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 27-MAR-2024, entry version 165. 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). RN [6] {ECO:0007744|PDB:6ZHX, ECO:0007744|PDB:6ZHY} RP STRUCTURE BY ELECTRON MICROSCOPY (2.50 ANGSTROMS) OF NUCLEOSOME CORE RP COMPLEX IN COMPLEX WITH CHD1L. RX PubMed=33357431; DOI=10.1016/j.celrep.2020.108529; RA Lehmann L.C., Bacic L., Hewitt G., Brackmann K., Sabantsev A., Gaullier G., RA Pytharopoulou S., Degliesposti G., Okkenhaug H., Tan S., Costa A., RA Skehel J.M., Boulton S.J., Deindl S.; RT "Mechanistic insights into regulation of the ALC1 remodeler by the RT nucleosome acidic patch."; RL Cell Rep. 33:108529-108529(2020). RN [7] {ECO:0007744|PDB:7OTQ} RP STRUCTURE BY ELECTRON MICROSCOPY (4.80 ANGSTROMS) OF NUCLEOSOME CORE RP COMPLEX IN COMPLEX WITH CHD1L. RX PubMed=34486521; DOI=10.7554/elife.71420; RA Bacic L., Gaullier G., Sabantsev A., Lehmann L.C., Brackmann K., RA Dimakou D., Halic M., Hewitt G., Boulton S.J., Deindl S.; RT "Structure and dynamics of the chromatin remodeler ALC1 bound to a RT PARylated nucleosome."; RL Elife 10:0-0(2021). RN [8] {ECO:0007744|PDB:7ENN} RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) OF 2-130 OF NUCLEOSOME RP CORE COMPLEX IN COMPLEX WITH CHD1L. RX PubMed=34210977; DOI=10.1038/s41467-021-24320-4; RA Wang L., Chen K., Chen Z.; RT "Structural basis of ALC1/CHD1L autoinhibition and the mechanism of RT activation by the nucleosome."; RL Nat. Commun. 12:4057-4057(2021). 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; 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; 7MBM; EM; -; I/M=2-130. DR PDB; 7MBN; EM; -; I/M=2-130. DR PDB; 7NKX; EM; 2.90 A; c/g=1-130. DR PDB; 7NKY; EM; 3.20 A; c/g=1-130. DR PDB; 7OH9; EM; 3.00 A; C/G=2-130. DR PDB; 7OHA; EM; 2.90 A; C/G=2-130. DR PDB; 7OHB; EM; 3.40 A; C/G=2-130. DR PDB; 7OHC; EM; 2.50 A; C/G=2-130. 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 PDB; 7UD5; EM; 4.25 A; C/G=1-130. DR PDB; 7VDT; EM; 2.80 A; C/G=1-130. DR PDB; 7VDV; EM; 3.40 A; C/G=1-130. DR PDB; 7VVU; EM; 3.40 A; N/S=1-130. DR PDB; 7VVZ; EM; 8.80 A; N/S=1-130. DR PDB; 7XFC; EM; 2.90 A; C/G=1-130. DR PDB; 7XFH; EM; 2.90 A; C/G=1-130. DR PDB; 7XFI; EM; 2.90 A; C/G=1-130. DR PDB; 7XFJ; EM; 3.00 A; C/G=1-130. DR PDB; 7XFL; EM; 2.80 A; C/G=1-130. DR PDB; 7XFM; EM; 3.10 A; C/G=1-130. DR PDB; 7XFN; EM; 2.80 A; C/G=1-130. DR PDB; 7XNP; EM; 2.90 A; C/G=1-130. DR PDB; 7XPX; EM; 3.20 A; C/G=2-130. DR PDB; 7ZS9; EM; 3.10 A; c/g=2-130. DR PDB; 7ZSA; EM; 4.00 A; c/g=2-130. DR PDB; 7ZSB; EM; 6.60 A; c/g=2-130. DR PDB; 8AAG; EM; 10.00 A; C/G=2-130. DR PDB; 8B0A; EM; 3.00 A; C/G=1-130. DR PDB; 8BVW; EM; 4.00 A; c/g=1-130. DR PDB; 8BYQ; EM; 4.10 A; c/g=1-130. DR PDB; 8BZ1; EM; 3.80 A; c/g=1-130. DR PDB; 8CWW; EM; 2.74 A; C/G=2-130. DR PDB; 8CZE; EM; 2.58 A; C/G=2-130. DR PDB; 8DU4; EM; 3.55 A; C/G=1-130. DR PDB; 8ETT; EM; 6.68 A; C=1-130. DR PDB; 8F86; EM; 3.10 A; C/G=2-130. DR PDB; 8GPN; EM; 3.20 A; C/G=1-130. DR PDB; 8OF4; EM; 2.94 A; C/G=1-130. DR PDB; 8SIY; EM; 2.90 A; E/I=2-130. DR PDB; 8SVF; EM; 3.20 A; C/G=1-130. DR PDB; 8T3T; EM; 3.21 A; C/G=2-130. DR PDB; 8T3W; EM; 3.25 A; C/G=2-130. DR PDB; 8T3Y; EM; 3.47 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; 7MBM; -. DR PDBsum; 7MBN; -. DR PDBsum; 7NKX; -. DR PDBsum; 7NKY; -. DR PDBsum; 7OH9; -. DR PDBsum; 7OHA; -. DR PDBsum; 7OHB; -. DR PDBsum; 7OHC; -. DR PDBsum; 7OTQ; -. DR PDBsum; 