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P62806 (H4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length103 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.11

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.14

Sequence similarities

Belongs to the histone H4 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Atad2Q8CDM12EBI-299632,EBI-2944582

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 103102Histone H4
PRO_0000158329

Regions

DNA binding17 – 215

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue21Phosphoserine Ref.10
Modified residue41Asymmetric dimethylarginine; by PRMT1; alternate Ref.11
Modified residue41Citrulline; alternate By similarity
Modified residue41Omega-N-methylarginine; by PRMT1; alternate By similarity
Modified residue41Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate Ref.11
Modified residue61N6-acetyllysine; alternate Ref.15 Ref.16
Modified residue61N6-crotonyllysine; alternate Ref.14
Modified residue91N6-acetyllysine; alternate Ref.15 Ref.16
Modified residue91N6-crotonyllysine; alternate Ref.14
Modified residue131N6-acetyllysine; alternate Ref.15 Ref.16
Modified residue131N6-crotonyllysine; alternate By similarity
Modified residue171N6-acetyllysine; alternate Ref.15 Ref.16
Modified residue171N6-crotonyllysine; alternate Ref.14
Modified residue211N6,N6,N6-trimethyllysine; alternate Ref.9
Modified residue211N6,N6-dimethyllysine; alternate By similarity
Modified residue211N6-methyllysine; alternate By similarity
Modified residue321N6-acetyllysine Ref.15
Modified residue481Phosphoserine; by PAK2 By similarity
Modified residue521Phosphotyrosine Ref.12 Ref.13
Modified residue891Phosphotyrosine Ref.13
Modified residue921N6-acetyllysine; alternate By similarity
Modified residue921N6-succinyllysine; alternate Ref.15
Cross-link92Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity

Experimental info

Sequence conflict341A → V in BAB26692. Ref.6
Sequence conflict801K → E in BAB27698. Ref.6
Sequence conflict901A → R in CAA31622. Ref.2

Secondary structure

............... 103
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P62806 [UniParc].

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

FASTA10311,367
        10         20         30         40         50         60 
MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK 

        70         80         90        100 
VFLENVIRDA VTYTEHAKRK TVTAMDVVYA LKRQGRTLYG FGG 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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]"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.
[12]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Mast cell.
[13]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[14]"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.
[15]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-9; LYS-13; LYS-17 AND LYS-32, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-92, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[16]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-9; LYS-13 AND LYS-17, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[17]"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.
CCDSCCDS26291.1.
CCDS26292.1.
CCDS26300.1.
CCDS26306.1.
CCDS26340.1.
CCDS26345.1.
CCDS26353.1.
CCDS26359.1.
CCDS26366.1.
CCDS26367.1.
CCDS39684.1.
CCDS51002.1.
PIRS03426.
S03427.
RefSeqNP_001182350.1. NM_001195421.1.
NP_291074.1. NM_033596.3.
NP_694813.1. NM_153173.4.
NP_783583.1. NM_175652.3.
NP_783585.1. NM_175654.2.
NP_783586.1. NM_175655.2.
NP_783587.1. NM_175656.3.
NP_783588.1. NM_175657.2.
NP_835499.1. NM_178192.2.
NP_835500.1. NM_178193.2.
NP_835515.1. NM_178208.2.
NP_835582.1. NM_178210.1.
NP_835583.1. NM_178211.2.
XP_006544162.1. XM_006544099.1.
UniGeneMm.14775.
Mm.158272.
Mm.227295.
Mm.228709.
Mm.246720.
Mm.255646.
Mm.260530.
Mm.261642.
Mm.261662.
Mm.261664.
Mm.442307.
Mm.486099.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F66X-ray2.60B/F1-103[»]
1U35X-ray3.00B/F1-103[»]
2WP2X-ray2.37P/Q2-21[»]
4AU7X-ray2.07C18-25[»]
4DOWX-ray1.95C/D15-26[»]
ProteinModelPortalP62806.
SMRP62806. Positions 21-102.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid213404. 1 interaction.
220610. 5 interactions.
235074. 1 interaction.
235079. 1 interaction.
235942. 8 interactions.
236472. 2 interactions.
236473. 1 interaction.
DIPDIP-45837N.
IntActP62806. 9 interactions.
MINTMINT-1866189.

PTM databases

PhosphoSiteP62806.

Proteomic databases

MaxQBP62806.
PaxDbP62806.
PRIDEP62806.

Protocols and materials databases

DNASU319156.
319157.
319159.
320332.
326620.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000087714; 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.
GeneID100041230.
102641229.
319155.
319156.
319157.
319158.
319159.
319160.
319161.
320332.
326619.
326620.
69386.
97122.
KEGGmmu:100041230.
mmu:102641229.
mmu:319155.
mmu:319156.
mmu:319157.
mmu:319158.
mmu:319159.
mmu:319160.
mmu:319161.
mmu:320332.
mmu:326619.
mmu:326620.
mmu:69386.
mmu:97122.
UCSCuc007pre.1. mouse.

Organism-specific databases

CTD100041230.
121504.
319161.
8294.
8359.
8360.
8361.
8362.
8363.
8364.
8365.
8366.
97122.
MGIMGI: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

eggNOGCOG2036.
GeneTreeENSGT00750000117310.
ENSGT00750000117311.
HOVERGENHBG051878.
InParanoidP62806.
KOK11254.
OMAYEEVRVV.
OrthoDBEOG77T174.
PhylomeDBP62806.

Enzyme and pathway databases

ReactomeREACT_188804. Cell Cycle.
REACT_200794. Mus musculus biological processes.
REACT_218274. Chromatin organization.

Gene expression databases

ArrayExpressP62806.
BgeeP62806.
CleanExMM_HIST1H4A.
MM_HIST1H4B.
MM_HIST1H4C.
MM_HIST1H4D.
MM_HIST1H4F.
MM_HIST1H4H.
MM_HIST1H4I.
MM_HIST1H4J.
MM_HIST1H4K.
MM_HIST1H4M.
MM_HIST2H4.
MM_HIST4H4.
GenevestigatorP62806.

Family and domain databases

Gene3D1.10.20.10. 1 hit.
InterProIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR001951. Histone_H4.
IPR019809. Histone_H4_CS.
[Graphical view]
PfamPF00125. Histone. 1 hit.
[Graphical view]
PRINTSPR00623. HISTONEH4.
SMARTSM00417. H4. 1 hit.
[Graphical view]
SUPFAMSSF47113. SSF47113. 1 hit.
PROSITEPS00047. HISTONE_H4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP62806.
NextBio329305.
PROP62806.
SOURCESearch...

Entry information

Entry nameH4_MOUSE
AccessionPrimary (citable) accession number: P62806
Secondary accession number(s): A0AUM5 expand/collapse secondary AC list , 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: July 9, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot