UniProt Accession

 H2AV_HUMAN; Q71UI9; A6NFA8; A6NKY0; A6NN01; A8MQC5; Q59GV8; Q6PK98 

Genbank Protein ID

 AF081192; AK023973; AB209001; AC004854; CH471128; CH471128; BC000098; BC004274; BC014885; BC070169; BE742590; BU543626 

Genbank Nucleotide ID

 AAC31938.1; BAG51243.1; BAD92238.1; AAS00365.1; EAW61075.1; EAW61077.1; AAH00098.1; AAH04274.3; AAH14885.1; AAH70169.1 

Protein Name

 Histone H2A.V 

Protein Synonyms/Alias

 H2A.F/Z 

Gene Name

 H2AFV 

Gene Synonyms/Alias

 H2AV 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
5	***MAGGKAGKDSGK	acetylation	[1, 2]
8	MAGGKAGKDSGKAKA	acetylation	[3]
12	KAGKDSGKAKAKAVS	acetylation	[3]
14	GKDSGKAKAKAVSRS	acetylation	[3]
102	EELDSLIKATIAGGG	ubiquitination	[4]
116	GVIPHIHKSLIGKKG	ubiquitination	[4]
121	IHKSLIGKKGQQKTA	ubiquitination	[4]
122	HKSLIGKKGQQKTA*	ubiquitination	[4]

Reference

 [1] Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase.
 Verreault A, Kaufman PD, Kobayashi R, Stillman B.
 Curr Biol. 1998 Jan 15;8(2):96-108. [PMID: 9427644]
 [2] Overlapping but distinct patterns of histone acetylation by the human coactivators p300 and PCAF within nucleosomal substrates.
 Schiltz RL, Mizzen CA, Vassilev A, Cook RG, Allis CD, Nakatani Y.
 J Biol Chem. 1999 Jan 15;274(3):1189-92. [PMID: 9880483]
 [3] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 

Functional 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). 

Sequence Annotation

 MOD_RES 5 5 N6-acetyllysine (By similarity).
 MOD_RES 8 8 N6-acetyllysine (By similarity).
 MOD_RES 12 12 N6-acetyllysine (By similarity).
 CROSSLNK 122 122 Glycyl lysine isopeptide (Lys-Gly)  

Keyword

 Acetylation; Alternative splicing; Chromosome; Complete proteome; DNA-binding; Isopeptide bond; Nucleosome core; Nucleus; Polymorphism; Reference proteome; Ubl conjugation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 128 AA 

Protein Sequence

Gene Ontology

 GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0006334; P:nucleosome assembly; IEA:InterPro. 

Interpro

 IPR009072; Histone-fold.
 IPR007125; Histone_core_D.
 IPR002119; Histone_H2A. 

Pfam

 PF00125; Histone 

SMART

 SM00414; H2A 

PROSITE

 PS00046; HISTONE_H2A 

PRINTS

 PR00620; HISTONEH2A.