H1-4
entrez
50709
canonical
uniprot
P43274
canonical
ensembl
ENSMUSG00000051627
resolver
ensp
ENSMUSP00000057308
resolver
enst
ENSMUST00000062045
resolver
genesymbol
H1-4
resolver
genesymbol_syn
H1f4
resolver
genesymbol_syn
Hist1h1e
resolver
uniprot
Q5EBH3
resolver
uniprot_entry
H14_MOUSE
resolver
uniprot_sec
Q5EBH3
resolver
amino_acid_sequence
MSETAPAAPAAPAPAEKTPVKKKARKAAGGAKRKTSGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEAKPKAKRAGAAKAKKPAGAAKKPKKAAGTATAKKSTKKTPKKAKKPAAAAGAKKAKSPKKAKATKAKKAPKSPAKAKTVKPKAAKPKTSKPKAAKPKKTAAKKK
uniprot
proteins
function
FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber (PubMed:12808097, PubMed:16377562). Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers and promote formation of the H3K27me3 mark by the PRC2/EED-EZH2 complex (PubMed:12808097, PubMed:16377562). Ability to associate with nucleosomes and compact chromatin depends on linker DNA length and trajectory (By similarity). Also acts as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (PubMed:12808097, PubMed:16377562). {ECO:0000250|UniProtKB:P10412, ECO:0000269|PubMed:12808097, ECO:0000269|PubMed:16377562}.
uniprot
proteins
mass_dalton
21977
uniprot
proteins
post_translational_modification
PTM: Deamidation of Asn-76 and Asn-77 by CTPS1 in response to DNA damage promotes subsequent acetylation of histone H1 at Lys-75 (H1K75ac). {ECO:0000250|UniProtKB:P10412}.; PTM: Acetylated at Lys-26. Deacetylated at Lys-26 by SIRT1. Acetylated at Lys-34 (H1.3K34ac) by KAT2A; H1.3K34ac is enriched at promoters of active genes and stimulates transcription by increasing H1 mobility and recruiting TAF1. Acetylated at Lys-75 (H1K75ac) by EP300 following deamidation of Asn-76 and Asn-77 by CTPS1 in response to DNA damage, thereby increasing chromatin accessibility to facilitate the recruitment of DNA repair proteins (By similarity). {ECO:0000250|UniProtKB:P10412}.; PTM: 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. {ECO:0000269|PubMed:24463520}.; PTM: ADP-ribosylated on Ser-55, Ser-113 and Ser-150 in response to DNA damage. {ECO:0000250|UniProtKB:P10412}.; PTM: Mono- and dimethylated at Lys-26 by EHMT2/G9a (H1.4K26me1 and H1.4K26me2, respectively). H1.4K26me1, H1.4K26me2 and H1.4K26me3 are demethylated by KDM4A. H1.4K26me is recognized by histone reader HP1 (CBX1, CBX3 and/or CBX5). {ECO:0000250|UniProtKB:P10412}.; PTM: H1 histones are progressively phosphorylated during the cell cycle, becoming maximally phosphorylated during late G2 phase and M phase, and being dephosphorylated sharply thereafter. Phosphorylation at Ser-36 by PKA during mitosis promotes dissociation from mitotic chromosome. Phosphorylation at Ser-187 by CDK9 is associated with transcription activation. Phosphorylation at Thr-146 highly increases during mitosis compared to interphase. {ECO:0000250|UniProtKB:P43275}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000250|UniProtKB:P43277}.
uniprot
proteins
protein_family
Histone H1/H5 family
uniprot
proteins
pubmed
12808097
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16377562
uniprot
proteins
pubmed
16452087
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
24463520
uniprot
proteins
pubmed
8190634
uniprot
proteins
pubmed
8416974
uniprot
proteins
pubmed
9655912
uniprot
proteins
sequence_length
219
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10412}. Chromosome {ECO:0000250|UniProtKB:P10412}. Note=Mainly localizes in heterochromatin. Distributed throughout the nucleus; displays a punctuate staining pattern in the nucleus. {ECO:0000250|UniProtKB:P10412}.
uniprot
proteins