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Protein

Histone H4

Gene

Hist1h4a

more
Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi17 – 215

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-1221633. Meiotic Synapsis.
R-MMU-201722. Formation of the beta-catenin:TCF transactivating complex.
R-MMU-212300. PRC2 methylates histones and DNA.
R-MMU-2299718. Condensation of Prophase Chromosomes.
R-MMU-2559580. Oxidative Stress Induced Senescence.
R-MMU-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-MMU-2559586. DNA Damage/Telomere Stress Induced Senescence.
R-MMU-3214841. PKMTs methylate histone lysines.
R-MMU-3214842. HDMs demethylate histones.
R-MMU-3214847. HATs acetylate histones.
R-MMU-3214858. RMTs methylate histone arginines.
R-MMU-427359. SIRT1 negatively regulates rRNA expression.
R-MMU-427413. NoRC negatively regulates rRNA expression.
R-MMU-4551638. SUMOylation of chromatin organization proteins.
R-MMU-5250924. B-WICH complex positively regulates rRNA expression.
R-MMU-5578749. Transcriptional regulation by small RNAs.
R-MMU-5625886. Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
R-MMU-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-MMU-5693571. Nonhomologous End-Joining (NHEJ).
R-MMU-573389. NoRC negatively regulates rRNA expression.
R-MMU-606279. Deposition of new CENPA-containing nucleosomes at the centromere.
R-MMU-69473. G2/M DNA damage checkpoint.
R-MMU-73728. RNA Polymerase I Promoter Opening.
R-MMU-73777. RNA Polymerase I Chain Elongation.
R-MMU-8936459. RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
R-MMU-8939236. RUNX1 regulates transcription of genes involved in differentiation of HSCs.
R-MMU-912497. Meiotic Recombination.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H4
Gene namesi
AND
Name:Hist1h4b
Synonyms:H4-53
AND
Name:Hist1h4c
Synonyms:H4-12
AND
AND
AND
AND
AND
AND
AND
AND
Name:Hist2h4a
Synonyms:Hist2h4
AND
Name:Hist4h4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componentsi: Chromosome 13, Chromosome 3, Chromosome 6

Organism-specific databases

MGIiMGI: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.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001583292 – 103Histone H4Add BLAST102

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei2Phosphoserine1 Publication1
Modified residuei4Asymmetric dimethylarginine; by PRMT1; alternate1 Publication1
Modified residuei4Citrulline; alternateBy similarity1
Modified residuei4Omega-N-methylarginine; by PRMT1; alternateBy similarity1
Modified residuei4Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate1 Publication1
Modified residuei6N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei6N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei6N6-acetyllysine; alternateCombined sources1
Modified residuei6N6-butyryllysine; alternate1 Publication1
Modified residuei6N6-crotonyllysine; alternate1 Publication1
Modified residuei9N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei9N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei9N6-acetyllysine; alternateCombined sources1
Modified residuei9N6-butyryllysine; alternate1 Publication1
Modified residuei9N6-crotonyllysine; alternate1 Publication1
Modified residuei9N6-propionyllysine; alternateBy similarity1
Modified residuei13N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei13N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei13N6-acetyllysine; alternateCombined sources1
Modified residuei13N6-butyryllysine; alternate1 Publication1
Modified residuei13N6-crotonyllysine; alternateBy similarity1
Cross-linki13Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei17N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei17N6-acetyllysine; alternateCombined sources1
Modified residuei17N6-butyryllysine; alternateBy similarity1
Modified residuei17N6-crotonyllysine; alternate1 Publication1
Modified residuei17N6-propionyllysine; alternateBy similarity1
Modified residuei21N6,N6,N6-trimethyllysine; alternate1 Publication1
Modified residuei21N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei21N6-methyllysine; alternateBy similarity1
Cross-linki21Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei32N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei32N6-acetyllysine; alternateCombined sources1
Modified residuei32N6-butyryllysine; alternateBy similarity1
Modified residuei32N6-propionyllysine; alternateBy similarity1
Modified residuei32N6-succinyllysine; alternate1 Publication1
Cross-linki32Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei45N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei45N6-butyryllysine; alternateBy similarity1
Modified residuei45N6-propionyllysine; alternateBy similarity1
Modified residuei48PhosphoserineCombined sources1
Modified residuei52PhosphotyrosineCombined sources1
Modified residuei60N6-(2-hydroxyisobutyryl)lysine1 Publication1
Cross-linki60Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei78N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei78N6-butyryllysine; alternateBy similarity1
Modified residuei78N6-propionyllysine; alternateBy similarity1
Modified residuei78N6-succinyllysine1 Publication1
Modified residuei80N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei80N6-butyryllysine; alternateBy similarity1
Modified residuei80N6-propionyllysine; alternateBy similarity1
Modified residuei80N6-succinyllysine1 Publication1
Cross-linki80Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei81PhosphothreonineCombined sources1
Modified residuei89PhosphotyrosineCombined sources1
Modified residuei92N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei92N6-acetyllysine; alternateBy similarity1
Modified residuei92N6-butyryllysine; alternateBy similarity1
Modified residuei92N6-propionyllysine; alternateBy similarity1
Modified residuei92N6-succinyllysine; alternateCombined sources1 Publication1
Cross-linki92Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki92Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity

