H2A1_XENLA
ID H2A1_XENLA Reviewed; 130 AA.
AC P06897; Q3B8I8;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Histone H2A type 1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (GENE CLUSTER X1H3).
RX PubMed=3863963; DOI=10.1016/0022-2836(85)90065-8;
RA Perry M., Thomsen G.H., Roeder R.G.;
RT "Genomic organization and nucleotide sequence of two distinct histone gene
RT clusters from Xenopus laevis. Identification of novel conserved upstream
RT sequence elements.";
RL J. Mol. Biol. 185:479-499(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=9305837; DOI=10.1038/38444;
RA Luger K., Mader A.W., Richmond R.K., Sargent D.F., Richmond T.J.;
RT "Crystal structure of the nucleosome core particle at 2.8 A resolution.";
RL Nature 389:251-260(1997).
RN [4] {ECO:0007744|PDB:6WZ5, ECO:0007744|PDB:6WZ9, ECO:0007744|PDB:6X0N}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.20 ANGSTROMS) OF 2-130 OF NUCLEOSOME
RP CORE COMPLEX IN COMPLEX WITH PARP2 AND HPF1.
RX PubMed=32939087; DOI=10.1038/s41586-020-2725-7;
RA Bilokapic S., Suskiewicz M.J., Ahel I., Halic M.;
RT "Bridging of DNA breaks activates PARP2-HPF1 to modify chromatin.";
RL Nature 585:609-613(2020).
RN [5] {ECO:0007744|PDB:6N1Z}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS).
RX PubMed=30855230; DOI=10.7554/elife.43630;
RA Padavannil A., Sarkar P., Kim S.J., Cagatay T., Jiou J., Brautigam C.A.,
RA Tomchick D.R., Sali A., D'Arcy S., Chook Y.M.;
RT "Importin-9 wraps around the H2A-H2B core to act as nuclear importer and
RT histone chaperone.";
RL Elife 8:0-0(2019).
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; X03018; CAA26817.1; -; Genomic_DNA.
DR EMBL; M21287; AAA49769.1; -; Genomic_DNA.
DR EMBL; BC106331; AAI06332.1; -; mRNA.
DR PIR; H24510; HSXLA1.
DR RefSeq; NP_001089684.1; NM_001096215.1.
DR PDB; 1AOI; X-ray; 2.80 A; C/G=5-120.
DR PDB; 1KX3; X-ray; 2.00 A; C/G=2-130.
DR PDB; 1KX4; X-ray; 2.60 A; C/G=2-130.
DR PDB; 1KX5; X-ray; 1.94 A; C/G=2-130.
DR PDB; 1M18; X-ray; 2.45 A; C/G=2-130.
DR PDB; 1M19; X-ray; 2.30 A; C/G=2-130.
DR PDB; 1M1A; X-ray; 2.65 A; C/G=2-130.
DR PDB; 1P34; X-ray; 2.70 A; C/G=2-130.
DR PDB; 1P3A; X-ray; 3.00 A; C/G=2-130.
DR PDB; 1P3B; X-ray; 3.00 A; C/G=2-130.
DR PDB; 1P3F; X-ray; 2.90 A; C/G=2-130.
DR PDB; 1P3G; X-ray; 2.70 A; C/G=2-130.
DR PDB; 1P3I; X-ray; 2.30 A; C/G=2-130.
DR PDB; 1P3K; X-ray; 2.90 A; C/G=2-130.
DR PDB; 1P3L; X-ray; 2.40 A; C/G=2-130.
DR PDB; 1P3M; X-ray; 2.90 A; C/G=2-130.
DR PDB; 1P3O; X-ray; 2.75 A; C/G=2-130.
DR PDB; 1P3P; X-ray; 2.70 A; C/G=2-130.
DR PDB; 1S32; X-ray; 2.05 A; C/G=2-120.
DR PDB; 1ZBB; X-ray; 9.00 A; C/G/c/g=2-130.
DR PDB; 1ZLA; X-ray; 2.90 A; C/G=2-130.
DR PDB; 2FJ7; X-ray; 3.20 A; C/G=2-130.
DR PDB; 2NZD; X-ray; 2.65 A; C/G=2-120.
DR PDB; 3B6F; X-ray; 3.45 A; C/G=2-130.
DR PDB; 3B6G; X-ray; 3.45 A; C/G=2-130.
DR PDB; 3C1B; X-ray; 2.20 A; C/G=2-130.
