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Protein

Histone H4

Gene

H4-I

more
Organism
Gallus gallus (Chicken)
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

Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-GGA-212300. PRC2 methylates histones and DNA.
R-GGA-2299718. Condensation of Prophase Chromosomes.
R-GGA-2559580. Oxidative Stress Induced Senescence.
R-GGA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-GGA-3214815. HDACs deacetylate histones.
R-GGA-3214841. PKMTs methylate histone lysines.
R-GGA-3214842. HDMs demethylate histones.
R-GGA-3214847. HATs acetylate histones.
R-GGA-3214858. RMTs methylate histone arginines.
R-GGA-427359. SIRT1 negatively regulates rRNA Expression.
R-GGA-5250924. B-WICH complex positively regulates rRNA expression.
R-GGA-5578749. Transcriptional regulation by small RNAs.
R-GGA-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-GGA-5693571. Nonhomologous End-Joining (NHEJ).
R-GGA-5693607. Processing of DNA double-strand break ends.
R-GGA-606279. Deposition of new CENPA-containing nucleosomes at the centromere.
R-GGA-69473. G2/M DNA damage checkpoint.
R-GGA-73728. RNA Polymerase I Promoter Opening.
R-GGA-73777. RNA Polymerase I Chain Elongation.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H4
Gene namesi
Name:H4-I
AND
Name:H4-II
AND
Name:H4-III
AND
Name:H4-IV
AND
Name:H4-V
AND
Name:H4-VI
AND
Name:H4-VII
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Chromosome 1

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001582962 – 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-acetyllysineBy similarity1
Modified residuei9N6-acetyllysineBy similarity1
Modified residuei13N6-acetyllysineBy similarity1
Modified residuei17N6-acetyllysineBy 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-acetyllysineBy similarity1
Modified residuei48Phosphoserine; by PAK2By similarity1
Modified residuei52PhosphotyrosineBy similarity1
Modified residuei60N6-acetyllysineBy similarity1
Modified residuei80N6-acetyllysineBy similarity1
Modified residuei89PhosphotyrosineBy similarity1
Modified residuei92N6-acetyllysine; 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

Keywords - PTMi

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

Proteomic databases

PaxDbiP62801.
PRIDEiP62801.

Expressioni

Gene expression databases

BgeeiENSGALG00000025786.

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

BioGridi679227. 7 interactors.
IntActiP62801. 2 interactors.
STRINGi9031.ENSGALP00000037292.

Structurei

Secondary structure

1103
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi26 – 29Combined sources4
Helixi32 – 41Combined sources10
Helixi51 – 76Combined sources26
Beta strandi80 – 82Combined sources3
Helixi84 – 93Combined sources10
Beta strandi97 – 100Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EQZX-ray2.50D/H1-103[»]
1HIOX-ray3.10D28-103[»]
1HQ3X-ray2.15D/H1-103[»]
1TZYX-ray1.90D/H1-103[»]
2AROX-ray2.10D/H1-103[»]
2HIOX-ray3.10D1-103[»]
3C9Kelectron microscopy20.00D/H2-103[»]
ProteinModelPortaliP62801.
SMRiP62801.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62801.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H4 family.Curated

Phylogenomic databases

eggNOGiKOG3467. Eukaryota.
COG2036. LUCA.
GeneTreeiENSGT00760000119019.
HOVERGENiHBG051878.
InParanoidiP62801.
KOiK11254.
OMAiSTHNERI.
OrthoDBiEOG091G0XGD.
PhylomeDBiP62801.

Family and domain databases

CDDicd00076. H4. 1 hit.
Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR001951. Histone_H4.
IPR019809. Histone_H4_CS.
IPR004823. TAF_TATA-bd.
[Graphical view]
PRINTSiPR00623. HISTONEH4.
SMARTiSM00417. H4. 1 hit.
SM00803. TAF. 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.

P62801-1 [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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02218 Genomic DNA. Translation: CAA26137.1.
X02218 Genomic DNA. Translation: CAA26140.1.
J00866 Genomic DNA. No translation available.
M74533 Genomic DNA. Translation: AAA73091.1.
M74534 Genomic DNA. Translation: AAA73092.1.
U37575 Genomic DNA. Translation: AAC59999.1.
U37575 Genomic DNA. Translation: AAC60001.1.
PIRiA02640. HSCH4.
JH0507.
RefSeqiNP_001032932.1. NM_001037843.1.
NP_001032934.1. NM_001037845.1.
NP_001268414.1. NM_001281485.1.
XP_001233180.1. XM_001233179.4.
XP_003640418.1. XM_003640370.3.
XP_004937726.1. XM_004937669.2.
XP_425458.2. XM_425458.5.
UniGeneiGga.39882.

