ID H2A_COCIM Reviewed; 133 AA. AC Q1E5N1; J3KL19; DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot. DT 11-JUL-2006, sequence version 1. DT 02-JUN-2021, entry version 78. DE RecName: Full=Histone H2A; GN Name=HTA1; ORFNames=CIMG_02132; OS Coccidioides immitis (strain RS) (Valley fever fungus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Coccidioides. OX NCBI_TaxID=246410; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RS; RX PubMed=19717792; DOI=10.1101/gr.087551.108; RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R., RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y., RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M., RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T., RA Henn M.R., Birren B.W., Taylor J.W.; RT "Comparative genomic analyses of the human fungal pathogens Coccidioides RT and their relatives."; RL Genome Res. 19:1722-1731(2009). RN [2] RP GENOME REANNOTATION. RC STRAIN=RS; RX PubMed=20516208; DOI=10.1101/gr.103911.109; RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J., RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D., RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A., RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J., RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R., RA Taylor J.W., Rounsley S.D.; RT "Population genomic sequencing of Coccidioides fungi reveals recent RT hybridization and transposon control."; RL Genome Res. 20:938-946(2010). 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-9; H2AS128ph = CC phosphorylated Ser-130. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; GG704911; EAS36778.3; -; Genomic_DNA. DR RefSeq; XP_001248361.1; XM_001248360.2. DR SMR; Q1E5N1; -. DR EnsemblFungi; EAS36778; EAS36778; CIMG_02132. DR GeneID; 4568207; -. DR KEGG; cim:CIMG_02132; -. DR VEuPathDB; FungiDB:CIMG_02132; -. DR InParanoid; Q1E5N1; -. DR OMA; ELAHNTC; -. DR OrthoDB; 1504122at2759; -. DR Proteomes; UP000001261; Unassembled WGS sequence. 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:0006281; P:DNA repair; IEA:UniProtKB-KW. 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 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..133 FT /note="Histone H2A" FT /id="PRO_0000297733" FT REGION 1..25 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 130..131 FT /note="[ST]-Q motif" FT COMPBIAS 1..23 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 120 FT /note="Not ubiquitinated" FT /evidence="ECO:0000305" FT MOD_RES 5 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250" FT MOD_RES 9 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250" FT MOD_RES 106 FT /note="N5-methylglutamine" FT /evidence="ECO:0000250" FT MOD_RES 130 FT /note="Phosphoserine" FT /evidence="ECO:0000250" SQ SEQUENCE 133 AA; 14219 MW; AA0FA27D95C01F8D CRC64; MTGGKSGGKA SGSKSSQSRS SKAGLAFPVG RVHRLLRKGN YAQRVGAGAP VYLAAVLEYL AAEILELAGN AARDNKKTRI IPRHLQLAIR NDEELNKLLG HVTIAQGGVM PYIHQNLLPK KTPKTGKNPS QEL //