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 30-NOV-2016, entry version 64. 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., RA Wortman J.R., Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., RA Zeng Q., Hung C.-Y., McMahan C., Muszewska A., Grynberg M., RA Mandel M.A., Kellner E.M., Barker B.M., Galgiani J.N., Orbach M.J., RA Kirkland T.N., Cole G.T., Henn M.R., Birren B.W., Taylor J.W.; RT "Comparative genomic analyses of the human fungal pathogens RT Coccidioides 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 CC in DNA double strand break (DSB) repair. 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. Chromosome. CC -!- DOMAIN: The [ST]-Q motif constitutes a recognition sequence for CC kinases from the PI3/PI4-kinase family. CC -!- PTM: Phosphorylated to form H2AS128ph (gamma-H2A) in response to CC DNA double-strand breaks (DSBs) generated by exogenous genotoxic CC agents and by stalled replication forks. Phosphorylation is CC dependent on the DNA damage checkpoint kinases MEC1/ATR and CC TEL1/ATM, spreads on either side of a detected DSB site and may CC mark the surrounding chromatin for recruitment of proteins CC required for DNA damage signaling and repair. Gamma-H2A is removed CC from the DNA prior to the strand invasion-primer extension step of CC 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. CC {ECO:0000250}. CC -!- MISCELLANEOUS: In contrast to vertebrates and insects, its C- CC terminus 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 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: H2AK4ac = acetylated Lys-5; CC H2AK7ac = acetylated Lys-9; H2AS128ph = phosphorylated Ser-130. CC {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 ProteinModelPortal; Q1E5N1; -. DR STRING; 246410.XP_001248361.1; -. DR PRIDE; Q1E5N1; -. DR EnsemblFungi; EAS36778; EAS36778; CIMG_02132. DR GeneID; 4568207; -. DR KEGG; cim:CIMG_02132; -. DR EuPathDB; FungiDB:CIMG_02132; -. DR eggNOG; KOG1756; Eukaryota. DR eggNOG; COG5262; LUCA. DR InParanoid; Q1E5N1; -. DR KO; K11251; -. DR OrthoDB; EOG092C5QJX; -. 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:0006281; P:DNA repair; IEA:UniProtKB-KW. 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; Complete proteome; DNA damage; DNA repair; KW DNA-binding; Methylation; Nucleosome core; Nucleus; Phosphoprotein; KW Reference proteome. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 133 Histone H2A. FT /FTId=PRO_0000297733. FT MOTIF 130 131 [ST]-Q motif. FT SITE 120 120 Not ubiquitinated. {ECO:0000305}. FT MOD_RES 5 5 N6-acetyllysine. {ECO:0000250}. FT MOD_RES 9 9 N6-acetyllysine. {ECO:0000250}. FT MOD_RES 106 106 N5-methylglutamine. {ECO:0000250}. FT MOD_RES 130 130 Phosphoserine. {ECO:0000250}. SQ SEQUENCE 133 AA; 14219 MW; AA0FA27D95C01F8D CRC64; MTGGKSGGKA SGSKSSQSRS SKAGLAFPVG RVHRLLRKGN YAQRVGAGAP VYLAAVLEYL AAEILELAGN AARDNKKTRI IPRHLQLAIR NDEELNKLLG HVTIAQGGVM PYIHQNLLPK KTPKTGKNPS QEL //