Tag | Content |
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CPLM ID | CPLM-007299 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Histone H2A |
Protein Synonyms/Alias | |
Gene Name | |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Plasmodium falciparum |
NCBI Taxa ID | 5833 |
Lysine Modification | Position | Peptide | Type | References |
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4 | ****MSAKGKTGRKK | acetylation | [1] | 6 | **MSAKGKTGRKKAS | acetylation | [1] |
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Reference | [1] Global histone analysis by mass spectrometry reveals a high content of acetylated lysine residues in the malaria parasite Plasmodium falciparum. Trelle MB, Salcedo-Amaya AM, Cohen AM, Stunnenberg HG, Jensen ON. J Proteome Res. 2009 Jul;8(7):3439-50. [ PMID: 19351122] |
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. |
Sequence Annotation | |
Keyword | Chromosome; DNA-binding; Nucleosome core; Nucleus. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 132 AA |
Protein Sequence | MSAKGKTGRK KASKGTSNSA KAGLQFPVGR IGRYLKKGKY AKRVGAGAPV YLAAVLEYLC 60 AEILELAGNA ARDNKKSRIT PRHIQLAVRN DEELNKFLAG VTFASGGVLP NIHNVLLPKK 120 SQLKAGTANQ DY 132 |
Gene Ontology | |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |