H2AZ_YEAST
ID H2AZ_YEAST Reviewed; 134 AA.
AC Q12692; D6W255;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Histone H2A.Z {ECO:0000303|PubMed:16543223};
GN Name=HTZ1 {ECO:0000303|PubMed:11090616};
GN Synonyms=H2AZ {ECO:0000303|PubMed:16543223}, HTA3;
GN OrderedLocusNames=YOL012C; ORFNames=O2345;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [2]
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 [3]
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 [4]
RP PROTEIN SEQUENCE OF 2-21, ACETYLATION AT SER-2; LYS-4; LYS-9; LYS-11 AND
RP LYS-15, IDENTIFICATION BY MASS SPECTROMETRY, AND FUNCTION.
RX PubMed=16543223; DOI=10.1101/gad.1395506;
RA Millar C.B., Xu F., Zhang K., Grunstein M.;
RT "Acetylation of H2AZ Lys 14 is associated with genome-wide gene activity in
RT yeast.";
RL Genes Dev. 20:711-722(2006).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [6]
RP SIMILARITY TO VARIANT H2A, AND GENE NAME.
RX PubMed=9009827; DOI=10.1016/s0968-0004(96)20028-3;
RA Jackson J.D., Falciano V.T., Gorovsky M.A.;
RT "A likely histone H2A.F/Z variant in Saccharomyces cerevisiae.";
RL Trends Biochem. Sci. 21:466-467(1996).
RN [7]
RP FUNCTION.
RX PubMed=11081628; DOI=10.1016/s0092-8674(00)00133-1;
RA Santisteban M.S., Kalashnikova T., Smith M.M.;
RT "Histone H2A.Z regulates transcription and is partially redundant with
RT nucleosome remodeling complexes.";
RL Cell 103:411-422(2000).
RN [8]
RP FUNCTION.
RX PubMed=11090616; DOI=10.1016/s1097-2765(00)00076-9;
RA Dhillon N., Kamakaka R.T.;
RT "A histone variant, Htz1p, and a Sir1p-like protein, Esc2p, mediate
RT silencing at HMR.";
RL Mol. Cell 6:769-780(2000).
RN [9]
RP FUNCTION.
RX PubMed=11000274; DOI=10.1093/nar/28.19.3811;
RA Jackson J.D., Gorovsky M.A.;
RT "Histone H2A.Z has a conserved function that is distinct from that of the
RT major H2A sequence variants.";
RL Nucleic Acids Res. 28:3811-3816(2000).
RN [10]
RP FUNCTION, AND INTERACTION WITH RPB1.
RX PubMed=11509669; DOI=10.1128/mcb.21.18.6270-6279.2001;
RA Adam M., Robert F., Larochelle M., Gaudreau L.;
RT "H2A.Z is required for global chromatin integrity and for recruitment of
RT RNA polymerase II under specific conditions.";
RL Mol. Cell. Biol. 21:6270-6279(2001).
RN [11]
RP FUNCTION.
RX PubMed=12628191; DOI=10.1016/s0092-8674(03)00123-5;
RA Meneghini M.D., Wu M., Madhani H.D.;
RT "Conserved histone variant H2A.Z protects euchromatin from the ectopic
RT spread of silent heterochromatin.";
RL Cell 112:725-736(2003).
RN [12]
RP FUNCTION OF THE SWR1 COMPLEX, IDENTIFICATION IN THE SWR1 COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690608; DOI=10.1016/s1097-2765(03)00497-0;
RA Krogan N.J., Keogh M.-C., Datta N., Sawa C., Ryan O.W., Ding H., Haw R.A.,
RA Pootoolal J., Tong A., Canadien V., Richards D.P., Wu X., Emili A.,
RA Hughes T.R., Buratowski S., Greenblatt J.F.;
RT "A Snf2 family ATPase complex required for recruitment of the histone H2A
RT variant Htz1.";
RL Mol. Cell 12:1565-1576(2003).
RN [13]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [14]
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 [15]
RP FUNCTION, IDENTIFICATION IN THE SWR1 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15045029; DOI=10.1371/journal.pbio.0020131;
RA Kobor M.S., Venkatasubrahmanyam S., Meneghini M.D., Gin J.W.,
RA Jennings J.L., Link A.J., Madhani H.D., Rine J.;
RT "A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p
RT deposits histone variant H2A.Z into euchromatin.";
RL PLoS Biol. 2:587-599(2004).
