H2AV_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: H2AV_DROME
• UniProt AC: P08985
• Protein Name: Histone H2A.v
• Gene Name: His2Av
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 141
• Subcellular Localization: Nucleus . Chromosome . Widely distributed in the genome, irrespective of the transcriptional status or coding capacity of the sequence.
• Protein Description: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. 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. Acts as a Polycomb group (PcG) protein required to maintain the transcriptionally repressive state of homeotic genes of the animal throughout development. Required for histone H3 'Lys-9' methylation and histone H4 'Lys-12' acetylation, two modifications that are essential for heterochromatin formation. Also involved in DNA double strand break (DSB) repair. Essential for early development..
• Protein Sequence: MAGGKAGKDSGKAKAKAVSRSARAGLQFPVGRIHRHLKSRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAGGGVIPHIHKSLIGKKEETVQDPQRKGNVILSQAY

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Acetylation	---MAGGKAGKDSGK ---CCCCCCCCCCHH	53.71	19608861
8	Acetylation	MAGGKAGKDSGKAKA CCCCCCCCCCHHHHH	54.29	21791702
12	Acetylation	KAGKDSGKAKAKAVS CCCCCCHHHHHHHHH	51.14	21791702
138	Phosphorylation	RKGNVILSQAY---- CCCCEEEECCC----	11.14	12202754

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
-	K	Ubiquitination	E3 ubiquitin ligase	Sce	Q9VB08	PMID:22199232

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of H2AV_DROME !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of H2AV_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
POXM_DROME	Poxm	physical	14605208
PARP_DROME	Parp	physical	17827147
DOM_DROME	dom	genetic	24244183
HP1_DROME	Su(var)205	physical	25591068
RAD50_DROME	rad50	physical	19424425

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Acetylation

"Acetylation by Tip60 is required for selective histone variantexchange at DNA lesions.";
Kusch T., Florens L., Macdonald W.H., Swanson S.K., Glaser R.L.,Yates J.R. III, Abmayr S.M., Washburn M.P., Workman J.L.;
Science 306:2084-2087(2004).
Cited for: ACETYLATION AT LYS-5.
PubMed: 15528408

Phosphorylation

"DNA double-strand break-induced phosphorylation of Drosophila histonevariant H2Av helps prevent radiation-induced apoptosis.";
Madigan J.P., Chotkowski H.L., Glaser R.L.;
Nucleic Acids Res. 30:3698-3705(2002).
Cited for: FUNCTION, AND PHOSPHORYLATION AT SER-138.
PubMed: 12202754