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P62803

- H4_BOVIN

UniProt

P62803 - H4_BOVIN

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Protein

Histone H4

Gene
N/A
Organism
Bos taurus (Bovine)
Status
Reviewed - 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

GO - Biological processi

  1. negative regulation of megakaryocyte differentiation Source: Ensembl
  2. nucleosome assembly Source: InterPro
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_203215. Senescence-Associated Secretory Phenotype (SASP).
REACT_206540. Amyloids.
REACT_207393. PRC2 methylates histones and DNA.
REACT_207666. Condensation of Prophase Chromosomes.
REACT_209769. Meiotic recombination.
REACT_211829. Meiotic synapsis.
REACT_211838. RNA Polymerase I Promoter Opening.
REACT_214253. NoRC negatively regulates rRNA expression.
REACT_214732. DNA Damage/Telomere Stress Induced Senescence.
REACT_217942. SIRT1 negatively regulates rRNA Expression.
REACT_217981. Deposition of new CENPA-containing nucleosomes at the centromere.
REACT_219482. HATs acetylate histones.
REACT_220535. Packaging Of Telomere Ends.
REACT_222355. formation of the beta-catenin:TCF transactivating complex.
REACT_225163. RNA Polymerase I Chain Elongation.
REACT_225657. Oxidative Stress Induced Senescence.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H4
Alternative name(s):
H4.1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 23, UP000009136: Chromosome 5

Subcellular locationi

GO - Cellular componenti

  1. actin cytoskeleton Source: Ensembl
  2. nucleolus Source: Ensembl
  3. nucleoplasm Source: Reactome
  4. 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 – 21Phosphoserine By similarity
Modified residuei4 – 41Asymmetric dimethylarginine; by PRMT1; alternate By similarity
Modified residuei4 – 41Citrulline; alternate By similarity
Modified residuei4 – 41Omega-N-methylarginine; by PRMT1; alternate By similarity
Modified residuei4 – 41Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate By similarity
Modified residuei6 – 61N6-acetyllysine; alternate By similarity
Modified residuei6 – 61N6-crotonyllysine; alternate By similarity
Modified residuei9 – 91N6-acetyllysine; alternate By similarity
Modified residuei9 – 91N6-crotonyllysine; alternate By similarity
Modified residuei13 – 131N6-acetyllysine; alternate By similarity
Modified residuei13 – 131N6-crotonyllysine; alternate By similarity
Modified residuei17 – 171N6-acetyllysine; alternate1 Publication
Modified residuei17 – 171N6-crotonyllysine; alternate By similarity
Modified residuei21 – 211N6,N6,N6-trimethyllysine; alternate By similarity
Modified residuei21 – 211N6,N6-dimethyllysine; alternate1 Publication
Modified residuei21 – 211N6-methyllysine; alternate1 Publication
Modified residuei32 – 321N6-acetyllysine By similarity
Modified residuei48 – 481Phosphoserine; by PAK2 By similarity
Modified residuei52 – 521Phosphotyrosine By similarity
Modified residuei89 – 891Phosphotyrosine By similarity
Modified residuei92 – 921N6-acetyllysine; alternate By similarity
Modified residuei92 – 921N6-succinyllysine; alternate By similarity
Cross-linki92 – 92Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By 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.1 Publication
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.1 Publication
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.1 Publication
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.
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.
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.

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. 4 interactions.
DIPiDIP-44668N.
IntActiP62803. 1 interaction.
STRINGi9913.ENSBTAP00000047761.

Structurei

3D structure databases

ProteinModelPortaliP62803.
SMRiP62803. Positions 21-102.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H4 family.

Phylogenomic databases

eggNOGiCOG2036.
GeneTreeiENSGT00750000117310.
ENSGT00750000117311.
HOGENOMiHOG000234654.
HOVERGENiHBG051878.
InParanoidiP62803.
KOiK11254.
OMAiYEEVRVV.
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

MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL    50
IYEETRGVLK VFLENVIRDA VTYTEHAKRK TVTAMDVVYA LKRQGRTLYG 100
FGG 103
Length:103
Mass (Da):11,367
Last modified:January 23, 2007 - v2
Checksum:iA9E5DFD3F8B97598
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551T → A in AAI42000. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_002684630.2.
XP_002686104.1. XM_002686058.2.
XP_002697516.1. XM_002697470.2.
XP_002697555.1. XM_002697509.2.
XP_002697556.1. XM_002697510.2.
XP_003581994.1. XM_003581946.2.
XP_005196696.1. XM_005196639.1.
XP_005196707.1. XM_005196650.1.
XP_005223784.1. XM_005223727.1.
XP_005223853.1. XM_005223796.1.
XP_005223857.1. XM_005223800.1.
XP_597168.2. XM_597168.3.
XP_605163.2. XM_605163.3.
XP_605779.2. XM_605779.3.
XP_874074.1. XM_868981.4.
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.
516742.
517138.
518961.
526789.
527388.
527645.
528329.
529647.
530773.
617875.
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:
EMBL
GenBank
DDBJ
Links Updated
AF001288 mRNA. Translation: AAC39176.1 .
BC114196 mRNA. Translation: AAI14197.1 .
BC141999 mRNA. Translation: AAI42000.1 .
BC142359 mRNA. Translation: AAI42360.1 .
PIRi A92050. HSBO4.
RefSeqi NP_001093194.1. NM_001099724.2.
NP_001139343.1. NM_001145871.2.
NP_776305.1. NM_173880.2.
XP_002684676.1. XM_002684630.2.
XP_002686104.1. XM_002686058.2.
XP_002697516.1. XM_002697470.2.
XP_002697555.1. XM_002697509.2.
XP_002697556.1. XM_002697510.2.
XP_003581994.1. XM_003581946.2.
XP_005196696.1. XM_005196639.1.
XP_005196707.1. XM_005196650.1.
XP_005223784.1. XM_005223727.1.
XP_005223853.1. XM_005223796.1.
XP_005223857.1. XM_005223800.1.
XP_597168.2. XM_597168.3.
XP_605163.2. XM_605163.3.
XP_605779.2. XM_605779.3.
XP_874074.1. XM_868981.4.
UniGenei Bt.104550.
Bt.113.
Bt.58502.
Bt.61355.

3D structure databases

ProteinModelPortali P62803.
SMRi P62803. Positions 21-102.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 158101. 4 interactions.
DIPi DIP-44668N.
IntActi P62803. 1 interaction.
STRINGi 9913.ENSBTAP00000047761.

Proteomic databases

PaxDbi P62803.
PRIDEi P62803.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000029245 ; 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 .
GeneIDi 280691.
516742.
517138.
518961.
526789.
527388.
527645.
528329.
529647.
530773.
617875.
KEGGi bta:280691.
bta:516742.
bta:517138.
bta:518961.
bta:526789.
bta:527388.
bta:527645.
bta:528329.
bta:529647.
bta:530773.
bta:617875.

Organism-specific databases

CTDi 373325.

Phylogenomic databases

eggNOGi COG2036.
GeneTreei ENSGT00750000117310.
ENSGT00750000117311.
HOGENOMi HOG000234654.
HOVERGENi HBG051878.
InParanoidi P62803.
KOi K11254.
OMAi YEEVRVV.
OrthoDBi EOG77T174.

Enzyme and pathway databases

Reactomei REACT_203215. Senescence-Associated Secretory Phenotype (SASP).
REACT_206540. Amyloids.
REACT_207393. PRC2 methylates histones and DNA.
REACT_207666. Condensation of Prophase Chromosomes.
REACT_209769. Meiotic recombination.
REACT_211829. Meiotic synapsis.
REACT_211838. RNA Polymerase I Promoter Opening.
REACT_214253. NoRC negatively regulates rRNA expression.
REACT_214732. DNA Damage/Telomere Stress Induced Senescence.
REACT_217942. SIRT1 negatively regulates rRNA Expression.
REACT_217981. Deposition of new CENPA-containing nucleosomes at the centromere.
REACT_219482. HATs acetylate histones.
REACT_220535. Packaging Of Telomere Ends.
REACT_222355. formation of the beta-catenin:TCF transactivating complex.
REACT_225163. RNA Polymerase I Chain Elongation.
REACT_225657. Oxidative Stress Induced Senescence.

Miscellaneous databases

NextBioi 20804878.

Family and domain databases

Gene3Di 1.10.20.10. 1 hit.
InterProi IPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR001951. Histone_H4.
IPR019809. Histone_H4_CS.
[Graphical view ]
Pfami PF00125. Histone. 1 hit.
[Graphical view ]
PRINTSi PR00623. HISTONEH4.
SMARTi SM00417. H4. 1 hit.
[Graphical view ]
SUPFAMi SSF47113. SSF47113. 1 hit.
PROSITEi PS00047. HISTONE_H4. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (H4-V.1).
    Tissue: Adrenal medulla.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (JUN-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(1970) [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(1969) [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(1969) [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: September 3, 2014
This is version 101 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

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