 0
# sp|P62799|H4_XENLA Exp number of AAs in TMHs: 0.00018
# sp|P62799|H4_XENLA Exp number, first 60 AAs: 0.00014
# sp|P62799|H4_XENLA Total prob of N-in: 0.21059
sp|P62799|H4_XENLA TMHMM2.0 outside 1 103 |
| DisProt Annotation | DisProt ID DP01390
UniProt Accession P62799
Protein Name Histone H4
Organism Xenopus laevis
Disorder content 20.39% |
| Predicted Disorder Regions | Use FASTA sequence on MFDp2 webserver.
spP62799H4_XENLA_Histone is 103 residues long, with 30 residues (29.13 %) predicted as disordered. The protein has 0 short (< 30 residues) disorder segments and 1 long (>= 30 residues) disorder segment.
Segment 1 - Long (>= 30 residues) disordered segment
Segment is located between positions 1 and 30 in the sequence.
The segment is 30 residues long (29.13 % of the total sequence length). |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | Histone.
Core component of nucleosome. |
| References for function | Kleinschmidt, J. A., & Franke, W. W. (1982). Soluble acidic complexes containing histones H3 and H4 in nuclei of Xenopus laevis oocytes. Cell, 29(3), 799-809.
Almouzni G, Khochbin S, Dimitrov S, Wolffe AP. Histone acetylation influences both gene expression and development of Xenopus laevis. Developmental biology. 1994 Oct 1;165(2):654-69. |
| E.C. number | |
| Location of functional site(s) | |
| Cellular location of function | nucleus |
| Comments | |
| Function 2 |
| Function description | copper reductase.
The histone H3-H4 tetramer is a copperreductase enzyme. |
| References for function | Attar N, Campos OA, Vogelauer M, Cheng C, Xue Y, Schmollinger S, Salwinski L, Mallipeddi NV, Boone BA, Yen L, Yang S, Zikovich S, Dardine J, Carey MF, Merchant SS, Kurdistani SK. The histone H3-H4 tetramer is a copper reductase enzyme. Science. 2020 Jul 3;369(6499):59-64. doi: 10.1126/science.aba8740. PMID: 32631887. |
| E.C. number | |
| Location of functional site(s) | |
| Cellular location of function | |
| Comments | |