7SWY; -. DR PDBsum; 7TN2; -. DR PDBsum; 7UD5; -. DR PDBsum; 7VDT; -. DR PDBsum; 7VDV; -. DR PDBsum; 7VVU; -. DR PDBsum; 7VVZ; -. DR PDBsum; 7XFC; -. DR PDBsum; 7XFH; -. DR PDBsum; 7XFI; -. DR PDBsum; 7XFJ; -. DR PDBsum; 7XFL; -. DR PDBsum; 7XFM; -. DR PDBsum; 7XFN; -. DR PDBsum; 7XNP; -. DR PDBsum; 7XPX; -. DR PDBsum; 7ZS9; -. DR PDBsum; 7ZSA; -. DR PDBsum; 7ZSB; -. DR PDBsum; 8AAG; -. DR PDBsum; 8B0A; -. DR PDBsum; 8BVW; -. DR PDBsum; 8BYQ; -. DR PDBsum; 8BZ1; -. DR PDBsum; 8CWW; -. DR PDBsum; 8CZE; -. DR PDBsum; 8DU4; -. DR PDBsum; 8ETT; -. DR PDBsum; 8F86; -. DR PDBsum; 8GPN; -. DR PDBsum; 8OF4; -. DR PDBsum; 8SIY; -. DR PDBsum; 8SVF; -. DR PDBsum; 8T3T; -. DR PDBsum; 8T3W; -. DR PDBsum; 8T3Y; -. DR AlphaFoldDB; P06897; -. DR EMDB; EMD-0458; -. DR EMDB; EMD-0468; -. DR EMDB; EMD-0480; -. DR EMDB; EMD-0693; -. DR EMDB; EMD-0694; -. DR EMDB; EMD-0695; -. DR EMDB; EMD-0777; -. DR EMDB; EMD-0779; -. DR EMDB; EMD-0974; -. DR EMDB; EMD-10058; -. DR EMDB; EMD-10059; -. DR EMDB; EMD-10069; -. DR EMDB; EMD-10415; -. DR EMDB; EMD-10465; -. DR EMDB; EMD-11102; -. DR EMDB; EMD-11220; -. DR EMDB; EMD-11221; -. DR EMDB; EMD-11910; -. DR EMDB; EMD-12449; -. DR EMDB; EMD-12450; -. DR EMDB; EMD-12897; -. DR EMDB; EMD-12898; -. DR EMDB; EMD-12899; -. DR EMDB; EMD-12900; -. DR EMDB; EMD-13065; -. DR EMDB; EMD-15777; -. DR EMDB; EMD-16842; -. DR EMDB; EMD-16845; -. DR EMDB; EMD-17944; -. DR EMDB; EMD-20281; -. DR EMDB; EMD-20512; -. DR EMDB; EMD-20513; -. DR EMDB; EMD-20514; -. DR EMDB; EMD-20934; -. DR EMDB; EMD-21157; -. DR EMDB; EMD-21484; -. DR EMDB; EMD-21542; -. DR EMDB; EMD-21543; -. DR EMDB; EMD-21544; -. DR EMDB; EMD-21707; -. DR EMDB; EMD-21970; -. DR EMDB; EMD-21971; -. DR EMDB; EMD-21980; -. DR EMDB; EMD-22691; -. DR EMDB; EMD-22692; -. DR EMDB; EMD-23738; -. DR EMDB; EMD-23739; -. DR EMDB; EMD-28598; -. DR EMDB; EMD-30453; -. DR EMDB; EMD-30455; -. DR EMDB; EMD-30456; -. DR EMDB; EMD-30457; -. DR EMDB; EMD-31020; -. DR EMDB; EMD-31106; -. DR EMDB; EMD-31217; -. DR EMDB; EMD-32148; -. DR EMDB; EMD-32150; -. DR EMDB; EMD-33171; -. DR EMDB; EMD-33172; -. DR EMDB; EMD-33173; -. DR EMDB; EMD-33174; -. DR EMDB; EMD-33175; -. DR EMDB; EMD-33176; -. DR EMDB; EMD-33177; -. DR EMDB; EMD-33322; -. DR EMDB; EMD-3765; -. DR EMDB; EMD-40522; -. DR EMDB; EMD-40789; -. DR EMDB; EMD-41011; -. DR EMDB; EMD-41015; -. DR EMDB; EMD-41016; -. DR EMDB; EMD-4297; -. DR EMDB; EMD-4298; -. DR EMDB; EMD-4299; -. DR EMDB; EMD-4318; -. DR EMDB; EMD-4336; -. DR EMDB; EMD-4429; -. DR EMDB; EMD-4704; -. DR EMDB; EMD-4705; -. DR EMDB; EMD-4710; -. DR EMDB; EMD-6699; -. DR EMDB; EMD-6700; -. DR EMDB; EMD-6879; -. DR EMDB; EMD-6880; -. DR EMDB; EMD-9356; -. DR EMDB; EMD-9384; -. DR EMDB; EMD-9720; -. DR EMDB; EMD-9748; -. DR EMDB; EMD-9998; -. DR EMDB; EMD-9999; -. 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 AGR; Xenbase:XB-GENE-6493983; -. DR CTD; 734746; -. DR Xenbase; XB-GENE-6493983; h2ax.S. DR OrthoDB; 4019611at2759; -. DR EvolutionaryTrace; P06897; -. DR Proteomes; UP000186698; Chromosome 3S. DR Bgee; 734746; Expressed in oocyte and 19 other cell types or 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; Histone, subunit A; 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; HISTONE H2A; 1. DR PANTHER; PTHR23430:SF407; HISTONE H2A TYPE 1-E; 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; 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 //