P62806 (H4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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

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	Nucleus By similarity. Chromosome By similarity.
Post-translational modification	Acetylation at Lys-6 (H4K5ac), Lys-9 (H4K8ac), Lys-13 (H4K12ac) and Lys-17 (H4K16ac) occurs in coding regions of the genome but not in heterochromatin. Citrullination at Arg-4 (H4R3ci) by PADI4 impairs methylation. Monomethylation and asymmetric dimethylation at Arg-4 (H4R3me1 and H4R3me2a, respectively) by PRMT1 favors acetylation at Lys-9 (H4K8ac) and Lys-13 (H4K12ac). Demethylation is performed by JMJD6. Symmetric dimethylation on Arg-4 (H4R3me2s) by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage By similarity. Monomethylated, dimethylated or trimethylated at Lys-21 (H4K20me1, H4K20me2, H4K20me3). Monomethylation is performed by SET8. Trimethylation is performed by SUV420H1 and SUV420H2 and induces gene silencing By similarity. Ref.9 Ref.12 Phosphorylated by PAK2 at Ser-48 (H4S47ph). This phosphorylation increases the association of H3.3-H4 with the histone chaperone HIRA, thus promoting nucleosome assembly of H3.3-H4 and inhibiting nucleosome assembly of H3.1-H4 By similarity. Ref.10 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. Monoubiquitinated at Lys-92 of histone H4 (H4K91ub1) in response to DNA damage. The exact role of H4K91ub1 in DNA damage response is still unclear but it may function as a licensing signal for additional histone H4 post-translational modifications such as H4 Lys-21 methylation (H4K20me) By similarity. Sumoylated, which is associated with transcriptional repression By similarity. Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. Ref.17
Sequence similarities	Belongs to the histone H4 family.

Ontologies

Keywords
Cellular component	Chromosome Nucleosome core Nucleus
Ligand	DNA-binding
PTM	Acetylation Citrullination Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of megakaryocyte differentiation Inferred from electronic annotation. Source: Compara nucleosome assembly Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	actin cytoskeleton Inferred from electronic annotation. Source: Compara nucleolus Inferred from electronic annotation. Source: Compara nucleoplasm Traceable author statement. Source: Reactome nucleosome Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	DNA binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Atad2	Q8CDM1	2	EBI-299632,EBI-2944582

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 103

102

Histone H4

PRO_0000158329

Regions

DNA binding

17 – 21

5

Amino acid modifications

Modified residue

2

1

N-acetylserine By similarity

Modified residue

2

1

Phosphoserine Ref.10

Modified residue

4

1

Asymmetric dimethylarginine; by PRMT1; alternate Ref.12

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 and PRMT7; alternate Ref.12

Modified residue

6

1

N6-acetyllysine; alternate Ref.11

Modified residue

6

1

N6-crotonyl-L-lysine; alternate Ref.17

Modified residue

9

1

N6-acetyllysine; alternate Ref.11

Modified residue

9

1

N6-crotonyl-L-lysine; alternate Ref.17

Modified residue

13

1

N6-acetyllysine; alternate Ref.11

Modified residue

13

1

N6-crotonyl-L-lysine; alternate By similarity

Modified residue

17

1

N6-acetyllysine; alternate Ref.11

Modified residue

17

1

N6-crotonyl-L-lysine; alternate Ref.17

Modified residue

21

1

N6,N6,N6-trimethyllysine; alternate Ref.9

Modified residue

21

1

N6,N6-dimethyllysine; alternate By similarity

Modified residue

21

1

N6-methyllysine; alternate By similarity

Modified residue

32

1

N6-acetyllysine By similarity

Modified residue

48

1

Phosphoserine; by PAK2 By similarity

Modified residue

52

1

Phosphotyrosine Ref.13 Ref.14

Modified residue

89

1

Phosphotyrosine Ref.14

Modified residue

92

1

N6-acetyllysine; alternate By similarity

Cross-link

92

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity

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...

Helix

26 – 29

4

Helix

32 – 41

10

Helix

51 – 76

26

Beta strand

80 – 82

3

Helix

84 – 93

10

Beta strand

98 – 101

4

Sequences

	Sequence		Length	Mass (Da)
	P62806 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: A9E5DFD3F8B97598	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

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Egg, Pancreas and Tongue.
[7]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, MASS SPECTROMETRY. Tissue: Melanoma.
[17]	"Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification." Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T., Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q., Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y. Cell 146:1016-1028(2011) [PubMed] [Europe PMC] [Abstract] Cited for: CROTONYLATION AT LYS-6; LYS-9 AND LYS-17.
[18]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH H2A-Z; H2B AND H3.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

