ID H2AZ_HUMAN Reviewed; 128 AA. AC P0C0S5; B2RD56; P17317; Q6I9U0; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 168. DE RecName: Full=Histone H2A.Z; DE Short=H2A/z; GN Name=H2AZ1 {ECO:0000312|HGNC:HGNC:4741}; GN Synonyms=H2AFZ {ECO:0000312|HGNC:HGNC:4741}, H2AZ GN {ECO:0000312|HGNC:HGNC:4741}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX PubMed=3344202; DOI=10.1093/nar/16.3.1113; RA Hatch C.L., Bonner W.M.; RT "Sequence of cDNAs for mammalian H2A.Z, an evolutionarily diverged but RT highly conserved basal histone H2A isoprotein species."; RL Nucleic Acids Res. 16:1113-1124(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1697587; DOI=10.1016/s0021-9258(18)77243-8; RA Hatch C.L., Bonner W.M.; RT "The human histone H2A.Z gene. Sequence and regulation."; RL J. Biol. Chem. 265:15211-15218(1990). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Tongue; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, Skeletal muscle, and Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP UBIQUITINATION AT LYS-122. RX PubMed=11835281; DOI=10.1002/bies.10038; RA Jason L.J.M., Moore S.C., Lewis J.D., Lindsey G., Ausio J.; RT "Histone ubiquitination: a tagging tail unfolds?"; RL Bioessays 24:166-174(2002). RN [9] RP FUNCTION. RX PubMed=15878876; DOI=10.1074/jbc.m501784200; RA Farris S.D., Rubio E.D., Moon J.J., Gombert W.M., Nelson B.H., Krumm A.; RT "Transcription-induced chromatin remodeling at the c-myc gene involves the RT local exchange of histone H2A.Z."; RL J. Biol. Chem. 280:25298-25303(2005). RN [10] RP MASS SPECTROMETRY. RX PubMed=16457589; DOI=10.1021/pr050269n; RA Boyne M.T. II, Pesavento J.J., Mizzen C.A., Kelleher N.L.; RT "Precise characterization of human histones in the H2A gene family by top RT down mass spectrometry."; RL J. Proteome Res. 5:248-253(2006). RN [11] RP ACETYLATION AT LYS-5; LYS-8 AND LYS-12, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=16627869; DOI=10.1074/mcp.m600007-mcp200; RA Beck H.C., Nielsen E.C., Matthiesen R., Jensen L.H., Sehested M., Finn P., RA Grauslund M., Hansen A.M., Jensen O.N.; RT "Quantitative proteomic analysis of post-translational modifications of RT human histones."; RL Mol. Cell. Proteomics 5:1314-1325(2006). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-5 AND LYS-8, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=16319397; DOI=10.1074/mcp.m500288-mcp200; RA Bonenfant D., Coulot M., Towbin H., Schindler P., van Oostrum J.; RT "Characterization of histones H2A and H2B variants and their post- RT translational modifications by mass spectrometry."; RL Mol. Cell. Proteomics 5:541-552(2006). RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-8; LYS-12 AND LYS-14, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [14] RP INTERACTION WITH ZNHIT1. RX PubMed=20473270; DOI=10.1038/emboj.2010.85; RA Cuadrado A., Corrado N., Perdiguero E., Lafarga V., Munoz-Canoves P., RA Nebreda A.R.; RT "Essential role of p18Hamlet/SRCAP-mediated histone H2A.Z chromatin RT incorporation in muscle differentiation."; RL EMBO J. 29:2014-2025(2010). RN [15] RP INTERACTION