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Protein

Histone H4

Gene
N/A
Organism
Bos taurus (Bovine)
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)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi17 – 215

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. poly(A) RNA binding Source: Ensembl

GO - Biological processi

  1. DNA replication-dependent nucleosome assembly Source: Ensembl
  2. DNA replication-independent nucleosome assembly Source: Ensembl
  3. negative regulation of megakaryocyte differentiation Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_278664. NoRC negatively regulates rRNA expression.
REACT_283854. Oxidative Stress Induced Senescence.
REACT_287687. PKMTs methylate histone lysines.
REACT_289105. Meiotic synapsis.
REACT_291460. RMTs methylate histone arginines.
REACT_299696. SIRT1 negatively regulates rRNA Expression.
REACT_301707. DNA methylation.
REACT_308874. RNA Polymerase I Promoter Opening.
REACT_311094. Transcriptional regulation by small RNAs.
REACT_322949. Deposition of new CENPA-containing nucleosomes at the centromere.
REACT_325565. Amyloids.
REACT_326216. DNA Damage/Telomere Stress Induced Senescence.
REACT_338219. PRC2 methylates histones and DNA.
REACT_344113. RNA Polymerase I Chain Elongation.
REACT_345668. HATs acetylate histones.
REACT_348678. Meiotic recombination.
REACT_350364. HDMs demethylate histones.
REACT_351362. Senescence-Associated Secretory Phenotype (SASP).
REACT_351822. Condensation of Prophase Chromosomes.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H4
Alternative name(s):
H4.1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componentsi: Chromosome 1, Chromosome 23, Chromosome 3, Chromosome 5

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. membrane Source: Ensembl
  3. nuclear chromosome Source: Ensembl
  4. nucleoplasm Source: Reactome
  5. nucleosome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 103102Histone H4PRO_0000158289Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei2 – 21PhosphoserineBy similarity
Modified residuei4 – 41Asymmetric dimethylarginine; by PRMT1; alternateBy similarity
Modified residuei4 – 41Citrulline; alternateBy similarity
Modified residuei4 – 41Omega-N-methylarginine; by PRMT1; alternateBy similarity
Modified residuei4 – 41Symmetric dimethylarginine; by PRMT5 and PRMT7; alternateBy similarity
Modified residuei6 – 61N6-acetyllysine; alternateBy similarity
Modified residuei6 – 61N6-crotonyllysine; alternateBy similarity
Modified residuei9 – 91N6-acetyllysine; alternateBy similarity
Modified residuei9 – 91N6-crotonyllysine; alternateBy similarity
Modified residuei13 – 131N6-acetyllysine; alternateBy similarity
Modified residuei13 – 131N6-crotonyllysine; alternateBy similarity
Modified residuei17 – 171N6-acetyllysine; alternate1 Publication
Modified residuei17 – 171N6-crotonyllysine; alternateBy similarity
Modified residuei21 – 211N6,N6,N6-trimethyllysine; alternateBy similarity
Modified residuei21 – 211N6,N6-dimethyllysine; alternate1 Publication
Modified residuei21 – 211N6-methyllysine; alternate1 Publication
Modified residuei32 – 321N6-acetyllysineBy similarity
Modified residuei48 – 481Phosphoserine; by PAK2By similarity
Modified residuei52 – 521PhosphotyrosineBy similarity
Modified residuei89 – 891PhosphotyrosineBy similarity
Modified residuei92 – 921N6-acetyllysine; alternateBy similarity
Modified residuei92 – 921N6-succinyllysine; alternateBy similarity
Cross-linki92 – 92Glycyl 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 (By similarity). 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 SUV420H1 and SUV420H2 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
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 (By similarity).By similarity

Keywords - PTMi

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

Proteomic databases

PaxDbiP62803.
PRIDEiP62803.

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.

Protein-protein interaction databases

BioGridi158101. 7 interactions.
DIPiDIP-44668N.
IntActiP62803. 1 interaction.
STRINGi9913.ENSBTAP00000047761.

Structurei

3D structure databases

ProteinModelPortaliP62803.
SMRiP62803. Positions 21-102.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H4 family.Curated

