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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)DescriptionActionsGraphical viewLength
DNA bindingi17 – 215

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDNA-binding

Enzyme and pathway databases

ReactomeiR-BTA-171306. Packaging Of Telomere Ends.
R-BTA-201722. Formation of the beta-catenin:TCF transactivating complex.
R-BTA-212300. PRC2 methylates histones and DNA.
R-BTA-2299718. Condensation of Prophase Chromosomes.
R-BTA-2559580. Oxidative Stress Induced Senescence.
R-BTA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-BTA-2559586. DNA Damage/Telomere Stress Induced Senescence.
R-BTA-3214815. HDACs deacetylate histones.
R-BTA-3214841. PKMTs methylate histone lysines.
R-BTA-3214842. HDMs demethylate histones.
R-BTA-3214847. HATs acetylate histones.
R-BTA-3214858. RMTs methylate histone arginines.
R-BTA-427359. SIRT1 negatively regulates rRNA expression.
R-BTA-427413. NoRC negatively regulates rRNA expression.
R-BTA-4551638. SUMOylation of chromatin organization proteins.
R-BTA-5250924. B-WICH complex positively regulates rRNA expression.
R-BTA-5578749. Transcriptional regulation by small RNAs.
R-BTA-5625886. Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
R-BTA-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-BTA-5693571. Nonhomologous End-Joining (NHEJ).
R-BTA-606279. Deposition of new CENPA-containing nucleosomes at the centromere.
R-BTA-69473. G2/M DNA damage checkpoint.
R-BTA-73728. RNA Polymerase I Promoter Opening.
R-BTA-73777. RNA Polymerase I Chain Elongation.
R-BTA-8936459. RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
R-BTA-8939236. RUNX1 regulates transcription of genes involved in differentiation of HSCs.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H4
Alternative name(s):
H4.1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componentsi: Chromosome 1, Chromosome 23, Chromosome 3, Chromosome 5

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 methionineiRemoved2 Publications
ChainiPRO_00001582892 – 103Histone H4Add BLAST102

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine1 Publication1
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-acetyllysine; alternateBy similarity1
Modified residuei6N6-butyryllysine; alternateBy similarity1
Modified residuei6N6-crotonyllysine; alternateBy similarity1
Modified residuei9N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei9N6-(beta-hydroxybutyryl)lysine; alternateBy similarity1
Modified residuei9N6-acetyllysine; alternateBy similarity1
Modified residuei9N6-butyryllysine; alternateBy similarity1
Modified residuei9N6-crotonyllysine; alternateBy similarity1
Modified residuei9N6-propionyllysine; alternateBy similarity1
Modified residuei13N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei13N6-(beta-hydroxybutyryl)lysine; alternateBy similarity1
Modified residuei13N6-acetyllysine; alternateBy similarity1
Modified residuei13N6-butyryllysine; alternateBy similarity1
Modified residuei13N6-crotonyllysine; alternateBy similarity1
Cross-linki13Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei17N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei17N6-acetyllysine; alternate1 Publication1
Modified residuei17N6-butyryllysine; alternateBy similarity1
Modified residuei17N6-crotonyllysine; alternateBy similarity1
Modified residuei17N6-propionyllysine; alternateBy similarity1
Modified residuei21N6,N6,N6-trimethyllysine; alternateBy similarity1
Modified residuei21N6,N6-dimethyllysine; alternate1 Publication1
Modified residuei21N6-methyllysine; alternate1 Publication1
Cross-linki21Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei32N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei32N6-acetyllysine; alternateBy similarity1
Modified residuei32N6-butyryllysine; alternateBy similarity1
Modified residuei32N6-propionyllysine; alternateBy similarity1
Modified residuei32N6-succinyllysine; alternateBy similarity1
Cross-linki32Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
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
Cross-linki60Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
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-butyryllysine; alternateBy similarity1
Modified residuei80N6-propionyllysine; alternateBy similarity1
Cross-linki80Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei81PhosphothreonineBy 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 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.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 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
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
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

PaxDbiP62803.
PeptideAtlasiP62803.
PRIDEiP62803.

PTM databases

iPTMnetiP62803.

Expressioni

Gene expression databases

BgeeiENSBTAG00000024178.

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.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi158101. 9 interactors.
DIPiDIP-44668N.
IntActiP62803. 2 interactors.
STRINGi9913.ENSBTAP00000054635.

Structurei

3D structure databases

ProteinModelPortaliP62803.
SMRiP62803.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H4 family.Curated

Phylogenomic databases

eggNOGiKOG3467. Eukaryota.
COG2036. LUCA.
GeneTreeiENSGT00760000119019.
HOGENOMiHOG000234654.
HOVERGENiHBG051878.
InParanoidiP62803.
KOiK11254.
OMAiYEEVRVV.
OrthoDBiEOG091G0XGD.

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.

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)DescriptionActionsGraphical viewLength
Sequence conflicti55T → A in AAI42000 (Ref. 2) Curated1

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_002697470.4.
XP_605163.2. XM_605163.4.
XP_874074.1. XM_868981.6.
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.
GeneIDi280691.
526789.
527645.
530773.
617875.
KEGGibta:280691.
bta:526789.
bta:527645.
bta:530773.
bta:617875.

Similar proteinsi

Entry informationi

Entry nameiH4_BOVIN
AccessioniPrimary (citable) accession number: P62803
Secondary accession number(s): A5PJ80
, A5PK53, A8QFF4, P02304, P02305
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 22, 2017
This is version 132 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families