WITH FH. RX PubMed=26237645; DOI=10.1038/ncb3209; RA Jiang Y., Qian X., Shen J., Wang Y., Li X., Liu R., Xia Y., Chen Q., RA Peng G., Lin S.Y., Lu Z.; RT "Local generation of fumarate promotes DNA repair through inhibition of RT histone H3 demethylation."; RL Nat. Cell Biol. 17:1158-1168(2015). RN [16] RP INTERACTION WITH PWWP2A. RX PubMed=28645917; DOI=10.15252/embj.201695757; RA Puenzeler S., Link S., Wagner G., Keilhauer E.C., Kronbeck N., RA Spitzer R.M., Leidescher S., Markaki Y., Mentele E., Regnard C., RA Schneider K., Takahashi D., Kusakabe M., Vardabasso C., Zink L.M., RA Straub T., Bernstein E., Harata M., Leonhardt H., Mann M., Rupp R.A., RA Hake S.B.; RT "Multivalent binding of PWWP2A to H2A.Z regulates mitosis and neural crest RT differentiation."; RL EMBO J. 36:2263-2279(2017). RN [17] RP INTERACTION WITH PWWP2A. RX PubMed=30327463; DOI=10.1038/s41467-018-06665-5; RA Link S., Spitzer R.M.M., Sana M., Torrado M., Voelker-Albert M.C., RA Keilhauer E.C., Burgold T., Puenzeler S., Low J.K.K., Lindstroem I., RA Nist A., Regnard C., Stiewe T., Hendrich B., Imhof A., Mann M., RA Mackay J.P., Bartkuhn M., Hake S.B.; RT "PWWP2A binds distinct chromatin moieties and interacts with an MTA1- RT specific core NuRD complex."; RL Nat. Commun. 9:4300-4300(2018). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH THE NUCLEOSOME. RX PubMed=11101893; DOI=10.1038/81971; RA Suto R.K., Clarkson M.J., Tremethick D.J., Luger K.; RT "Crystal structure of a nucleosome core particle containing the variant RT histone H2A.Z."; RL Nat. Struct. Biol. 7:1121-1124(2000). RN [19] RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 19-128 IN COMPLEX WITH ANP32E AND RP HISTONE H2B, AND INTERACTION WITH ANP32E. RX PubMed=24463511; DOI=10.1038/nature12922; RA Obri A., Ouararhni K., Papin C., Diebold M.L., Padmanabhan K., Marek M., RA Stoll I., Roy L., Reilly P.T., Mak T.W., Dimitrov S., Romier C., RA Hamiche A.; RT "ANP32E is a histone chaperone that removes H2A.Z from chromatin."; RL Nature 505:648-653(2014). RN [20] RP METHYLATION AT LYS-5 AND LYS-8. RX PubMed=23324626; DOI=10.4161/epi.23416; RA Binda O., Sevilla A., LeRoy G., Lemischka I.R., Garcia B.A., Richard S.; RT "SETD6 monomethylates H2AZ on lysine 7 and is required for the maintenance RT of embryonic stem cell self-renewal."; RL Epigenetics 8:177-183(2013). RN [21] RP ACETYLATION AT LYS-5; LYS-8; LYS-12 AND LYS-14, AND MUTAGENESIS OF RP 5-LYS--LYS-14; 5-LYS--LYS-8 AND 12-LYS--LYS-14. RX PubMed=31527837; DOI=10.1038/s41589-019-0354-y; RA Semer M., Bidon B., Larnicol A., Caliskan G., Catez P., Egly J.M., Coin F., RA Le May N.; RT "DNA repair complex licenses acetylation of H2A.Z.1 by KAT2A during RT transcription."; RL Nat. Chem. Biol. 15:992-1000(2019). RN [22] RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 19-128 IN COMPLEX WITH H2BC11 AND RP VPS72, INTERACTION WITH H2BC11 AND VPS72, AND MUTAGENESIS OF THR-83; RP GLY-93; ASP-98 AND ILE-101. RX PubMed=26974126; DOI=10.1038/nsmb.3189; RA Latrick C.M., Marek M., Ouararhni K., Papin C., Stoll I., Ignatyeva M., RA Obri