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 29-SEP-2021, entry version 196. 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; Saccharomycetes; OC 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 II: RT 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; DOI=10.1002/j.1460-2075.1994.tb06923.x; 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., Glansdorff N., RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., RA 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., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and 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., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT 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 cycle RT 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 in RT 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-terminal RT 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., Dephoure N., RA 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., Petrini J.H.J., RA Haber J.E., Lichten M.; RT "Distribution and dynamics of chromatin modification induced by a defined RT 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., Haber J.E., RA 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 H2A at RT 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., Dokmanovic M., RA Dorsey J.A., Whelan K.A., Krsmanovic M., Lane W.S., Meluh P.B., RA Johnson E.S., Berger S.L.; RT "Histone sumoylation is a negative regulator in Saccharomyces cerevisiae RT and shows dynamic interplay with positive-acting histone 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., Lieberman J., RA Shen X., Buratowski S., Haber J.E., Durocher D., Greenblatt J.F., RA 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 BY RP 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 phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [18] RP SUCCINYLATION AT LYS-14 AND LYS-22, AND MALONYLATION AT LYS-120. RX PubMed=22389435; DOI=10.1074/mcp.m111.015875; RA Xie Z., Dai J., Dai L., Tan M., Cheng Z., Wu Y., Boeke J.D., Zhao Y.; RT "Lysine succinylation and lysine malonylation in histones."; RL Mol. Cell. Proteomics 11:100-107(2012). RN [19] RP METHYLATION AT GLN-106. RX PubMed=24352239; DOI=10.1038/nature12819; RA Tessarz P., Santos-Rosa H., Robson S.C., Sylvestersen K.B., Nelson C.J., RA 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 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. {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 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. Interacts with NAP1. {ECO:0000269|PubMed:15610740, CC ECO:0000269|PubMed:18086883}. 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 interacts with ARP4, a shared component of the NuA4 histone CC acetyltransferase complex and the INO80 and SWR1 chromatin remodeling CC complexes, and serves to recruit first NuA4, mediating histone H4 CC acetylation, and subsequently the INO80/SWR1 complexes, facilitating CC DNA resection, to DSB sites. Gamma-H2A is required for sequestering CC cohesin around the break site, which is important for efficient post- CC replicative double-strand break repair by homologous recombination, CC holding the damaged chromatid close to its undamaged sister template. 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. {ECO:0000269|PubMed:11140636, CC ECO:0000269|PubMed:15458641, 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 ribosomal CC DNA locus and impairs binding of the FACT complex (PubMed:24352239). CC {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-terminus CC 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 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-8; H2AK126su = sumoylated CC Lys-127; 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 SMR; P04912; -. DR BioGRID; 32699; 320. DR ComplexPortal; CPX-1610; Nucleosome, variant HTA2-HTB2. DR ComplexPortal; CPX-1611; Nucleosome, variant HTA2-HTB1. DR DIP; DIP-6377N; -. DR IntAct; P04912; 162. DR MINT; P04912; -. DR STRING; 4932.YBL003C; -. DR iPTMnet; P04912; -. DR MaxQB; P04912; -. DR PaxDb; P04912; -. DR PRIDE; P04912; -. DR TopDownProteomics; P04912; -. DR EnsemblFungi; YBL003C_mRNA; YBL003C; YBL003C. DR GeneID; 852283; -. DR KEGG; sce:YBL003C; -. DR SGD; S000000099; HTA2. DR VEuPathDB; FungiDB:YBL003C; -. DR eggNOG; KOG1756; Eukaryota. DR GeneTree; ENSGT00940000153118; -. DR HOGENOM; CLU_062828_3_0_1; -. DR InParanoid; P04912; -. DR OMA; VMPYIHP; -. DR PRO; PR:P04912; -. DR Proteomes; UP000002311; Chromosome II. DR RNAct; P04912; protein. DR GO; GO:0000786; C:nucleosome; TAS:SGD. DR GO; GO:0031298; C:replication fork protection complex; IDA:SGD. DR GO; GO:0003677; F:DNA binding; IBA:GO_Central. DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro. 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 CDD; cd00074; H2A; 1. DR Gene3D; 1.10.20.10; -; 1. DR IDEAL; IID50137; -. 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; 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:0000269|PubMed:12915400" FT CHAIN 2..132 FT /note="Histone H2A.2" FT /id="PRO_0000055327" FT MOTIF 129..130 FT /note="[ST]-Q motif" FT SITE 120 FT /note="Not ubiquitinated" FT /evidence="ECO:0000305" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000269|PubMed:12915400" FT MOD_RES 5 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:10082517" FT MOD_RES 8 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:10082517, FT ECO:0000269|PubMed:11545749" FT MOD_RES 14 FT /note="N6-succinyllysine" FT /evidence="ECO:0000269|PubMed:22389435" FT MOD_RES 22 FT /note="N6-succinyllysine" FT /evidence="ECO:0000269|PubMed:22389435" FT MOD_RES 106 FT /note="N5-methylglutamine" FT /evidence="ECO:0000269|PubMed:24352239" FT MOD_RES 120 FT /note="N6-malonyllysine" FT /evidence="ECO:0000269|PubMed:22389435" FT MOD_RES 129 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:11140636, FT ECO:0007744|PubMed:18407956" FT CROSSLNK 127 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT MUTAGEN 129 FT /note="S->A: Causes hypersensitivity to DNA-damage-inducing FT agents." FT /evidence="ECO:0000269|PubMed:11140636" FT MUTAGEN 129 FT /note="S->E,T: No effect." FT /evidence="ECO:0000269|PubMed:11140636" FT HELIX 19..22 FT /evidence="ECO:0007829|PDB:4JJN" FT HELIX 29..37 FT /evidence="ECO:0007829|PDB:4JJN" FT TURN 38..40 FT /evidence="ECO:0007829|PDB:4JJN" FT STRAND 43..45 FT /evidence="ECO:0007829|PDB:4JJN" FT HELIX 49..74 FT /evidence="ECO:0007829|PDB:4JJN" FT STRAND 78..80 FT /evidence="ECO:0007829|PDB:4JJN" FT HELIX 82..89 FT /evidence="ECO:0007829|PDB:4JJN" FT HELIX 93..98 FT /evidence="ECO:0007829|PDB:4JJN" FT TURN 99..101 FT /evidence="ECO:0007829|PDB:4JJN" FT STRAND 102..104 FT /evidence="ECO:0007829|PDB:4JJN" FT HELIX 115..117 FT /evidence="ECO:0007829|PDB:4JJN" SQ SEQUENCE 132 AA; 13989 MW; E808C94A0363CD53 CRC64; MSGGKGGKAG SAAKASQSRS AKAGLTFPVG RVHRLLRRGN YAQRIGSGAP VYLTAVLEYL AAEILELAGN AARDNKKTRI IPRHLQLAIR NDDELNKLLG NVTIAQGGVL PNIHQNLLPK KSAKTAKASQ EL //