RN [16]
RP FUNCTION.
RX PubMed=15353583; DOI=10.1073/pnas.0405753101;
RA Krogan N.J., Baetz K., Keogh M.-C., Datta N., Sawa C., Kwok T.C.Y.,
RA Thompson N.J., Davey M.G., Pootoolal J., Hughes T.R., Emili A.,
RA Buratowski S., Hieter P., Greenblatt J.F.;
RT "Regulation of chromosome stability by the histone H2A variant Htz1, the
RT Swr1 chromatin remodeling complex, and the histone acetyltransferase
RT NuA4.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13513-13518(2004).
RN [17]
RP IDENTIFICATION IN THE SWR1 COMPLEX, FUNCTION OF THE SWR1 COMPLEX,
RP INTERACTION WITH HISTONE H2B, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14645854; DOI=10.1126/science.1090701;
RA Mizuguchi G., Shen X., Landry J., Wu W.-H., Sen S., Wu C.;
RT "ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin
RT remodeling complex.";
RL Science 303:343-348(2004).
RN [18]
RP FUNCTION.
RX PubMed=16239142; DOI=10.1016/j.cell.2005.10.002;
RA Raisner R.M., Hartley P.D., Meneghini M.D., Bao M.Z., Liu C.L.,
RA Schreiber S.L., Rando O.J., Madhani H.D.;
RT "Histone variant H2A.Z marks the 5' ends of both active and inactive genes
RT in euchromatin.";
RL Cell 123:233-248(2005).
RN [19]
RP INTERACTION WITH VPS72.
RX PubMed=16299513; DOI=10.1038/nsmb1023;
RA Wu W.-H., Alami S., Luk E., Wu C.-H., Sen S., Mizuguchi G., Wei D., Wu C.;
RT "Swc2 is a widely conserved H2AZ-binding module essential for ATP-dependent
RT histone exchange.";
RL Nat. Struct. Mol. Biol. 12:1064-1071(2005).
RN [20]
RP FUNCTION.
RX PubMed=16344463; DOI=10.1073/pnas.0507975102;
RA Li B., Pattenden S.G., Lee D., Gutierrez J., Chen J., Seidel C., Gerton J.,
RA Workman J.L.;
RT "Preferential occupancy of histone variant H2AZ at inactive promoters
RT influences local histone modifications and chromatin remodeling.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18385-18390(2005).
RN [21]
RP ACETYLATION AT LYS-4; LYS-9; LYS-11 AND LYS-15, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND FUNCTION.
RX PubMed=16543222; DOI=10.1101/gad.1386306;
RA Babiarz J.E., Halley J.E., Rine J.;
RT "Telomeric heterochromatin boundaries require NuA4-dependent acetylation of
RT histone variant H2A.Z in Saccharomyces cerevisiae.";
RL Genes Dev. 20:700-710(2006).
RN [22]
RP LACK OF SUMOYLATION.
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 [23]
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 [24]
RP FUNCTION, AND INTERACTION WITH MPS3.
RX PubMed=21518795; DOI=10.1083/jcb.201011017;
RA Gardner J.M., Smoyer C.J., Stensrud E.S., Alexander R., Gogol M.,
RA Wiegraebe W., Jaspersen S.L.;
RT "Targeting of the SUN protein Mps3 to the inner nuclear membrane by the
RT histone variant H2A.Z.";
RL J. Cell Biol. 193:489-507(2011).
CC -!- FUNCTION: Variant histone H2A which can replace H2A in some
CC nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting
CC DNA accessibility to the cellular machineries which require DNA as a
CC template. Histones thereby play a central role in transcription
CC regulation, DNA 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 nucleosome
CC remodeling. This variant is enriched at promoters, it may keep them in
CC a repressed state until the appropriate activation signal is received
CC (PubMed:11000274, PubMed:11081628, PubMed:11090616, PubMed:11509669,
CC PubMed:12628191, PubMed:14645854, PubMed:14690608, PubMed:15045029,
CC PubMed:16239142, PubMed:16344463, PubMed:16543223). Near telomeres, it
CC may counteract gene silencing caused by the spread of heterochromatin
CC proteins (PubMed:16543222). Required for the RNA polymerase II and
CC SPT15/TBP recruitment to the target genes (PubMed:11509669). Involved
CC in chromosome stability (PubMed:15353583). Required to target MPS3 to
CC the inner membrane of the nuclear envelope (PubMed:21518795).
