H3Y1
entrez
391769
canonical
uniprot
P0DPK2
canonical
ensembl
ENSG00000269466
resolver
ensp
ENSP00000496014
resolver
enst
ENST00000598383
resolver
genesymbol
H3Y1
resolver
hgnc
HGNC:43735
resolver
uniprot_entry
H3Y1_HUMAN
resolver
amino_acid_sequence
MARTKQTARKATAWQAPRKPLATKAAGKRAPPTGGIKKPHRYKPGTLALREIRKYQKSTQLLLRKLPFQRLVREIAQAISPDLRFQSAAIGALQEASEAYLVQLFEDTNLCAIHARRVTIMPRDMQLARRLRREGP
uniprot
proteins
function
FUNCTION: Primate-specific variant histone H3, which constitutes a core component of nucleosomes (PubMed:20819935, PubMed:27016736). Histone H3.Y-containing nucleosomes accumulate around transcription start sites and have flexible DNA ends, suggesting that they form relaxed chromatin that allows transcription factor access (PubMed:27016736). Histone H1 binds less efficiently to histone H3.Y-containing nucleosomes (PubMed:27016736). 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 (Probable). {ECO:0000269|PubMed:20819935, ECO:0000269|PubMed:27016736, ECO:0000305}.
uniprot
proteins
mass_dalton
15423
uniprot
proteins
mutagenesis
MUTAGEN 43..47; /note="KPGTL->RPGTV: Triggers interaction with DAXX."; /evidence="ECO:0000269|PubMed:28334823"; MUTAGEN 43; /note="K->R: Enhanced binding of histone H1 to histone H3.Y-containing nucleosomes. Does not greatly affect the stability of the nucleosome."; /evidence="ECO:0000269|PubMed:27016736, ECO:0000269|PubMed:28118111"; MUTAGEN 47; /note="L->V: Triggers interaction with DAXX; when associated with I-63."; /evidence="ECO:0000269|PubMed:28334823"; MUTAGEN 60; /note="Q->E: Does not establish interaction with DAXX."; /evidence="ECO:0000269|PubMed:28334823"; MUTAGEN 63; /note="L->I: Does not affect stability of the nucleosome. Triggers interaction with DAXX; when associated with V-47."; /evidence="ECO:0000269|PubMed:28118111, ECO:0000269|PubMed:28334823"; MUTAGEN 125; /note="M->I: Impaired association between H3.Y and H4 and stability of the nucleosome."; /evidence="ECO:0000269|PubMed:28118111"; MUTAGEN 131; /note="L->I: Does not affect association between H3.Y and H4."; /evidence="ECO:0000269|PubMed:28118111"; MUTAGEN 133; /note="R->G: Does not affect association between H3.Y and H4."; /evidence="ECO:0000269|PubMed:28118111"; MUTAGEN 135; /note="G->R: Impaired association between H3.Y and H4."; /evidence="ECO:0000269|PubMed:28118111
uniprot
proteins
post_translational_modification
PTM: Acetylation is generally linked to gene activation. Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me). {ECO:0000250|UniProtKB:P84243}.; PTM: Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) impairs methylation and represses transcription. {ECO:0000250|UniProtKB:P84243}.; PTM: Asymmetric dimethylation at Arg-18 (H3R17me2a) is linked to gene activation. Symmetric dimethylation at Arg-9 (H3R8me2s) is linked to gene repression. Asymmetric dimethylation at Arg-3 (H3R2me2a) is linked to gene repression and is mutually exclusive with H3 Lys-5 methylation (H3K4me2 and H3K4me3). H3R2me2a is present at the 3' of genes regardless of their transcription state and is enriched on inactive promoters, while it is absent on active promoters. {ECO:0000250|UniProtKB:P84243}.; PTM: Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation of H3 and H4. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me), which are linked to gene repression, are underrepresented. Methylation at Lys-10 (H3K9me) is a specific target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents subsequent acetylation of H3 and H4. {ECO:0000250|UniProtKB:P84243}.; PTM: Phosphorylation at Thr-7 (H3T6ph) is a specific tag for epigenetic transcriptional activation that prevents demethylation of Lys-5 (H3K4me) by LSD1/KDM1A. At centromeres, specifically phosphorylated at Thr-12 (H3T11ph) from prophase to early anaphase. Phosphorylation at Thr-12 (H3T11ph) is a specific tag for epigenetic transcriptional activation that promotes demethylation of Lys-10 (H3K9me). Phosphorylation at Tyr-42 (H3Y41ph) promotes exclusion of CBX5 (HP1 alpha) from chromatin. {ECO:0000250|UniProtKB:P84243}.; PTM: Lysine deamination at Lys-5 (H3K4all) to form allysine. Allysine formation only takes place on H3K4me3 and results in gene repression. {ECO:0000250|UniProtKB:P84243}.; 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:0000250|UniProtKB:P84243}.; PTM: Butyrylation of histones marks active promoters and competes with histone acetylation. It is present during late spermatogenesis. {ECO:0000250|UniProtKB:P68433}.
uniprot
proteins
protein_family
Histone H3 family
uniprot
proteins
pubmed
15372022
uniprot
proteins
pubmed
20819935
uniprot
proteins
pubmed
27016736
uniprot
proteins
pubmed
28118111
uniprot
proteins
pubmed
28334823
uniprot
proteins
sequence_length
136
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20819935}. Chromosome {ECO:0000269|PubMed:27016736, ECO:0000269|PubMed:28334823, ECO:0000305|PubMed:20819935}. Note=Histone H3.Y-containing nucleosomes are depleted from repressive post-translational histone modifications (PubMed:28334823). Histone H3.Y-containing nucleosomes accumulate around transcription start sites (PubMed:27016736). {ECO:0000269|PubMed:27016736, ECO:0000269|PubMed:28334823}.
uniprot
proteins