DR PDB; 3C1C; X-ray; 3.15 A; C/G=2-130.
DR PDB; 3KUY; X-ray; 2.90 A; C/G=2-120.
DR PDB; 3KWQ; X-ray; 3.50 A; C/G=15-121.
DR PDB; 3LJA; X-ray; 2.75 A; C/G=2-130.
DR PDB; 3MNN; X-ray; 2.50 A; C/G=2-120.
DR PDB; 3O62; X-ray; 3.22 A; C/G=2-130.
DR PDB; 3REH; X-ray; 2.50 A; C/G=2-130.
DR PDB; 3REI; X-ray; 2.65 A; C/G=2-130.
DR PDB; 3REJ; X-ray; 2.55 A; C/G=2-130.
DR PDB; 3REK; X-ray; 2.60 A; C/G=2-130.
DR PDB; 3REL; X-ray; 2.70 A; C/G=2-130.
DR PDB; 3TU4; X-ray; 3.00 A; C/G=2-130.
DR PDB; 3UT9; X-ray; 2.20 A; C/G=2-130.
DR PDB; 3UTA; X-ray; 2.07 A; C/G=2-130.
DR PDB; 3UTB; X-ray; 2.20 A; C/G=2-130.
DR PDB; 4J8U; X-ray; 2.38 A; C/G=2-130.
DR PDB; 4J8V; X-ray; 2.58 A; C/G=2-130.
DR PDB; 4J8W; X-ray; 2.41 A; C/G=2-130.
DR PDB; 4J8X; X-ray; 2.87 A; C/G=2-130.
DR PDB; 4LD9; X-ray; 3.31 A; C/G=1-130.
DR PDB; 4R8P; X-ray; 3.28 A; C/G=2-130.
DR PDB; 4WU8; X-ray; 2.45 A; C/G=2-130.
DR PDB; 4WU9; X-ray; 2.60 A; C/G=2-130.
DR PDB; 4XUJ; X-ray; 3.18 A; C/G=2-130.
DR PDB; 4XZQ; X-ray; 2.40 A; C/G=15-121.
DR PDB; 4YS3; X-ray; 3.00 A; C/G=15-121.
DR PDB; 4Z66; X-ray; 2.50 A; C/G=15-121.
DR PDB; 4ZUX; X-ray; 3.82 A; C/G/M/Q=1-130.
DR PDB; 5CP6; X-ray; 2.60 A; C/G=2-130.
DR PDB; 5DNM; X-ray; 2.81 A; C/G=2-130.
DR PDB; 5DNN; X-ray; 2.80 A; C/G=2-130.
DR PDB; 5E5A; X-ray; 2.81 A; C/G=1-130.
DR PDB; 5F99; X-ray; 2.63 A; C/G=2-130.
DR PDB; 5G2E; X-ray; 6.70 A; C/G/K/O/S/W=14-119.
DR PDB; 5HQ2; X-ray; 4.50 A; G=2-130.
DR PDB; 5MLU; X-ray; 2.80 A; C/G=15-119.
DR PDB; 5NL0; X-ray; 5.40 A; C/G/M=2-130.
DR PDB; 5O9G; EM; 4.80 A; C/G=1-130.
DR PDB; 5OMX; X-ray; 2.32 A; C/G=2-130.
DR PDB; 5ONG; X-ray; 2.80 A; C/G=2-130.
DR PDB; 5ONW; X-ray; 2.80 A; C/G=2-130.
DR PDB; 5OXV; X-ray; 6.72 A; C/G/M/Q=1-130.
DR PDB; 5OY7; X-ray; 5.77 A; C/G/K/O/S/W/a/e=1-130.
DR PDB; 5X0X; EM; 3.97 A; C/G=1-130.
DR PDB; 5X0Y; EM; 4.69 A; C/G=2-130.
DR PDB; 5XF6; X-ray; 2.63 A; C/G=2-130.
DR PDB; 5Z3L; EM; 4.31 A; C/G=2-130.
DR PDB; 5Z3O; EM; 3.62 A; C/G=2-130.
DR PDB; 6FQ5; EM; 3.80 A; C/G=10-119.
DR PDB; 6FQ6; EM; 4.00 A; C/G=10-119.
DR PDB; 6FQ8; EM; 4.80 A; C/G=10-119.
DR PDB; 6FTX; EM; 4.50 A; C/G=1-130.
DR PDB; 6G0L; EM; 4.50 A; C/G=1-130.
