P43274 · H14_MOUSE

  • Protein
    Histone H1.4
  • Gene
    H1-4
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componenteuchromatin
Cellular Componentheterochromatin
Cellular Componentnucleosome
Cellular Componentnucleus
Molecular FunctionADP binding
Molecular FunctionAMP binding
Molecular FunctionATP binding
Molecular Functioncalcium ion binding
Molecular FunctiondATP binding
Molecular FunctionDNA binding
Molecular Functiondouble-stranded DNA binding
Molecular FunctionGTP binding
Molecular Functionhistone deacetylase binding
Molecular Functionnucleosomal DNA binding
Molecular Functionnucleotide binding
Molecular Functionstructural constituent of chromatin
Biological Processchromatin organization
Biological Processchromosome condensation
Biological Processnegative regulation of DNA recombination
Biological Processnegative regulation of transcription by RNA polymerase II
Biological Processnucleosome assembly
Biological Processregulation of transcription by RNA polymerase II

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Histone H1.4
  • Alternative names
    • H1 VAR.2
    • H1e

Gene names

    • Name
      H1-4
    • Synonyms
      H1f4
      , Hist1h1e

Organism names

  • Taxonomic identifier
  • Strain
    • BALB/cJ
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    P43274
  • Secondary accessions
    • Q5EBH3

Proteomes

Organism-specific databases

Subcellular Location

Note: Mainly localizes in heterochromatin. Dysplays a punctuate staining pattern in the nucleus.

Keywords

Phenotypes & Variants

Disruption phenotype

Triple-deficient mice (H1-2, H1-3 and H1-4) die by midgestation with a broad range of defects. These embryos have about 50% of the normal ratio of H1 to nucleosomes. This proves at least that a correct stoichiometry of linker histone deposition on chromatin is essential.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 4 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylserine
Modified residue2Phosphoserine
ChainPRO_00001959172-219Histone H1.4
Modified residue17N6-acetyllysine
Modified residue18Phosphothreonine
Modified residue26N6-acetyllysine; alternate
Modified residue26N6-methyllysine; alternate
Modified residue34N6-(beta-hydroxybutyryl)lysine; alternate
Modified residue34N6-succinyllysine; alternate
Modified residue36Phosphoserine
Modified residue52N6-(beta-hydroxybutyryl)lysine
Modified residue54Citrulline
Modified residue64N6-(beta-hydroxybutyryl)lysine
Modified residue85N6-(beta-hydroxybutyryl)lysine
Modified residue90N6-(beta-hydroxybutyryl)lysine
Modified residue106N6-(beta-hydroxybutyryl)lysine
Modified residue146Phosphothreonine
Modified residue150ADP-ribosylserine
Modified residue187Phosphoserine

Post-translational modification

Citrullination at Arg-54 (H1R54ci) by PADI4 takes place within the DNA-binding site of H1 and results in its displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance.
ADP-ribosylated on Ser-55, Ser-113 and Ser-150 in response to DNA damage.
H1 histones are progressively phosphorylated during the cell cycle, becoming maximally phosphorylated during late G2 phase and M phase, and being dephosphorylated sharply thereafter.
Acetylated at Lys-26. Deacetylated at Lys-26 by SIRT1.
Hydroxybutyrylation of histones is induced by starvation.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, domain, compositional bias.

TypeIDPosition(s)Description
Region1-41Disordered
Domain36-109H15
Region92-219Disordered
Compositional bias150-219Basic residues

Domain

The C-terminal domain is required for high-affinity binding to chromatin.

Sequence similarities

Belongs to the histone H1/H5 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    219
  • Mass (Da)
    21,977
  • Last updated
    2007-01-23 v2
  • Checksum
    9463467F699F3625
MSETAPAAPAAPAPAEKTPVKKKARKAAGGAKRKTSGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEAKPKAKRAGAAKAKKPAGAAKKPKKAAGTATAKKSTKKTPKKAKKPAAAAGAKKAKSPKKAKATKAKKAPKSPAKAKTVKPKAAKPKTSKPKAAKPKKTAAKKK

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias150-219Basic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
L26163
EMBL· GenBank· DDBJ
AAA37760.1
EMBL· GenBank· DDBJ
Genomic DNA
L04141
EMBL· GenBank· DDBJ
AAA37814.1
EMBL· GenBank· DDBJ
Genomic DNA
Y12292
EMBL· GenBank· DDBJ
CAA72971.1
EMBL· GenBank· DDBJ
Genomic DNA
BC089600
EMBL· GenBank· DDBJ
AAH89600.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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