(data stored in ACNUC8465 zone)

SWISSPROT: H3_CANGA

ID   H3_CANGA                Reviewed;         136 AA.
AC   P61833; Q8NJS5;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   30-AUG-2017, entry version 96.
DE   RecName: Full=Histone H3;
GN   Name=HHT1; OrderedLocusNames=CAGL0C04114g;
GN   and
GN   Name=HHT2; OrderedLocusNames=CAGL0H09856g;
GN   and
GN   Name=HHT3; OrderedLocusNames=CAGL0M06655g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=12093907; DOI=10.1073/pnas.142101099;
RA   Wong S., Butler G., Wolfe K.H.;
RT   "Gene order evolution and paleopolyploidy in hemiascomycete yeasts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9272-9277(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   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
CC       compact DNA into chromatin, limiting DNA accessibility to the
CC       cellular machineries which require DNA as a template. Histones
CC       thereby play a central role in transcription regulation, DNA
CC       repair, DNA replication and chromosomal stability. DNA
CC       accessibility is regulated via a complex set of post-translational
CC       modifications of histones, also called histone code, and
CC       nucleosome remodeling.
CC   -!- SUBUNIT: The nucleosome is a histone octamer containing two
CC       molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4
CC       heterotetramer and two H2A-H2B heterodimers. The octamer wraps
CC       approximately 147 bp of DNA.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylated by IPL1 to form H3S10ph. H3S10ph promotes
CC       subsequent H3K14ac formation by GCN5 and is required for
CC       transcriptional activation through TBP recruitment to the
CC       promoters (By similarity). {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
CC       levels, and occurs in a 5' to 3' gradient with H3K4me3 enrichment
CC       at the 5'-end of genes, shifting to H3K4me2 and then H3K4me1.
CC       Methylated by SET2 to form H3K36me. H3K36me represses gene
CC       expression. Methylated by DOT1 to form H3K79me. H3K79me is
CC       required for association of SIR proteins with telomeric regions
CC       and for telomeric silencing. The COMPASS-mediated formation of
CC       H3K4me2/3 and the DOT1-mediated formation of H3K79me require
CC       H2BK123ub1 (By similarity). {ECO:0000250}.
CC   -!- PTM: Acetylation of histone H3 leads to transcriptional
CC       activation. H3K14ac formation by GCN5 is promoted by H3S10ph.
CC       H3K14ac can also be formed by ESA1. H3K56ac formation occurs
CC       predominantly in newly synthesized H3 molecules during G1, S and
CC       G2/M of the cell cycle and may be involved in DNA repair (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
CC   -!- CAUTION: To ensure consistency between histone entries, we follow
CC       the 'Brno' nomenclature for histone modifications, with positions
CC       referring to those used in the literature for the 'closest' model
CC       organism. Due to slight variations in histone sequences between
CC       organisms and to the presence of initiator methionine in
CC       UniProtKB/Swiss-Prot sequences, the actual positions of modified
CC       amino acids in the sequence generally differ. In this entry the
CC       following conventions are used: H3K4me1/2/3 = mono-, di- and
CC       trimethylated Lys-5; H3K9ac = acetylated Lys-10; H3K9me1 =
CC       monomethylated Lys-10; H3S10ph = phosphorylated Ser-11; H3K14ac =
CC       acetylated Lys-15; H3K14me2 = dimethylated Lys-15; H3K18ac =
CC       acetylated Lys-19; H3K18me1 = monomethylated Lys-19; H3K23ac =
CC       acetylated Lys-24; H3K23me1 = monomethylated Lys-24; H3K27ac =
CC       acetylated Lys-28; H3K27me1/2/3 = mono-, di- and trimethylated
CC       Lys-28; H3K36ac = acetylated Lys-37; H3K36me1/2/3 = mono-, di- and
CC       trimethylated Lys-37; H3K56ac = acetylated Lys-57; H3K64ac =
CC       acetylated Lys-65; H3K79me1/2/3 = mono-, di- and trimethylated
CC       Lys-80. {ECO:0000305}.
DR   EMBL; AF520060; AAM74211.1; -; Genomic_DNA.
DR   EMBL; AF520061; AAM74217.1; -; Genomic_DNA.
DR   EMBL; CR380949; CAG58260.1; -; Genomic_DNA.
DR   EMBL; CR380954; CAG60159.1; -; Genomic_DNA.
DR   EMBL; CR380959; CAG62613.1; -; Genomic_DNA.
DR   RefSeq; XP_445354.1; XM_445354.1.
