H2AV_CHICK
ID H2AV_CHICK Reviewed; 128 AA.
AC P02272;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Histone H2A.V;
DE AltName: Full=H2A.F/Z;
GN Name=H2AZ2 {ECO:0000250|UniProtKB:Q71UI9}; Synonyms=H2AF;
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 [MRNA].
RX PubMed=6574451; DOI=10.1073/pnas.80.10.2819;
RA Harvey R.P., Whiting J.A., Coles L.S., Krieg P.A., Wells J.R.E.;
RT "H2A.F: an extremely variant histone H2A sequence expressed in the chicken
RT embryo.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:2819-2823(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2493634; DOI=10.1093/nar/17.4.1745;
RA Dalton S., Robins A.J., Harvey R.P., Wells J.R.E.;
RT "Transcription from the intron-containing chicken histone H2A.F gene is not
RT S-phase regulated.";
RL Nucleic Acids Res. 17:1745-1756(1989).
RN [3]
RP FUNCTION, AND 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. May be involved in the formation of constitutive
CC heterochromatin. May be required for chromosome segregation during cell
CC division (By similarity). {ECO:0000250, ECO:0000269|PubMed:16204459}.
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 H2AF forms a heterodimer with H2B (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- DEVELOPMENTAL STAGE: Expressed in the chicken embryo.
CC -!- PTM: Monoubiquitination of Lys-122 gives a specific tag for epigenetic
CC transcriptional repression. {ECO:0000250}.
CC -!- PTM: Acetylated on Lys-5, Lys-8 and Lys-12 when associated with the 5'-
CC end of active genes. {ECO:0000269|PubMed:16204459}.
CC -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR EMBL; V00414; CAA23705.1; -; mRNA.
DR EMBL; X13894; CAA32094.1; ALT_SEQ; Genomic_DNA.
DR PIR; S03282; HSCH2F.
DR RefSeq; XP_015128745.1; XM_015273259.1.
DR AlphaFoldDB; P02272; -.
DR SMR; P02272; -.
DR iPTMnet; P02272; -.
DR Ensembl; ENSGALT00000086325; ENSGALP00000064273; ENSGALG00000033447.
DR GeneID; 426617; -.
DR KEGG; gga:426617; -.
DR CTD; 94239; -.
DR VEuPathDB; HostDB:geneid_426617; -.
DR GeneTree; ENSGT00900000140979; -.
DR InParanoid; P02272; -.
DR OMA; FPCGRIK; -.
DR OrthoDB; 1504122at2759; -.
DR PhylomeDB; P02272; -.
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:P02272; -.
DR Proteomes; UP000000539; Chromosome 22.
DR Bgee; ENSGALG00000033447; Expressed in granulocyte and 13 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; Nucleosome core;
KW Nucleus; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..128
FT /note="Histone H2A.V"
FT /id="PRO_0000055308"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:16204459"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:16204459"
FT MOD_RES 12
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|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; 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"
SQ SEQUENCE 128 AA; 13509 MW; 1F3C388F6854041C CRC64;
MAGGKAGKDS GKAKAKAVSR SQRAGLQFPV GRIHRHLKTR TTSHGRVGAT AAVYSAAILE
YLTAEVLELA GNASKDLKVK RITPRHLQLA IRGDEELDSL IKATIAGGGV IPHIHKSLIG
KKGQQKTA
