H2AZ_MOUSE
ID H2AZ_MOUSE Reviewed; 128 AA.
AC P0C0S6; B2RXZ3; P17317; Q3UA55; Q3UK43; Q68FD2;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Histone H2A.Z;
DE Short=H2A/z;
GN Name=H2az1 {ECO:0000312|MGI:MGI:1888388};
GN Synonyms=H2afz {ECO:0000312|MGI:MGI:1888388}, H2az {ECO:0000303|Ref.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Rocha D., Carrier A., Anderson E., Botcherby M., Guenet J.-L., Jordan B.;
RT "Molecular cloning of the murine histone H2A.Z cDNA and chromosomal
RT localization of mouse H2A.Z related sequences.";
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6 X CBA;
RA Le Provost F., Charlier M.;
RT "Histone H2A.Z expression and regulation in mouse mammary gland.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, C57BL/6J, DBA/2J, and NOD;
RC TISSUE=Bone marrow, Spleen, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
RP ACETYLATION, AND LACK OF PHOSPHORYLATION.
RX PubMed=7217105; DOI=10.1016/s0021-9258(19)69487-1;
RA Pantazis P., Bonner W.M.;
RT "Quantitative determination of histone modification. H2A acetylation and
RT phosphorylation.";
RL J. Biol. Chem. 256:4669-4675(1981).
RN [6]
RP FUNCTION.
RX PubMed=11516949; DOI=10.1016/s0960-9822(01)00329-3;
RA Faast R., Thonglairoam V., Schulz T.C., Beall J., Wells J.R.E., Taylor H.,
RA Matthaei K., Rathjen P.D., Tremethick D.J., Lyons I.;
RT "Histone variant H2A.Z is required for early mammalian development.";
RL Curr. Biol. 11:1183-1187(2001).
RN [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH INCENP.
RX PubMed=12660166; DOI=10.1093/emboj/cdg160;
RA Rangasamy D., Berven L., Ridgway P., Tremethick D.J.;
RT "Pericentric heterochromatin becomes enriched with H2A.Z during early
RT mammalian development.";
RL EMBO J. 22:1599-1607(2003).
RN [8]
RP FUNCTION.
RX PubMed=15546624; DOI=10.1016/j.molcel.2004.10.023;
RA Fan J.Y., Rangasamy D., Luger K., Tremethick D.J.;
RT "H2A.Z alters the nucleosome surface to promote HP1alpha-mediated chromatin
RT fiber folding.";
RL Mol. Cell 16:655-661(2004).
RN [9]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=15195148; DOI=10.1038/nsmb786;
RA Rangasamy D., Greaves I., Tremethick D.J.;
RT "RNA interference demonstrates a novel role for H2A.Z in chromosome
RT segregation.";
RL Nat. Struct. Mol. Biol. 11:650-655(2004).
RN [10]
RP ACETYLATION AT LYS-5; LYS-8 AND LYS-12.
RX PubMed=16204459; DOI=10.1093/nar/gki874;
RA Bruce K., Myers F.A., Mantouvalou E., Lefevre P., Greaves I., Bonifer C.,
RA Tremethick D.J., Thorne A.W., Crane-Robinson C.;
RT "The replacement histone H2A.Z in a hyperacetylated form is a feature of
RT active genes in the chicken.";
RL Nucleic Acids Res. 33:5633-5639(2005).
RN [11]
RP LACTYLATION AT LYS-12 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).
RN [12]
RP ACETYLATION.
RX PubMed=32542325; DOI=10.1182/blood.2019001279;
RA Numata A., Kwok H.S., Zhou Q.L., Li J., Tirado-Magallanes R.,
RA Angarica V.E., Hannah R., Park J., Wang C.Q., Krishnan V., Rajagopalan D.,
RA Zhang Y., Zhou S., Welner R.S., Osato M., Jha S., Bohlander S.K.,
RA Goettgens B., Yang H., Benoukraf T., Lough J.W., Bararia D., Tenen D.G.;
RT "Lysine acetyltransferase Tip60 is required for hematopoietic stem cell
RT maintenance.";
RL Blood 136:1735-1747(2020).
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. Essential for early development.
CC {ECO:0000269|PubMed:11516949, ECO:0000269|PubMed:15195148,
CC ECO:0000269|PubMed:15546624}.