DR   RefSeq; XP_447226.1; XM_447226.1.
DR   RefSeq; XP_449637.1; XM_449637.1.
DR   ProteinModelPortal; P61833; -.
DR   SMR; P61833; -.
DR   STRING; 284593.XP_449637.1; -.
DR   EnsemblFungi; CAG58260; CAG58260; CAGL0C04114g.
DR   EnsemblFungi; CAG60159; CAG60159; CAGL0H09856g.
DR   EnsemblFungi; CAG62613; CAG62613; CAGL0M06655g.
DR   KEGG; cgr:CAGL0C04114g; -.
DR   KEGG; cgr:CAGL0H09856g; -.
DR   KEGG; cgr:CAGL0M06655g; -.
DR   CGD; CAL0130591; CAGL0H09856g.
DR   CGD; CAL0136971; CAGL0M06655g.
DR   CGD; CAL0127444; HHT2.
DR   eggNOG; KOG1745; Eukaryota.
DR   eggNOG; COG2036; LUCA.
DR   HOGENOM; HOG000155290; -.
DR   InParanoid; P61833; -.
DR   KO; K11253; -.
DR   OMA; KRIEPEY; -.
DR   OrthoDB; EOG092C5B6S; -.
DR   Proteomes; UP000002428; Chromosome C.
DR   Proteomes; UP000002428; Chromosome H.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0043505; C:CENP-A containing nucleosome; IEA:EnsemblFungi.
DR   GO; GO:0031298; C:replication fork protection complex; IEA:EnsemblFungi.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0070911; P:global genome nucleotide-excision repair; IEA:EnsemblFungi.
DR   GO; GO:0009303; P:rRNA transcription; IEA:EnsemblFungi.
DR   GO; GO:0043935; P:sexual sporulation resulting in formation of a cellular spore; IEA:EnsemblFungi.
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;
DR   PRODOM; P61833.
DR   SWISS-2DPAGE; P61833.
KW   Acetylation; Chromosome; Complete proteome; DNA-binding; Methylation;
KW   Nucleosome core; Nucleus; Phosphoprotein; Reference proteome.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    136       Histone H3.
FT                                /FTId=PRO_0000221358.
FT   MOD_RES       5      5       N6,N6,N6-trimethyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES       5      5       N6,N6-dimethyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES       5      5       N6-methyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES      10     10       N6-acetyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES      10     10       N6-methyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES      11     11       Phosphoserine. {ECO:0000250}.
FT   MOD_RES      15     15       N6,N6-dimethyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES      15     15       N6-acetyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES      15     15       N6-methyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES      19     19       N6-acetyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES      19     19       N6-methyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES      24     24       N6-acetyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES      24     24       N6-methyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES      28     28       N6,N6,N6-trimethyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES      28     28       N6,N6-dimethyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES      28     28       N6-acetyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES      28     28       N6-methyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES      37     37       N6,N6,N6-trimethyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES      37     37       N6,N6-dimethyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES      37     37       N6-acetyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES      37     37       N6-methyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES      57     57       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES      65     65       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES      80     80       N6,N6,N6-trimethyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES      80     80       N6,N6-dimethyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES      80     80       N6-methyllysine; alternate.
FT                                {ECO:0000250}.
FT   CONFLICT    123    123       K -> N (in Ref. 1; AAM74217).
FT                                {ECO:0000305}.
SQ   SEQUENCE   136 AA;  15356 MW;  A6115FEB480AC67A CRC64;
     MARTKQTARK STGGKAPRKQ LASKAARKSA PSTGGVKKPH RYKPGTVALR EIRRFQKSTE
     LLIRKLPFQR LVREIAQDFK TDLRFQSSAI GALQESVEAY LVSLFEDTNL AAIHAKRVTI
     QKKDIKLARR LRGERS
//

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