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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)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi17 – 215

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

DNA-binding

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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 103102Histone H4PRO_0000158296Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
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-acetyllysineBy similarity
Modified residuei9 – 91N6-acetyllysineBy similarity
Modified residuei13 – 131N6-acetyllysineBy similarity
Modified residuei17 – 171N6-acetyllysineBy similarity
Modified residuei21 – 211N6,N6,N6-trimethyllysine; alternateBy similarity
Modified residuei21 – 211N6,N6-dimethyllysine; alternateBy similarity
Modified residuei21 – 211N6-methylated lysineBy similarity
Modified residuei21 – 211N6-methyllysine; alternateBy similarity
Modified residuei32 – 321N6-acetyllysineBy similarity
Modified residuei48 – 481Phosphoserine; by PAK2By similarity
Modified residuei52 – 521PhosphotyrosineBy similarity
Modified residuei60 – 601N6-acetyllysineBy similarity
Modified residuei80 – 801N6-acetyllysineBy similarity
Modified residuei89 – 891PhosphotyrosineBy similarity
Modified residuei92 – 921N6-acetyllysine; 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. 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

ExpressionAtlasiP62801. baseline and differential.

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 interactions.
IntActiP62801. 2 interactions.
STRINGi9031.ENSGALP00000037292.

Structurei

Secondary structure

1
103
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi26 – 294Combined sources
Helixi32 – 4110Combined sources
Helixi51 – 7626Combined sources
Beta strandi80 – 823Combined sources
Helixi84 – 9310Combined sources
Beta strandi97 – 1004Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 21-102.
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.
PhylomeDBiP62801.

Family and domain databases

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.
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
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. Positions 21-102.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi679227. 7 interactions.
IntActiP62801. 2 interactions.
STRINGi9031.ENSGALP00000037292.

Proteomic databases

PaxDbiP62801.
PRIDEiP62801.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000046233; ENSGALP00000041526; ENSGALG00000025786.
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.
PhylomeDBiP62801.

Miscellaneous databases

EvolutionaryTraceiP62801.
PROiP62801.

Gene expression databases

ExpressionAtlasiP62801. baseline and differential.

Family and domain databases

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...

Publicationsi

  1. "Inverted duplication of histone genes in chicken and disposition of regulatory sequences."
    Wang S.W., Robins A.J., D'Andrea R., Wells J.R.E.
    Nucleic Acids Res. 13:1369-1387(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Genomic organization, DNA sequence, and expression of chicken embryonic histone genes."
    Sugarman B.J., Dodgson J.B., Engel J.D.
    J. Biol. Chem. 258:9005-9016(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Nucleotide sequences of two members of the chicken H4 histone-encoding gene family."
    Nakayama T., Takechi S., Ohshige T., Kondo K., Yamamoto K.
    Gene 108:311-312(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (H4-III AND H4-IV).
  4. "Organization of the chicken histone genes in a major gene cluster and generation of an almost complete set of the core histone protein sequences."
    Takami Y., Higashio M., Fukuoka T., Takechi S., Nakayama T.
    DNA Res. 3:95-99(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (H4-VI AND H4-VII).
    Strain: White leghorn.
    Tissue: Liver.
  5. "The nucleosomal core histone octamer at 3.1 A resolution: a tripartite protein assembly and a left-handed superhelix."
    Arents G., Burlingame R.W., Wang B.-C., Love W.E., Moudrianakis E.N.
    Proc. Natl. Acad. Sci. U.S.A. 88:10148-10152(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
  6. "Asymmetries in the nucleosome core particle at 2.5 A resolution."
    Harp J.M., Hanson B.L., Timm D.E., Bunick G.J.
    Acta Crystallogr. D 56:1513-1534(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

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: July 6, 2016
This is version 117 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.