H2A1_BOVIN
ID H2A1_BOVIN Reviewed; 130 AA.
AC P0C0S9; A5PJH1; P02261;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Histone H2A type 1;
DE AltName: Full=H2A.1b;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-130, AND ACETYLATION AT SER-2.
RC TISSUE=Thymus;
RX PubMed=4856314; DOI=10.1111/j.1432-1033.1974.tb03298.x;
RA Sautiere P., Tyrou D., Laine B., Mizon J., Ruffin P., Biserte G.;
RT "Covalent structure of calf-thymus ALK-histone.";
RL Eur. J. Biochem. 41:563-576(1974).
RN [3]
RP PROTEIN SEQUENCE OF 2-30.
RC TISSUE=Thymus;
RX PubMed=4667695;
RA Olson M.O.J., Sugano N., Yeoman L.C., Johnson B.R., Jordan J.J.,
RA Taylor C.W., Starbuck W.C., Busch H.;
RT "Homology of the amino terminal sequences of the AL and GAR calf thymus
RT histones.";
RL Physiol. Chem. Phys. 4:10-16(1972).
RN [4]
RP PROTEIN SEQUENCE OF 31-82.
RC TISSUE=Thymus;
RX PubMed=4568599; DOI=10.1016/s0021-9258(19)44757-1;
RA Yeoman L.C., Olson M.O.J., Sugano N., Jordan J.J., Taylor C.W.,
RA Starbuck W.C., Busch H.;
RT "Amino acid sequence of the center of the arginine-lysine-rich histone from
RT calf thymus. The total sequence.";
RL J. Biol. Chem. 247:6018-6023(1972).
RN [5]
RP PROTEIN SEQUENCE OF 83-130.
RC TISSUE=Thymus;
RX PubMed=4555425; DOI=10.1016/s0021-9258(19)45181-8;
RA Sugano N., Olson M.O.J., Yeoman L.C., Johnson B.R., Taylor C.W.,
RA Starbuck W.C., Busch H.;
RT "Amino acid sequence of the COOH-terminal portion of the arginine-lysine-
RT rich histone of calf thymus.";
RL J. Biol. Chem. 247:3589-3591(1972).
RN [6]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=1010839; DOI=10.1093/oxfordjournals.jbchem.a131327;
RA Hayashi H., Iwai K.;
RT "Calf thymus histone H2A. Purification and tryptic peptides.";
RL J. Biochem. 80:681-692(1976).
RN [7]
RP PROTEIN SEQUENCE OF 87-121.
RX PubMed=1999173; DOI=10.1210/endo-128-3-1580;
RA Badamchian M., Spangelo B.L., Damavandy T., McLeod R.M., Goldstein A.L.;
RT "Complete amino acid sequence analysis of a peptide isolated from the
RT thymus that enhances release of growth hormone and prolactin.";
RL Endocrinology 128:1580-1588(1991).
RN [8]
RP PROTEIN SEQUENCE OF 124-130, ACETYLATION AT SER-2, AND UBIQUITINATION AT
RP LYS-120.
RX PubMed=265581; DOI=10.1073/pnas.74.3.864;
RA Goldknopf I.L., Busch H.;
RT "Isopeptide linkage between nonhistone and histone 2A polypeptides of
RT chromosomal conjugate-protein A24.";
RL Proc. Natl. Acad. Sci. U.S.A. 74:864-868(1977).
RN [9]
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: Deiminated on Arg-4 in granulocytes upon calcium entry.
CC {ECO:0000250|UniProtKB:P0C0S8}.
CC -!- PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM37 and
CC RNF2/RING2 complex gives a specific tag for epigenetic transcriptional
CC repression and participates in X chromosome inactivation of female
CC mammals. It is involved in the initiation of both imprinted and random
CC X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome
CC chromatin. Ubiquitination of H2A functions downstream of methylation of
CC 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be
CC induced by ultraviolet and may be involved in DNA repair. Following DNA
CC double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63'
CC linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases
CC RNF8 and RNF168, leading to the recruitment of repair proteins to sites
CC of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and
CC H2AK15Ub, respectively) in response to DNA damage is initiated by
CC RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-
CC linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to
CC extend 'Lys-63'-linked ubiquitin chains in vitro. H2AK119Ub and
CC ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and
CC H2AK15Ub) are distinct events. {ECO:0000250|UniProtKB:P0C0S8,
CC ECO:0000269|PubMed:265581, ECO:0000269|PubMed:2713375}.
CC -!- PTM: Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis.
CC Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses
CC transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by
CC RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is
CC present in the regulatory region of many tumor suppresor genes and
CC down-regulates their transcription. {ECO:0000250|UniProtKB:P0C0S8}.
CC -!- PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may
CC play a crucial role in the germ-cell lineage.
CC {ECO:0000250|UniProtKB:P22752}.
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.
CC {ECO:0000250|UniProtKB:P0C0S8}.
CC -!- PTM: Crotonylation (Kcr) is specifically present in male germ cells and
CC marks testis-specific genes in post-meiotic cells, including X-linked
CC genes that escape sex chromosome inactivation in haploid cells.
CC Crotonylation marks active promoters and enhancers and confers
CC resistance to transcriptional repressors. It is also associated with
CC post-meiotically activated genes on autosomes.
CC {ECO:0000250|UniProtKB:P0C0S8}.