Genome annotation databases

EnsembliENSGALT00000046233; ENSGALP00000041526; ENSGALG00000025786.
ENSGALT00000049482; ENSGALP00000054690; ENSGALG00000032272.
ENSGALT00000053533; ENSGALP00000054121; ENSGALG00000032933.
ENSGALT00000066061; ENSGALP00000045681; ENSGALG00000032198.
ENSGALT00000067674; ENSGALP00000051551; ENSGALG00000035445.
ENSGALT00000070686; ENSGALP00000058410; ENSGALG00000037322.
ENSGALT00000079865; ENSGALP00000056887; ENSGALG00000041398.
ENSGALT00000080967; ENSGALP00000049875; ENSGALG00000042491.
GeneIDi100858049.
100858319.
417946.
417950.
427884.
770005.
770142.
KEGGigga:100858049.
gga:100858319.
gga:417946.
gga:417950.
gga:427884.
gga:770005.
gga:770142.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02218 Genomic DNA. Translation: CAA26137.1.
X02218 Genomic DNA. Translation: CAA26140.1.
J00866 Genomic DNA. No translation available.
M74533 Genomic DNA. Translation: AAA73091.1.
M74534 Genomic DNA. Translation: AAA73092.1.
U37575 Genomic DNA. Translation: AAC59999.1.
U37575 Genomic DNA. Translation: AAC60001.1.
PIRiA02640. HSCH4.
JH0507.
RefSeqiNP_001032932.1. NM_001037843.1.
NP_001032934.1. NM_001037845.1.
NP_001268414.1. NM_001281485.1.
XP_001233180.1. XM_001233179.4.
XP_003640418.1. XM_003640370.3.
XP_004937726.1. XM_004937669.2.
XP_425458.2. XM_425458.5.
UniGeneiGga.39882.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EQZX-ray2.50D/H1-103[»]
1HIOX-ray3.10D28-103[»]
1HQ3X-ray2.15D/H1-103[»]
1TZYX-ray1.90D/H1-103[»]
2AROX-ray2.10D/H1-103[»]
2HIOX-ray3.10D1-103[»]
3C9Kelectron microscopy20.00D/H2-103[»]
ProteinModelPortaliP62801.
SMRiP62801.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi679227. 7 interactors.
IntActiP62801. 2 interactors.
STRINGi9031.ENSGALP00000037292.

Proteomic databases

PaxDbiP62801.
PRIDEiP62801.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000046233; ENSGALP00000041526; ENSGALG00000025786.
ENSGALT00000049482; ENSGALP00000054690; ENSGALG00000032272.
ENSGALT00000053533; ENSGALP00000054121; ENSGALG00000032933.
ENSGALT00000066061; ENSGALP00000045681; ENSGALG00000032198.
ENSGALT00000067674; ENSGALP00000051551; ENSGALG00000035445.
ENSGALT00000070686; ENSGALP00000058410; ENSGALG00000037322.
ENSGALT00000079865; ENSGALP00000056887; ENSGALG00000041398.
ENSGALT00000080967; ENSGALP00000049875; ENSGALG00000042491.
GeneIDi100858049.
100858319.
417946.
417950.
427884.
770005.
770142.
KEGGigga:100858049.
gga:100858319.
gga:417946.
gga:417950.
gga:427884.
gga:770005.
gga:770142.

Organism-specific databases

CTDi100858049.
417946.
554313.
770142.
8294.
8359.
8360.

Phylogenomic databases

eggNOGiKOG3467. Eukaryota.
COG2036. LUCA.
GeneTreeiENSGT00760000119019.
HOVERGENiHBG051878.
InParanoidiP62801.
KOiK11254.
OMAiSTHNERI.
OrthoDBiEOG091G0XGD.
PhylomeDBiP62801.

Enzyme and pathway databases

ReactomeiR-GGA-212300. PRC2 methylates histones and DNA.
R-GGA-2299718. Condensation of Prophase Chromosomes.
R-GGA-2559580. Oxidative Stress Induced Senescence.
R-GGA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-GGA-3214815. HDACs deacetylate histones.
R-GGA-3214841. PKMTs methylate histone lysines.
R-GGA-3214842. HDMs demethylate histones.
R-GGA-3214847. HATs acetylate histones.
R-GGA-3214858. RMTs methylate histone arginines.
R-GGA-427359. SIRT1 negatively regulates rRNA Expression.
R-GGA-5250924. B-WICH complex positively regulates rRNA expression.
R-GGA-5578749. Transcriptional regulation by small RNAs.
R-GGA-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-GGA-5693571. Nonhomologous End-Joining (NHEJ).
R-GGA-5693607. Processing of DNA double-strand break ends.
R-GGA-606279. Deposition of new CENPA-containing nucleosomes at the centromere.
R-GGA-69473. G2/M DNA damage checkpoint.
R-GGA-73728. RNA Polymerase I Promoter Opening.
R-GGA-73777. RNA Polymerase I Chain Elongation.

Miscellaneous databases

EvolutionaryTraceiP62801.
PROiP62801.

Gene expression databases

BgeeiENSGALG00000025786.

Family and domain databases

CDDicd00076. H4. 1 hit.
Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR001951. Histone_H4.
IPR019809. Histone_H4_CS.
IPR004823. TAF_TATA-bd.
[Graphical view]
PRINTSiPR00623. HISTONEH4.
SMARTiSM00417. H4. 1 hit.
SM00803. TAF. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00047. HISTONE_H4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiH4_CHICK
AccessioniPrimary (citable) accession number: P62801
Secondary accession number(s): P02304, P02305
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 121 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.