CC {ECO:0000269|PubMed:11000274, ECO:0000269|PubMed:11081628,
CC ECO:0000269|PubMed:11090616, ECO:0000269|PubMed:11509669,
CC ECO:0000269|PubMed:12628191, ECO:0000269|PubMed:14645854,
CC ECO:0000269|PubMed:14690608, ECO:0000269|PubMed:15045029,
CC ECO:0000269|PubMed:15353583, ECO:0000269|PubMed:16239142,
CC ECO:0000269|PubMed:16344463, ECO:0000269|PubMed:16543222,
CC ECO:0000269|PubMed:16543223, ECO:0000269|PubMed:21518795}.
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 (Probable). The octamer wraps approximately
CC 147 bp of DNA. H2A or its variant H2A.Z forms a heterodimer with H2B.
CC H2A.Z associates with the VPS72/SWC2 subunit of the SWR1 chromatin
CC remodeling complex. Interacts also with RBP1/DNA-directed RNA
CC polymerase II largest subunit (PubMed:11509669). Interacts with NAP1
CC (PubMed:14645854, PubMed:14690608, PubMed:15045029, PubMed:16299513,
CC PubMed:18086883). Interacts with MPS3 (PubMed:21518795).
CC {ECO:0000269|PubMed:11509669, ECO:0000269|PubMed:14645854,
CC ECO:0000269|PubMed:14690608, ECO:0000269|PubMed:15045029,
CC ECO:0000269|PubMed:16299513, ECO:0000269|PubMed:18086883,
CC ECO:0000269|PubMed:21518795, ECO:0000305}.
CC -!- INTERACTION:
CC Q12692; P35817: BDF1; NbExp=5; IntAct=EBI-8080, EBI-3493;
CC Q12692; P53551: HHO1; NbExp=3; IntAct=EBI-8080, EBI-8064;
CC Q12692; Q12692: HTZ1; NbExp=3; IntAct=EBI-8080, EBI-8080;
CC Q12692; P47069: MPS3; NbExp=3; IntAct=EBI-8080, EBI-25811;
CC Q12692; Q05471: SWR1; NbExp=9; IntAct=EBI-8080, EBI-22102;
CC Q12692; Q03433: VPS71; NbExp=6; IntAct=EBI-8080, EBI-27814;
CC Q12692; Q03388: VPS72; NbExp=9; IntAct=EBI-8080, EBI-38035;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. Chromosome
CC {ECO:0000269|PubMed:14562095}.
CC -!- PTM: Acetylated by ESA1, a component of the NuA4 histone
CC acetyltransferase (HAT) complex, and/or by GCN5, a component of the
CC SAGA complex, to form H2A.ZK3Ac, H2A.ZK8Ac, H2A.ZK10Ac and H2A.ZK14Ac
CC once deposited into chromatin (PubMed:16543223). Acetylation is
CC required for function at telomeres (PubMed:16543222). H2A.ZK14Ac is
CC acetylated at the promoters of active genes (PubMed:16543223).
CC {ECO:0000269|PubMed:16543222, ECO:0000269|PubMed:16543223}.
CC -!- MISCELLANEOUS: Present with 2840 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: In contrast to H2A1 and H2A2, appears to be weakly or
CC not sumoylated. {ECO:0000269|PubMed:16598039}.
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: H2A.ZK3ac =
CC acetylated Lys-4; H2A.ZK8ac = acetylated Lys-9; H2A.ZK10ac = acetylated
CC Lys-11; H2A.ZK14ac = acetylated Lys-15. {ECO:0000305}.
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DR EMBL; Z74754; CAA99011.1; -; Genomic_DNA.
DR EMBL; AY558000; AAS56326.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10771.1; -; Genomic_DNA.
DR PIR; S66694; S66694.
DR RefSeq; NP_014631.1; NM_001183266.1.
