ID H2A2_YEAST STANDARD; PRT; 131 AA. AC P04912; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-1987, sequence version 1. DT 27-JUN-2006, entry version 69. DE Histone H2A.2. GN Name=HTA2; Synonyms=H2A2; OrderedLocusNames=YBL003C; ORFNames=YBL0103; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=82174624; PubMed=7041122; RA Choe J., Kolodrubetz D., Grunstein M.; RT "The two yeast histone H2A genes encode similar protein subtypes."; RL Proc. Natl. Acad. Sci. U.S.A. 79:1484-1487(1982). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=S288c; RX MEDLINE=94378721; PubMed=8091860; RA Wolfe K.H., Lohan A.J.E.; RT "Sequence around the centromere of Saccharomyces cerevisiae chromosome RT II: similarity of CEN2 to CEN4."; RL Yeast 10:S41-S46(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S288c; RX MEDLINE=95112788; PubMed=7813418; RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H., RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., RA Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., RA Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., RA Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., RA Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., RA Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., RA Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., RA Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., RA Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., RA Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., RA Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., RA van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., RA Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., RA Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.; RT "Complete DNA sequence of yeast chromosome II."; RL EMBO J. 13:5795-5809(1994). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=S288c; RA Marsischky G., Rolfs A., Richardson A., Kane M., Baqui M., Taycher E., RA Hu Y., Vannberg F., Weger J., Kramer J., Moreira D., Kelley F., RA Zuo D., Raphael J., Hogle C., Jepson D., Williamson J., Camargo A., RA Gonzaga L., Vasconcelos A.T., Simpson A., Kolodner R., Harlow E., RA LaBaer J.; RT "Creation of the YFLEX clone resource: cloning of Saccharomyces RT cerevisiae ORFs in the Gateway recombinational cloning system."; RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP FUNCTION, MUTAGENESIS OF SER-128, AND PHOSPHORYLATION AT SER-128. RX PubMed=11140636; DOI=10.1038/35050000; RA Downs J.A., Lowndes N.F., Jackson S.P.; RT "A role for Saccharomyces cerevisiae histone H2A in DNA repair."; RL Nature 408:1001-1004(2000). RN [6] RP ACETYLATION AT LYS-7. RX PubMed=11545749; DOI=10.1016/S1097-2765(01)00301-X; RA Suka N., Suka Y., Carmen A.A., Wu J., Grunstein M.; RT "Highly specific antibodies determine histone acetylation site usage RT in yeast heterochromatin and euchromatin."; RL Mol. Cell 8:473-479(2001). RN [7] RP ACETYLATION AT SER-1. RX PubMed=12915400; DOI=10.1074/jbc.C300355200; RA Song O.-K., Wang X., Waterborg J.H., Sternglanz R.; RT "An Nalpha-acetyltransferase responsible for acetylation of the N- RT terminal residues of histones H4 and H2A."; RL J. Biol. Chem. 278:38109-38112(2003). RN [8] RP LEVEL OF PROTEIN EXPRESSION. RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [9] RP FUNCTION, AND PHOSPHORYLATION. RX PubMed=15458641; DOI=10.1016/j.cub.2004.09.047; RA Shroff R., Arbel-Eden A., Pilch D.R., Ira G., Bonner W.M., RA Petrini J.H.J., Haber J.E., Lichten M.; RT "Distribution and dynamics of chromatin modification induced by a RT defined DNA double-strand break."; RL Curr. Biol. 14:1703-1711(2004). RN [10] RP FUNCTION, AND PHOSPHORYLATION. RX PubMed=15610741; DOI=10.1016/j.molcel.2004.11.027; RA Uenal E., Arbel-Eden A., Sattler U., Shroff R., Lichten M., RA Haber J.E., Koshland D.; RT "DNA damage response pathway uses histone modification to assemble a RT double-strand break-specific cohesin domain."; RL Mol. Cell 16:991-1002(2004). RN [11] RP INTERACTION WITH ARP4. RX PubMed=15610740; DOI=10.1016/j.molcel.2004.12.003; RA Downs J.A., Allard S., Jobin-Robitaille O., Javaheri A., Auger A., RA Bouchard N., Kron S.J., Jackson S.P., Cote J.; RT "Binding of chromatin-modifying activities to phosphorylated histone RT H2A at DNA damage sites."; RL Mol. Cell 16:979-990(2004). RN [12] RP SUMOYLATION AT LYS-126. RX PubMed=16598039; DOI=10.1101/gad.1404206; RA Nathan D., Ingvarsdottir K., Sterner D.E., Bylebyl G.R., RA Dokmanovic M., Dorsey J.A., Whelan K.A., Krsmanovic M., Lane W.S., RA Meluh P.B., Johnson E.S., Berger S.L.; RT "Histone sumoylation is a negative regulator in Saccharomyces RT cerevisiae and shows dynamic interplay with positive-acting histone RT modifications."; RL Genes Dev. 20:966-976(2006). RN [13] RP FUNCTION, AND DEPHOSPHORYLATION. RX PubMed=16299494; DOI=10.1038/nature04384; RA Keogh M.