P62805
uniprot
P62805
canonical
amino_acid_sequence
MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
uniprot
proteins
disease_involvement
DISEASE: Tessadori-Bicknell-Van Haaften neurodevelopmental syndrome 1 (TEBIVANED1) [MIM:619758]: An autosomal dominant disorder with onset in infancy, characterized by poor overall growth, microcephaly, hypotonia, profound global developmental delay, impaired intellectual development, poor or absent speech, and characteristic dysmorphic facial features, including hypertelorism and abnormal nose. Other variable neurologic and systemic features may also occur. {ECO:0000269|PubMed:28920961, ECO:0000269|PubMed:35202563}. Note=The disease is caused by variants affecting the gene represented in this entry. TEBIVANED1 is caused by variants in H4C3. {ECO:0000269|PubMed:28920961, ECO:0000269|PubMed:35202563}.; DISEASE: Tessadori-Bicknell-Van Haaften neurodevelopmental syndrome 2 (TEBIVANED2) [MIM:619759]: An autosomal dominant disorder characterized by poor overall growth, microcephaly, hypotonia, profound global developmental delay, impaired intellectual development, absent speech, and characteristic dysmorphic facial features, including hypertelorism, abnormal nose, and wide mouth. {ECO:0000269|PubMed:31804630, ECO:0000269|PubMed:35202563}. Note=The disease is caused by variants affecting the gene represented in this entry. TEBIVANED2 is caused by variants in H4C11. {ECO:0000269|PubMed:31804630, ECO:0000269|PubMed:35202563}.; DISEASE: Tessadori-Bicknell-Van Haaften neurodevelopmental syndrome 3 (TEBIVANED3) [MIM:619950]: An autosomal dominant disorder characterized by global developmental delay with poor overall growth, impaired intellectual development, and speech difficulties. More variable features include hypotonia, microcephaly, and dysmorphic facies. {ECO:0000269|PubMed:35202563}. Note=The disease is caused by variants affecting the gene represented in this entry. TEBIVANED3 is caused by variants in H4C5. {ECO:0000269|PubMed:35202563}.; DISEASE: Tessadori-Bicknell-Van Haaften neurodevelopmental syndrome 4 (TEBIVANED4) [MIM:619951]: An autosomal dominant disorder characterized by global developmental delay with poor overall growth, variably impaired intellectual development, learning difficulties, distal skeletal anomalies, and dysmorphic facies. Some patients have visual or hearing deficits. {ECO:0000269|PubMed:35202563}. Note=The disease is caused by variants affecting the gene represented in this entry. TEBIVANED4 is caused by variants in H4C9. {ECO:0000269|PubMed:35202563}.; DISEASE: Note=Chromosomal aberrations involving HISTONE H4 is a cause of B-cell non-Hodgkin lymphomas (B-cell NHL). Translocation t(3;6)(q27;p21), with BCL6. {ECO:0000269|PubMed:12414651}.
uniprot
proteins
function
FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
uniprot
proteins
mass_dalton
11367
uniprot
proteins
mutagenesis
MUTAGEN 13; /note="K->A: Impaired methylation by N6AMT1."; /evidence="ECO:0000269|PubMed:31061526"; MUTAGEN 32; /note="K->R: Abolished ufmylation."; /evidence="ECO:0000269|PubMed:30886146
uniprot
proteins
post_translational_modification
PTM: Acetylation at Lys-6 (H4K5ac), Lys-9 (H4K8ac), Lys-13 (H4K12ac) and Lys-17 (H4K16ac) occurs in coding regions of the genome but not in heterochromatin. Acetylated as part of spermatogenesis progression prior to histone-to-protamine exchange (By similarity). {ECO:0000250|UniProtKB:P62806, ECO:0000269|PubMed:17967882, ECO:0000269|PubMed:2474456, ECO:0000269|PubMed:7664735}.; PTM: Citrullination at Arg-4 (H4R3ci) by PADI4 impairs methylation. {ECO:0000269|PubMed:11387442, ECO:0000269|PubMed:11448779, ECO:0000269|PubMed:15345777, ECO:0000269|PubMed:16567635}.; PTM: Monomethylation and asymmetric dimethylation at Arg-4 (H4R3me1 and H4R3me2a, respectively) by PRMT1 favors acetylation at Lys-9 (H4K8ac) and Lys-13 (H4K12ac). Demethylation is performed by JMJD6. Symmetric dimethylation on Arg-4 (H4R3me2s) by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage. {ECO:0000269|PubMed:11387442, ECO:0000269|PubMed:11448779, ECO:0000269|PubMed:15345777}.; PTM: Monomethylated, dimethylated or trimethylated at Lys-21 (H4K20me1, H4K20me2, H4K20me3) (PubMed:12086618, PubMed:15964846, PubMed:17967882). Monomethylation is performed by KMT5A/SET8 (PubMed:15964846). Dimethylation and trimethylation is performed by KMT5B and KMT5C and induces gene silencing (By similarity). Monomethylated at Lys-13 (H4K12me1) by N6AMT1; H4K12me1 modification is present at the promoters of numerous genes encoding cell cycle regulators (PubMed:31061526). H4K20me2 and H4K20me3 are demethylated into monomethyl (H4K20me1) by RSBN1 (By similarity). H4K20me1, H4K20me2 and H4K20me3 are demethylated by RAD23A and RAD23B (PubMed:32209475). H4K20me1 is demethylated by PHF8 (PubMed:20622854). {ECO:0000250|UniProtKB:P62806, ECO:0000269|PubMed:12086618, ECO:0000269|PubMed:15964846, ECO:0000269|PubMed:17967882, ECO:0000269|PubMed:20622854, ECO:0000269|PubMed:31061526, ECO:0000269|PubMed:32209475}.; PTM: Acetyl-methylated at Lys-6 and Lys-13 (H4K5acme and H4K12acme, respectively), acetyl-methylation is an epigenetic mark of active chromatin associated with increased transcriptional initiation (PubMed:37731000). Acetyl-methylation is formed by acetylation by EP300/p300 of lysine residues that are already monomethylated on the same side chain (PubMed:37731000). H4K5acme and H4K12acme marks specifically bind BRD2 (PubMed:37731000). {ECO:0000269|PubMed:37731000}.; PTM: Phosphorylated by PAK2 at Ser-48 (H4S47ph). This phosphorylation increases the association of H3.3-H4 with the histone chaperone HIRA, thus promoting nucleosome assembly of H3.3-H4 and inhibiting nucleosome assembly of H3.1-H4. {ECO:0000269|PubMed:17967882, ECO:0000269|PubMed:21724829}.; PTM: Ubiquitinated by the CUL4-DDB-RBX1 complex in response to ultraviolet irradiation. This may weaken the interaction between histones and DNA and facilitate DNA accessibility to repair proteins. Monoubiquitinated at Lys-92 of histone H4 (H4K91ub1) in response to DNA damage. The exact role of H4K91ub1 in DNA damage response is still unclear but it may function as a licensing signal for additional histone H4 post-translational modifications such as H4 Lys-21 methylation (H4K20me). Ubiquitinated; by PHF7 (By similarity). {ECO:0000250|UniProtKB:P62806, ECO:0000269|PubMed:12086618, ECO:0000269|PubMed:15964846, ECO:0000269|PubMed:16678110, ECO:0000269|PubMed:17967882, ECO:0000269|PubMed:19818714}.; PTM: Ufmylated; monofmylated by UFL1 at Lys-32 (H4K31Ufm1) in response to DNA damage. {ECO:0000269|PubMed:30886146}.; PTM: Sumoylated, which is associated with transcriptional repression. {ECO:0000269|PubMed:14578449}.; 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: Butyrylation of histones marks active promoters and competes with histone acetylation. {ECO:0000250|UniProtKB:P62806}.; PTM: Glutarylation at Lys-92 (H4K91glu) destabilizes nucleosomes by promoting dissociation of the H2A-H2B dimers from nucleosomes. {ECO:0000269|PubMed:31542297}.; PTM: Lactylated in macrophages by EP300/P300 by using lactoyl-CoA directly derived from endogenous or exogenous lactate, leading to stimulates gene transcription (PubMed:31645732). Delactylated by SIRT3 at Lys-17 (H4K16la) (PubMed:37720100). {ECO:0000269|PubMed:31645732, ECO:0000269|PubMed:37720100}.
uniprot
proteins
protein_family
Histone H4 family
uniprot
proteins
pubmed
11387442
uniprot
proteins
pubmed
11448779
uniprot
proteins
pubmed
12086618
uniprot
proteins
pubmed
12408966
uniprot
proteins
pubmed
12414651
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14578449
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
15345777
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15527963
uniprot
proteins
pubmed
15592455
uniprot
proteins
pubmed
15951514
uniprot
proteins
pubmed
15964846
uniprot
proteins
pubmed
16567635
uniprot
proteins
pubmed
16678110
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17267393
uniprot
proteins
pubmed
17967882
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
1916825
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19818714
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20622854
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21724829
uniprot
proteins
pubmed
21925322
uniprot
proteins
pubmed
22195965
uniprot
proteins
pubmed
22389435
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24681537
uniprot
proteins
pubmed
2474456
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
27016736
uniprot
proteins
pubmed
27105113
uniprot
proteins
pubmed
27105115
uniprot
proteins
pubmed
27338793
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28497810
uniprot
proteins
pubmed
28920961
uniprot
proteins
pubmed
30154464
uniprot
proteins
pubmed
3035717
uniprot
proteins
pubmed
30886146
uniprot
proteins
pubmed
31061526
uniprot
proteins
pubmed
31542297
uniprot
proteins
pubmed
31645732
uniprot
proteins
pubmed
31804630
uniprot
proteins
pubmed
32209475
uniprot
proteins
pubmed
32911480
uniprot
proteins
pubmed
32911481
uniprot
proteins
pubmed
32911482
uniprot
proteins
pubmed
32912999
uniprot
proteins
pubmed
32913000
uniprot
proteins
pubmed
33051594
uniprot
proteins
pubmed
33141820
uniprot
proteins
pubmed
3340182
uniprot
proteins
pubmed
33857403
uniprot
proteins
pubmed
34545082
uniprot
proteins
pubmed
34961760
uniprot
proteins
pubmed
35202563
uniprot
proteins
pubmed
35390161
uniprot
proteins
pubmed
36435862
uniprot
proteins
pubmed
37720100
uniprot
proteins
pubmed
37731000
uniprot
proteins
pubmed
6314274
uniprot
proteins
pubmed
7626218
uniprot
proteins
pubmed
7664735
uniprot
proteins
pubmed
8988030
uniprot
proteins
pubmed
9031620
uniprot
proteins
pubmed
9119399
uniprot
proteins
pubmed
9439656
uniprot
proteins
sequence_length
103
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P62806}. Chromosome. Note=Localized to the nucleus when acetylated in step 11 spermatids. {ECO:0000250|UniProtKB:P62806}.
uniprot
proteins