DR PDB; 6I84; EM; 4.40 A; Q/V=1-130.
DR PDB; 6IRO; EM; 3.40 A; C/G=2-130.
DR PDB; 6IY2; EM; 3.47 A; C/G=10-122.
DR PDB; 6IY3; EM; 3.67 A; C/G=10-122.
DR PDB; 6KIU; EM; 3.20 A; C/G=2-130.
DR PDB; 6KIV; EM; 4.00 A; C/G=2-130.
DR PDB; 6KIW; EM; 4.00 A; C/G=2-130.
DR PDB; 6KIX; EM; 4.10 A; C/G=2-130.
DR PDB; 6KIZ; EM; 4.50 A; C/G=2-130.
DR PDB; 6KW3; EM; 7.13 A; O/S=1-130.
DR PDB; 6KW4; EM; 7.55 A; O/S=1-130.
DR PDB; 6KW5; EM; 10.13 A; O/T=1-130.
DR PDB; 6LTJ; EM; 3.70 A; C/G=1-130.
DR PDB; 6N1Z; X-ray; 2.70 A; B/E=1-130.
DR PDB; 6NE3; EM; 3.90 A; C/G=1-130.
DR PDB; 6NJ9; EM; 2.96 A; C/G=2-130.
DR PDB; 6NN6; EM; 3.90 A; C/G=2-130.
DR PDB; 6NOG; EM; 3.90 A; C/G=2-130.
DR PDB; 6NQA; EM; 3.54 A; C/G=2-130.
DR PDB; 6NZO; EM; 3.80 A; C/G=18-130.
DR PDB; 6O96; EM; 3.50 A; C/G=1-130.
DR PDB; 6OM3; X-ray; 3.30 A; C/G/O/S=1-130.
DR PDB; 6PA7; EM; 2.94 A; C/G=2-130.
DR PDB; 6PWV; EM; 6.20 A; I/M=2-130.
DR PDB; 6PWW; EM; 4.40 A; I/M=2-130.
DR PDB; 6PWX; EM; 4.20 A; I/M=2-130.
DR PDB; 6PX1; EM; 3.30 A; C/G=18-130.
DR PDB; 6PX3; EM; 4.10 A; C/G=18-130.
DR PDB; 6R1T; EM; 3.70 A; C/G=11-121.
DR PDB; 6R1U; EM; 4.36 A; C/G=2-130.
DR PDB; 6R25; EM; 4.61 A; C/G=2-130.
DR PDB; 6RYR; EM; 3.10 A; C/G=1-130.
DR PDB; 6RYU; EM; 4.00 A; C/G=1-130.
DR PDB; 6S01; EM; 3.20 A; C/G=2-130.
DR PDB; 6T9L; EM; 3.60 A; C/G=2-130.
DR PDB; 6TDA; EM; 15.00 A; C/G=2-130.
DR PDB; 6TEM; EM; 3.90 A; C/G=2-130.
DR PDB; 6UXW; EM; 8.96 A; T/X=2-130.
DR PDB; 6VEN; EM; 3.37 A; C/G=2-130.
DR PDB; 6VYP; X-ray; 4.99 A; C/G/c/g=2-130.
DR PDB; 6VZ4; EM; 3.90 A; C/G=1-130.
DR PDB; 6W4L; X-ray; 1.31 A; A=14-105.
DR PDB; 6W5I; EM; 6.90 A; I/M=2-130.
DR PDB; 6W5M; EM; 4.60 A; I/M=2-130.
DR PDB; 6W5N; EM; 6.00 A; I/M=2-130.
DR PDB; 6WKR; EM; 3.50 A; K/R=1-130.
DR PDB; 6WZ5; EM; 2.20 A; C/G=2-130.
DR PDB; 6WZ9; EM; 2.80 A; C/G=2-130.
DR PDB; 6X0N; EM; 10.00 A; C/G/c/g=2-130.
DR PDB; 6Z6P; EM; 4.43 A; G=15-119.
DR PDB; 6ZHX; EM; 2.50 A; C/G=1-130.
DR PDB; 6ZHY; EM; 3.00 A; C=1-130.
DR PDB; 7AT8; EM; 4.40 A; F/J=2-130.
DR PDB; 7CRO; EM; 3.75 A; C/G=2-130.
DR PDB; 7CRP; EM; 3.20 A; C/G=2-130.
DR PDB; 7CRQ; EM; 3.15 A; C/G=2-130.
DR PDB; 7CRR; EM; 3.48 A; C/G=2-130.
