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Histone H4

Cairina moschata (Muscovy duck)
Reviewed-Annotation score: -Protein inferred from homologyi


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.


Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi17 – 215

GO - Molecular functioni

GO - Biological processi


Molecular functionDNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H4
OrganismiCairina moschata (Muscovy duck)
Taxonomic identifieri8855 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeAnseriformesAnatidaeAnatinaeCairina

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_00001582912 – 103Histone H4Add BLAST102

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei2PhosphoserineBy similarity1
Modified residuei4Asymmetric dimethylarginine; by PRMT1; alternateBy similarity1
Modified residuei4Citrulline; alternateBy similarity1
Modified residuei4Omega-N-methylarginine; by PRMT1; alternateBy similarity1
Modified residuei4Symmetric dimethylarginine; by PRMT5 and PRMT7; alternateBy similarity1
Modified residuei6N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei6N6-acetyllysineBy similarity1
Modified residuei6N6-butyryllysine; alternateBy similarity1
Modified residuei9N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei9N6-acetyllysineBy similarity1
Modified residuei9N6-butyryllysine; alternateBy similarity1
Modified residuei9N6-propionyllysine; alternateBy similarity1
Modified residuei13N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei13N6-acetyllysineBy similarity1
Modified residuei13N6-butyryllysine; alternateBy similarity1
Modified residuei17N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei17N6-acetyllysineBy similarity1
Modified residuei17N6-butyryllysine; alternateBy similarity1
Modified residuei17N6-propionyllysine; alternateBy similarity1
Modified residuei21N6,N6,N6-trimethyllysine; alternateBy similarity1
Modified residuei21N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei21N6-methylated lysineBy similarity1
Modified residuei21N6-methyllysine; alternateBy similarity1
Modified residuei32N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei32N6-acetyllysineBy similarity1
Modified residuei32N6-butyryllysine; alternateBy similarity1
Modified residuei32N6-propionyllysine; alternateBy similarity1
Modified residuei32N6-succinyllysine; alternateBy similarity1
Modified residuei45N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei45N6-butyryllysine; alternateBy similarity1
Modified residuei45N6-propionyllysine; alternateBy similarity1
Modified residuei48Phosphoserine; by PAK2By similarity1
Modified residuei52PhosphotyrosineBy similarity1
Modified residuei60N6-(2-hydroxyisobutyryl)lysineBy similarity1
Modified residuei60N6-acetyllysineBy similarity1
Modified residuei78N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei78N6-butyryllysine; alternateBy similarity1
Modified residuei78N6-propionyllysine; alternateBy similarity1
Modified residuei78N6-succinyllysineBy similarity1
Modified residuei80N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei80N6-acetyllysineBy similarity1
Modified residuei80N6-butyryllysine; alternateBy similarity1
Modified residuei80N6-propionyllysine; alternateBy similarity1
Modified residuei89PhosphotyrosineBy similarity1
Modified residuei92N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei92N6-acetyllysine; alternateBy similarity1
Modified residuei92N6-butyryllysine; alternateBy similarity1
Modified residuei92N6-propionyllysine; alternateBy similarity1
Modified residuei92N6-succinyllysine; alternateBy similarity1
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.By similarity
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.By similarity

Keywords - PTMi

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

Proteomic databases



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.

GO - Molecular functioni


3D structure databases


Family & Domainsi

Sequence similaritiesi

Belongs to the histone H4 family.Curated

Phylogenomic databases


Family and domain databases

CDDicd00076 H4, 1 hit
Gene3Di1.10.20.10, 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
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


Sequence statusi: Complete.

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

P62800-1 [UniParc]FASTAAdd to basket

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Mass (Da):11,367
Last modified:January 23, 2007 - v2

Sequence databases

Select the link destinations:
Links Updated
X14732 Genomic DNA Translation: CAA32854.1
X14732 Genomic DNA Translation: CAA32857.1

Similar proteinsi

Entry informationi

Entry nameiH4_CAIMO
AccessioniPrimary (citable) accession number: P62800
Secondary accession number(s): P02304, P02305
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 74 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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