ID H2A2_YEAST Reviewed; 132 AA. AC P04912; D6VPZ9; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 15-MAR-2017, entry version 162. DE RecName: Full=Histone H2A.2; GN Name=HTA2; Synonyms=H2A2; OrderedLocusNames=YBL003C; ORFNames=YBL0103; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7041122; DOI=10.1073/pnas.79.5.1484; 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=ATCC 204508 / S288c; RX PubMed=8091860; DOI=10.1002/yea.320100006; 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=ATCC 204508 / S288c; RX 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 GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., RA Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and RT now."; RL G3 (Bethesda) 4:389-398(2014). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., RA Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., RA Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., RA Kolodner R.D., LaBaer J.; RT "Approaching a complete repository of sequence-verified protein- RT encoding clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [6] RP ACETYLATION AT LYS-5 AND LYS-8. RX PubMed=10082517; DOI=10.1128/MCB.19.4.2515; RA Clarke A.S., Lowell J.E., Jacobson S.J., Pillus L.; RT "Esa1p is an essential histone acetyltransferase required for cell RT cycle progression."; RL Mol. Cell. Biol. 19:2515-2526(1999). RN [7] RP FUNCTION, MUTAGENESIS OF SER-129, AND PHOSPHORYLATION AT SER-129. 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 [8] RP ACETYLATION AT LYS-8. 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 [9] RP ACETYLATION AT SER-2. 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 [10] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX 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 [11] 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 [12] 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 [13] 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 [14] RP SUMOYLATION AT LYS-127. 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 [15] 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). RN [16] RP INTERACTION WITH NAP1, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=18086883; DOI=10.1128/MCB.01035-07; RA Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F., RA Pemberton L.F.; RT "Phosphorylation by casein kinase 2 regulates Nap1 localization and RT function."; RL Mol. Cell. Biol. 28:1313-1325(2008). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth RT phosphoproteome analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [18] RP METHYLATION AT GLN-106. RX PubMed=24352239; DOI=10.1038/nature12819; RA Tessarz P., Santos-Rosa H., Robson S.C., Sylvestersen K.B., RA Nelson C.J., Nielsen M.L., Kouzarides T.; RT "Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated RT modification."; RL Nature 505:564-568(2014). 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. {ECO:0000269|PubMed:11140636, CC ECO:0000269|PubMed:15458641, ECO:0000269|PubMed:15610741, CC ECO:0000269|PubMed:16299494}. 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. Interacts with NAP1. CC {ECO:0000269|PubMed:15610740, ECO:0000269|PubMed:18086883}. 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 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, a component of CC the histone H2A phosphatase complex (HTP-C). Dephosphorylation is CC necessary for efficient recovery from the DNA damage checkpoint. CC {ECO:0000269|PubMed:11140636, ECO:0000269|PubMed:15458641, CC ECO:0000269|PubMed:15610741}. CC -!- PTM: N-acetylated by NAT4. CC -!- PTM: Acetylated by ESA1, a component of the NuA4 histone CC acetyltransferase (HAT) complex, to form H2AK4ac and H2AK7ac. CC -!