CC -!- PTM: Lactylated in macrophages by EP300/P300 by using lactoyl-CoA
CC directly derived from endogenous or exogenous lactate, leading to
CC stimulates gene transcription. {ECO:0000250|UniProtKB:P0C0S5}.
CC -!- MISCELLANEOUS: Describes the first characterization of a ubiquitinated
CC protein (PubMed:265581).
CC -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR EMBL; BC142109; AAI42110.1; -; mRNA.
DR PIR; A91216; HSBO2A.
DR RefSeq; NP_001092190.1; NM_001098720.2.
DR RefSeq; XP_002697551.1; XM_002697505.4.
DR RefSeq; XP_005196697.1; XM_005196640.2.
DR RefSeq; XP_005223785.1; XM_005223728.2.
DR RefSeq; XP_010816763.1; XM_010818461.2.
DR RefSeq; XP_010816815.1; XM_010818513.2.
DR RefSeq; XP_010823700.1; XM_010825398.2.
DR RefSeq; XP_010823710.1; XM_010825408.2.
DR RefSeq; XP_876240.1; XM_871147.5.
DR PDB; 6FML; EM; 4.34 A; O/S=2-130.
DR PDBsum; 6FML; -.
DR AlphaFoldDB; P0C0S9; -.
DR SMR; P0C0S9; -.
DR IntAct; P0C0S9; 1.
DR MINT; P0C0S9; -.
DR STRING; 9913.ENSBTAP00000014123; -.
DR iPTMnet; P0C0S9; -.
DR PaxDb; P0C0S9; -.
DR PeptideAtlas; P0C0S9; -.
DR PRIDE; P0C0S9; -.
DR Ensembl; ENSBTAT00000014123; ENSBTAP00000014123; ENSBTAG00000048599.
DR Ensembl; ENSBTAT00000033373; ENSBTAP00000033286; ENSBTAG00000051969.
DR Ensembl; ENSBTAT00000068092; ENSBTAP00000066065; ENSBTAG00000053792.
DR GeneID; 104968446; -.
DR GeneID; 104975683; -.
DR GeneID; 529277; -.
DR GeneID; 616790; -.
DR GeneID; 618824; -.
DR KEGG; bta:104968446; -.
DR KEGG; bta:104975683; -.
DR KEGG; bta:529277; -.
DR KEGG; bta:616790; -.
DR KEGG; bta:618824; -.
DR CTD; 3013; -.
DR CTD; 319173; -.
DR CTD; 8331; -.
DR CTD; 8332; -.
DR VEuPathDB; HostDB:ENSBTAG00000048599; -.
DR VEuPathDB; HostDB:ENSBTAG00000051969; -.
DR VEuPathDB; HostDB:ENSBTAG00000053792; -.
DR VGNC; VGNC:83577; H2AC11.
DR VGNC; VGNC:83584; H2AC14.
DR VGNC; VGNC:83565; H2AC7.
DR eggNOG; KOG1756; Eukaryota.
DR GeneTree; ENSGT00940000153125; -.
DR HOGENOM; CLU_062828_3_1_1; -.
DR InParanoid; P0C0S9; -.
DR OMA; AVRNDEX; -.
DR OrthoDB; 1504122at2759; -.
DR TreeFam; TF300137; -.
DR Reactome; R-BTA-3214815; HDACs deacetylate histones.
DR Reactome; R-BTA-3214847; HATs acetylate histones.
DR Reactome; R-BTA-3214858; RMTs methylate histone arginines.
DR Reactome; R-BTA-5689880; Ub-specific processing proteases.
DR Reactome; R-BTA-5689901; Metalloprotease DUBs.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000048599; Expressed in spiral colon and 51 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 3D-structure; Acetylation; Chromosome; Citrullination;
KW Direct protein sequencing; DNA-binding; Hydroxylation; Isopeptide bond;
KW Methylation; Nucleosome core; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:265581,
FT ECO:0000269|PubMed:4667695, ECO:0000269|PubMed:4856314"
FT CHAIN 2..130
FT /note="Histone H2A type 1"
FT /id="PRO_0000055241"
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:265581,
FT ECO:0000269|PubMed:4856314"
FT MOD_RES 2
FT /note="Phosphoserine; by RPS6KA5"
FT /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT MOD_RES 4
FT /note="Citrulline; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT MOD_RES 4
FT /note="Symmetric dimethylarginine; by PRMT5; alternate"
FT /evidence="ECO:0000250|UniProtKB:P22752"
FT MOD_RES 6
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P0C0S8"
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; alternate"
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 37
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:C0HKE1"
FT MOD_RES 37
FT /note="N6-crotonyllysine; 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; alternate"
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|UniProtKB:P0C0S8"
FT MOD_RES 119
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT MOD_RES 119
FT /note="N6-crotonyllysine; 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-crotonyllysine; 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 121
FT /note="Phosphothreonine; by DCAF1"
FT /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT MOD_RES 126
FT /note="N6-crotonyllysine; 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|UniProtKB:P0C0S8"
FT CROSSLNK 16
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT CROSSLNK 120
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:265581"
SQ SEQUENCE 130 AA; 14091 MW; 48DD539793FE8256 CRC64;
MSGRGKQGGK ARAKAKTRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YLAAVLEYLT
AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGK VTIAQGGVLP NIQAVLLPKK
TESHHKAKGK