DR PDB; 7E8I; EM; 3.10 A; C/G=2-130.
DR PDB; 7EG6; EM; 3.10 A; C/G=2-130.
DR PDB; 7ENN; EM; 2.80 A; C/G=2-130.
DR PDB; 7K6P; EM; 3.20 A; C/G=13-119.
DR PDB; 7K6Q; EM; 3.10 A; C/G=13-119.
DR PDB; 7NKX; EM; 2.90 A; c/g=1-130.
DR PDB; 7NKY; EM; 3.20 A; c/g=1-130.
DR PDB; 7OTQ; EM; 4.80 A; C/G=1-130.
DR PDB; 7SWY; EM; 2.60 A; C/G=2-130.
DR PDB; 7TN2; EM; 2.30 A; C/G=2-130.
DR PDBsum; 1AOI; -.
DR PDBsum; 1KX3; -.
DR PDBsum; 1KX4; -.
DR PDBsum; 1KX5; -.
DR PDBsum; 1M18; -.
DR PDBsum; 1M19; -.
DR PDBsum; 1M1A; -.
DR PDBsum; 1P34; -.
DR PDBsum; 1P3A; -.
DR PDBsum; 1P3B; -.
DR PDBsum; 1P3F; -.
DR PDBsum; 1P3G; -.
DR PDBsum; 1P3I; -.
DR PDBsum; 1P3K; -.
DR PDBsum; 1P3L; -.
DR PDBsum; 1P3M; -.
DR PDBsum; 1P3O; -.
DR PDBsum; 1P3P; -.
DR PDBsum; 1S32; -.
DR PDBsum; 1ZBB; -.
DR PDBsum; 1ZLA; -.
DR PDBsum; 2FJ7; -.
DR PDBsum; 2NZD; -.
DR PDBsum; 3B6F; -.
DR PDBsum; 3B6G; -.
DR PDBsum; 3C1B; -.
DR PDBsum; 3C1C; -.
DR PDBsum; 3KUY; -.
DR PDBsum; 3KWQ; -.
DR PDBsum; 3LJA; -.
DR PDBsum; 3MNN; -.
DR PDBsum; 3O62; -.
DR PDBsum; 3REH; -.
DR PDBsum; 3REI; -.
DR PDBsum; 3REJ; -.
DR PDBsum; 3REK; -.
DR PDBsum; 3REL; -.
DR PDBsum; 3TU4; -.
DR PDBsum; 3UT9; -.
DR PDBsum; 3UTA; -.
DR PDBsum; 3UTB; -.
DR PDBsum; 4J8U; -.
DR PDBsum; 4J8V; -.
DR PDBsum; 4J8W; -.
DR PDBsum; 4J8X; -.
DR PDBsum; 4LD9; -.
DR PDBsum; 4R8P; -.
DR PDBsum; 4WU8; -.
DR PDBsum; 4WU9; -.
DR PDBsum; 4XUJ; -.
DR PDBsum; 4XZQ; -.
DR PDBsum; 4YS3; -.
DR PDBsum; 4Z66; -.
DR PDBsum; 4ZUX; -.
DR PDBsum; 5CP6; -.
DR PDBsum; 5DNM; -.
DR PDBsum; 5DNN; -.
DR PDBsum; 5E5A; -.
DR PDBsum; 5F99; -.
DR PDBsum; 5G2E; -.
DR PDBsum; 5HQ2; -.
DR PDBsum; 5MLU; -.
DR PDBsum; 5NL0; -.
DR PDBsum; 5O9G; -.
DR PDBsum; 5OMX; -.
DR PDBsum; 5ONG; -.
DR PDBsum; 5ONW; -.
DR PDBsum; 5OXV; -.
DR PDBsum; 5OY7; -.
DR PDBsum; 5X0X; -.
DR PDBsum; 5X0Y; -.
DR PDBsum; 5XF6; -.
DR PDBsum; 5Z3L; -.
DR PDBsum; 5Z3O; -.
DR PDBsum; 6FQ5; -.
DR PDBsum; 6FQ6; -.
DR PDBsum; 6FQ8; -.
DR PDBsum; 6FTX; -.
DR PDBsum; 6G0L; -.
DR PDBsum; 6I84; -.
DR PDBsum; 6IRO; -.
DR PDBsum; 6IY2; -.
DR PDBsum; 6IY3; -.
DR PDBsum; 6KIU; -.
DR PDBsum; 6KIV; -.
