H1-2
entrez
50708
canonical
uniprot
P15864
canonical
ensembl
ENSMUSG00000036181
resolver
ensp
ENSMUSP00000045816
resolver
enst
ENSMUST00000040914
resolver
genesymbol
H1-2
resolver
genesymbol
H1f2
resolver
genesymbol_syn
H1f2
resolver
genesymbol_syn
Hist1h1c
resolver
uniprot
Q5SZA3
resolver
uniprot_entry
H12_MOUSE
resolver
uniprot_entry
Q5SZA3_MOUSE
resolver
amino_acid_sequence
MSEAAPAAPAAAPPAEKAPAKKKAAKKPAGVRRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGILVQTKGTGASGSFKLNKKAASGEAKPQAKKAGAAKAKKPAGAAKKPKKATGAATPKKAAKKTPKKAKKPAAAAVTKKVAKSPKKAKVTKPKKVKSASKAVKPKAAKPKVAKAKKVAAKKK
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). Histone H1-2 is required for the condensation of nucleosome chains into higher-order structured fibers (PubMed:12808097, PubMed:16377562). Histone H1-2 also acts as a histone reader: specifically recognizes and binds histone H3 trimethylated at 'lys-27' (H3K27me3) (By similarity). Histones H1 also promote formation of the H3K27me3 mark by the PRC2/EED-EZH2 complex, possibly by facilitating restoration of H3K27me3 post-replication (By similarity). Together with histone H1-3, histone H1-2 acts as a regulator of splicing, most specifically exon skipping and intron retention events: histone H1-2 has a high affinity for exons 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 (By similarity). {ECO:0000250|UniProtKB:P16403, ECO:0000269|PubMed:12808097, ECO:0000269|PubMed:16377562}.
uniprot
proteins
mass_dalton
21267
uniprot
proteins
mutagenesis
MUTAGEN 54; /note="R->A: Mimics the charge change that accompanies citrullination, resulting in impaired nucleosome-binding."; /evidence="ECO:0000269|PubMed:24463520"; MUTAGEN 54; /note="R->K: Retains the positive charge, resulting in slightly decreased nucleosome-binding."; /evidence="ECO:0000269|PubMed:24463520
uniprot
proteins
post_translational_modification
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}.; PTM: 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. {ECO:0000269|PubMed:21925322}.; 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-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. {ECO:0000250|UniProtKB:P10412}.; PTM: ADP-ribosylated on Ser-187 in response to DNA damage. {ECO:0000250|UniProtKB:P16403}.; 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: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000250|UniProtKB:P43277}.
uniprot
proteins
protein_family
Histone H1/H5 family
uniprot
proteins
pubmed
12408966
uniprot
proteins
pubmed
12808097
uniprot
proteins
pubmed
16377562
uniprot
proteins
pubmed
21925322
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
24463520
uniprot
proteins
pubmed
24681537
uniprot
proteins
pubmed
2780558
uniprot
proteins
pubmed
2824517
uniprot
proteins
pubmed
8639656
uniprot
proteins
pubmed
9655912
uniprot
proteins
sequence_length
212
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P16403}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P16403}. Chromosome {ECO:0000250|UniProtKB:P16403}. Note=Enriched at the nuclear periphery and colocalizes with compacted DNA (heterochromatin). Enriched withi lamina-associated domains. {ECO:0000250|UniProtKB:P16403}.
uniprot
proteins