V00753 Genomic DNA. Translation: CAA24130.1.
X13235 Genomic DNA. Translation: CAA31621.1.
X13236 Genomic DNA. Translation: CAA31622.1.
U62672 Genomic DNA. Translation: AAB04766.1.
Y12290 Genomic DNA. Translation: CAA72967.1.
AY158956 Genomic DNA. Translation: AAO06266.1.
AY158957 Genomic DNA. Translation: AAO06267.1.
AY158958 Genomic DNA. Translation: AAO06268.1.
AY158959 Genomic DNA. Translation: AAO06269.1.
AY158960 Genomic DNA. Translation: AAO06270.1.
AY158961 Genomic DNA. Translation: AAO06271.1.
AY158962 Genomic DNA. Translation: AAO06272.1.
AY158963 Genomic DNA. Translation: AAO06273.1.
AY158964 Genomic DNA. Translation: AAO06274.1.
AY158965 Genomic DNA. Translation: AAO06275.1.
AY158966 Genomic DNA. Translation: AAO06276.1.
AY158967 Genomic DNA. Translation: AAO06277.1.
AK007642 mRNA. Translation: BAB25157.1.
AK010085 mRNA. Translation: BAB26692.1.
AK011560 mRNA. Translation: BAB27698.1.
AK139521 mRNA. Translation: BAE24047.1.
AL589651 Genomic DNA. Translation: CAI24108.1.
AL589651 Genomic DNA. Translation: CAI24109.1.
AL590388 Genomic DNA. Translation: CAI25838.1.
AL590388 Genomic DNA. Translation: CAI25839.1.
AL590614 Genomic DNA. Translation: CAI26128.1.
BC028550 mRNA. Translation: AAH28550.3.
BC052219 mRNA. No translation available.
BC057955 mRNA. Translation: AAH57955.1.
BC058529 mRNA. Translation: AAH58529.2.
BC087952 mRNA. Translation: AAH87952.1.
BC092144 mRNA. Translation: AAH92144.1.
BC115446 mRNA. Translation: AAI15447.1.
BC115447 mRNA. Translation: AAI15448.1.
BC115451 mRNA. Translation: AAI15452.1.
BC115448 mRNA. Translation: AAI15449.1.
BC115449 mRNA. Translation: AAI15450.1.
BC115450 mRNA. Translation: AAI15451.1.
BC117010 mRNA. Translation: AAI17011.1.
BC117012 mRNA. Translation: AAI17013.1.
BC111813 mRNA. Translation: AAI11814.1.
BC119241 mRNA. Translation: AAI19242.1.
BC119243 mRNA. Translation: AAI19244.1.
BC119611 mRNA. Translation: AAI19612.1.
BC119612 mRNA. Translation: AAI19613.1.
BC125598 mRNA. Translation: AAI25599.1.
BC125600 mRNA. Translation: AAI25601.1.
BC132186 mRNA. Translation: AAI32187.1.
BC132212 mRNA. Translation: AAI32213.1.
BC139809 mRNA. Translation: AAI39810.1.
BC152397 mRNA. Translation: AAI52398.1.

IPI

IPI00407339.

PIR

S03426.
S03427.

RefSeq

NP_001182350.1. NM_001195421.1.
NP_291074.1. NM_033596.2.
NP_694813.1. NM_153173.3.
NP_783583.1. NM_175652.2.
NP_783585.1. NM_175654.1.
NP_783586.1. NM_175655.1.
NP_783587.1. NM_175656.2.
NP_783588.1. NM_175657.1.
NP_835499.1. NM_178192.1.
NP_835500.1. NM_178193.1.
NP_835515.1. NM_178208.1.
NP_835582.1. NM_178210.1.
NP_835583.1. NM_178211.1.

UniGene

Mm.14775.
Mm.158272.
Mm.227295.
Mm.228709.
Mm.246720.
Mm.255646.
Mm.260530.
Mm.261642.
Mm.261662.
Mm.261664.
Mm.377875.
Mm.442307.
Mm.486099.
Mm.489077.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F66	X-ray	2.60	B/F	1-103	[»]
1U35	X-ray	3.00	B/F	1-103	[»]
2WP2	X-ray	2.37	P/Q	2-21	[»]
4DOW	X-ray	1.95	C/D	15-26	[»]

ProteinModelPortal

P62806.

ModBase

Search...

Protein-protein interaction databases

IntAct

P62806. 6 interactions.

PTM databases

PhosphoSite

P62806.

Proteomic databases

PaxDb

P62806.

PRIDE

P62806.

