ID H2A4_CHICK Reviewed; 129 AA. AC P02263; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 194. DE RecName: Full=Histone H2A-IV; 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=4000938; DOI=10.1093/nar/13.4.1369; RA Wang S.W., Robins A.J., D'Andrea R., Wells J.R.E.; RT "Inverted duplication of histone genes in chicken and disposition of RT regulatory sequences."; RL Nucleic Acids Res. 13:1369-1387(1985). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Takechi S., Ohsige T., Nakayama T.; RL Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6269072; DOI=10.1093/nar/9.13.3119; RA D'Andrea R., Harvey R.P., Wells J.R.E.; RT "Vertebrate histone genes: nucleotide sequence of a chicken H2A gene and RT regulatory flanking sequences."; RL Nucleic Acids Res. 9:3119-3128(1981). RN [4] RP PROTEIN SEQUENCE OF 2-129, AND ACETYLATION AT SER-2. RC TISSUE=Erythrocyte; RX PubMed=667168; DOI=10.1016/s0300-9084(78)80747-0; RA Laine B., Kmiecik D., Sautiere P., Biserte G.; RT "Primary structure of chicken erythrocyte histone H2A."; RL Biochimie 60:147-150(1978). RN [5] 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 [6] 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). RN [7] RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS). RX PubMed=1946434; DOI=10.1073/pnas.88.22.10148; RA Arents G., Burlingame R.W., Wang B.-C., Love W.E., Moudrianakis E.N.; RT "The nucleosomal core histone octamer at 3.1 A resolution: a tripartite RT protein assembly and a left-handed superhelix."; RL Proc. Natl. Acad. Sci. U.S.A. 88:10148-10152(1991). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D11055; BAA01798.1; -; Genomic_DNA. DR EMBL; V00413; CAA23704.1; -; Genomic_DNA. DR EMBL; X02218; CAA26139.1; -; Genomic_DNA. DR PIR; B93556; HSCH2A. DR RefSeq; NP_001072943.1; NM_001079475.1. DR RefSeq; NP_001264997.1; NM_001278068.1. DR RefSeq; NP_001268410.1; NM_001281481.1. DR RefSeq; XP_004937728.1; XM_004937671.2. DR RefSeq; XP_425455.2; XM_425455.4. DR RefSeq; XP_425465.1; XM_425465.3. DR RefSeq; XP_425469.1; XM_425469.5. DR PDB; 1EQZ; X-ray; 2.50 A; A/E=1-129. DR PDB; 1HIO; X-ray; 3.10 A; A=16-110. DR PDB; 1HQ3; X-ray; 2.15 A; A/E=1-129. DR PDB; 1TZY; X-ray; 1.90 A; A/E=1-129. DR PDB; 2ARO; X-ray; 2.10 A; A/E=1-129. DR PDB; 2HIO; X-ray; 3.10 A; A=2-129. DR PDB; 2XQL; EM; 19.50 A; A/C/E/G/I=16-106. DR PDB; 3C9K; EM; 20.00 A; A/E=2-129. DR PDBsum; 1EQZ; -. DR PDBsum; 1HIO; -. DR PDBsum; 1HQ3; -. DR PDBsum; 1TZY; -. DR PDBsum; 2ARO; -. DR PDBsum; 2HIO; -. DR PDBsum; 2XQL; -. DR PDBsum; 3C9K; -. DR AlphaFoldDB; P02263; -. DR EMDB; EMD-1469; -. DR EMDB; EMD-1777; -. DR SMR; P02263; -. DR BioGRID; 676813; 3. DR IntAct; P02263; 3. DR STRING; 9031.ENSGALP00000044632; -. DR iPTMnet; P02263; -. DR PaxDb; 9031-ENSGALP00000040653; -. DR Ensembl; ENSGALT00000049616; ENSGALP00000050888; ENSGALG00000059359. DR Ensembl; ENSGALT00000112767; ENSGALP00000074700; ENSGALG00000063407. DR Ensembl; ENSGALT00000113266; ENSGALP00000089781; ENSGALG00000063849. DR Ensembl; ENSGALT00010029564.1; ENSGALP00010017191.1; ENSGALG00010012350.1. DR Ensembl; ENSGALT00010032636.1; ENSGALP00010019341.1; ENSGALG00010013579.1. DR Ensembl; ENSGALT00015023849; ENSGALP00015013985; ENSGALG00015009784. DR Ensembl; ENSGALT00015023851; ENSGALP00015013987; ENSGALG00015009784. DR Ensembl; ENSGALT00015024455; ENSGALP00015014590; ENSGALG00015009989. DR GeneID; 101749238; -. DR GeneID; 404299; -. DR GeneID; 417955; -. DR GeneID; 427895; -. DR KEGG; gga:100858459; -. DR KEGG; gga:101749238; -. DR KEGG; gga:404299; -. DR KEGG; gga:417955; -. DR KEGG; gga:427881; -. DR KEGG; gga:427891; -. DR KEGG; gga:427895; -. DR CTD; 101749238; -. DR CTD; 404299; -. DR CTD; 417955; -. DR CTD; 427895; -. DR VEuPathDB; HostDB:geneid_100858459; -. DR VEuPathDB; HostDB:geneid_101749238; -. DR VEuPathDB; HostDB:geneid_404299; -. DR VEuPathDB; HostDB:geneid_417955; -. DR VEuPathDB; HostDB:geneid_427881; -. DR VEuPathDB; HostDB:geneid_427891; -. DR VEuPathDB; HostDB:geneid_427895; -. DR eggNOG; KOG1756; Eukaryota. DR GeneTree; ENSGT00940000161385; -. DR HOGENOM; CLU_062828_3_1_1; -. DR InParanoid; P02263; -. DR OMA; CEAWHAE; -. DR OrthoDB; 235643at2759; -. DR PhylomeDB; P02263; -. DR TreeFam; TF300137; -. 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-5689901; Metalloprotease DUBs. DR Reactome; R-GGA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks. DR Reactome; R-GGA-5693571; Nonhomologous End-Joining (NHEJ). DR Reactome; R-GGA-5693607; Processing of DNA double-strand break ends. DR Reactome; R-GGA-606279; Deposition of new CENPA-containing nucleosomes at the centromere. DR Reactome; R-GGA-68616; Assembly of the ORC complex at the origin of replication. DR Reactome; R-GGA-69473; G2/M DNA damage checkpoint. 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 EvolutionaryTrace; P02263; -. DR PRO; PR:P02263; -. DR Proteomes; UP000000539; Chromosome 1. DR Bgee; ENSGALG00000031571; Expressed in granulocyte and 12 other cell types or tissues. DR ExpressionAtlas; P02263; baseline and differential. 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 DisProt; DP01205; -. DR Gene3D; 1.10.20.10; Histone, subunit A; 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; HISTONE H2A; 1. DR PANTHER; PTHR23430:SF355; HISTONE H2A.J; 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; Histone-fold; 1. DR PROSITE; PS00046; HISTONE_H2A; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Chromosome; Direct protein sequencing; KW DNA-binding; Hydroxylation; Isopeptide bond; Methylation; Nucleosome core; KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:667168" FT CHAIN 2..129 FT /note="Histone H2A-IV" FT /id="PRO_0000055215" 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:667168" 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" FT CONFLICT 50 FT /note="V -> L (in Ref. 3; CAA23704)" FT /evidence="ECO:0000305" FT CONFLICT 127..128 FT /note="KA -> AG (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 11..14 FT /evidence="ECO:0007829|PDB:1EQZ" FT HELIX 18..21 FT /evidence="ECO:0007829|PDB:1TZY" FT HELIX 28..37 FT /evidence="ECO:0007829|PDB:1TZY" FT STRAND 40..44 FT /evidence="ECO:0007829|PDB:1TZY" FT HELIX 47..73 FT /evidence="ECO:0007829|PDB:1TZY" FT STRAND 77..79 FT /evidence="ECO:0007829|PDB:1TZY" FT HELIX 81..89 FT /evidence="ECO:0007829|PDB:1TZY" FT HELIX 92..97 FT /evidence="ECO:0007829|PDB:1TZY" FT TURN 98..100 FT /evidence="ECO:0007829|PDB:1TZY" FT STRAND 101..103 FT /evidence="ECO:0007829|PDB:1TZY" FT TURN 104..106 FT /evidence="ECO:0007829|PDB:2HIO" FT HELIX 114..116 FT /evidence="ECO:0007829|PDB:1TZY" SQ SEQUENCE 129 AA; 13940 MW; C148297D1C525360 CRC64; MSGRGKQGGK ARAKAKSRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGK VTIAQGGVLP NIQAVLLPKK TDSHKAKAK //