| General Information |
| MoonProt ID | 470 |
| First appeared in release | 3.0 |
| Name(s) | H3 histone |
| UniProt ID | Q92132 (Q92132_XENLA) |
| GO terms | GO:0000786 nucleosome
GO:0005634 nucleus |
| Organisms for which functions have been demonstrated | Xenopus laevis (African clawed frog, an amphibian) |
| Sequence length | 136 amino acids |
| FASTA sequence | >tr|Q92132|Q92132_XENLA Histone H3 OS=Xenopus laevis OX=8355 GN=H3r PE=3 SV=1
MARTKQTARKSTGGKAPRKQLATKAARKSAPATGESKKPHRYRPGTAALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTXLRFQSSAVMALQXASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA |
| Structure Information |
| PDB ID | NA |
| 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 | |
| CATH | |
| TM Helix Prediction | no TM helices |
| DisProt Annotation | |
| Predicted Disorder Regions | Use FASTA sequence on MFDp2 webserver.
trQ92132Q92132_XENLA_His is 136 residues long, with 67 residues (49.26 %) predicted as disordered. The protein has 1 short (< 30 residues) disorder segment and 1 long (>= 30 residues) disorder segment.
Segment 1 - Long (>= 30 residues) disordered segment
Segment is located between positions 1 and 57 in the sequence.
The segment is 57 residues long (41.91 % of the total sequence length).
Segment 2 - Short (< 30 residues) disordered segment
Segment is located between positions 127 and 136 in the sequence.
The segment is 10 residues long (7.35 % of the total sequence length). |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | Histone |
| References for function | Kleinschmidt JA, Franke WW. Soluble acidic complexes containing histones H3 and H4 in nuclei of Xenopus laevis oocytes. Cell. 1982 Jul 1;29(3):799-809. |
| 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 copper reductase 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 | |