ID   H2AJ_CHICK              Reviewed;         129 AA.
AC   P70082;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Histone H2A.J;
DE            Short=H2a/j;
DE   AltName: Full=Histone H2A-IX;
GN   Name=H2A-IX;
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 [GENOMIC DNA].
RX   PubMed=8804862; DOI=10.1093/dnares/3.2.95;
RA   Takami Y., Higashio M., Fukuoka T., Takechi S., Nakayama T.;
RT   "Organization of the chicken histone genes in a major gene cluster and
RT   generation of an almost complete set of the core histone protein
RT   sequences.";
RL   DNA Res. 3:95-99(1996).
CC   -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact
CC       DNA into chromatin, limiting DNA accessibility to the cellular
CC       machineries which require DNA as a template. Histones thereby play a
CC       central role in transcription regulation, DNA repair, DNA replication
CC       and chromosomal stability. DNA accessibility is regulated via a complex
CC       set of post-translational modifications of histones, also called
CC       histone code, and nucleosome remodeling.
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.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC   -!- PTM: Monoubiquitination of Lys-120 (H2AXK119ub) gives a specific tag
CC       for epigenetic transcriptional repression. Following DNA double-strand
CC       breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of
CC       ubiquitin moieties (By similarity). {ECO:0000250}.
CC   -!- PTM: Phosphorylation on Ser-2 is enhanced during mitosis.
CC       Phosphorylation on Ser-2 directly represses transcription (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR   EMBL; U38934; AAC60009.1; -; Genomic_DNA.
DR   RefSeq; NP_001025924.1; NM_001030753.1.
DR   AlphaFoldDB; P70082; -.
DR   SMR; P70082; -.
DR   BioGRID; 679225; 2.
DR   STRING; 9031.ENSGALP00000040715; -.
DR   PaxDb; P70082; -.
DR   PRIDE; P70082; -.
DR   Ensembl; ENSGALT00000045162; ENSGALP00000040715; ENSGALG00000049859.
DR   GeneID; 417947; -.
DR   KEGG; gga:417947; -.
DR   CTD; 417947; -.
DR   VEuPathDB; HostDB:geneid_417947; -.
DR   GeneTree; ENSGT00940000153118; -.
DR   InParanoid; P70082; -.
DR   OMA; NKTESHH; -.
DR   OrthoDB; 1504122at2759; -.
DR   PhylomeDB; P70082; -.
DR   PRO; PR:P70082; -.
DR   Proteomes; UP000000539; Chromosome 1.
DR   Bgee; ENSGALG00000049859; Expressed in granulocyte and 12 other tissues.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Acetylation; Chromosome; DNA-binding; Isopeptide bond; Methylation;
KW   Nucleosome core; Nucleus; Phosphoprotein; Reference proteome;
KW   Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..129
FT                   /note="Histone H2A.J"
FT                   /id="PRO_0000344251"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         6
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         10
FT                   /note="N6-lactoyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT   MOD_RES         105
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        14
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        16
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        120
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   129 AA;  14016 MW;  E28AE20D0B531900 CRC64;
     MSGRGKQGGK VRAKAKSRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YMAAVLEYLT
     AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGK VTIAQGGVLP NIQAVLLPKK
     TESHKAKSK