-C., Kim J.-A., Downey M., Fillingham J., Chowdhury D., RA Harrison J.C., Onishi M., Datta N., Galicia S., Emili A., RA Lieberman J., Shen X., Buratowski S., Haber J.E., Durocher D., RA Greenblatt J.F., Krogan N.J.; RT "A phosphatase complex that dephosphorylates gamma-H2AX regulates DNA RT damage checkpoint recovery."; RL Nature 439:497-501(2006). CC -!- FUNCTION: Involved in DNA double strand break (DSB) repair. CC -!- SUBUNIT: The nucleosome is an octamer containing two molecules CC each of H2A, H2B, H3 and H4. The octamer wraps approximately 146 CC bp of DNA. H2A interacts with ARP4 when phosphorylated on Ser-128. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- DOMAIN: The [ST]-Q motif constitutes a recognition sequence for CC kinases from the PI3/PI4-kinase family. CC -!- PTM: Phosphorylated on Ser-128 (to form 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 interacts CC with ARP4, a shared component of the NuA4 histone CC acetyltransferase complex and the INO80 and SWR1 chromatin CC remodeling complexes, and serves to recruit first NuA4, mediating CC histone H4 acetylation, and subsequently the INO80/SWR1 complexes, CC facilitating DNA resection, to DSB sites. Gamma-H2A is required CC for sequestering cohesin around the break site, which is important CC for efficient post-replicative double-strand break repair by CC homologous recombination, holding the damaged chromatid close to CC its undamaged sister template. Gamma-H2A is removed from the DNA CC prior to the strand invasion-primer extension step of the repair CC process and subsequently dephosphorylated by PPH3 as part of the CC histone H2A phosphatase complex (HTP-C). Dephosphorylation is CC necessary for efficient recovery from the DNA damage checkpoint. CC -!- PTM: N-acetylated by NAT4. CC -!- PTM: Sumoylation on Lys-126 may lead to transcriptional CC repression. CC -!- MISCELLANEOUS: In contrast to vertebrates and insects, its C- CC terminus is not monoubiquitinated (Probable). CC -!- MISCELLANEOUS: Present with 32100 molecules/cell. CC -!- SIMILARITY: Belongs to the histone H2A family. 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; V01305; CAA24612.1; -; Genomic_DNA. DR EMBL; Z26494; CAA81267.1; -; Genomic_DNA. DR EMBL; Z35764; CAA84818.1; -; Genomic_DNA. DR EMBL; AY693115; AAT93134.1; -; Genomic_DNA. DR PIR; S05814; HSBYA2. DR HSSP; P04911; 1ID3. DR SMR; P04912; 13-120. DR IntAct; P04912; -. DR GermOnline; 138438; -. DR Ensembl; YBL003C; Saccharomyces cerevisiae. DR GenomeReviews; Y13134_GR; YBL003C. DR SGD; S000000099; HTA2. DR LinkHub; P04912; -. DR GO; GO:0000788; C:nuclear nucleosome; TAS. DR GO; GO:0003677; F:DNA binding; TAS. DR GO; GO:0006333; P:chromatin assembly or disassembly; TAS. DR GO; GO:0006281; P:DNA repair; IMP. DR InterPro; IPR007124; Hist_TAF. DR InterPro; IPR009072; Histone-fold. DR InterPro; IPR007125; Histone_core_D. DR InterPro; IPR002119; Histone_H2A. DR Pfam; PF00125; Histone; 1. DR PRINTS; PR00620; HISTONEH2A. DR ProDom; PD000522; Histone_H2A; 1. DR SMART; SM00414; H2A; 1. DR PROSITE; PS00046; HISTONE_H2A; 1. KW Acetylation; Chromosomal protein; Complete proteome; DNA damage; KW DNA repair; DNA-binding; Nuclear protein; Nucleosome core; KW Phosphorylation; Ubl conjugation. FT INIT_MET 0 0 FT CHAIN 1 131 Histone H2A.2. FT /FTId=PRO_0000055327. FT MOTIF 128 129 [ST]-Q motif. FT SITE 119 119 Not ubiquitinated (Probable). FT MOD_RES 1 1 N-acetylserine. FT MOD_RES 7 7 N6-acetyllysine. FT MOD_RES 128 128 Phosphoserine (By similarity). FT CROSSLNK 126 126 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO). FT MUTAGEN 128 128 S->A: Causes hypersensitivity to DNA- FT damage-inducing agents. FT MUTAGEN 128 128 S->E,T: No effect. SQ SEQUENCE 131 AA; 13858 MW; E857F073CA053D53 CRC64; SGGKGGKAGS AAKASQSRSA KAGLTFPVGR VHRLLRRGNY AQRIGSGAPV YLTAVLEYLA AEILELAGNA ARDNKKTRII PRHLQLAIRN DDELNKLLGN VTIAQGGVLP NIHQNLLPKK SAKTAKASQE L //