P43274 · H14_MOUSE
- ProteinHistone H1.4
- GeneH1-4
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids219 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | euchromatin | |
Cellular Component | heterochromatin | |
Cellular Component | nucleosome | |
Cellular Component | nucleus | |
Molecular Function | ADP binding | |
Molecular Function | AMP binding | |
Molecular Function | ATP binding | |
Molecular Function | calcium ion binding | |
Molecular Function | dATP binding | |
Molecular Function | DNA binding | |
Molecular Function | double-stranded DNA binding | |
Molecular Function | GTP binding | |
Molecular Function | histone deacetylase binding | |
Molecular Function | nucleosomal DNA binding | |
Molecular Function | nucleotide binding | |
Molecular Function | structural constituent of chromatin | |
Biological Process | chromatin organization | |
Biological Process | chromosome condensation | |
Biological Process | negative regulation of DNA recombination | |
Biological Process | negative regulation of transcription by RNA polymerase II | |
Biological Process | nucleosome assembly | |
Biological Process | regulation of transcription by RNA polymerase II |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameHistone H1.4
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP43274
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Mainly localizes in heterochromatin. Dysplays a punctuate staining pattern in the nucleus.
Keywords
- Cellular component
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.
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylserine | ||||
Sequence: S | ||||||
Modified residue | 2 | Phosphoserine | ||||
Sequence: S | ||||||
Chain | PRO_0000195917 | 2-219 | Histone H1.4 | |||
Sequence: SETAPAAPAAPAPAEKTPVKKKARKAAGGAKRKTSGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEAKPKAKRAGAAKAKKPAGAAKKPKKAAGTATAKKSTKKTPKKAKKPAAAAGAKKAKSPKKAKATKAKKAPKSPAKAKTVKPKAAKPKTSKPKAAKPKKTAAKKK | ||||||
Modified residue | 17 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 18 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 26 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 26 | N6-methyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 34 | N6-(beta-hydroxybutyryl)lysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 34 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 36 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 52 | N6-(beta-hydroxybutyryl)lysine | ||||
Sequence: K | ||||||
Modified residue | 54 | Citrulline | ||||
Sequence: R | ||||||
Modified residue | 64 | N6-(beta-hydroxybutyryl)lysine | ||||
Sequence: K | ||||||
Modified residue | 85 | N6-(beta-hydroxybutyryl)lysine | ||||
Sequence: K | ||||||
Modified residue | 90 | N6-(beta-hydroxybutyryl)lysine | ||||
Sequence: K | ||||||
Modified residue | 106 | N6-(beta-hydroxybutyryl)lysine | ||||
Sequence: K | ||||||
Modified residue | 146 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 150 | ADP-ribosylserine | ||||
Sequence: S | ||||||
Modified residue | 187 | Phosphoserine | ||||
Sequence: S |
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
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-41 | Disordered | ||||
Sequence: MSETAPAAPAAPAPAEKTPVKKKARKAAGGAKRKTSGPPVS | ||||||
Domain | 36-109 | H15 | ||||
Sequence: SGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNK | ||||||
Region | 92-219 | Disordered | ||||
Sequence: TLVQTKGTGASGSFKLNKKAASGEAKPKAKRAGAAKAKKPAGAAKKPKKAAGTATAKKSTKKTPKKAKKPAAAAGAKKAKSPKKAKATKAKKAPKSPAKAKTVKPKAAKPKTSKPKAAKPKKTAAKKK | ||||||
Compositional bias | 150-219 | Basic residues | ||||
Sequence: STKKTPKKAKKPAAAAGAKKAKSPKKAKATKAKKAPKSPAKAKTVKPKAAKPKTSKPKAAKPKKTAAKKK |
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 statusComplete
- Length219
- Mass (Da)21,977
- Last updated2007-01-23 v2
- Checksum9463467F699F3625
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 150-219 | Basic residues | ||||
Sequence: STKKTPKKAKKPAAAAGAKKAKSPKKAKATKAKKAPKSPAKAKTVKPKAAKPKTSKPKAAKPKKTAAKKK |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |