H3Y1_HUMAN
ID H3Y1_HUMAN Reviewed; 136 AA.
AC P0DPK2;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Histone H3.Y {ECO:0000303|PubMed:20819935};
DE AltName: Full=Histone H3.Y1 {ECO:0000305};
GN Name=H3Y1 {ECO:0000312|HGNC:HGNC:43735};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [2]
RP SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=20819935; DOI=10.1083/jcb.201002043;
RA Wiedemann S.M., Mildner S.N., Boenisch C., Israel L., Maiser A.,
RA Matheisl S., Straub T., Merkl R., Leonhardt H., Kremmer E., Schermelleh L.,
RA Hake S.B.;
RT "Identification and characterization of two novel primate-specific histone
RT H3 variants, H3.X and H3.Y.";
RL J. Cell Biol. 190:777-791(2010).
RN [3]
RP MUTAGENESIS OF LYS-43; LEU-63; MET-125; LEU-131; ARG-133 AND GLY-135.
RX PubMed=28118111; DOI=10.1080/19491034.2016.1277303;
RA Kujirai T., Horikoshi N., Xie Y., Taguchi H., Kurumizaka H.;
RT "Identification of the amino acid residues responsible for stable
RT nucleosome formation by histone H3.Y.";
RL Nucleus 8:239-248(2017).
RN [4]
RP SUBCELLULAR LOCATION, INTERACTION WITH HIRA, AND MUTAGENESIS OF
RP 43-LYS--VAL-47; LEU-47; GLN-60 AND LEU-63.
RX PubMed=28334823; DOI=10.1093/nar/gkx131;
RA Zink L.M., Delbarre E., Eberl H.C., Keilhauer E.C., Boenisch C.,
RA Puenzeler S., Bartkuhn M., Collas P., Mann M., Hake S.B.;
RT "H3.Y discriminates between HIRA and DAXX chaperone complexes and reveals
RT unexpected insights into human DAXX-H3.3-H4 binding and deposition
RT requirements.";
RL Nucleic Acids Res. 45:5691-5706(2017).
RN [5] {ECO:0007744|PDB:5AY8}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 39-135 IN COMPLEX WITH H2A; H2B
RP AND H4, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF LYS-43.
RX PubMed=27016736; DOI=10.1093/nar/gkw202;
RA Kujirai T., Horikoshi N., Sato K., Maehara K., Machida S., Osakabe A.,
RA Kimura H., Ohkawa Y., Kurumizaka H.;
RT "Structure and function of human histone H3.Y nucleosome.";
RL Nucleic Acids Res. 44:6127-6141(2016).
CC -!- FUNCTION: Primate-specific variant histone H3, which constitutes a core
CC component of nucleosomes (PubMed:20819935, PubMed:27016736). Histone
CC H3.Y-containing nucleosomes accumulate around transcription start sites
CC and have flexible DNA ends, suggesting that they form relaxed chromatin
CC that allows transcription factor access (PubMed:27016736). Histone H1
CC binds less efficiently to histone H3.Y-containing nucleosomes
CC (PubMed:27016736). Nucleosomes wrap and compact DNA into chromatin,
CC limiting DNA accessibility to the cellular machineries which require
CC DNA as a template. Histones thereby play a central role in
CC transcription regulation, DNA repair, DNA replication and chromosomal
CC stability. DNA accessibility is regulated via a complex set of post-
CC translational modifications of histones, also called histone code, and
CC nucleosome remodeling (Probable). {ECO:0000269|PubMed:20819935,
CC ECO:0000269|PubMed:27016736, ECO:0000305}.
CC -!- SUBUNIT: The nucleosome is a histone octamer containing two molecules
CC each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and
CC two H2A-H2B heterodimers (PubMed:20819935, PubMed:27016736). The
CC octamer wraps approximately 147 bp of DNA (Probable). Interacts with
CC HIRA, a chaperone required for its incorporation into nucleosomes
CC (PubMed:28334823). Does not interact with DAXX chaperone
CC (PubMed:28334823). {ECO:0000269|PubMed:20819935,
CC ECO:0000269|PubMed:27016736, ECO:0000269|PubMed:28334823, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20819935}. Chromosome
CC {ECO:0000269|PubMed:27016736, ECO:0000269|PubMed:28334823,
CC ECO:0000305|PubMed:20819935}. Note=Histone H3.Y-containing nucleosomes
CC are depleted from repressive post-translational histone modifications
CC (PubMed:28334823). Histone H3.Y-containing nucleosomes accumulate
CC around transcription start sites (PubMed:27016736).
