dbPTM

H2AV_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	H2AV_MOUSE
UniProt AC	Q3THW5
Protein Name	Histone H2A.V
Gene Name	H2afv
Organism	Mus musculus (Mouse).
Sequence Length	128
Subcellular Localization	Nucleus. Chromosome.
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. May be involved in the formation of constitutive heterochromatin. May be required for chromosome segregation during cell division (By similarity)..
Protein Sequence	MAGGKAGKDSGKAKAKAVSRSQRAGLQFPVGRIHRHLKTRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAGGGVIPHIHKSLIGKKGQQKTA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Acetylation	---MAGGKAGKDSGK ---CCCCCCCCCCHH	53.71	16204459
8	Acetylation	MAGGKAGKDSGKAKA CCCCCCCCCCHHHHH	54.29	16204459
12	Acetylation	KAGKDSGKAKAKAVS CCCCCCHHHHHHHHH	51.14	16204459
12	Lactoylation	KAGKDSGKAKAKAVS CCCCCCHHHHHHHHH	51.14	-
14	Acetylation	GKDSGKAKAKAVSRS CCCCHHHHHHHHHHH	54.64	19852031
14	Lactoylation	GKDSGKAKAKAVSRS CCCCHHHHHHHHHHH	54.64	-
75	Ubiquitination	ELAGNASKDLKVKRI HHCCCCCCCCCEEEE	65.75	-
78	Ubiquitination	GNASKDLKVKRITPR CCCCCCCCEEEECHH	56.71	-
99	Phosphorylation	RGDEELDSLIKATIA CCCHHHHHHHHHHHC	44.62	28066266
116	Ubiquitination	GVIPHIHKSLIGKKG CCHHHHHHHHCCCCC	46.48	-
116	Lactoylation	GVIPHIHKSLIGKKG CCHHHHHHHHCCCCC	46.48	-
117	Phosphorylation	VIPHIHKSLIGKKGQ CHHHHHHHHCCCCCC	15.85	-
121	Acetylation	IHKSLIGKKGQQKTA HHHHHCCCCCCCCCC	46.89	20608373
121	Ubiquitination	IHKSLIGKKGQQKTA HHHHHCCCCCCCCCC	46.89	-
122	Ubiquitination	HKSLIGKKGQQKTA- HHHHCCCCCCCCCC-	57.66	-
126	Ubiquitination	IGKKGQQKTA----- CCCCCCCCCC-----	38.23	-

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
Oops, there are no upstream regulatory protein records of H2AV_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
5	K	Acetylation	16204459
Acetylated on Lys-5, Lys-8 and Lys-12 during interphase.
8	K	Acetylation	16204459
Acetylated on Lys-5, Lys-8 and Lys-12 during interphase.
12	K	Acetylation	16204459
Acetylated on Lys-5, Lys-8 and Lys-12 during interphase.
122	K	ubiquitylation	-
Monoubiquitination of Lys-122 gives a specific tag for epigenetic transcriptional repression.

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of H2AV_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of H2AV_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of H2AV_MOUSE

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"The replacement histone H2A.Z in a hyperacetylated form is a featureof active genes in the chicken."; Bruce K., Myers F.A., Mantouvalou E., Lefevre P., Greaves I.,Bonifer C., Tremethick D.J., Thorne A.W., Crane-Robinson C.; Nucleic Acids Res. 33:5633-5639(2005). Cited for: ACETYLATION AT LYS-5; LYS-8 AND LYS-12.	16204459 [Abstract]