A., Ennifar E., Dimitrov S., Romier C., Hamiche A.; RT "Molecular basis and specificity of H2A.Z-H2B recognition and deposition by RT the histone chaperone YL1."; RL Nat. Struct. Mol. Biol. 23:309-316(2016). RN [23] RP LACTYLATION AT LYS-12; LYS-14 AND LYS-116. RX PubMed=31645732; DOI=10.1038/s41586-019-1678-1; RA Zhang D., Tang Z., Huang H., Zhou G., Cui C., Weng Y., Liu W., Kim S., RA Lee S., Perez-Neut M., Ding J., Czyz D., Hu R., Ye Z., He M., Zheng Y.G., RA Shuman H.A., Dai L., Ren B., Roeder R.G., Becker L., Zhao Y.; RT "Metabolic regulation of gene expression by histone lactylation."; RL Nature 574:575-580(2019). CC -!- FUNCTION: Variant histone H2A which replaces conventional H2A in a CC subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, CC limiting DNA accessibility to the cellular machineries which require CC DNA as a template. Histones thereby play a central role in CC transcription regulation, DNA repair, DNA replication and chromosomal CC stability. DNA accessibility is regulated via a complex set of post- CC translational modifications of histones, also called histone code, and CC nucleosome remodeling. May be involved in the formation of constitutive CC heterochromatin. May be required for chromosome segregation during cell CC division. {ECO:0000269|PubMed:15878876}. 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. H2A or its variant H2AZ1 forms a heterodimer with H2B. H2AZ1 CC interacts with INCENP (By similarity). Interacts (via M6 cassette) with CC ANP32E; leading to removal of H2A.Z/H2AZ1 from the nucleosome. CC Heterodimer H2BC11 and H2AZ1 interacts with VPS72 (via N-terminal CC domain) (PubMed:26974126). The interaction of HZAZ1 and VPS72 is CC enhanced by VPS72 phosphorylation which is promoted by ZNHIT1 (By CC similarity). Interacts with PWWP2A (PubMed:28645917, PubMed:30327463). CC Interacts with FH (when phosphorylated by PRKDC) (PubMed:26237645). CC Interacts with ZNHIT1; the interaction results in recruitment of H2AZ1 CC to the MYOG promoter region which is required for muscle-specific gene CC expression (PubMed:20473270). {ECO:0000250|UniProtKB:P0C0S6, CC ECO:0000269|PubMed:11101893, ECO:0000269|PubMed:20473270, CC ECO:0000269|PubMed:24463511, ECO:0000269|PubMed:26237645, CC ECO:0000269|PubMed:26974126, ECO:0000269|PubMed:28645917, CC ECO:0000269|PubMed:30327463}. CC -!- INTERACTION: CC P0C0S5; P01023: A2M; NbExp=3; IntAct=EBI-1199859, EBI-640741; CC P0C0S5; Q9GZN1: ACTR6; NbExp=3; IntAct=EBI-1199859, EBI-769329; CC P0C0S5; P50570-2: DNM2; NbExp=3; IntAct=EBI-1199859, EBI-10968534; CC P0C0S5; P07954: FH; NbExp=5; IntAct=EBI-1199859, EBI-1050358; CC P0C0S5; O14656-2: TOR1A; NbExp=3; IntAct=EBI-1199859, EBI-25847109; CC P0C0S5; O43257: ZNHIT1; NbExp=5; IntAct=EBI-1199859, EBI-347522; CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. CC -!- PTM: Monoubiquitination of Lys-122 gives a specific tag for epigenetic CC transcriptional repression. {ECO:0000269|PubMed:11835281}. CC -!