H2AZ_CHICK
ID H2AZ_CHICK Reviewed; 128 AA.
AC Q5ZMD6;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Histone H2A.Z;
DE Short=H2A/z;
GN Name=H2AFZ; ORFNames=RCJMB04_2h11;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
RN [2]
RP UBIQUITINATION.
RX PubMed=8280071; DOI=10.1042/bj2960737;
RA Li W., Nagaraja S., Delcuve G.P., Hendzel M.J., Davie J.R.;
RT "Effects of histone acetylation, ubiquitination and variants on nucleosome
RT stability.";
RL Biochem. J. 296:737-744(1993).
RN [3]
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15983376; DOI=10.1073/pnas.0503189102;
RA Coon J.J., Ueberheide B., Syka J.E.P., Dryhurst D.D., Ausio J.,
RA Shabanowitz J., Hunt D.F.;
RT "Protein identification using sequential ion/ion reactions and tandem mass
RT spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:9463-9468(2005).
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 (By similarity). {ECO:0000250|UniProtKB:P0C0S5,
CC ECO:0000250|UniProtKB:P0C0S6}.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
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 and Lys-12 during interphase.
CC Acetylation disappears at mitosis (By similarity).
CC {ECO:0000250|UniProtKB:P0C0S6}.
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 -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR EMBL; AJ719448; CAG31107.1; -; mRNA.
DR RefSeq; NP_001026545.1; NM_001031374.1.
DR AlphaFoldDB; Q5ZMD6; -.
DR SMR; Q5ZMD6; -.
DR BioGRID; 686040; 1.
DR STRING; 9031.ENSGALP00000028277; -.
DR iPTMnet; Q5ZMD6; -.
DR PaxDb; Q5ZMD6; -.
DR PRIDE; Q5ZMD6; -.
DR Ensembl; ENSGALT00000028340; ENSGALP00000028277; ENSGALG00000014023.
DR GeneID; 426361; -.
DR KEGG; gga:426361; -.
DR CTD; 426361; -.
DR VEuPathDB; HostDB:geneid_426361; -.
DR eggNOG; KOG1757; Eukaryota.
DR GeneTree; ENSGT00900000140979; -.
DR HOGENOM; CLU_062828_2_2_1; -.
DR InParanoid; Q5ZMD6; -.
DR OMA; WHCQAGG; -.
DR OrthoDB; 1504122at2759; -.
DR PhylomeDB; Q5ZMD6; -.
DR TreeFam; TF354232; -.
DR Reactome; R-GGA-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-GGA-212300; PRC2 methylates histones and DNA.
DR Reactome; R-GGA-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-GGA-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-GGA-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-GGA-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-GGA-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-GGA-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-GGA-73728; RNA Polymerase I Promoter Opening.
DR Reactome; R-GGA-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-GGA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-GGA-9018519; Estrogen-dependent gene expression.
DR PRO; PR:Q5ZMD6; -.
DR Proteomes; UP000000539; Chromosome 4.
DR Bgee; ENSGALG00000014023; Expressed in spermatid and 14 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; DNA-binding; Isopeptide bond; Methylation;
KW Nucleosome core; Nucleus; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..128
FT /note="Histone H2A.Z"
FT /id="PRO_0000055302"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..100
FT /note="M6 cassette"
FT /evidence="ECO:0000250"
FT MOD_RES 5
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000305|PubMed:16204459"
FT MOD_RES 5
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000305|PubMed:16204459"
FT MOD_RES 8
FT /note="N6-methyllysine"
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:0000250|UniProtKB:P0C0S5"
FT MOD_RES 14
FT /note="N6-lactoyllysine"
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:0000305|PubMed:8280071"
SQ SEQUENCE 128 AA; 13583 MW; E031E537B2930371 CRC64;
MAGGKAGKDS GKTKTKAVSR SQRAGLQFPV GRIHRHLKSR TTSHGRVGAT AAVYSAAILE
YLTAEVLELA GNASKDLKVK RITPRHLQLA IRGDEELDSL IKATIAGGGV IPHIHKSLIG
KKGQQKTV
