UniProt Accession

 H4_DROME; P84040; A4V2W8; P02307; Q4AB71; Q4ABE0; Q6AWN1; Q9VFH7 

Genbank Protein ID

 X14215; X97437; X97438; AE014297; AE014134; AE014297; AE014297; AE014134; AE014134; AE014134; AE014134; AE014134; AE014134; AE014134; AE014134; AE014134; AE014134; AE014134; AE014134; AE014134; AE014134; AE014134; AE014134; AE014134; AE014134; AE014134; AE014134; AE014134; BT001842; BT015217 

Genbank Nucleotide ID

 CAA32435.1; CAA66067.1; CAA66068.1; AAF55080.1; AAN11126.1; AAN13612.1; AAN13613.1; AAZ66480.1; AAZ66484.1; AAZ66489.1; AAZ66493.1; AAZ66498.1; AAZ66503.1; AAZ66508.1; AAZ66513.1; AAZ66518.1; AAZ66523.1; AAZ66528.1; AAZ66533.1; AAZ66538.1; AAZ66543.1; AAZ66548.1; AAZ66553.1; AAZ66558.1; AAZ66563.1; AAZ66568.1; AAZ66573.1; AAZ66578.1; AAN71603.1; AAT94446.1 

Protein Name

 Histone H4 

Protein Synonyms/Alias

  

Gene Name

 His4; His4r; His4:CG31611; His4:CG33869; His4:CG33871; His4:CG33873; His4:CG33875; His4:CG33877; His4:CG33879; His4:CG33881; His4:CG33883; His4:CG33885; His4:CG33887; His4:CG33889; His4:CG33891; His4:CG33893; His4:CG33895; His4:CG33897; His4:CG33899; His4:CG33901; His4:CG33903; His4:CG33905; His4:CG33907; His4:CG33909 

Gene Synonyms/Alias

 H4; H4r; CG3379; CG31611; CG33869; CG33871; CG33873; CG33875; CG33877; CG33879; CG33881; CG33883; CG33885; CG33887; CG33889; CG33891; CG33893; CG33895; CG33897; CG33899; CG33901; CG33903; CG33905; CG33907; CG33909 

Created Date

 July 27, 2013 

Organism

 Drosophila melanogaster (Fruit fly) 

NCBI Taxa ID

 7227 

Lysine Modification

Position	Peptide	Type	References
6	**MTGRGKGGKGLGK	acetylation	[1, 2, 3, 4, 5]
9	TGRGKGGKGLGKGGA	acetylation	[1, 2, 4, 5]
13	KGGKGLGKGGAKRHR	acetylation	[1, 2, 3, 4, 5, 6]
17	GLGKGGAKRHRKVLR	acetylation	[1, 2, 4, 5, 7, 8, 9]
32	DNIQGITKPAIRRLA	acetylation	[5]
32	DNIQGITKPAIRRLA	succinylation	[10]
78	VTYTEHAKRKTVTAM	succinylation	[10]
80	YTEHAKRKTVTAMDV	acetylation	[5]
80	YTEHAKRKTVTAMDV	succinylation	[10]
92	MDVVYALKRQGRTLY	succinylation	[10]

Reference

 [1] Histone H4 acetylation in Drosophila. Frequency of acetylation at different sites defined by immunolabelling with site-specific antibodies.
 Munks RJ, Moore J, O'Neill LP, Turner BM.
 FEBS Lett. 1991 Jun 24;284(2):245-8. [PMID: 2060643]
 [2] Histone acetylase from Drosophila melanogaster specific for H4.
 Wiegand RC, Brutlag DL.
 J Biol Chem. 1981 May 10;256(9):4578-83. [PMID: 6783663]
 [3] Conservation of deposition-related acetylation sites in newly synthesized histones H3 and H4.
 Sobel RE, Cook RG, Perry CA, Annunziato AT, Allis CD.
 Proc Natl Acad Sci U S A. 1995 Feb 14;92(4):1237-41. [PMID: 7862667]
 [4] A combination of different mass spectroscopic techniques for the analysis of dynamic changes of histone modifications.
 Bonaldi T, Imhof A, Regula JT.
 Proteomics. 2004 May;4(5):1382-96. [PMID: 15188406]
 [5] Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation.
 Weinert BT, Wagner SA, Horn H, Henriksen P, Liu WR, Olsen JV, Jensen LJ, Choudhary C.
 Sci Signal. 2011 Jul 26;4(183):ra48. [PMID: 21791702]
 [6] Non-random acetylation of histone H4 by a cytoplasmic histone acetyltransferase as determined by novel methodology.
 Sobel RE, Cook RG, Allis CD.
 J Biol Chem. 1994 Jul 15;269(28):18576-82. [PMID: 8034606]
 [7] The drosophila MSL complex acetylates histone H4 at lysine 16, a chromatin modification linked to dosage compensation.
 Smith ER, Pannuti A, Gu W, Steurnagel A, Cook RG, Allis CD, Lucchesi JC.
 Mol Cell Biol. 2000 Jan;20(1):312-8. [PMID: 10594033]
 [8] Activation of transcription through histone H4 acetylation by MOF, an acetyltransferase essential for dosage compensation in Drosophila.
 Akhtar A, Becker PB.
 Mol Cell. 2000 Feb;5(2):367-75. [PMID: 10882077]
 [9] A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16.
 Smith ER, Cayrou C, Huang R, Lane WS, Côté J, Lucchesi JC.
 Mol Cell Biol. 2005 Nov;25(21):9175-88. [PMID: 16227571]
 [10] Lysine succinylation and lysine malonylation in histones.
 Xie Z, Dai J, Dai L, Tan M, Cheng Z, Wu Y, Boeke JD, Zhao Y.
 Mol Cell Proteomics. 2012 May;11(5):100-7. [PMID: 22389435] 

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

 DNA_BIND 17 21
 MOD_RES 6 6 N6-acetyllysine.
 MOD_RES 13 13 N6-acetyllysine.
 MOD_RES 81 81 Phosphothreonine.
 MOD_RES 83 83 Phosphothreonine.  

Keyword

 3D-structure; Acetylation; Chromosome; Complete proteome; DNA-binding; Nucleosome core; Nucleus; Phosphoprotein; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 103 AA 

Protein Sequence

Gene Ontology

 GO:0005811; C:lipid particle; IDA:FlyBase.
 GO:0000786; C:nucleosome; IDA:UniProtKB.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0003677; F:DNA binding; IDA:UniProtKB.
 GO:0051298; P:centrosome duplication; IMP:FlyBase.
 GO:0006334; P:nucleosome assembly; IDA:UniProtKB. 

Interpro

 IPR009072; Histone-fold.
 IPR007125; Histone_core_D.
 IPR001951; Histone_H4.
 IPR019809; Histone_H4_CS. 

Pfam

 PF00125; Histone 

SMART

 SM00417; H4 

PROSITE

 PS00047; HISTONE_H4 

PRINTS

 PR00623; HISTONEH4.