- PTM: Acetylated on Lys-5, Lys-8, Lys-12 and Lys-14 by KAT2A; KAT2A is CC recruited by the XPC complex in absence of DNA damage CC (PubMed:31527837). Acetylated on Lys-5, Lys-8 and Lys-12 during CC interphase; acetylation disappears at mitosis (By similarity). CC Acetylation by the NuA4 histone acetyltransferase complex is required CC for hematopoietic stem cell maintenance (By similarity). CC {ECO:0000250|UniProtKB:P0C0S6, ECO:0000269|PubMed:31527837}. CC -!- PTM: Monomethylated on Lys-5 and Lys-8 by SETD6. SETD6 predominantly CC methylates Lys-8, lys-5 being a possible secondary site. CC {ECO:0000269|PubMed:23324626}. CC -!- PTM: Not phosphorylated. {ECO:0000250|UniProtKB:P0C0S4}. CC -!- PTM: Lactylated in macrophages by EP300/P300 by using lactoyl-CoA CC directly derived from endogenous or exogenous lactate, leading to CC stimulates gene transcription. {ECO:0000269|PubMed:31645732}. CC -!- MASS SPECTROMETRY: Mass=13413.4; Method=Electrospray; CC Note=Monoisotopic, not modified.; CC Evidence={ECO:0000269|PubMed:16457589}; CC -!- SIMILARITY: Belongs to the histone H2A family. {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; X52317; CAA36553.1; -; mRNA. DR EMBL; M37583; AAA35984.1; -; mRNA. DR EMBL; L10138; AAC61625.1; -; Genomic_DNA. DR EMBL; CR457415; CAG33696.1; -; mRNA. DR EMBL; AK315413; BAG37803.1; -; mRNA. DR EMBL; AC097460; AAY41013.1; -; Genomic_DNA. DR EMBL; CH471057; EAX06118.1; -; Genomic_DNA. DR EMBL; BC018002; AAH18002.1; -; mRNA. DR EMBL; BC020936; AAH20936.1; -; mRNA. DR EMBL; BC103743; AAI03744.1; -; mRNA. DR CCDS; CCDS3654.1; -. DR PIR; A35881; A35881. DR RefSeq; NP_002097.1; NM_002106.3. DR PDB; 1F66; X-ray; 2.60 A; C/G=1-128. DR PDB; 3WA9; X-ray; 3.07 A; C/G=1-128. DR PDB; 4CAY; X-ray; 1.48 A; A=19-128. DR PDB; 4NFT; X-ray; 2.61 A; A/B/C/D=16-114. DR PDB; 5B31; X-ray; 2.20 A; G=1-128. DR PDB; 5B32; X-ray; 2.35 A; G=1-128. DR PDB; 5B33; X-ray; 2.92 A; C/G=1-128. DR PDB; 5CHL; X-ray; 1.89 A; B=22-113. DR PDB; 5FUG; X-ray; 2.70 A; A/D/G/J=19-128. DR PDB; 5Z30; X-ray; 2.45 A; C/G=1-128. DR PDB; 6JOU; X-ray; 2.17 A; C/G=1-128. DR PDB; 6KO2; X-ray; 1.50 A; B=4-10. DR PDB; 7YRD; EM; 3.20 A; C/G=16-123. DR PDB; 8JHF; EM; 3.68 A; C/G=14-126. DR PDB; 8T9F; EM; 2.60 A; C/G=1-128. DR PDB; 8THU; EM; 3.10 A; C/G=1-128. DR PDBsum; 1F66; -. DR PDBsum; 3WA9; -. DR PDBsum; 4CAY; -. DR PDBsum; 4NFT; -. DR PDBsum; 5B31; -. DR PDBsum; 5B32; -. DR PDBsum; 5B33; -. DR PDBsum; 5CHL; -. DR PDBsum; 5FUG; -. DR PDBsum; 5Z30; -. DR PDBsum; 6JOU; -. DR PDBsum; 6KO2; -. DR PDBsum; 7YRD; -. DR PDBsum; 8JHF; -. DR PDBsum; 8T9F; -. DR PDBsum; 8THU; -. DR AlphaFoldDB; P0C0S5; -. DR EMDB; EMD-34053; -. DR EMDB; EMD-36264; -. DR EMDB; EMD-41109; -. DR EMDB; EMD-41113; -. DR EMDB; EMD-41272; -. DR SMR; P0C0S5; -. DR BioGRID; 109269; 358. DR ComplexPortal; CPX-5670; Nucleosome, variant H3.1-H2A.Z-H2B.1. DR CORUM; P0C0S5; -. DR DIP; DIP-38593N; -. DR IntAct; P0C0S5; 101. DR MINT; P0C0S5; -. DR STRING; 9606.ENSP00000296417; -. DR GlyCosmos; P0C0S5; 1 site, 1 glycan. DR GlyGen; P0C0S5; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P0C0S5; -. DR PhosphoSitePlus; P0C0S5; -. DR SwissPalm; P0C0S5; -. DR BioMuta; H2AFZ; -. DR DMDM; 83288408; -. DR