H3_YARLI
ID H3_YARLI Reviewed; 139 AA.
AC Q6C0C4;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Histone H3;
GN Name=HHT1; OrderedLocusNames=YALI0F25905g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact
CC DNA into chromatin, limiting DNA accessibility to the cellular
CC machineries which require DNA as a template. Histones thereby play a
CC central role in transcription regulation, DNA repair, DNA replication
CC and chromosomal stability. DNA accessibility is regulated via a complex
CC set of post-translational modifications of histones, also called
CC histone code, and nucleosome remodeling (By similarity). {ECO:0000250}.
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. The octamer wraps approximately 147 bp of DNA
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- PTM: Mono-, di- and trimethylated by the COMPASS complex to form
CC H3K4me1/2/3. H3K4me activates gene expression by regulating
CC transcription elongation and plays a role in telomere length
CC maintenance. H3K4me enrichment correlates with transcription levels,
CC and occurs in a 5' to 3' gradient with H3K4me3 enrichment at the 5'-end
CC of genes, shifting to H3K4me2 and then H3K4me1. Methylated by SET2 to
CC form H3K36me. H3K36me represses gene expression. Methylated by DOT1 to
CC form H3K79me. H3K79me is required for association of SIR proteins with
CC telomeric regions and for telomeric silencing. The COMPASS-mediated
CC formation of H3K4me2/3 and the DOT1-mediated formation of H3K79me
CC require H2BK123ub1 (By similarity). {ECO:0000250}.
CC -!- PTM: Acetylation of histone H3 leads to transcriptional activation.
CC Acetylated by GCN5 to form H3K14ac. H3K14ac can also be formed by ESA1.
CC H3K56ac formation occurs predominantly in newly synthesized H3
CC molecules during G1, S and G2/M of the cell cycle and may be involved
CC in DNA repair (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
CC -!- CAUTION: To ensure consistency between histone entries, we follow the
CC 'Brno' nomenclature for histone modifications, with positions referring
CC to those used in the literature for the 'closest' model organism. Due
CC to slight variations in histone sequences between organisms and to the
CC presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the
CC actual positions of modified amino acids in the sequence generally
CC differ. In this entry the following conventions are used: H3K4me1/2/3 =
CC mono-, di- and trimethylated Lys-5; H3K9ac = acetylated Lys-12; H3K9me1
CC = monomethylated Lys-12; H3K14ac = acetylated Lys-17; H3K14me2 =
CC dimethylated Lys-17; H3K18ac = acetylated Lys-21; H3K18me1 =
CC monomethylated Lys-21; H3K23ac = acetylated Lys-26; H3K23me1 =
CC monomethylated Lys-26; H3K27ac = acetylated Lys-30; H3K27me1/2/3 =
CC mono-, di- and trimethylated Lys-30; H3K36ac = acetylated Lys-40;
CC H3K36me1/2/3 = mono-, di- and trimethylated Lys-40; H3K56ac =
CC acetylated Lys-62; H3K64ac = acetylated Lys-70; H3K79me1/2/3 = mono-,
CC di- and trimethylated Lys-85. {ECO:0000305}.
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DR EMBL; CR382132; CAG78699.1; -; Genomic_DNA.
DR RefSeq; XP_505888.1; XM_505888.1.
DR AlphaFoldDB; Q6C0C4; -.
DR SMR; Q6C0C4; -.
DR STRING; 4952.CAG78699; -.
DR PRIDE; Q6C0C4; -.
DR EnsemblFungi; CAG78699; CAG78699; YALI0_F25905g.
DR GeneID; 2907691; -.
DR KEGG; yli:YALI0F25905g; -.
DR VEuPathDB; FungiDB:YALI0_F25905g; -.
DR HOGENOM; CLU_078295_4_0_1; -.
DR InParanoid; Q6C0C4; -.
DR OMA; HIVMART; -.
DR Proteomes; UP000001300; Chromosome F.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0009303; P:rRNA transcription; IBA:GO_Central.
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; PS00322; HISTONE_H3_1; 1.
DR PROSITE; PS00959; HISTONE_H3_2; 1.
PE 3: Inferred from homology;
KW Acetylation; Chromosome; DNA-binding; Methylation; Nucleosome core;
KW Nucleus; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..139
FT /note="Histone H3"
FT /id="PRO_0000297755"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 5
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 5
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 12
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 12
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 17
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 17
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 21
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 21
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 26
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 26
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 30
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 30
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 30
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 30
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 42
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 42
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 42
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 42
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 62
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 70
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 85
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 85
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 85
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 139 AA; 15611 MW; 26D019BABA509719 CRC64;
MARTKSTVIA RKVTGGKAPR KQIGSKAARK SAAPSNTSGG VKKPHRYKPG TVALREIRRY
QKSTELLIRK LPFQRLVREI AQDFKTDLRF QSSAIGALQE SVEAYLVSLF EDTNLCAIHA
KRVTIQKKDI HLARRLRGE