CC -!- SUBUNIT: Interacts (via M6 cassette) with ANP32E; leading to removal of
CC H2A.Z/H2AZ1 from the nucleosome (By similarity). The nucleosome is a
CC histone octamer containing two molecules each of H2A, H2B, H3 and H4
CC assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The
CC octamer wraps approximately 147 bp of DNA. H2A or its variant H2AZ1
CC forms a heterodimer with H2B (By similarity). H2AZ1 interacts with
CC INCENP (PubMed:12660166). Interacts with VPS72 (via N-terminal domain).
CC Interacts with PWWP2A (By similarity). Interacts with FH (when
CC phosphorylated by PRKDC) (By similarity).
CC {ECO:0000250|UniProtKB:P0C0S5, ECO:0000269|PubMed:12660166}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12660166}. Chromosome
CC {ECO:0000269|PubMed:12660166, ECO:0000269|PubMed:15195148}.
CC Note=Enriched in constitutive heterochromatin (PubMed:12660166,
CC PubMed:15195148). Absent from facultative heterochromatin of the
CC inactive X chromosome (PubMed:12660166). {ECO:0000269|PubMed:12660166,
CC ECO:0000269|PubMed:15195148}.
CC -!- PTM: Monoubiquitination of Lys-122 gives a specific tag for epigenetic
CC transcriptional repression. {ECO:0000250|UniProtKB:P0C0S5}.
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 (By similarity).
CC Acetylated on Lys-5, Lys-8 and Lys-12 during interphase; acetylation
CC disappears at mitosis (PubMed:16204459, PubMed:7217105). Acetylation by
CC the NuA4 histone acetyltransferase complex is required for
CC hematopoietic stem cell maintenance (PubMed:32542325).
CC {ECO:0000250|UniProtKB:P0C0S5, ECO:0000269|PubMed:16204459,
CC ECO:0000269|PubMed:32542325, ECO:0000269|PubMed:7217105}.
CC -!- PTM: Not phosphorylated. {ECO:0000269|PubMed:7217105}.
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:0000250|UniProtKB:P0C0S5}.
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:0000250|UniProtKB:P0C0S5}.
CC -!- MISCELLANEOUS: Down-regulation of H2az1 by RNA interference leads to
CC death at early embryonic stages.
CC -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR EMBL; U70494; AAB09578.1; -; mRNA.
DR EMBL; AY074806; AAL71864.1; -; mRNA.
DR EMBL; AK028176; BAC25791.1; -; mRNA.
DR EMBL; AK088704; BAC40515.1; -; mRNA.
DR EMBL; AK143572; BAE25443.1; -; mRNA.
DR EMBL; AK146181; BAE26959.1; -; mRNA.
DR EMBL; AK150454; BAE29574.1; -; mRNA.
DR EMBL; AK151052; BAE30069.1; -; mRNA.
DR EMBL; AK151509; BAE30460.1; -; mRNA.
DR EMBL; AK151868; BAE30756.1; -; mRNA.
DR EMBL; AK152398; BAE31186.1; -; mRNA.
DR EMBL; AK152848; BAE31541.1; -; mRNA.
DR EMBL; AK168178; BAE40138.1; -; mRNA.
DR EMBL; BC079903; AAH79903.1; -; mRNA.
DR EMBL; BC147478; AAI47479.1; -; mRNA.
DR EMBL; BC158035; AAI58036.1; -; mRNA.
DR EMBL; BC171999; AAI71999.1; -; mRNA.
DR CCDS; CCDS38647.1; -.
DR RefSeq; NP_058030.1; NM_016750.3.
DR PDB; 7M1X; EM; 3.70 A; C/G=1-128.
DR PDBsum; 7M1X; -.
DR AlphaFoldDB; P0C0S6; -.
DR SMR; P0C0S6; -.
DR BioGRID; 206173; 9.
DR ComplexPortal; CPX-5715; Nucleosome, variant H3.1-H2A.Z-H2B.1.
DR IntAct; P0C0S6; 10.
DR MINT; P0C0S6; -.
DR STRING; 10090.ENSMUSP00000036907; -.
DR iPTMnet; P0C0S6; -.
