H2A3_CHICK
ID H2A3_CHICK Reviewed; 129 AA.
AC P35062; Q92016;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Histone H2A-III;
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=8406011; DOI=10.1016/0378-1119(93)90293-c;
RA Ohshige T., Takechi S., Nakayama T.;
RT "Presence of particular transcription regulatory elements in the 5'-
RT intergenic region shared by the chicken H2A-III and H2B-V pair.";
RL Gene 131:193-199(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25.
RX PubMed=3267232; DOI=10.1093/nar/16.17.8571;
RA Sturm R.A., Dalton S., Wells J.R.E.;
RT "Conservation of histone H2A/H2B intergene regions: a role for the H2B
RT specific element in divergent transcription.";
RL Nucleic Acids Res. 16:8571-8586(1988).
RN [3]
RP PROTEIN SEQUENCE OF 5-12, ACETYLATION AT LYS-6 AND LYS-10, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12450536; DOI=10.1016/s1570-0232(02)00631-1;
RA Zhang K., Tang H.;
RT "Analysis of core histones by liquid chromatography-mass spectrometry and
RT peptide mapping.";
RL J. Chromatogr. B 783:173-179(2003).
RN [4]
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: 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. Chromosome.
CC -!- PTM: Monoubiquitination of Lys-120 (H2AK119Ub) gives a specific tag for
CC epigenetic transcriptional repression. Following DNA double-strand
CC breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of
CC ubiquitin moieties, leading to the recruitment of repair proteins to
CC sites of DNA damage. H2AK119Ub and ionizing radiation-induced 'Lys-63'-
CC linked ubiquitination are distinct events (By similarity).
CC {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 -!- PTM: Glutamine methylation at Gln-105 (H2AQ104me) by FBL is
CC specifically dedicated to polymerase I. It is present at 35S ribosomal
CC DNA locus and impairs binding of the FACT complex (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR EMBL; D11054; BAA01797.1; -; Genomic_DNA.
DR EMBL; X07764; CAA30591.1; -; Genomic_DNA.
DR EMBL; X07765; CAA30593.1; -; Genomic_DNA.
DR AlphaFoldDB; P35062; -.
DR SMR; P35062; -.
DR iPTMnet; P35062; -.
DR VEuPathDB; HostDB:geneid_417947; -.
DR Proteomes; UP000000539; Unplaced.
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 Hydroxylation; Isopeptide bond; Methylation; Nucleosome core; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..129
FT /note="Histone H2A-III"
FT /id="PRO_0000055214"
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-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT MOD_RES 6
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:12450536"
FT MOD_RES 10
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT MOD_RES 10
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:12450536"
FT MOD_RES 10
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT MOD_RES 10
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT MOD_RES 37
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT MOD_RES 75
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT MOD_RES 76
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT MOD_RES 96
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT MOD_RES 96
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT MOD_RES 96
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT MOD_RES 100
FT /note="N6-glutaryllysine"
FT /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT MOD_RES 105
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000250"
FT MOD_RES 119
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT MOD_RES 119
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT MOD_RES 120
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S8"
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:0000305|PubMed:2713375"
SQ SEQUENCE 129 AA; 13966 MW; C148296C0D524271 CRC64;
MSGRGKQGGK ARAKAKSRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YLAAVLEYLT
AEILELAGNP ARDNKKTRII PRHLQLAIRN DEELNKLLGK VTIAQGGVLP NIQAVLLPKK
TDSHKAKAK
