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H2A1_CANGA
ID   H2A1_CANGA              Reviewed;         131 AA.
AC   Q6FWM7;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Histone H2A.1;
GN   Name=HTA1; OrderedLocusNames=CAGL0C04411g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
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., 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 which plays a central role in
CC       DNA double strand break (DSB) repair. Nucleosomes wrap and compact DNA
CC       into chromatin, limiting DNA accessibility to the cellular machineries
CC       which require DNA as a template. Histones thereby play a central role
CC       in transcription regulation, DNA repair, DNA replication and
CC       chromosomal stability. DNA accessibility is regulated via a complex set
CC       of post-translational modifications of histones, also called histone
CC       code, and nucleosome remodeling.
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
CC       DNA.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC   -!- DOMAIN: The [ST]-Q motif constitutes a recognition sequence for kinases
CC       from the PI3/PI4-kinase family.
CC   -!- PTM: Phosphorylated to form H2AS128ph (gamma-H2A) in response to DNA
CC       double-strand breaks (DSBs) generated by exogenous genotoxic agents and
CC       by stalled replication forks. Phosphorylation is dependent on the DNA
CC       damage checkpoint kinases MEC1/ATR and TEL1/ATM, spreads on either side
CC       of a detected DSB site and may mark the surrounding chromatin for
CC       recruitment of proteins required for DNA damage signaling and repair.
CC       Gamma-H2A is removed from the DNA prior to the strand invasion-primer
CC       extension step of the repair process and subsequently dephosphorylated
CC       by PPH3, a component of the histone H2A phosphatase complex (HTP-C).
CC       Dephosphorylation is necessary for efficient recovery from the DNA
CC       damage checkpoint (By similarity). {ECO:0000250}.
CC   -!- PTM: Acetylated by ESA1 to form H2AK4ac and H2AK7ac. {ECO:0000250}.
CC   -!- MISCELLANEOUS: In contrast to vertebrates and insects, its C-terminus
CC       is not monoubiquitinated. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the histone H2A 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: H2AK4ac =
CC       acetylated Lys-5; H2AK7ac = acetylated Lys-8; H2AS128ph =
CC       phosphorylated Ser-128. {ECO:0000305}.
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DR   EMBL; CR380949; CAG58273.1; -; Genomic_DNA.
DR   RefSeq; XP_445367.1; XM_445367.1.
DR   AlphaFoldDB; Q6FWM7; -.
DR   SMR; Q6FWM7; -.
DR   STRING; 5478.XP_445367.1; -.
DR   EnsemblFungi; CAG58273; CAG58273; CAGL0C04411g.
DR   GeneID; 2886776; -.
DR   KEGG; cgr:CAGL0C04411g; -.
DR   CGD; CAL0127584; CAGL0C04411g.
DR   VEuPathDB; FungiDB:CAGL0C04411g; -.
DR   eggNOG; KOG1756; Eukaryota.
DR   HOGENOM; CLU_062828_3_0_1; -.
DR   InParanoid; Q6FWM7; -.
DR   OMA; VMPYIHP; -.
DR   Proteomes; UP000002428; Chromosome C.
DR   GO; GO:0005576; C:extracellular region; IDA:CGD.
DR   GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
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:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR   GO; GO:0061587; P:transfer RNA gene-mediated silencing; IEA:EnsemblFungi.
DR   CDD; cd00074; H2A; 1.
DR   Gene3D; 1.10.20.10; -; 1.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR002119; Histone_H2A.
DR   InterPro; IPR007125; Histone_H2A/H2B/H3.
DR   InterPro; IPR032454; Histone_H2A_C.
DR   InterPro; IPR032458; Histone_H2A_CS.
DR   PANTHER; PTHR23430; PTHR23430; 1.
DR   Pfam; PF00125; Histone; 1.
DR   Pfam; PF16211; Histone_H2A_C; 1.
DR   PRINTS; PR00620; HISTONEH2A.
DR   SMART; SM00414; H2A; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
DR   PROSITE; PS00046; HISTONE_H2A; 1.
PE   3: Inferred from homology;
KW   Acetylation; Chromosome; DNA damage; DNA repair; DNA-binding; Methylation;
KW   Nucleosome core; Nucleus; Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..131
FT                   /note="Histone H2A.1"
FT                   /id="PRO_0000055212"
FT   MOTIF           128..129
FT                   /note="[ST]-Q motif"
FT   SITE            120
FT                   /note="Not ubiquitinated"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         5
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         8
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         106
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         128
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   131 AA;  13873 MW;  B3E1DC2B0D30652D CRC64;
     MSGGKGGKAG SAAKASQTRS AKAGLTFPVG RVHRLLRRGN YAQRIGSGAP VYLTAVLEYL
     AAEILELAGN AARDNKKSRI IPRHLQLAIR NDDELNKLLG NVTIAQGGVL PNIHQNLLPK
     KSAKPSASQE L
 
 
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