EPD; P0C0S5; -. DR jPOST; P0C0S5; -. DR MassIVE; P0C0S5; -. DR MaxQB; P0C0S5; -. DR PaxDb; 9606-ENSP00000296417; -. DR PeptideAtlas; P0C0S5; -. DR ProteomicsDB; 52295; -. DR Pumba; P0C0S5; -. DR TopDownProteomics; P0C0S5; -. DR ABCD; P0C0S5; 1 sequenced antibody. DR Antibodypedia; 45022; 586 antibodies from 38 providers. DR DNASU; 3015; -. DR Ensembl; ENST00000296417.6; ENSP00000296417.5; ENSG00000164032.12. DR GeneID; 3015; -. DR KEGG; hsa:3015; -. DR MANE-Select; ENST00000296417.6; ENSP00000296417.5; NM_002106.4; NP_002097.1. DR UCSC; uc003hvo.2; human. DR AGR; HGNC:4741; -. DR CTD; 3015; -. DR DisGeNET; 3015; -. DR GeneCards; H2AZ1; -. DR HGNC; HGNC:4741; H2AZ1. DR HPA; ENSG00000164032; Tissue enhanced (bone). DR MIM; 142763; gene. DR neXtProt; NX_P0C0S5; -. DR OpenTargets; ENSG00000164032; -. DR VEuPathDB; HostDB:ENSG00000164032; -. DR eggNOG; KOG1757; Eukaryota. DR GeneTree; ENSGT00900000140979; -. DR HOGENOM; CLU_062828_2_2_1; -. DR InParanoid; P0C0S5; -. DR OMA; PVGRIHT; -. DR OrthoDB; 235643at2759; -. DR PhylomeDB; P0C0S5; -. DR TreeFam; TF354232; -. DR PathwayCommons; P0C0S5; -. DR Reactome; R-HSA-977225; Amyloid fiber formation. DR SignaLink; P0C0S5; -. DR SIGNOR; P0C0S5; -. DR BioGRID-ORCS; 3015; 370 hits in 1122 CRISPR screens. DR ChiTaRS; H2AFZ; human. DR EvolutionaryTrace; P0C0S5; -. DR GeneWiki; H2AFZ; -. DR GenomeRNAi; 3015; -. DR Pharos; P0C0S5; Tbio. DR PRO; PR:P0C0S5; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; P0C0S5; Protein. DR Bgee; ENSG00000164032; Expressed in ventricular zone and 209 other cell types or tissues. DR ExpressionAtlas; P0C0S5; baseline and differential. DR GO; GO:0000791; C:euchromatin; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0000792; C:heterochromatin; IDA:UniProtKB. DR GO; GO:0000786; C:nucleosome; IPI:ComplexPortal. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; IBA:GO_Central. DR GO; GO:0031492; F:nucleosomal DNA binding; IDA:UniProtKB. 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:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro. DR GO; GO:0071392; P:cellular response to estradiol stimulus; IMP:UniProtKB. DR GO; GO:0006325; P:chromatin organization; NAS:ComplexPortal. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB. DR CDD; cd00074; H2A; 1. DR Gene3D; 1.10.20.10; Histone, subunit A; 1. DR IDEAL; IID00019; -. 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; HISTONE H2A; 1. DR PANTHER; PTHR23430:SF47; HISTONE H2A.Z; 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; Histone-fold; 1. DR PROSITE; PS00046; HISTONE_H2A; 1. DR Genevisible; P0C0S5; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Chromosome; DNA-binding; Isopeptide bond; KW Methylation; Nucleosome core; Nucleus; Reference proteome; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000305" FT CHAIN 2..128 FT /note="Histone H2A.Z" FT /id="PRO_0000055297" FT REGION 1..25 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1..17 FT /note="Required for interaction with INCENP" FT /evidence="ECO:0000250" FT REGION 89..100 FT /note="M6 cassette" FT REGION 