DR PDB; 2JSS; NMR; -; A=23-119.
DR PDB; 4M6B; X-ray; 1.78 A; A/D=23-119.
DR PDB; 5J9Q; X-ray; 3.25 A; L/M/O=12-21.
DR PDB; 6AE8; X-ray; 1.65 A; A/B=23-119.
DR PDBsum; 2JSS; -.
DR PDBsum; 4M6B; -.
DR PDBsum; 5J9Q; -.
DR PDBsum; 6AE8; -.
DR AlphaFoldDB; Q12692; -.
DR SMR; Q12692; -.
DR BioGRID; 34392; 658.
DR ComplexPortal; CPX-1613; Nucleosome, variant HTZ1-HTB1.
DR ComplexPortal; CPX-1614; Nucleosome, variant HTZ1-HTB2.
DR DIP; DIP-1381N; -.
DR IntAct; Q12692; 129.
DR MINT; Q12692; -.
DR STRING; 4932.YOL012C; -.
DR CarbonylDB; Q12692; -.
DR iPTMnet; Q12692; -.
DR MaxQB; Q12692; -.
DR PaxDb; Q12692; -.
DR PRIDE; Q12692; -.
DR EnsemblFungi; YOL012C_mRNA; YOL012C; YOL012C.
DR GeneID; 854150; -.
DR KEGG; sce:YOL012C; -.
DR SGD; S000005372; HTZ1.
DR VEuPathDB; FungiDB:YOL012C; -.
DR eggNOG; KOG1757; Eukaryota.
DR GeneTree; ENSGT00940000174660; -.
DR HOGENOM; CLU_062828_2_1_1; -.
DR InParanoid; Q12692; -.
DR OMA; FPCGRIK; -.
DR BioCyc; YEAST:G3O-33428-MON; -.
DR Reactome; R-SCE-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-SCE-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-SCE-427359; SIRT1 negatively regulates rRNA expression.
DR Reactome; R-SCE-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-SCE-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-SCE-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-SCE-9018519; Estrogen-dependent gene expression.
DR EvolutionaryTrace; Q12692; -.
DR PRO; PR:Q12692; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12692; protein.
DR GO; GO:0000785; C:chromatin; IDA:SGD.
DR GO; GO:0000791; C:euchromatin; IDA:UniProtKB.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006338; P:chromatin remodeling; IMP:SGD.
DR GO; GO:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IGI:SGD.
DR CDD; cd00074; H2A; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR IDEAL; IID50226; -.
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 PANTHER; PTHR23430; PTHR23430; 1.
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; Activator; Chromatin regulator; Chromosome;
KW Direct protein sequencing; DNA-binding; Nucleosome core; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:16543223,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..134
FT /note="Histone H2A.Z"
FT /id="PRO_0000055340"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..108
FT /note="Interaction with VPS72"
FT /evidence="ECO:0000269|PubMed:16299513"
FT COMPBIAS 16..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:16543223,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 4
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:16543222,
FT ECO:0000269|PubMed:16543223"
FT MOD_RES 9
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:16543222,
FT ECO:0000269|PubMed:16543223"
FT MOD_RES 11
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:16543222,
FT ECO:0000269|PubMed:16543223"
FT MOD_RES 15
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:16543222,
FT ECO:0000269|PubMed:16543223"
FT HELIX 25..28
FT /evidence="ECO:0007829|PDB:6AE8"
FT HELIX 35..43
FT /evidence="ECO:0007829|PDB:6AE8"
FT HELIX 54..81
FT /evidence="ECO:0007829|PDB:6AE8"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:6AE8"
FT HELIX 89..97
FT /evidence="ECO:0007829|PDB:6AE8"
FT HELIX 100..108
FT /evidence="ECO:0007829|PDB:6AE8"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:2JSS"
SQ SEQUENCE 134 AA; 14283 MW; 1D8FCEE3C8A504E7 CRC64;
MSGKAHGGKG KSGAKDSGSL RSQSSSARAG LQFPVGRIKR YLKRHATGRT RVGSKAAIYL
TAVLEYLTAE VLELAGNAAK DLKVKRITPR HLQLAIRGDD ELDSLIRATI ASGGVLPHIN
KALLLKVEKK GSKK