Phylogenomic databases

eggNOGiCOG2036.
GeneTreeiENSGT00760000119019.
HOGENOMiHOG000234654.
HOVERGENiHBG051878.
InParanoidiP62803.
KOiK11254.
OMAiFAMSGRG.
OrthoDBiEOG77T174.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR001951. Histone_H4.
IPR019809. Histone_H4_CS.
[Graphical view]
PfamiPF00125. Histone. 1 hit.
[Graphical view]
PRINTSiPR00623. HISTONEH4.
SMARTiSM00417. H4. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00047. HISTONE_H4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P62803-1 [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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551T → A in AAI42000 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF001288 mRNA. Translation: AAC39176.1.
BC114196 mRNA. Translation: AAI14197.1.
BC141999 mRNA. Translation: AAI42000.1.
BC142359 mRNA. Translation: AAI42360.1.
PIRiA92050. HSBO4.
RefSeqiNP_001093194.1. NM_001099724.2.
NP_001139343.1. NM_001145871.2.
NP_776305.1. NM_173880.2.
XP_002684676.1. XM_002684630.3.
XP_002697516.1. XM_002697470.3.
XP_005196744.2. XM_005196687.2.
XP_005223853.1. XM_005223796.2.
XP_005223857.1. XM_005223800.2.
XP_010816809.1. XM_010818507.1.
XP_010816812.1. XM_010818510.1.
XP_010816819.1. XM_010818517.1.
XP_010823707.1. XM_010825405.1.
XP_010823709.1. XM_010825407.1.
XP_010823713.1. XM_010825411.1.
XP_010823717.1. XM_010825415.1.
XP_605163.2. XM_605163.4.
XP_874074.1. XM_868981.5.
UniGeneiBt.104550.
Bt.113.
Bt.58502.
Bt.61355.

Genome annotation databases

EnsembliENSBTAT00000029245; ENSBTAP00000029245; ENSBTAG00000030504.
ENSBTAT00000033367; ENSBTAP00000033280; ENSBTAG00000024178.
ENSBTAT00000033368; ENSBTAP00000033281; ENSBTAG00000024179.
ENSBTAT00000033375; ENSBTAP00000033288; ENSBTAG00000024185.
ENSBTAT00000044974; ENSBTAP00000042409; ENSBTAG00000031719.
ENSBTAT00000044998; ENSBTAP00000042428; ENSBTAG00000039812.
ENSBTAT00000045033; ENSBTAP00000042460; ENSBTAG00000031756.
ENSBTAT00000045043; ENSBTAP00000042466; ENSBTAG00000031762.
ENSBTAT00000045044; ENSBTAP00000042467; ENSBTAG00000031763.
ENSBTAT00000052402; ENSBTAP00000047761; ENSBTAG00000040277.
ENSBTAT00000054510; ENSBTAP00000052235; ENSBTAG00000025391.
ENSBTAT00000056505; ENSBTAP00000053034; ENSBTAG00000040155.
ENSBTAT00000063932; ENSBTAP00000054635; ENSBTAG00000032453.
GeneIDi104968814.
280691.
517139.
518961.
526789.
527388.
527645.
529647.
530773.
617875.
617905.
KEGGibta:280691.
bta:516742.
bta:517138.
bta:518961.
bta:526789.
bta:527388.
bta:527645.
bta:528329.
bta:529647.
bta:530773.
bta:617875.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF001288 mRNA. Translation: AAC39176.1.
BC114196 mRNA. Translation: AAI14197.1.
BC141999 mRNA. Translation: AAI42000.1.
BC142359 mRNA. Translation: AAI42360.1.
PIRiA92050. HSBO4.
RefSeqiNP_001093194.1. NM_001099724.2.
NP_001139343.1. NM_001145871.2.
NP_776305.1. NM_173880.2.
XP_002684676.1. XM_002684630.3.
XP_002697516.1. XM_002697470.3.
XP_005196744.2. XM_005196687.2.
XP_005223853.1. XM_005223796.2.
XP_005223857.1. XM_005223800.2.
XP_010816809.1. XM_010818507.1.
XP_010816812.1. XM_010818510.1.
XP_010816819.1. XM_010818517.1.
XP_010823707.1. XM_010825405.1.
XP_010823709.1. XM_010825407.1.
XP_010823713.1. XM_010825411.1.
XP_010823717.1. XM_010825415.1.
XP_605163.2. XM_605163.4.
XP_874074.1. XM_868981.5.
UniGeneiBt.104550.
Bt.113.
Bt.58502.
Bt.61355.

3D structure databases

ProteinModelPortaliP62803.
SMRiP62803. Positions 21-102.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi158101. 7 interactions.
DIPiDIP-44668N.
IntActiP62803. 1 interaction.
STRINGi9913.ENSBTAP00000047761.

Chemistry

BindingDBiP62803.

