H1-3
entrez
3007
canonical
uniprot
P16402
canonical
ensembl
ENSG00000124575
resolver
ensp
ENSP00000244534
resolver
enst
ENST00000244534
resolver
genesymbol
H1-3
resolver
genesymbol_syn
H1F3
resolver
genesymbol_syn
HIST1H1D
resolver
hgnc
HGNC:4717
resolver
uniprot
B2R751
resolver
uniprot
Q2M2I2
resolver
uniprot_entry
H13_HUMAN
resolver
uniprot_sec
B2R751
resolver
uniprot_sec
Q2M2I2
resolver
amino_acid_sequence
MSETAPLAPTIPAPAEKTPVKKKAKKAGATAGKRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEGKPKAKKAGAAKPRKPAGAAKKPKKVAGAATPKKSIKKTPKKVKKPATAAGTKKVAKSAKKVKTPQPKKAAKSPAKAKAPKPKAAKPKSGKPKVTKAKKAAPKKK
uniprot
proteins
function
FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber (PubMed:37922872). 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:40516528). 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 (PubMed:37922872). Also acts as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250|UniProtKB:P43277, ECO:0000269|PubMed:37922872, ECO:0000269|PubMed:40516528}.
uniprot
proteins
mass_dalton
22350
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: 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:0000250|UniProtKB:P43277}.
uniprot
proteins
protein_family
Histone H1/H5 family
uniprot
proteins
pubmed
10997781
uniprot
proteins
pubmed
11746507
uniprot
proteins
pubmed
12408966
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15911621
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
1916825
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
2613692
uniprot
proteins
pubmed
27105115
uniprot
proteins
pubmed
30154464
uniprot
proteins
pubmed
34545082
uniprot
proteins
pubmed
34961760
uniprot
proteins
pubmed
37922872
uniprot
proteins
pubmed
38530350
uniprot
proteins
pubmed
40240600
uniprot
proteins
pubmed
40516528
uniprot
proteins
pubmed
40516529
uniprot
proteins
pubmed
8003976
uniprot
proteins
sequence_length
221
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:38530350}. Chromosome {ECO:0000269|PubMed:10997781, ECO:0000269|PubMed:15911621, ECO:0000269|PubMed:38530350}. Note=Enriched at the nuclear periphery and colocalizes with compacted DNA (heterochromatin) (PubMed:38530350). According to PubMed:15911621 more commonly found in euchromatin. According to PubMed:10997781 is associated with inactive chromatin. {ECO:0000269|PubMed:38530350}.
uniprot
proteins