H1-2
entrez
3006
canonical
uniprot
P16403
canonical
ensembl
ENSG00000187837
resolver
ensp
ENSP00000339566
resolver
ensp
ENSP00000520720
resolver
enst
ENST00000343677
resolver
enst
ENST00000718281
resolver
genesymbol
H1-2
resolver
genesymbol_syn
H1F2
resolver
genesymbol_syn
HIST1H1C
resolver
hgnc
HGNC:4716
resolver
uniprot
A8K4I2
resolver
uniprot_entry
H12_HUMAN
resolver
uniprot_sec
A8K4I2
resolver
amino_acid_sequence
MSETAPAAPAAAPPAEKAPVKKKAAKKAGGTPRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEAKPKVKKAGGTKPKKPVGAAKKPKKAAGGATPKKSAKKTPKKAKKPAAATVTKKVAKSPKKAKVAKPKKAAKSAAKAVKPKAAKPKVVKPKKAAPKKK
uniprot
proteins
function
FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber (PubMed:26581166, PubMed:38530350). Histone H1-2 is required for the condensation of nucleosome chains into higher-order structured fibers (PubMed:38530350). Compared to other histone H1 variants, H1-2 plays an essential role in nucleosome condensation: its absence leads to global chromatin decompaction, which is not observed when depleting other histone H1 variants (PubMed:38530350). Histone H1-2 also acts as a histone reader: specifically recognizes and binds histone H3 trimethylated at 'lys-27' (H3K27me3) (PubMed:26581166). Histones H1 also promote formation of the H3K27me3 mark by the PRC2/EED-EZH2 complex, possibly by facilitating restoration of H3K27me3 post-replication (PubMed:37429872, PubMed:40516528). 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 (PubMed:37922872). Also acts as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (PubMed:38530350). {ECO:0000269|PubMed:26581166, ECO:0000269|PubMed:37429872, ECO:0000269|PubMed:37922872, ECO:0000269|PubMed:38530350, ECO:0000269|PubMed:40516528}.
uniprot
proteins
mass_dalton
21365
uniprot
proteins
mutagenesis
MUTAGEN 120..132; /note="VKKAGGTKPKKPV->AKKAGGAKPKKPA: Impared ability to recognize and bind histone H3 trimethylated at 'lys-27' (H3K27me3)."; /evidence="ECO:0000269|PubMed:26581166"; MUTAGEN 187; /note="K->R: Abolishes methylation."; /evidence="ECO:0000269|PubMed:20334638
uniprot
proteins
post_translational_modification
PTM: Deamidation of Asn-76 and Asn-77 by CTPS1 in response to DNA damage promotes subsequent acetylation of histo75 (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: 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). Phosphorylation at Thr-165 is associated with condensed chromosomes, with maximum levels occurring at metaphase and drastically dropping down at later mitotic phases (PubMed:38530350). During interphase, phosphorylation at Thr-165 is enriched within nucleoli (PubMed:38530350). {ECO:0000250|UniProtKB:P15864, ECO:0000269|PubMed:38530350}.; 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: 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:P15864}.; PTM: ADP-ribosylated on Ser-188 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
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15911621
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19054851
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20334638
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21925322
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24681537
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
2613692
uniprot
proteins
pubmed
26581166
uniprot
proteins
pubmed
2759094
uniprot
proteins
pubmed
27723750
uniprot
proteins
pubmed
28539972
uniprot
proteins
pubmed
29301938
uniprot
proteins
pubmed
30154464
uniprot
proteins
pubmed
34545082
uniprot
proteins
pubmed
34681573
uniprot
proteins
pubmed
34961760
uniprot
proteins
pubmed
36435862
uniprot
proteins
pubmed
37429872
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
213
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:38530350}. Nucleus, nucleolus {ECO:0000269|PubMed:29301938, ECO:0000269|PubMed:38530350}. Chromosome {ECO:0000269|PubMed:26581166, ECO:0000269|PubMed:29301938, ECO:0000269|PubMed:38530350}. Note=Enriched at the nuclear periphery and colocalizes with compacted DNA (heterochromatin) (PubMed:26581166, PubMed:38530350). Enriched within lamina-associated domains (PubMed:38530350). {ECO:0000269|PubMed:26581166, ECO:0000269|PubMed:38530350}.
uniprot
proteins