H2A_ONCMY
ID H2A_ONCMY Reviewed; 128 AA.
AC P02264; P83327;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Histone H2A;
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6439879; DOI=10.1007/bf02104730;
RA Connor W., States J.C., Mezquita J., Dixon G.H.;
RT "Organization and nucleotide sequence of rainbow trout histone H2A and H3
RT genes.";
RL J. Mol. Evol. 20:236-250(1984).
RN [2]
RP PROTEIN SEQUENCE OF 2-128.
RX PubMed=4768909; DOI=10.1016/s0021-9258(19)43626-0;
RA Bailey G.S., Dixon G.H.;
RT "Histone IIb1 from rainbow trout. Comparison in amino acid sequence with
RT calf thymus IIB1.";
RL J. Biol. Chem. 248:5463-5472(1973).
RN [3]
RP PROTEIN SEQUENCE OF 2-18, PHOSPHORYLATION AT SER-2, AND ACETYLATION AT
RP LYS-6.
RX PubMed=5033394; DOI=10.1016/s0021-9258(19)45115-6;
RA Candido E.P.M., Dixon G.H.;
RT "Acetylation of trout testis histones in vivo. Site of the modification in
RT histone IIb 1.";
RL J. Biol. Chem. 247:3868-3873(1972).
RN [4]
RP PROTEIN SEQUENCE OF 41-52, ACETYLATION AT SER-2, FUNCTION, TISSUE
RP SPECIFICITY, AND MASS SPECTROMETRY.
RC TISSUE=Skin mucus;
RX PubMed=12164782; DOI=10.1042/bj20020980;
RA Fernandes J.M.O., Kemp G.D., Molle M.G., Smith V.J.;
RT "Anti-microbial properties of histone H2A from skin secretions of rainbow
RT trout, Oncorhynchus mykiss.";
RL Biochem. J. 368:611-620(2002).
RN [5]
RP UBIQUITINATION AT LYS-120.
RX PubMed=2540826; DOI=10.1021/bi00429a007;
RA Nickel B.E., Davie J.R.;
RT "Structure of polyubiquitinated histone H2A.";
RL Biochemistry 28:964-968(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. {ECO:0000269|PubMed:12164782}.
CC -!- FUNCTION: The secreted form has antibacterial activity against Gram-
CC positive bacteria and antifungal activity against S.cerevisiae.
CC {ECO:0000269|PubMed:12164782}.
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. Note=A secreted form has
CC been detected in skin secretions.
CC -!- TISSUE SPECIFICITY: Expressed and secreted by skin epithelium.
CC {ECO:0000269|PubMed:12164782}.
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 -!- MASS SPECTROMETRY: Mass=13639; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12164782};
CC -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=Ref.2; Type=Miscellaneous discrepancy; Note=Differs from that shown extensively.; Evidence={ECO:0000305};
CC Sequence=Ref.3; Type=Miscellaneous discrepancy; Note=Differs from that shown extensively.; Evidence={ECO:0000305};
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DR EMBL; X01064; CAA25528.1; -; Genomic_DNA.
DR PIR; A92959; HSTR21.
DR AlphaFoldDB; P02264; -.
DR SMR; P02264; -.
DR iPTMnet; P02264; -.
DR Ensembl; ENSOMYT00000127112; ENSOMYP00000122407; ENSOMYG00000047912.
DR OrthoDB; 1504122at2759; -.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
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; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:AgBase.
DR GO; GO:0045087; P:innate immune response; IDA:AgBase.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR GO; GO:0051673; P:membrane disruption in another organism; IDA:AgBase.
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; Antibiotic; Antimicrobial; Chromosome;
KW Direct protein sequencing; DNA-binding; Fungicide; Hydroxylation;
KW Isopeptide bond; Methylation; Nucleosome core; Nucleus; Phosphoprotein;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12164782,
FT ECO:0000269|PubMed:4768909, ECO:0000269|PubMed:5033394"
FT CHAIN 2..128
FT /note="Histone H2A"
FT /id="PRO_0000055277"
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:0000269|PubMed:12164782"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:5033394"
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:5033394"
FT MOD_RES 10
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S8"
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 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 MOD_RES 126
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:0000269|PubMed:2540826"
SQ SEQUENCE 128 AA; 13731 MW; 7ABD417BA2B0783B CRC64;
MSGRGKTGGK ARAKAKTRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YLAAVLEYLT
AEILELAGNA ARDNKKTRII PRHLQLAVRN DEELNKLLGG VTIAQGGVLP NIQAVLLPKK
TEKAVKAK
