H2AZ_BOVIN
ID H2AZ_BOVIN Reviewed; 128 AA.
AC P0C0S4; P17317; Q32L66;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Histone H2A.Z;
DE Short=H2A/z;
GN Name=H2AZ1; Synonyms=H2AZ;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
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 [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-31, AND LACK OF PHOSPHORYLATION.
RC TISSUE=Thymus;
RX PubMed=6832364; DOI=10.1016/0014-5793(83)80896-5;
RA Ball D.J., Slaughter C.A., Hensley P., Garrard W.T.;
RT "Amino acid sequence of the N-terminal domain of calf thymus histone
RT H2A.Z.";
RL FEBS Lett. 154:166-170(1983).
RN [4]
RP FUNCTION, AND UBIQUITINATION.
RX PubMed=6306766; DOI=10.1126/science.6306766;
RA Hatch C.L., Bonner W.M., Moudrianakis E.N.;
RT "Minor histone 2A variants and ubiquinated forms in the native H2A:H2B
RT dimer.";
RL Science 221:468-470(1983).
RN [5]
RP UBIQUITINATION.
RX PubMed=2713375; DOI=10.1021/bi00429a006;
RA Nickel B.E., Allis C.D., Davie J.R.;
RT "Ubiquitinated histone H2B is preferentially located in transcriptionally
RT active chromatin.";
RL Biochemistry 28:958-963(1989).
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 (By similarity). {ECO:0000250|UniProtKB:P0C0S5,
CC ECO:0000250|UniProtKB:P0C0S6, ECO:0000269|PubMed:6306766}.
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. Interacts (via M6 cassette) with ANP32E; leading
CC to removal of H2A.Z/H2AZ1 from the nucleosome. Interacts with VPS72
CC (via N-terminal domain). Interacts with PWWP2A. Interacts with FH (when
CC phosphorylated by PRKDC). {ECO:0000250|UniProtKB:P0C0S5,
CC ECO:0000250|UniProtKB:P0C0S6}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
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 (By similarity). Acetylation by the NuA4 histone
CC acetyltransferase complex is required for hematopoietic stem cell
CC maintenance (By similarity). {ECO:0000250|UniProtKB:P0C0S5,
CC ECO:0000250|UniProtKB:P0C0S6}.
CC -!- PTM: Not phosphorylated. {ECO:0000269|PubMed:6832364}.
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 -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR EMBL; X52318; CAA36554.1; -; mRNA.
DR EMBL; M37585; AAA30566.1; -; mRNA.
DR EMBL; BC109743; AAI09744.1; -; mRNA.
DR PIR; S03642; S03642.
DR RefSeq; NP_777234.1; NM_174809.2.
DR RefSeq; XP_010804249.1; XM_010805947.2.
DR AlphaFoldDB; P0C0S4; -.
DR SMR; P0C0S4; -.
DR STRING; 9913.ENSBTAP00000005802; -.
DR PeptideAtlas; P0C0S4; -.
DR PRIDE; P0C0S4; -.
DR Ensembl; ENSBTAT00000005802; ENSBTAP00000005802; ENSBTAG00000004428.
DR GeneID; 287016; -.
DR KEGG; bta:287016; -.
DR CTD; 3015; -.
DR VEuPathDB; HostDB:ENSBTAG00000004428; -.
DR VGNC; VGNC:83610; H2AZ1.
DR GeneTree; ENSGT00900000140979; -.
DR InParanoid; P0C0S4; -.
DR OMA; WHCQAGG; -.
DR OrthoDB; 1504122at2759; -.
DR Reactome; R-BTA-110330; Recognition and association of DNA glycosylase with site containing an affected purine.
DR Reactome; R-BTA-110331; Cleavage of the damaged purine.
DR Reactome; R-BTA-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-BTA-212300; PRC2 methylates histones and DNA.
DR Reactome; R-BTA-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-BTA-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-BTA-427359; SIRT1 negatively regulates rRNA expression.
DR Reactome; R-BTA-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-BTA-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-BTA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-BTA-73728; RNA Polymerase I Promoter Opening.
DR Reactome; R-BTA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-BTA-9670095; Inhibition of DNA recombination at telomere.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000004428; Expressed in spermatocyte and 105 other tissues.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
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 Acetylation; Chromosome; Direct protein sequencing; DNA-binding;
KW Isopeptide bond; Methylation; Nucleosome core; Nucleus; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6832364"
FT CHAIN 2..128
FT /note="Histone H2A.Z"
FT /id="PRO_0000055296"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..17
FT /note="Required for interaction with INCENP"
FT /evidence="ECO:0000250"
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:0000250"
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:0000250|UniProtKB:P0C0S5"
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:0000250|UniProtKB:P0C0S5"
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:0000250|UniProtKB:P0C0S5"
FT MOD_RES 12
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S5"
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:0000250|UniProtKB:P0C0S5"
FT CROSSLNK 122
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0C0S5, ECO:0000305"
SQ SEQUENCE 128 AA; 13553 MW; E024E53818230371 CRC64;
MAGGKAGKDS GKAKTKAVSR SQRAGLQFPV GRIHRHLKSR TTSHGRVGAT AAVYSAAILE
YLTAEVLELA GNASKDLKVK RITPRHLQLA IRGDEELDSL IKATIAGGGV IPHIHKSLIG
KKGQQKTV
