H1-5
entrez
3009
canonical
uniprot
P16401
canonical
ensembl
ENSG00000184357
resolver
ensp
ENSP00000330074
resolver
enst
ENST00000331442
resolver
genesymbol
H1-5
resolver
genesymbol_syn
H1F5
resolver
genesymbol_syn
HIST1H1B
resolver
hgnc
HGNC:4719
resolver
uniprot
Q14529
resolver
uniprot
Q3MJ42
resolver
uniprot_entry
H15_HUMAN
resolver
uniprot_sec
Q14529
resolver
uniprot_sec
Q3MJ42
resolver
amino_acid_sequence
MSETAPAETATPAPVEKSPAKKKATKKAAGAGAAKRKATGPPVSELITKAVAASKERNGLSLAALKKALAAGGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEAKPKAKKAGAAKAKKPAGATPKKAKKAAGAKKAVKKTPKKAKKPAAAGVKKVAKSPKKAKAAAKPKKATKSPAKPKAVKPKAAKPKAAKPKAAKPKAAKAKKAAAKKK
uniprot
proteins
function
FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber (By similarity). 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). 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:40516528}.
uniprot
proteins
mass_dalton
22580
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 (By similarity). Phosphorylated at Thr-11 by GSK3B during mitosis in prometaphase and dephosphorylated in telophase. {ECO:0000250, ECO:0000269|PubMed:16377619, ECO:0000269|PubMed:19136008}.; 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:P43276}.
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
15489334
uniprot
proteins
pubmed
15911621
uniprot
proteins
pubmed
16377619
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19136008
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19552482
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
2613692
uniprot
proteins
pubmed
28539972
uniprot
proteins
pubmed
30154464
uniprot
proteins
pubmed
34545082
uniprot
proteins
pubmed
34961760
uniprot
proteins
pubmed
38530350
uniprot
proteins
pubmed
40516528
uniprot
proteins
pubmed
40516529
uniprot
proteins
pubmed
9031620
uniprot
proteins
sequence_length
226
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10997781, ECO:0000269|PubMed:15911621, ECO:0000269|PubMed:38530350}. Chromosome {ECO:0000269|PubMed:38530350}. Note=Enriched at the nuclear periphery and colocalizes with compacted DNA (heterochromatin) (PubMed:15911621, PubMed:38530350). Also associates with actively transcribed chromatin (PubMed:10997781). {ECO:0000269|PubMed:10997781, ECO:0000269|PubMed:15911621, ECO:0000269|PubMed:38530350}.
uniprot
proteins