H1-3
entrez
14957
canonical
uniprot
P43277
canonical
ensembl
ENSMUSG00000052565
resolver
ensp
ENSMUSP00000044395
resolver
enst
ENSMUST00000045301
resolver
genesymbol
H1-3
resolver
genesymbol
H1f3
resolver
genesymbol_syn
H1f3
resolver
genesymbol_syn
Hist1h1d
resolver
uniprot
Q149Z9
resolver
uniprot
Q8C6M4
resolver
uniprot_entry
H13_MOUSE
resolver
uniprot_entry
Q149Z9_MOUSE
resolver
uniprot_sec
Q8C6M4
resolver
amino_acid_sequence
MSETAPAAPAAPAPVEKTPVKKKAKKTGAAAGKRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEAKPKAKKAGAAKAKKPAGAAKKPKKATGAATPKKTAKKTPKKAKKPAAAAGAKKVSKSPKKVKAAKPKKAAKSPAKAKAPKAKASKPKASKPKATKAKKAAPRKK
uniprot
proteins
function
FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber (PubMed:12808097). 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). Together with histone H1-3, histone H1-3 acts as a regulator of splicing, most specifically exon skipping and intron retention events: histone H1-3 has a high affinity for introns and regulates splicing by affecting RNA polymerase II (RNAPII) elongation (By similarity). Also acts as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (PubMed:12808097). {ECO:0000250|UniProtKB:P16402, ECO:0000269|PubMed:12808097}.
uniprot
proteins
mass_dalton
22100
uniprot
proteins
post_translational_modification
PTM: Deamidation of Asn-77 and Asn-78 by CTPS1 in response to DNA damage promotes subsequent acetylation of histone H1 at Lys-76 (H1K75ac). {ECO:0000250|UniProtKB:P10412}.; PTM: Acetylated at Lys-76 (H1K75ac) by EP300 following deamidation of Asn-77 and Asn-78 by CTPS1 in response to DNA damage, thereby increasing chromatin accessibility to facilitate the recruitment of DNA repair proteins. {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. {ECO:0000250|UniProtKB:P43275}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}.; PTM: Citrullination at Arg-55 (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}.
uniprot
proteins
protein_family
Histone H1/H5 family
uniprot
proteins
pubmed
12408966
uniprot
proteins
pubmed
12808097
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
24463520
uniprot
proteins
pubmed
27105115
uniprot
proteins
pubmed
8589518
uniprot
proteins
pubmed
8639656
uniprot
proteins
pubmed
8858344
uniprot
proteins
sequence_length
221
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P16402}. Chromosome {ECO:0000250|UniProtKB:P16402}. Note=Enriched at the nuclear periphery and colocalizes with compacted DNA (heterochromatin). {ECO:0000250|UniProtKB:P16402}.
uniprot
proteins