DR PhosphoSitePlus; P0C0S6; -.
DR EPD; P0C0S6; -.
DR jPOST; P0C0S6; -.
DR MaxQB; P0C0S6; -.
DR PaxDb; P0C0S6; -.
DR PRIDE; P0C0S6; -.
DR TopDownProteomics; P0C0S6; -.
DR ABCD; P0C0S6; 1 sequenced antibody.
DR Antibodypedia; 45022; 536 antibodies from 38 providers.
DR DNASU; 51788; -.
DR Ensembl; ENSMUST00000041045; ENSMUSP00000036907; ENSMUSG00000037894.
DR GeneID; 51788; -.
DR KEGG; mmu:51788; -.
DR UCSC; uc008rmo.2; mouse.
DR CTD; 3015; -.
DR MGI; MGI:1888388; H2az1.
DR VEuPathDB; HostDB:ENSMUSG00000037894; -.
DR eggNOG; KOG1757; Eukaryota.
DR GeneTree; ENSGT00900000140979; -.
DR HOGENOM; CLU_062828_2_2_1; -.
DR InParanoid; P0C0S6; -.
DR OMA; WHCQAGG; -.
DR OrthoDB; 1504122at2759; -.
DR PhylomeDB; P0C0S6; -.
DR TreeFam; TF354232; -.
DR Reactome; R-MMU-110330; Recognition and association of DNA glycosylase with site containing an affected purine.
DR Reactome; R-MMU-110331; Cleavage of the damaged purine.
DR Reactome; R-MMU-212300; PRC2 methylates histones and DNA.
DR Reactome; R-MMU-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-MMU-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-MMU-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-MMU-427359; SIRT1 negatively regulates rRNA expression.
DR Reactome; R-MMU-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-MMU-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-MMU-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-MMU-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-MMU-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-MMU-73728; RNA Polymerase I Promoter Opening.
DR Reactome; R-MMU-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
DR Reactome; R-MMU-9670095; Inhibition of DNA recombination at telomere.
DR BioGRID-ORCS; 51788; 29 hits in 73 CRISPR screens.
DR ChiTaRS; H2afz; mouse.
DR PRO; PR:P0C0S6; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P0C0S6; protein.
DR Bgee; ENSMUSG00000037894; Expressed in ventricular zone and 68 other tissues.
DR ExpressionAtlas; P0C0S6; baseline and differential.
DR Genevisible; P0C0S6; MM.
DR GO; GO:0000791; C:euchromatin; ISO:MGI.
DR GO; GO:0000792; C:heterochromatin; ISO:MGI.
DR GO; GO:0000786; C:nucleosome; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0031490; F:chromatin DNA binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0031492; F:nucleosomal DNA binding; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; ISO:MGI.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR CDD; cd00074; H2A; 1.
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 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; Developmental protein; DNA-binding;
KW Isopeptide bond; Methylation; Nucleosome core; Nucleus; Reference proteome;
KW 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_0000055298"
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:0000269|PubMed:12660166"
FT REGION 89..100
FT /note="M6 cassette"
FT /evidence="ECO:0000250"
FT REGION 93..103
FT /note="Required for interaction with INCENP"
FT /evidence="ECO:0000269|PubMed:12660166"
FT REGION 120..128
FT /note="Required for interaction with PWWP2A"
FT /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT MOD_RES 5
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000305|PubMed:16204459"
FT MOD_RES 5
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT MOD_RES 8
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000305|PubMed:16204459"
FT MOD_RES 8
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT MOD_RES 12
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000305|PubMed:16204459"
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:0000250|UniProtKB:P0C0S5"
FT MOD_RES 14
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S5"
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:0000250|UniProtKB:P0C0S5"
FT CONFLICT 12
FT /note="K -> E (in Ref. 3; BAE30460)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="P -> A (in Ref. 3; BAE26959)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 128 AA; 13553 MW; E024E53818230371 CRC64;
MAGGKAGKDS GKAKTKAVSR SQRAGLQFPV GRIHRHLKSR TTSHGRVGAT AAVYSAAILE
YLTAEVLELA GNASKDLKVK RITPRHLQLA IRGDEELDSL IKATIAGGGV IPHIHKSLIG
KKGQQKTV
