| Tag | Content |
|---|
| CPLM ID | CPLM-032533 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Histone H4 |
Protein Synonyms/Alias | |
Gene Name | TGGT1_051710, TGME49_039260, TGVEG_092350 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Toxoplasma gondii |
NCBI Taxa ID | 5811 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 6 | **MSGRGKGGKGLGK | acetylation | [1] | | 9 | SGRGKGGKGLGKGGA | acetylation | [1] | | 13 | KGGKGLGKGGAKRHR | acetylation | [1, 2] | | 17 | GLGKGGAKRHRKVLR | acetylation | [1, 2] | | 32 | DNIQGITKPAIRRLA | acetylation | [1, 2] |
|
Reference | [1] Protein intrinsic disorder in the acetylome of intracellular and extracellular Toxoplasma gondii. Xue B, Jeffers V, Sullivan WJ, Uversky VN. Mol Biosyst. 2013 Apr 5;9(4):645-57. [ PMID: 23403842] [2] Lysine acetylation is widespread on proteins of diverse function and localization in the protozoan parasite Toxoplasma gondii. Jeffers V, Sullivan WJ Jr. Eukaryot Cell. 2012 Jun;11(6):735-42. [ PMID: 22544907] |
Functional Description | Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling (By similarity). |
Sequence Annotation | |
Keyword | Chromosome; Complete proteome; DNA-binding; Nucleosome core; Nucleus; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 103 AA |
Protein Sequence | MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEEIRGVLK 60
VFLENIIKDS VTYTEHARRK TVTAMDIVYS LKRQGRTLYG FGG 103 |
Gene Ontology | |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |