H2A4_CHICK
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 03-AUG-2022, entry version 186.
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}.
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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 SMR; P02263; -.
DR BioGRID; 676813; 3.
DR IntAct; P02263; 3.
DR STRING; 9031.ENSGALP00000040653; -.
DR iPTMnet; P02263; -.
DR PaxDb; P02263; -.
DR Ensembl; ENSGALT00000046827; ENSGALP00000056288; ENSGALG00000032645.
DR Ensembl; ENSGALT00000049616; ENSGALP00000050888; ENSGALG00000052284.
DR Ensembl; ENSGALT00000058977; ENSGALP00000044632; ENSGALG00000031571.
DR Ensembl; ENSGALT00000093393; ENSGALP00000071368; ENSGALG00000048212.
DR Ensembl; ENSGALT00000094867; ENSGALP00000066955; ENSGALG00000049268.
DR Ensembl; ENSGALT00000095522; ENSGALP00000072929; ENSGALG00000052030.
DR Ensembl; ENSGALT00000108326; ENSGALP00000067139; ENSGALG00000054083.
DR GeneID; 100858459; -.
DR GeneID; 101749238; -.
DR GeneID; 404299; -.
DR GeneID; 417955; -.
DR GeneID; 427881; -.
DR GeneID; 427891; -.
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; 100125271; -.
DR CTD; 100858459; -.
DR CTD; 101749238; -.
DR CTD; 417955; -.
DR CTD; 427891; -.
DR CTD; 427895; -.
DR CTD; 606720; -.
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; VIVECAC; -.
DR OrthoDB; 1504122at2759; -.
DR PhylomeDB; P02263; -.
DR TreeFam; TF300137; -.
DR Reactome; R-GGA-201722; Formation of the beta-catenin:TCF transactivating complex.
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-3214815; HDACs deacetylate histones.
DR Reactome; R-GGA-3214847; HATs acetylate histones.
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-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-GGA-5689603; UCH proteinases.
DR Reactome; R-GGA-5689880; Ub-specific processing proteases.
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-5693607; Processing of DNA double-strand break ends.
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 tissues.
DR ExpressionAtlas; P02263; baseline.
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; -; 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; 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