- PTM: Glutamine methylation at Gln-106 (H2AQ105me) by NOP1 is CC specifically dedicated to polymerase I. It is present at 35S CC ribosomal DNA locus and impairs binding of the FACT complex CC (PubMed:24352239). {ECO:0000269|PubMed:24352239}. CC -!- PTM: Sumoylated to from H2AK126su. May lead to transcriptional CC repression. {ECO:0000269|PubMed:16598039}. CC -!- MISCELLANEOUS: In contrast to vertebrates and insects, its C- CC terminus is not monoubiquitinated. {ECO:0000305}. CC -!- MISCELLANEOUS: Present with 32100 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. 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-8; H2AK126su = sumoylated Lys-127; CC H2AS128ph = phosphorylated Ser-129. {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; 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 EMBL; BK006936; DAA07119.1; -; Genomic_DNA. DR PIR; S05814; HSBYA2. DR RefSeq; NP_009552.1; NM_001178243.1. DR PDB; 4JJN; X-ray; 3.09 A; C/G=2-132. DR PDB; 4KUD; X-ray; 3.20 A; C/G=1-132. DR PDBsum; 4JJN; -. DR PDBsum; 4KUD; -. DR ProteinModelPortal; P04912; -. DR SMR; P04912; -. DR BioGrid; 32699; 303. DR DIP; DIP-6377N; -. DR IntAct; P04912; 158. DR MINT; MINT-637879; -. DR iPTMnet; P04912; -. DR MaxQB; P04912; -. DR PRIDE; P04912; -. DR TopDownProteomics; P04912; -. DR EnsemblFungi; YBL003C; YBL003C; YBL003C. DR GeneID; 852283; -. DR KEGG; sce:YBL003C; -. DR EuPathDB; FungiDB:YBL003C; -. DR SGD; S000000099; HTA2. DR GeneTree; ENSGT00860000133717; -. DR HOGENOM; HOG000234652; -. DR InParanoid; P04912; -. DR KO; K11251; -. DR OMA; YARSEVQ; -. DR OrthoDB; EOG092C5QJX; -. DR BioCyc; YEAST:G3O-28909-MONOMER; -. DR PRO; PR:P04912; -. DR Proteomes; UP000002311; Chromosome II. DR GO; GO:0000788; C:nuclear nucleosome; TAS:SGD. DR GO; GO:0031298; C:replication fork protection complex; IDA:SGD. DR GO; GO:0003677; F:DNA binding; TAS:SGD. DR GO; GO:0006333; P:chromatin assembly or disassembly; TAS:SGD. DR GO; GO:0006342; P:chromatin silencing; IBA:GO_Central. DR GO; GO:0006281; P:DNA repair; IMP:SGD. 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 1: Evidence at protein level; KW 3D-structure; Acetylation; Chromosome; Complete proteome; DNA damage; KW DNA repair; DNA-binding; Isopeptide bond; Methylation; KW Nucleosome core; Nucleus; Phosphoprotein; Reference proteome; KW Ubl conjugation. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:12915400}. FT CHAIN 2 132 Histone H2A.2. FT /FTId=PRO_0000055327. FT MOTIF 129 130 [ST]-Q motif. FT SITE 120 120 Not ubiquitinated. {ECO:0000305}. FT MOD_RES 2 2 N-acetylserine. FT {ECO:0000269|PubMed:12915400}. FT MOD_RES 5 5 N6-acetyllysine. FT {ECO:0000269|PubMed:10082517}. FT MOD_RES 8 8 N6-acetyllysine. FT {ECO:0000269|PubMed:10082517, FT ECO:0000269|PubMed:11545749}. FT MOD_RES 106 106 N5-methylglutamine. FT {ECO:0000269|PubMed:24352239}. FT MOD_RES 129 129 Phosphoserine. FT {ECO:0000244|PubMed:18407956, FT ECO:0000269|PubMed:11140636}. FT CROSSLNK 127 127 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO). FT MUTAGEN 129 129 S->A: Causes hypersensitivity to DNA- FT damage-inducing agents. FT {ECO:0000269|PubMed:11140636}. FT MUTAGEN 129 129 S->E,T: No effect. FT {ECO:0000269|PubMed:11140636}. FT HELIX 19 22 {ECO:0000244|PDB:4JJN}. FT HELIX 29 37 {ECO:0000244|PDB:4JJN}. FT TURN 38 40 {ECO:0000244|PDB:4JJN}. FT STRAND 43 45 {ECO:0000244|PDB:4JJN}. FT HELIX 49 74 {ECO:0000244|PDB:4JJN}. FT STRAND 78 80 {ECO:0000244|PDB:4JJN}. FT HELIX 82 89 {ECO:0000244|PDB:4JJN}. FT HELIX 93 98 {ECO:0000244|PDB:4JJN}. FT TURN 99 101 {ECO:0000244|PDB:4JJN}. FT STRAND 102 104 {ECO:0000244|PDB:4JJN}. FT HELIX 115 117 {ECO:0000244|PDB:4JJN}. SQ SEQUENCE 132 AA; 13989 MW; E808C94A0363CD53 CRC64; MSGGKGGKAG SAAKASQSRS AKAGLTFPVG RVHRLLRRGN YAQRIGSGAP VYLTAVLEYL AAEILELAGN AARDNKKTRI IPRHLQLAIR NDDELNKLLG NVTIAQGGVL PNIHQNLLPK KSAKTAKASQ EL //