93..103 FT /note="Required for interaction with INCENP" FT /evidence="ECO:0000250" FT REGION 120..128 FT /note="Required for interaction with PWWP2A" FT /evidence="ECO:0000269|PubMed:28645917" FT MOD_RES 5 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:16627869, FT ECO:0000269|PubMed:31527837, ECO:0007744|PubMed:16319397" FT MOD_RES 5 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000269|PubMed:23324626" FT MOD_RES 8 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:16627869, FT ECO:0000269|PubMed:31527837, ECO:0007744|PubMed:16319397, FT ECO:0007744|PubMed:19608861" FT MOD_RES 8 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000269|PubMed:23324626" FT MOD_RES 12 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:16627869, FT ECO:0000269|PubMed:31527837, ECO:0007744|PubMed:19608861" FT MOD_RES 12 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000269|PubMed:31645732" FT MOD_RES 14 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:31527837, FT ECO:0007744|PubMed:19608861" FT MOD_RES 14 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000269|PubMed:31645732" FT MOD_RES 116 FT /note="N6-lactoyllysine" FT /evidence="ECO:0000269|PubMed:31645732" FT CROSSLNK 122 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:11835281" FT MUTAGEN 5..14 FT /note="KAGKDSGKAK->AAGKDSGAAA: Decreased acetylation by FT KAT2A." FT /evidence="ECO:0000269|PubMed:31527837" FT MUTAGEN 5..8 FT /note="KAGK->AAGA: Decreased acetylation by KAT2A." FT /evidence="ECO:0000269|PubMed:31527837" FT MUTAGEN 12..14 FT /note="KAK->AAA: Decreased acetylation by KAT2A." FT /evidence="ECO:0000269|PubMed:31527837" FT MUTAGEN 83 FT /note="T->I: Decreases interaction with VPS72. Almost FT abolishes interaction with VPS72; when associated with FT N-93. Abolishes interaction with VPS72; when associated FT with N-93 and IG-101." FT /evidence="ECO:0000269|PubMed:26974126" FT MUTAGEN 93 FT /note="G->N: Decreases interaction with VPS72. Almost FT abolishes interaction with VPS72; when associated with FT I-83. Abolishes interaction with VPS72; when associated FT with I-83 and IG-101." FT /evidence="ECO:0000269|PubMed:26974126" FT MUTAGEN 98 FT /note="D->N: No effect on interaction with VPS72." FT /evidence="ECO:0000269|PubMed:26974126" FT MUTAGEN 101 FT /note="I->IG: Abolishes interaction with VPS72; when FT associated with I-83 and N-93." FT /evidence="ECO:0000269|PubMed:26974126" FT HELIX 20..23 FT /evidence="ECO:0007829|PDB:4CAY" FT HELIX 30..39 FT /evidence="ECO:0007829|PDB:4CAY" FT STRAND 40..42 FT /evidence="ECO:0007829|PDB:5Z30" FT STRAND 43..45 FT /evidence="ECO:0007829|PDB:5CHL" FT HELIX 49..76 FT /evidence="ECO:0007829|PDB:4CAY" FT STRAND 80..82 FT /evidence="ECO:0007829|PDB:4CAY" FT HELIX 84..92 FT /evidence="ECO:0007829|PDB:4CAY" FT HELIX 95..106 FT /evidence="ECO:0007829|PDB:4CAY" FT HELIX 116..118 FT /evidence="ECO:0007829|PDB:6JOU" SQ SEQUENCE 128 AA; 13553 MW; E024E53818230371 CRC64; MAGGKAGKDS GKAKTKAVSR SQRAGLQFPV GRIHRHLKSR TTSHGRVGAT AAVYSAAILE YLTAEVLELA GNASKDLKVK RITPRHLQLA IRGDEELDSL IKATIAGGGV IPHIHKSLIG KKGQQKTV //