H2A2_ASHGO
ID H2A2_ASHGO Reviewed; 131 AA.
AC Q757L4; Q8J1F9;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Histone H2A.2;
GN Name=HTA2; OrderedLocusNames=AEL003C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-104.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RA Wendland J., Dietrich F.S., Mohr C., Philippsen P.;
RT "Isolation and functional analysis of centromeric DNA of the filamentous
RT ascomycete Ashbya gossypii.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
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: Sumoylation on Lys-126 may lead to transcriptional repression.
CC {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-4; H2AK7ac = acetylated Lys-7; H2AS128ph =
CC phosphorylated Ser-128. {ECO:0000305}.
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DR EMBL; AE016818; AAS52682.1; -; Genomic_DNA.
DR EMBL; AF384989; AAO15409.1; -; Genomic_DNA.
DR RefSeq; NP_984858.1; NM_210212.1.
DR AlphaFoldDB; Q757L4; -.
DR SMR; Q757L4; -.
DR STRING; 33169.AAS52682; -.
DR EnsemblFungi; AAS52682; AAS52682; AGOS_AEL003C.
DR GeneID; 4621057; -.
DR KEGG; ago:AGOS_AEL003C; -.
DR eggNOG; KOG1756; Eukaryota.
DR HOGENOM; CLU_062828_3_1_1; -.
DR InParanoid; Q757L4; -.
DR OMA; FQMAGRG; -.
DR Proteomes; UP000000591; Chromosome V.
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; IBA:GO_Central.
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;
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.2"
FT /id="PRO_0000055206"
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 4
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; 13847 MW; 12E2AD8E4D1539AB CRC64;
MSGKGGKAGS AAKASQSRSA KAGLTFPVGR VHRLLRKGNY AQRIGSGAPV YLTAVLEYLA
AEILELAGNA ARDNKKTRII PRHLQLAIRN DDELNKLLGN VTIAQGGVLP NIHANLLPKK
SAKATKASQE L
