Histone H4 - Mus musculus (Mouse)

Names and origin

Protein names

Recommended name:
Histone H4

Gene names

Name:	Hist1h4a
AND
Name:	Hist1h4b
Synonyms:	H4-53
AND
Name:	Hist1h4c
Synonyms:	H4-12
AND
Name:	Hist1h4d
AND
Name:	Hist1h4f
AND
Name:	Hist1h4h
AND
Name:	Hist1h4i
AND
Name:	Hist1h4j
AND
Name:	Hist1h4k
AND
Name:	Hist1h4m
AND
Name:	Hist2h4a
Synonyms:	Hist2h4
AND
Name:	Hist4h4

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Hide | Top

Protein attributes

Sequence length	103 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

Hide | Top

General annotation (Comments)

Function	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.
Subunit structure	The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.
Subcellular location	NucleusBy similarity.
Post-translational modification	Acetylation at Lys-6, Lys-9, Lys-13 and Lys-17 occurs in coding regions of the genome but not in heterochromatin By similarity. Citrullination at Arg-4 by PADI4 impairs methylation. Monomethylation at Arg-4 by PRMT1 favors acetylation at Lys-9 and Lys-13. Demethylation is performed by JMJD6. Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage. Monomethylated, dimethylated or trimethylated at Lys-21. Monomethylation is performed by SET8. Trimethylation is performed by SUV420H1 and SUV420H2 and induces gene silencing. Ubiquitinated by the CUL4-DDB-RBX1 complex in response to ultraviolet irradiation. This may weaken the interaction between histones and DNA and facilitate DNA accessibility to repair proteins By similarity. Sumoylated, which is associated with transcriptional repression By similarity.
Sequence similarities	Belongs to the histone H4 family.

Hide | Top

Ontologies

Keywords
Cellular component	Chromosomal protein Nucleosome core Nucleus
Ligand	DNA-binding
PTM	Acetylation Citrullination Methylation Phosphoprotein Ubl conjugation
Technical term	3D-structure
Gene Ontology (GO)
None. [Check GOA]

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Initiator methionine

1

Removed By similarity

Chain

2 – 103

102

Histone H4

Regions

DNA binding

17 – 21

5

Amino acid modifications

Modified residue

2

1

N-acetylserine By similarity

Modified residue

2

1

Phosphoserine

Modified residue

4

1

Citrulline; alternate By similarity

Modified residue

4

1

Omega-N-methylarginine; by PRMT1; alternate By similarity

Modified residue

4

1

Symmetric dimethylarginine; by PRMT5; alternate

Modified residue

6

1

N6-acetyllysine

Modified residue

9

1

N6-acetyllysine

Modified residue

13

1

N6-acetyllysine

Modified residue

17

1

N6-acetyllysine

Modified residue

21

1

N6,N6,N6-trimethyllysine; alternate

Modified residue

21

1

N6,N6-dimethyllysine; alternate By similarity

Modified residue

21

1

N6-methyllysine; alternate By similarity

Modified residue

48

1

Phosphoserine

Modified residue

52

1

Phosphotyrosine

Modified residue

89

1

Phosphotyrosine

Experimental info

Sequence conflict

34

1

A → V in BAB26692. Ref.6

Sequence conflict

80

1

K → E in BAB27698. Ref.6

Sequence conflict

90

1

A → R in CAA31622. Ref.2

Secondary structure

1

.

103

Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P62806-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: A9E5DFD3F8B97598
Show »

FASTA

103

11,367

        10         20         30         40         50         60 
MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK 

        70         80         90        100 
VFLENVIRDA VTYTEHAKRK TVTAMDVVYA LKRQGRTLYG FGG

« Hide

Hide | Top

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and expression in L-cells of a cloned H4 histone gene of the mouse." Seiler-Tuyns A., Birnstiel M.L. J. Mol. Biol. 151:607-625(1981) [PubMed: 6276563] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Nucleotide sequence of two mouse histone H4 genes." Meier V.S., Boehni R., Schuemperli D. Nucleic Acids Res. 17:795-795(1989) [PubMed: 2915930] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H4B AND HIST1H4C).
[3]	"Characterization of the mouse histone gene cluster on chromosome 13: 45 histone genes in three patches spread over 1Mb." Wang Z.-F., Krasikov T., Frey M.R., Wang J., Matera A.G., Marzluff W.F. Genome Res. 6:688-701(1996) [PubMed: 8858344] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H4A). Strain: C57BL/6.
[4]	Franke K., Drabent B., Doenecke D. Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129/Sv.
[5]	"The human and mouse replication-dependent histone genes." Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J. Genomics 80:487-498(2002) [PubMed: 12408966] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H4A; HIST1H4B; HIST1H4C; HIST1H4D; HIST1H4F; HIST1H44; HIST1H4I; HIST1H4J; HIST1H4K; HIST1H4M; HIST2H4A AND HIST4H4).
[6]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Egg, Pancreas and Tongue.
[7]	The mouse genome sequencing consortium Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Brain, Embryo, Eye, Heart, Mammary gland and Testis.
[9]	"A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin." Schotta G., Lachner M., Sarma K., Ebert A., Sengupta R., Reuter G., Reinberg D., Jenuwein T. Genes Dev. 18:1251-1262(2004) [PubMed: 15145825] [Abstract] Cited for: METHYLATION AT LYS-21.
[10]	"Phosphorylation of histone H4 Ser1 regulates sporulation in yeast and is conserved in fly and mouse spermatogenesis." Krishnamoorthy T., Chen X., Govin J., Cheung W.L., Dorsey J., Schindler K., Winter E., Allis C.D., Guacci V., Khochbin S., Fuller M.T., Berger S.L. Genes Dev. 20:2580-2592(2006) [PubMed: 16980586] [Abstract] Cited for: PHOSPHORYLATION AT SER-2.
[11]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-9; LYS-13 AND LYS-17, MASS SPECTROMETRY.
[12]	"Blimp1 associates with Prmt5 and directs histone arginine methylation in mouse germ cells." Ancelin K., Lange U.C., Hajkova P., Schneider R., Bannister A.J., Kouzarides T., Surani M.A. Nat. Cell Biol. 8:623-630(2006) [PubMed: 16699504] [Abstract] Cited for: METHYLATION AT ARG-4.
[13]	"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling." Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R. J. Immunol. 179:5864-5876(2007) [PubMed: 17947660] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-52, MASS SPECTROMETRY. Tissue: Mast cell.
[14]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-52 AND TYR-89, MASS SPECTROMETRY. Tissue: Brain.
[15]	Lubec G., Kang S. Submitted (APR-2007) to UniProtKB Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, MASS SPECTROMETRY. Tissue: Brain.
[16]	"Crystal structure of a nucleosome core particle containing the variant histone H2A.Z." Suto R.K., Clarkson M.J., Tremethick D.J., Luger K. Nat. Struct. Biol. 7:1121-1124(2000) [PubMed: 11101893] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH H2A-Z; H2B AND H3.