ID   H2A1_PICST              Reviewed;         131 AA.
AC   A3LZZ0;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=Histone H2A.1;
GN   Name=HTA2; ORFNames=PICST_37161;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
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       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-7; H2AK126su = sumoylated
CC       Lys-126; H2AS128ph = phosphorylated Ser-128. {ECO:0000305}.
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DR   EMBL; CP000502; ABN68622.1; -; Genomic_DNA.
DR   RefSeq; XP_001386651.1; XM_001386614.1.
DR   AlphaFoldDB; A3LZZ0; -.
DR   SMR; A3LZZ0; -.
DR   STRING; 322104.A3LZZ0; -.
DR   GeneID; 4840891; -.
DR   KEGG; pic:PICST_37161; -.
DR   eggNOG; KOG1756; Eukaryota.
DR   HOGENOM; CLU_062828_3_1_1; -.
DR   InParanoid; A3LZZ0; -.
DR   OMA; VEMDAMS; -.
DR   OrthoDB; 235643at2759; -.
DR   Proteomes; UP000002258; Chromosome 8.
DR   GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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   CDD; cd00074; H2A; 1.
DR   Gene3D; 1.10.20.10; Histone, subunit A; 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; HISTONE H2A; 1.
DR   PANTHER; PTHR23430:SF50; HISTONE H2A; 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; Histone-fold; 1.
DR   PROSITE; PS00046; HISTONE_H2A; 1.
PE   3: Inferred from homology;
KW   Acetylation; Chromosome; DNA damage; DNA repair; DNA-binding;
KW   Isopeptide bond; Methylation; Nucleosome core; Nucleus; Phosphoprotein;
KW   Reference proteome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..131
FT                   /note="Histone H2A.1"
FT                   /id="PRO_0000297740"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           128..129
FT                   /note="[ST]-Q motif"
FT   SITE            119
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         7
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         105
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         128
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        126
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   131 AA;  13948 MW;  7FCE748283C8D4AA CRC64;
     MSGGKGKAGS SEKASTSRSA KAGLTFPVGR VHRLLRKGNY AQRVGSGAPV YLTSVLEYLA
     AEILELAGNA ARDNKKSRII PRHLQLAIRN DEELNKLLGH VTIAQGGVLP NIHQNLLPKK
     SGKSAKASQE L
//