Post-translational modificationi

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.By similarity
Citrullination at Arg-4 (H4R3ci) by PADI4 impairs methylation.2 Publications
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).By similarity
Monomethylated, dimethylated or trimethylated at Lys-21 (H4K20me1, H4K20me2, H4K20me3). Monomethylation is performed by SET8. Trimethylation is performed by KMT5B and KMT5C and induces gene silencing (By similarity).By similarity
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).By similarity
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).By similarity
Sumoylated, which is associated with transcriptional repression.By similarity
Butyrylation of histones marks active promoters and competes with histone acetylation. It is present during late spermatogenesis.1 Publication
Hydroxybutyrylation of histones is induced by starvation.1 Publication
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.1 Publication

Keywords - PTMi

Acetylation, Citrullination, Hydroxylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP62806.
MaxQBiP62806.
PaxDbiP62806.
PRIDEiP62806.
TopDownProteomicsiP62806.

PTM databases

iPTMnetiP62806.
PhosphoSitePlusiP62806.

Expressioni

Gene expression databases

BgeeiENSMUSG00000060093.
CleanExiMM_HIST1H4A.
MM_HIST1H4B.
MM_HIST1H4C.
MM_HIST1H4D.
MM_HIST1H4F.
MM_HIST1H4H.
MM_HIST1H4I.
MM_HIST1H4J.
MM_HIST1H4K.
MM_HIST1H4M.
MM_HIST2H4.
MM_HIST4H4.
ExpressionAtlasiP62806. baseline and differential.
GenevisibleiP62806. MM.

Interactioni

Subunit structurei

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.1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi213404. 1 interactor.
220610. 5 interactors.
235074. 1 interactor.
235075. 1 interactor.
235079. 1 interactor.
235942. 10 interactors.
236472. 3 interactors.
236473. 1 interactor.
CORUMiP62806.
DIPiDIP-45837N.
IntActiP62806. 13 interactors.
MINTiMINT-1866189.
STRINGi10090.ENSMUSP00000136357.

Structurei

Secondary structure

1103
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi21 – 23Combined sources3
Helixi27 – 29Combined sources3
Helixi32 – 41Combined sources10
Helixi51 – 76Combined sources26
Beta strandi80 – 82Combined sources3
Helixi84 – 93Combined sources10
Beta strandi97 – 101Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5B1LX-ray2.35B/F1-103[»]
5B1MX-ray2.34B/F1-103[»]
ProteinModelPortaliP62806.
SMRiP62806.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62806.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H4 family.Curated

Phylogenomic databases

eggNOGiKOG3467. Eukaryota.
COG2036. LUCA.
GeneTreeiENSGT00760000119019.
HOVERGENiHBG051878.
InParanoidiP62806.
KOiK11254.
OMAiYEEVRVV.
OrthoDBiEOG091G0XGD.
PhylomeDBiP62806.

Family and domain databases

CDDicd00076. H4. 1 hit.
InterProiView protein in InterPro
IPR035425. CENP-T/H4_C.
IPR009072. Histone-fold.
IPR001951. Histone_H4.
IPR019809. Histone_H4_CS.
IPR004823. TAF_TATA-bd.
PfamiView protein in Pfam
PF15511. CENP-T_C. 1 hit.
PRINTSiPR00623. HISTONEH4.
SMARTiView protein in SMART
SM00417. H4. 1 hit.
SM00803. TAF. 1 hit.
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiView protein in PROSITE
PS00047. HISTONE_H4. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P62806-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL
60 70 80 90 100
IYEETRGVLK VFLENVIRDA VTYTEHAKRK TVTAMDVVYA LKRQGRTLYG

FGG
Length:103
Mass (Da):11,367
Last modified:January 23, 2007 - v2
Checksum:iA9E5DFD3F8B97598
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti34A → V in BAB26692 (PubMed:16141072).Curated1
Sequence conflicti80K → E in BAB27698 (PubMed:16141072).Curated1
Sequence conflicti90A → R in CAA31622 (PubMed:2915930).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS26291.1.
CCDS26292.1.
CCDS26300.1.
CCDS26306.1.
CCDS26340.1.
CCDS26345.1.
CCDS26353.1.
CCDS26359.1.
CCDS26366.1.
CCDS26367.1.
CCDS39684.1.
CCDS51002.1.
PIRiS03426.
S03427.
RefSeqiNP_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_178210.2.
NP_835583.1. NM_178211.2.
UniGeneiMm.14775.
Mm.158272.
Mm.227295.
Mm.228709.
Mm.246720.
Mm.255646.
Mm.260530.
Mm.261642.
Mm.261662.
Mm.261664.
Mm.442307.
Mm.486099.

Genome annotation databases

EnsembliENSMUST00000087714; 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.
GeneIDi100041230.
319155.
319156.
319157.
319158.
319159.
319160.
319161.
320332.
326619.
326620.
69386.
97122.
KEGGimmu: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.
UCSCiuc007pre.1. mouse.

Similar proteinsi

Entry informationi

Entry nameiH4_MOUSE
AccessioniPrimary (citable) accession number: P62806
Secondary accession number(s): A0AUM5
, A4FUP8, A4QMY0, P02304, P02305, Q0VDL9, Q2M2Q5, Q5T006, Q6PDS7, Q811M0, Q9D0C9, Q9D6Q8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 22, 2017
This is version 153 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families