CC {ECO:0000269|PubMed:27016736, ECO:0000269|PubMed:28334823}.
CC -!- TISSUE SPECIFICITY: Expressed at low level in some tissues, such as
CC testis and brain. {ECO:0000269|PubMed:20819935}.
CC -!- PTM: Acetylation is generally linked to gene activation. Acetylation on
CC Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s). Acetylation on
CC Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18
CC (H3R17me). {ECO:0000250|UniProtKB:P84243}.
CC -!- PTM: Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) impairs
CC methylation and represses transcription.
CC {ECO:0000250|UniProtKB:P84243}.
CC -!- PTM: Asymmetric dimethylation at Arg-18 (H3R17me2a) is linked to gene
CC activation. Symmetric dimethylation at Arg-9 (H3R8me2s) is linked to
CC gene repression. Asymmetric dimethylation at Arg-3 (H3R2me2a) is linked
CC to gene repression and is mutually exclusive with H3 Lys-5 methylation
CC (H3K4me2 and H3K4me3). H3R2me2a is present at the 3' of genes
CC regardless of their transcription state and is enriched on inactive
CC promoters, while it is absent on active promoters.
CC {ECO:0000250|UniProtKB:P84243}.
CC -!- PTM: Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation
CC of H3 and H4. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me),
CC which are linked to gene repression, are underrepresented. Methylation
CC at Lys-10 (H3K9me) is a specific target for HP1 proteins (CBX1, CBX3
CC and CBX5) and prevents subsequent acetylation of H3 and H4.
CC {ECO:0000250|UniProtKB:P84243}.
CC -!- PTM: Phosphorylation at Thr-7 (H3T6ph) is a specific tag for epigenetic
CC transcriptional activation that prevents demethylation of Lys-5
CC (H3K4me) by LSD1/KDM1A. At centromeres, specifically phosphorylated at
CC Thr-12 (H3T11ph) from prophase to early anaphase. Phosphorylation at
CC Thr-12 (H3T11ph) is a specific tag for epigenetic transcriptional
CC activation that promotes demethylation of Lys-10 (H3K9me).
CC Phosphorylation at Tyr-42 (H3Y41ph) promotes exclusion of CBX5 (HP1
CC alpha) from chromatin. {ECO:0000250|UniProtKB:P84243}.
CC -!- PTM: Lysine deamination at Lys-5 (H3K4all) to form allysine. Allysine
CC formation only takes place on H3K4me3 and results in gene repression.
CC {ECO:0000250|UniProtKB:P84243}.
CC -!- PTM: Crotonylation (Kcr) is specifically present in male germ cells and
CC marks testis-specific genes in post-meiotic cells, including X-linked
CC genes that escape sex chromosome inactivation in haploid cells.
CC Crotonylation marks active promoters and enhancers and confers
CC resistance to transcriptional repressors. It is also associated with
CC post-meiotically activated genes on autosomes.
CC {ECO:0000250|UniProtKB:P84243}.
CC -!- PTM: Butyrylation of histones marks active promoters and competes with
CC histone acetylation. It is present during late spermatogenesis.
CC {ECO:0000250|UniProtKB:P68433}.
CC -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC233724; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS87290.1; -.
DR PDB; 5AY8; X-ray; 2.80 A; A/E=39-135.
DR PDBsum; 5AY8; -.
DR AlphaFoldDB; P0DPK2; -.
DR SMR; P0DPK2; -.
DR MassIVE; P0DPK2; -.
DR PeptideAtlas; P0DPK2; -.
DR PRIDE; P0DPK2; -.
DR Ensembl; ENST00000598383.3; ENSP00000496014.2; ENSG00000269466.4.
DR MANE-Select; ENST00000598383.3; ENSP00000496014.2; NM_001355258.2; NP_001342187.1.
DR GeneCards; H3Y1; -.
DR HGNC; HGNC:43735; H3Y1.
DR HPA; ENSG00000269466; Not detected.
DR neXtProt; NX_P0DPK2; -.
DR OpenTargets; ENSG00000269466; -.
DR VEuPathDB; HostDB:ENSG00000269466; -.
DR GeneTree; ENSGT01050000244889; -.
DR OMA; LKEIRMY; -.