DR PDBsum; 6KIW; -.
DR PDBsum; 6KIX; -.
DR PDBsum; 6KIZ; -.
DR PDBsum; 6KW3; -.
DR PDBsum; 6KW4; -.
DR PDBsum; 6KW5; -.
DR PDBsum; 6LTJ; -.
DR PDBsum; 6N1Z; -.
DR PDBsum; 6NE3; -.
DR PDBsum; 6NJ9; -.
DR PDBsum; 6NN6; -.
DR PDBsum; 6NOG; -.
DR PDBsum; 6NQA; -.
DR PDBsum; 6NZO; -.
DR PDBsum; 6O96; -.
DR PDBsum; 6OM3; -.
DR PDBsum; 6PA7; -.
DR PDBsum; 6PWV; -.
DR PDBsum; 6PWW; -.
DR PDBsum; 6PWX; -.
DR PDBsum; 6PX1; -.
DR PDBsum; 6PX3; -.
DR PDBsum; 6R1T; -.
DR PDBsum; 6R1U; -.
DR PDBsum; 6R25; -.
DR PDBsum; 6RYR; -.
DR PDBsum; 6RYU; -.
DR PDBsum; 6S01; -.
DR PDBsum; 6T9L; -.
DR PDBsum; 6TDA; -.
DR PDBsum; 6TEM; -.
DR PDBsum; 6UXW; -.
DR PDBsum; 6VEN; -.
DR PDBsum; 6VYP; -.
DR PDBsum; 6VZ4; -.
DR PDBsum; 6W4L; -.
DR PDBsum; 6W5I; -.
DR PDBsum; 6W5M; -.
DR PDBsum; 6W5N; -.
DR PDBsum; 6WKR; -.
DR PDBsum; 6WZ5; -.
DR PDBsum; 6WZ9; -.
DR PDBsum; 6X0N; -.
DR PDBsum; 6Z6P; -.
DR PDBsum; 6ZHX; -.
DR PDBsum; 6ZHY; -.
DR PDBsum; 7AT8; -.
DR PDBsum; 7CRO; -.
DR PDBsum; 7CRP; -.
DR PDBsum; 7CRQ; -.
DR PDBsum; 7CRR; -.
DR PDBsum; 7E8I; -.
DR PDBsum; 7EG6; -.
DR PDBsum; 7ENN; -.
DR PDBsum; 7K6P; -.
DR PDBsum; 7K6Q; -.
DR PDBsum; 7NKX; -.
DR PDBsum; 7NKY; -.
DR PDBsum; 7OTQ; -.
DR PDBsum; 7SWY; -.
DR PDBsum; 7TN2; -.
DR AlphaFoldDB; P06897; -.
DR SASBDB; P06897; -.
DR SMR; P06897; -.
DR BioGRID; 592527; 6.
DR DIP; DIP-39144N; -.
DR IntAct; P06897; 17.
DR DNASU; 734746; -.
DR GeneID; 734746; -.
DR KEGG; xla:734746; -.
DR CTD; 734746; -.
DR Xenbase; XB-GENE-6493983; h2ax.lS.
DR OrthoDB; 1504122at2759; -.
DR EvolutionaryTrace; P06897; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 734746; Expressed in oocyte and 19 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; 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 CDD; cd00074; H2A; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR IDEAL; IID50139; -.
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; DNA-binding; Hydroxylation;
KW Isopeptide bond; Methylation; Nucleosome core; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..130
FT /note="Histone H2A type 1"
FT /id="PRO_0000055294"
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:0000250"
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 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:0000250"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:1AOI"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:1AOI"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:6W4L"
FT HELIX 28..37
FT /evidence="ECO:0007829|PDB:6W4L"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:6W4L"
FT HELIX 47..73
FT /evidence="ECO:0007829|PDB:6W4L"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:6W4L"
FT HELIX 81..89
FT /evidence="ECO:0007829|PDB:6W4L"
FT HELIX 92..97
FT /evidence="ECO:0007829|PDB:6W4L"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:1KX5"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:1KX5"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:1KX5"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:1KX3"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:1KX5"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:1KX5"
SQ SEQUENCE 130 AA; 13966 MW; 09946ABF27FA52A9 CRC64;
MSGRGKQGGK TRAKAKTRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YLAAVLEYLT
AEILELAGNA ARDNKKTRII PRHLQLAVRN DEELNKLLGG VTIAQGGVLP NIQSVLLPKK
TESAKSAKSK
