H2AZ_HUMAN
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 03-AUG-2022, entry version 159.
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},
GN H2AZ {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 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 [15]
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 [16]
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 [17]
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 [18]
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 [19]
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 [20]
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 [21]
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 [22]
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). Interacts with PWWP2A (PubMed:28645917,
CC PubMed:30327463). Interacts with FH (when phosphorylated by PRKDC)
CC (PubMed:26237645). {ECO:0000250|UniProtKB:P0C0S6,
CC ECO:0000269|PubMed:11101893, ECO:0000269|PubMed:24463511,
CC ECO:0000269|PubMed:26237645, ECO:0000269|PubMed:26974126,
CC ECO:0000269|PubMed:28645917, 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}.
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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 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 AlphaFoldDB; P0C0S5; -.
DR SMR; P0C0S5; -.
DR BioGRID; 109269; 240.
DR ComplexPortal; CPX-5670; Nucleosome, variant H3.1-H2A.Z-H2B.1.
DR CORUM; P0C0S5; -.
DR DIP; DIP-38593N; -.
DR IntAct; P0C0S5; 100.
DR MINT; P0C0S5; -.
DR STRING; 9606.ENSP00000296417; -.
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; P0C0S5; -.
DR PeptideAtlas; P0C0S5; -.
DR PRIDE; P0C0S5; -.
DR ProteomicsDB; 52295; -.
DR TopDownProteomics; P0C0S5; -.
DR ABCD; P0C0S5; 1 sequenced antibody.
DR Antibodypedia; 45022; 536 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 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; WHCQAGG; -.
DR OrthoDB; 1504122at2759; -.
DR PhylomeDB; P0C0S5; -.
DR TreeFam; TF354232; -.
DR PathwayCommons; P0C0S5; -.
DR Reactome; R-HSA-110328; Recognition and association of DNA glycosylase with site containing an affected pyrimidine.
DR Reactome; R-HSA-110329; Cleavage of the damaged pyrimidine.
DR Reactome; R-HSA-110330; Recognition and association of DNA glycosylase with site containing an affected purine.
DR Reactome; R-HSA-110331; Cleavage of the damaged purine.
DR Reactome; R-HSA-1221632; Meiotic synapsis.
DR Reactome; R-HSA-171306; Packaging Of Telomere Ends.
DR Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
DR Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-HSA-212300; PRC2 methylates histones and DNA.
DR Reactome; R-HSA-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-HSA-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-HSA-3214858; RMTs methylate histone arginines.
DR Reactome; R-HSA-427359; SIRT1 negatively regulates rRNA expression.
DR Reactome; R-HSA-427389; ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-HSA-5334118; DNA methylation.
DR Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
DR Reactome; R-HSA-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-HSA-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-HSA-73728; RNA Polymerase I Promoter Opening.
DR Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR Reactome; R-HSA-912446; Meiotic recombination.
DR Reactome; R-HSA-9616222; Transcriptional regulation of granulopoiesis.
DR Reactome; R-HSA-9670095; Inhibition of DNA recombination at telomere.
DR Reactome; R-HSA-9710421; Defective pyroptosis.
DR Reactome; R-HSA-977225; Amyloid fiber formation.
DR SignaLink; P0C0S5; -.
DR SIGNOR; P0C0S5; -.
DR BioGRID-ORCS; 3015; 351 hits in 1046 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 207 other tissues.
DR ExpressionAtlas; P0C0S5; baseline and differential.
DR Genevisible; P0C0S5; HS.
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:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR CDD; cd00074; H2A; 1.
DR Gene3D; 1.10.20.10; -; 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; 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; 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 N-
FT 93. Abolishes interaction with VPS72; when associated with
FT 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 I-
FT 83. Abolishes interaction with VPS72; when associated with
FT 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
