H1-1
entrez
3024
canonical
uniprot
Q02539
canonical
ensembl
ENSG00000124610
resolver
ensp
ENSP00000244573
resolver
enst
ENST00000244573
resolver
genesymbol
H1-1
resolver
genesymbol_syn
H1F1
resolver
genesymbol_syn
HIST1H1A
resolver
hgnc
HGNC:4715
resolver
uniprot
Q3MJ34
resolver
uniprot_entry
H11_HUMAN
resolver
uniprot_sec
Q3MJ34
resolver
amino_acid_sequence
MSETVPPAPAASAAPEKPLAGKKAKKPAKAAAASKKKPAGPSVSELIVQAASSSKERGGVSLAALKKALAAAGYDVEKNNSRIKLGIKSLVSKGTLVQTKGTGASGSFKLNKKASSVETKPGASKVATKTKATGASKKLKKATGASKKSVKTPKKAKKPAATRKSSKNPKKPKTVKPKKVAKSPAKAKAVKPKAAKARVTKPKTAKPKKAAPKKK
uniprot
proteins
function
FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber (PubMed:11130728). 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:11130728). Also acts as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250|UniProtKB:P10412, ECO:0000269|PubMed:11130728}.
uniprot
proteins
mass_dalton
21842
uniprot
proteins
mutagenesis
MUTAGEN 152; /note="T->E: Significant destabilization of binding to chromatin."; /evidence="ECO:0000269|PubMed:14985337"; MUTAGEN 183; /note="S->E: Significant destabilization of binding to chromatin."; /evidence="ECO:0000269|PubMed:14985337
uniprot
proteins
post_translational_modification
PTM: Deamidation of Asn-79 and Asn-80 by CTPS1 in response to DNA damage promotes subsequent acetylation of histone H1 at Lys-78 (H1K75ac). {ECO:0000250|UniProtKB:P10412}.; PTM: Acetylated at Lys-78 (H1K75ac) by EP300 following deamidation of Asn-79 and Asn-80 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: Citrullination at Arg-57 (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:0000250|UniProtKB:P43275}.
uniprot
proteins
protein_family
Histone H1/H5 family
uniprot
proteins
pubmed
11130728
uniprot
proteins
pubmed
12408966
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14985337
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15911621
uniprot
proteins
pubmed
19882353
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
2759094
uniprot
proteins
pubmed
30154464
uniprot
proteins
pubmed
34545082
uniprot
proteins
pubmed
34961760
uniprot
proteins
pubmed
8003976
uniprot
proteins
sequence_length
215
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00837, ECO:0000269|PubMed:15911621}. Chromosome {ECO:0000255|PROSITE-ProRule:PRU00837, ECO:0000269|PubMed:14985337, ECO:0000269|PubMed:15911621, ECO:0000269|PubMed:19882353}. Note=Mainly localizes in euchromatin. {ECO:0000269|PubMed:15911621}.
uniprot
proteins