H1-4
entrez
3008
canonical
uniprot
P10412
canonical
ensembl
ENSG00000168298
resolver
ensp
ENSP00000307705
resolver
enst
ENST00000304218
resolver
genesymbol
H1-4
resolver
genesymbol
HIST1H1E
resolver
genesymbol_syn
H1F4
resolver
genesymbol_syn
HIST1H1E
resolver
hgnc
HGNC:4718
resolver
uniprot
A3R0T8
resolver
uniprot
Q4VB25
resolver
uniprot_entry
A3R0T8_HUMAN
resolver
uniprot_entry
H14_HUMAN
resolver
uniprot_sec
Q4VB25
resolver
amino_acid_sequence
MSETAPAAPAAPAPAEKTPVKKKARKSAGAAKRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEAKPKAKKAGAAKAKKPAGAAKKPKKATGAATPKKSAKKTPKKAKKPAAAAGAKKAKSPKKAKAAKPKKAPKSPAKAKAVKPKAAKPKTAKPKAAKPKKAAAKKK
uniprot
proteins
disease_involvement
DISEASE: Rahman syndrome (RMNS) [MIM:617537]: An autosomal dominant syndrome characterized by intellectual disability and overgrowth manifesting as increased birth length, height, weight, and/or head circumference. {ECO:0000269|PubMed:28475857, ECO:0000269|PubMed:34788807}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber (PubMed:35581345, PubMed:40240600). 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:35581345, PubMed:40240600, PubMed:40516528). Ability to associate with nucleosomes and compact chromatin depends on linker DNA length and trajectory (PubMed:35581345). Also acts as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (PubMed:40240600). {ECO:0000269|PubMed:35581345, ECO:0000269|PubMed:40240600, ECO:0000269|PubMed:40516528}.
uniprot
proteins
mass_dalton
21865
uniprot
proteins
mutagenesis
MUTAGEN 27; /note="S->A: Abolished phosphorylation by AURKB."; /evidence="ECO:0000269|PubMed:21511733"; MUTAGEN 75; /note="K->Q: Mimics acetylation; increased chromatin accessibility."; /evidence="ECO:0000269|PubMed:40240600"; MUTAGEN 75; /note="K->R: Abolished acetylation by EP300 in response to DNA damage."; /evidence="ECO:0000269|PubMed:40240600"; MUTAGEN 76..77; /note="NN->DD: Promotes acetylation at K-75 and DNA repair in response to DNA damage."; /evidence="ECO:0000269|PubMed:40240600
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:0000269|PubMed:40240600}.; PTM: Acetylated at Lys-26 (PubMed:15469825). Deacetylated at Lys-26 by SIRT1 (PubMed:15469825). 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 (PubMed:22465951). 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 (PubMed:40240600). {ECO:0000269|PubMed:15469825, ECO:0000269|PubMed:22465951, ECO:0000269|PubMed:40240600}.; PTM: Mono- and dimethylated at Lys-26 by EHMT2/G9a (H1.4K26me1 and H1.4K26me2, respectively) (PubMed:19144645). H1.4K26me1, H1.4K26me2 and H1.4K26me3 are demethylated by KDM4A (PubMed:19144645, PubMed:30156264). H1.4K26me is recognized by histone reader HP1 (CBX1, CBX3 and/or CBX5) (PubMed:16127177). {ECO:0000269|PubMed:16127177, ECO:0000269|PubMed:19144645, ECO:0000269|PubMed:30156264}.; 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 (By similarity). Phosphorylated at Ser-27 by AURKB during mitosis (PubMed:21511733). Simultaneous methylation at Lys-26 (H1.4K26me) and phosphorylation at Ser-27 (H1.4S27Ph) prevents binding by histone reader HP1 (CBX1, CBX3 and/or CBX5) (PubMed:16127177). Phosphorylation at Ser-36 by PKA during mitosis promotes dissociation from mitotic chromosome (PubMed:21852232). Phosphorylation at Ser-187 by CDK9 is associated with transcription activation (PubMed:28539972, PubMed:33238524). Phosphorylation at Thr-146 highly increases during mitosis compared to interphase (PubMed:38530350). {ECO:0000250|UniProtKB:P43275, ECO:0000269|PubMed:16127177, ECO:0000269|PubMed:21511733, ECO:0000269|PubMed:21852232, ECO:0000269|PubMed:28539972, ECO:0000269|PubMed:33238524, ECO:0000269|PubMed:38530350}.; 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:0000250|UniProtKB:P43274}.; PTM: ADP-ribosylated on Ser-150 in response to DNA damage. {ECO:0000269|PubMed:27723750}.
uniprot
proteins
protein_family
Histone H1/H5 family
uniprot
proteins
pubmed
10997781
uniprot
proteins
pubmed
12408966
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
15469825
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15911621
uniprot
proteins
pubmed
16127177
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19144645
uniprot
proteins
pubmed
1916825
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21511733
uniprot
proteins
pubmed
21852232
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22465951
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
27723750
uniprot
proteins
pubmed
28475857
uniprot
proteins
pubmed
28539972
uniprot
proteins
pubmed
30154464
uniprot
proteins
pubmed
30156264
uniprot
proteins
pubmed
33238161
uniprot
proteins
pubmed
33238524
uniprot
proteins
pubmed
34545082
uniprot
proteins
pubmed
34788807
uniprot
proteins
pubmed
34961760
uniprot
proteins
pubmed
35581345
uniprot
proteins
pubmed
3782055
uniprot
proteins
pubmed
38530350
uniprot
proteins
pubmed
40240600
uniprot
proteins
pubmed
40516528
uniprot
proteins
pubmed
40516529
uniprot
proteins
sequence_length
219
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:38530350, ECO:0000269|PubMed:40240600}. Chromosome {ECO:0000269|PubMed:15911621, ECO:0000269|PubMed:21852232, ECO:0000269|PubMed:38530350, ECO:0000269|PubMed:40240600}. Note=Mainly localizes in heterochromatin (PubMed:40240600). Distributed throughout the nucleus; displays a punctuate staining pattern in the nucleus (PubMed:38530350, PubMed:40240600). {ECO:0000269|PubMed:38530350, ECO:0000269|PubMed:40240600}.
uniprot
proteins