DR SIGNOR; P0DPK2; -.
DR Pharos; P0DPK2; Tbio.
DR PRO; PR:P0DPK2; -.
DR Proteomes; UP000005640; Chromosome 5.
DR Bgee; ENSG00000269466; Expressed in thoracic aorta and 6 other tissues.
DR GO; GO:0000786; C:nucleosome; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031492; F:nucleosomal DNA binding; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR000164; Histone_H3/CENP-A.
DR PANTHER; PTHR11426; PTHR11426; 1.
DR Pfam; PF00125; Histone; 1.
DR PRINTS; PR00622; HISTONEH3.
DR SMART; SM00428; H3; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00959; HISTONE_H3_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromosome; Citrullination; Hydroxylation;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..136
FT /note="Histone H3.Y"
FT /id="PRO_0000445074"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 3
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 3
FT /note="Citrulline; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 4
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 5
FT /note="Allysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 5
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 5
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 5
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 5
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 5
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 5
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 5
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 6
FT /note="5-glutamyl dopamine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 6
FT /note="5-glutamyl serotonin; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 7
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 9
FT /note="Citrulline; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 9
FT /note="Symmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P84244"
FT MOD_RES 10
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 10
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 10
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 10
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 10
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 10
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 10
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 10
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 10
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 12
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 18
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 18
FT /note="Citrulline; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 19
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 19
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 19
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 19
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 19
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 19
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 19
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 19
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 24
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 24
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 24
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 24
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 24
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 24
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 24
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 24
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 28
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 28
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 28
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 28
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 28
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 28
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 28
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 28
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 28
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 37
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 37
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 37
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 37
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 37
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 38
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 42
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 57
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 57
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 57
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 57
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 57
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 57
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 57
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68433"
FT MOD_RES 57
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 57
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 65
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 65
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 108
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q71DI3"
FT MUTAGEN 43..47
FT /note="KPGTL->RPGTV: Triggers interaction with DAXX."
FT /evidence="ECO:0000269|PubMed:28334823"
FT MUTAGEN 43
FT /note="K->R: Enhanced binding of histone H1 to histone
FT H3.Y-containing nucleosomes. Does not greatly affect the
FT stability of the nucleosome."
FT /evidence="ECO:0000269|PubMed:27016736,
FT ECO:0000269|PubMed:28118111"
FT MUTAGEN 47
FT /note="L->V: Triggers interaction with DAXX; when
FT associated with I-63."
FT /evidence="ECO:0000269|PubMed:28334823"
FT MUTAGEN 60
FT /note="Q->E: Does not establish interaction with DAXX."
FT /evidence="ECO:0000269|PubMed:28334823"
FT MUTAGEN 63
FT /note="L->I: Does not affect stability of the nucleosome.
FT Triggers interaction with DAXX; when associated with V-47."
FT /evidence="ECO:0000269|PubMed:28118111,
FT ECO:0000269|PubMed:28334823"
FT MUTAGEN 125
FT /note="M->I: Impaired association between H3.Y and H4 and
FT stability of the nucleosome."
FT /evidence="ECO:0000269|PubMed:28118111"
FT MUTAGEN 131
FT /note="L->I: Does not affect association between H3.Y and
FT H4."
FT /evidence="ECO:0000269|PubMed:28118111"
FT MUTAGEN 133
FT /note="R->G: Does not affect association between H3.Y and
FT H4."
FT /evidence="ECO:0000269|PubMed:28118111"
FT MUTAGEN 135
FT /note="G->R: Impaired association between H3.Y and H4."
FT /evidence="ECO:0000269|PubMed:28118111"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:5AY8"
FT HELIX 65..79
FT /evidence="ECO:0007829|PDB:5AY8"
FT HELIX 87..114
FT /evidence="ECO:0007829|PDB:5AY8"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:5AY8"
FT HELIX 122..130
FT /evidence="ECO:0007829|PDB:5AY8"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:5AY8"
SQ SEQUENCE 136 AA; 15423 MW; EB5A98626A634A93 CRC64;
MARTKQTARK ATAWQAPRKP LATKAAGKRA PPTGGIKKPH RYKPGTLALR EIRKYQKSTQ
LLLRKLPFQR LVREIAQAIS PDLRFQSAAI GALQEASEAY LVQLFEDTNL CAIHARRVTI
MPRDMQLARR LRREGP