Protocols and materials databases

DNASU

319156.
319157.
319159.
320332.
326620.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000087714; ENSMUSP00000085006; ENSMUSG00000067455.
ENSMUST00000102964; ENSMUSP00000100029; ENSMUSG00000060093.
ENSMUST00000102965; ENSMUSP00000100030; ENSMUSG00000069266.
ENSMUST00000102967; ENSMUSP00000100032; ENSMUSG00000060678.
ENSMUST00000102968; ENSMUSP00000100033; ENSMUSG00000061482.
ENSMUST00000102971; ENSMUSP00000100036; ENSMUSG00000069274.
ENSMUST00000102972; ENSMUSP00000100037; ENSMUSG00000060981.
ENSMUST00000102977; ENSMUSP00000100042; ENSMUSG00000060639.
ENSMUST00000102979; ENSMUSP00000100044; ENSMUSG00000069305.
ENSMUST00000102983; ENSMUSP00000100048; ENSMUSG00000064288.
ENSMUST00000104941; ENSMUSP00000100546; ENSMUSG00000069306.
ENSMUST00000171473; ENSMUSP00000129930; ENSMUSG00000091405.
ENSMUST00000179285; ENSMUSP00000136357; ENSMUSG00000096010.

GeneID

100041230.
319155.
319156.
319157.
319158.
319159.
319160.
319161.
320332.
326619.
326620.
69386.
97122.

KEGG

mmu:100041230.
mmu:319155.
mmu:319156.
mmu:319157.
mmu:319158.
mmu:319159.
mmu:319160.
mmu:319161.
mmu:320332.
mmu:326619.
mmu:326620.
mmu:69386.
mmu:97122.

Organism-specific databases

CTD

100041230.
121504.
319161.
8294.
8359.
8360.
8361.
8362.
8363.
8364.
8365.
8366.
97122.

MGI

MGI:2448419. Hist1h4a.
MGI:2448420. Hist1h4b.
MGI:2448421. Hist1h4c.
MGI:2448423. Hist1h4d.
MGI:2448425. Hist1h4f.
MGI:2448427. Hist1h4h.
MGI:2448432. Hist1h4i.
MGI:2448436. Hist1h4j.
MGI:2448439. Hist1h4k.
MGI:2448441. Hist1h4m.
MGI:2140113. Hist2h4.
MGI:2448443. Hist4h4.

Phylogenomic databases

eggNOG

COG2036.

GeneTree

ENSGT00690000101710.
ENSGT00690000101714.

HOVERGEN

HBG051878.

InParanoid

P62806.

KO

K11254.

OMA

TAMDIVY.

OrthoDB

EOG4KD6NP.

Enzyme and pathway databases

Reactome

REACT_118161. Cell Cycle.
REACT_120463. Meiosis.
REACT_27235. Meiotic Recombination (mouse).
REACT_75800. Meiotic Synapsis (mouse).

Gene expression databases

ArrayExpress

P62806.

Bgee

P62806.

CleanEx

MM_HIST1H4A.
MM_HIST1H4B.
MM_HIST1H4C.
MM_HIST1H4D.
MM_HIST1H4F.
MM_HIST1H4H.
MM_HIST1H4I.
MM_HIST1H4J.
MM_HIST1H4K.
MM_HIST1H4M.
MM_HIST2H4.
MM_HIST4H4.

Genevestigator

P62806.

GermOnline

ENSMUSG00000060093. Mus musculus.
ENSMUSG00000060639. Mus musculus.
ENSMUSG00000060678. Mus musculus.
ENSMUSG00000060832. Mus musculus.
ENSMUSG00000060981. Mus musculus.
ENSMUSG00000061482. Mus musculus.
ENSMUSG00000064288. Mus musculus.
ENSMUSG00000068851. Mus musculus.
ENSMUSG00000069266. Mus musculus.
ENSMUSG00000069274. Mus musculus.
ENSMUSG00000069305. Mus musculus.
ENSMUSG00000069306. Mus musculus.

Family and domain databases

Gene3D

1.10.20.10. 1 hit.

InterPro

IPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR001951. Histone_H4.
IPR019809. Histone_H4_CS.
[Graphical view]

PANTHER

PTHR10484. PTHR10484. 1 hit.

Pfam

PF00125. Histone. 1 hit.
[Graphical view]

PRINTS

PR00623. HISTONEH4.

SMART

SM00417. H4. 1 hit.
[Graphical view]

SUPFAM

SSF47113. Histone-fold. 1 hit.

PROSITE

PS00047. HISTONE_H4. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P62806.

NextBio

329305.

SOURCE

Search...

Entry information

Entry name

H4_MOUSE

Accession

Primary (citable) accession number: P62806
Secondary accession number(s): A0AUM5 , A4FUP8, A4QMY0, P02304, P02305, Q0VDL9, Q2M2Q5, Q5T006, Q6PDS7, Q811M0, Q9D0C9, Q9D6Q8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 107 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program