Proteomic databases

PaxDbiP62803.
PRIDEiP62803.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000029245; ENSBTAP00000029245; ENSBTAG00000030504.
ENSBTAT00000033367; ENSBTAP00000033280; ENSBTAG00000024178.
ENSBTAT00000033368; ENSBTAP00000033281; ENSBTAG00000024179.
ENSBTAT00000033375; ENSBTAP00000033288; ENSBTAG00000024185.
ENSBTAT00000044974; ENSBTAP00000042409; ENSBTAG00000031719.
ENSBTAT00000044998; ENSBTAP00000042428; ENSBTAG00000039812.
ENSBTAT00000045033; ENSBTAP00000042460; ENSBTAG00000031756.
ENSBTAT00000045043; ENSBTAP00000042466; ENSBTAG00000031762.
ENSBTAT00000045044; ENSBTAP00000042467; ENSBTAG00000031763.
ENSBTAT00000052402; ENSBTAP00000047761; ENSBTAG00000040277.
ENSBTAT00000054510; ENSBTAP00000052235; ENSBTAG00000025391.
ENSBTAT00000056505; ENSBTAP00000053034; ENSBTAG00000040155.
ENSBTAT00000063932; ENSBTAP00000054635; ENSBTAG00000032453.
GeneIDi104968814.
280691.
517139.
518961.
526789.
527388.
527645.
529647.
530773.
617875.
617905.
KEGGibta:280691.
bta:516742.
bta:517138.
bta:518961.
bta:526789.
bta:527388.
bta:527645.
bta:528329.
bta:529647.
bta:530773.
bta:617875.

Organism-specific databases

CTDi373325.

Phylogenomic databases

eggNOGiCOG2036.
GeneTreeiENSGT00760000119019.
HOGENOMiHOG000234654.
HOVERGENiHBG051878.
InParanoidiP62803.
KOiK11254.
OMAiFAMSGRG.
OrthoDBiEOG77T174.

Enzyme and pathway databases

ReactomeiREACT_278664. NoRC negatively regulates rRNA expression.
REACT_283854. Oxidative Stress Induced Senescence.
REACT_287687. PKMTs methylate histone lysines.
REACT_289105. Meiotic synapsis.
REACT_291460. RMTs methylate histone arginines.
REACT_299696. SIRT1 negatively regulates rRNA Expression.
REACT_301707. DNA methylation.
REACT_308874. RNA Polymerase I Promoter Opening.
REACT_311094. Transcriptional regulation by small RNAs.
REACT_322949. Deposition of new CENPA-containing nucleosomes at the centromere.
REACT_325565. Amyloids.
REACT_326216. DNA Damage/Telomere Stress Induced Senescence.
REACT_338219. PRC2 methylates histones and DNA.
REACT_344113. RNA Polymerase I Chain Elongation.
REACT_345668. HATs acetylate histones.
REACT_348678. Meiotic recombination.
REACT_350364. HDMs demethylate histones.
REACT_351362. Senescence-Associated Secretory Phenotype (SASP).
REACT_351822. Condensation of Prophase Chromosomes.

Miscellaneous databases

NextBioi20804878.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR001951. Histone_H4.
IPR019809. Histone_H4_CS.
[Graphical view]
PfamiPF00125. Histone. 1 hit.
[Graphical view]
PRINTSiPR00623. HISTONEH4.
SMARTiSM00417. H4. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00047. HISTONE_H4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Poly A-containing histone H4 mRNA variant (H4-v.1): isolation and sequence determination from bovine adrenal medulla."
    Gendron N., Dumont M., Gagne M.-F., Lemaire S.
    Biochim. Biophys. Acta 1396:32-38(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (H4-V.1).
    Tissue: Adrenal medulla.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus and Hereford.
    Tissue: Hypothalamus, Ileum and Thymus.
  3. "Structure of the glycine-rich, arginine-rich histone of the Novikoff hepatoma."
    Wilson R.K., Starbuck W.C., Taylor C.W., Jordan J.J., Busch H.
    Cancer Res. 30:2942-2951(1969) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-103, ACETYLATION AT SER-2 AND LYS-17, METHYLATION AT LYS-21.
  4. "Structural analysis of the glycine-rich, arginine-rich histone. 3. Sequence of the amino-terminal half of the molecule containing the modified lysine residues and the total sequence."
    Ogawa Y., Quagliarotti G., Jordan J.J., Taylor C.W., Starbuck W.C., Busch H.
    J. Biol. Chem. 244:4387-4392(1968) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-50.
    Tissue: Thymus.
  5. "Structural analysis of the glycine-rich, arginine-rich histone. II. Sequence of the half of the molecule containing the aromatic amino acids."
    Quagliarotti G., Ogawa Y., Taylor C.W., Sautiere P., Jordan J., Starbuck W.C., Busch H.
    J. Biol. Chem. 244:1796-1802(1968) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 51-103.
    Tissue: Thymus.

Entry informationi

Entry nameiH4_BOVIN
AccessioniPrimary (citable) accession number: P62803
Secondary accession number(s): A5PJ80
, A5PK53, A8QFF4, P02304, P02305
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.