H2A1_HUMAN
ID H2A1_HUMAN Reviewed; 130 AA.
AC P0C0S8; P02261; Q2M1R2; Q76PA6;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Histone H2A type 1;
DE Short=H2A.1;
DE AltName: Full=Histone H2A/ptl;
GN Name=H2AC11 {ECO:0000312|HGNC:HGNC:4737}; Synonyms=H2AFP, HIST1H2AG;
GN and
GN Name=H2AC13 {ECO:0000312|HGNC:HGNC:4725}; Synonyms=H2AFC, HIST1H2AI;
GN and
GN Name=H2AC15 {ECO:0000312|HGNC:HGNC:4726}; Synonyms=H2AFD, HIST1H2AK;
GN and
GN Name=H2AC16 {ECO:0000312|HGNC:HGNC:4730}; Synonyms=H2AFI, HIST1H2AL;
GN and
GN Name=H2AC17 {ECO:0000312|HGNC:HGNC:4735}; Synonyms=H2AFN, HIST1H2AM;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (H2AC13; H2AC15 AND H2AC16).
RX PubMed=9439656; DOI=10.1007/s004390050630;
RA Albig W., Doenecke D.;
RT "The human histone gene cluster at the D6S105 locus.";
RL Hum. Genet. 101:284-294(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (H2AC13; H2AC15 AND H2AC16).
RX PubMed=10064132; DOI=10.1515/bc.1999.002;
RA Albig W., Trappe R., Kardalinou E., Eick S., Doenecke D.;
RT "The human H2A and H2B histone gene complement.";
RL Biol. Chem. 380:7-18(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE (H2AC17).
RX PubMed=1768865; DOI=10.3109/10425179109020799;
RA Dobner T., Wolf I., Mai B., Lipp M.;
RT "A novel divergently transcribed human histone H2A/H2B gene pair.";
RL DNA Seq. 1:409-413(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE (H2AC11).
RX PubMed=8179821; DOI=10.1089/dna.1994.13.161;
RA Mannironi C., Orr A., Hatch C., Pilch D., Ivanova V., Bonner W.;
RT "The relative expression of human histone H2A genes is similar in different
RT types of proliferating cells.";
RL DNA Cell Biol. 13:161-170(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (H2AC11; H2AC13; H2AC15; H2AC16 AND
RP H2AC17).
RX PubMed=12408966; DOI=10.1006/geno.2002.6850;
RA Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.;
RT "The human and mouse replication-dependent histone genes.";
RL Genomics 80:487-498(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (H2AC13; H2AC15; H2AC16 AND
RP H2AC17).
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, and Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP AMINO-ACID COMPOSITION OF TRYPTIC PEPTIDES.
RC TISSUE=Spleen;
RX PubMed=7410338;
RA Hayashi T., Ohe Y., Hayashi H., Iwai K.;
RT "Human spleen histone H2A. Isolation and four variant sequences.";
RL J. Biochem. 88:27-34(1980).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-2, AND
RP ACETYLATION AT SER-2.
RX PubMed=11709551; DOI=10.1074/jbc.m107894200;
RA Galasinski S.C., Louie D.F., Gloor K.K., Resing K.A., Ahn N.G.;
RT "Global regulation of post-translational modifications on core histones.";
RL J. Biol. Chem. 277:2579-2588(2002).
RN [10]
RP PHOSPHORYLATION AT THR-121.
RX PubMed=15078818; DOI=10.1101/gad.1184604;
RA Aihara H., Nakagawa T., Yasui K., Ohta T., Hirose S., Dhomae N., Takio K.,
RA Kaneko M., Takeshima Y., Muramatsu M., Ito T.;
RT "Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 during mitosis in
RT the early Drosophila embryo.";
RL Genes Dev. 18:877-888(2004).
RN [11]
RP PHOSPHORYLATION AT SER-2, AND MUTAGENESIS OF SER-2.
RX PubMed=15010469; DOI=10.1074/jbc.m400099200;
RA Zhang Y., Griffin K., Mondal N., Parvin J.D.;
RT "Phosphorylation of histone H2A inhibits transcription on chromatin
RT templates.";
RL J. Biol. Chem. 279:21866-21872(2004).
RN [12]
RP UBIQUITINATION AT LYS-120.
RX PubMed=15386022; DOI=10.1038/nature02985;
RA Wang H., Wang L., Erdjument-Bromage H., Vidal M., Tempst P., Jones R.S.,
RA Zhang Y.;
RT "Role of histone H2A ubiquitination in Polycomb silencing.";
RL Nature 431:873-878(2004).
RN [13]
RP ACETYLATION AT SER-2, CITRULLINATION AT ARG-4, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15823041; DOI=10.1021/bi047505c;
RA Hagiwara T., Hidaka Y., Yamada M.;
RT "Deimination of histone H2A and H4 at arginine 3 in HL-60 granulocytes.";
RL Biochemistry 44:5827-5834(2005).
RN [14]
RP UBIQUITINATION AT LYS-120.
RX PubMed=16359901; DOI=10.1016/j.molcel.2005.12.002;
RA Cao R., Tsukada Y., Zhang Y.;
RT "Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing.";
RL Mol. Cell 20:845-854(2005).
RN [15]
RP UBIQUITINATION AT LYS-120.
RX PubMed=16702407; DOI=10.1101/gad.373706;
RA Bergink S., Salomons F.A., Hoogstraten D., Groothuis T.A.M., de Waard H.,
RA Wu J., Yuan L., Citterio E., Houtsmuller A.B., Neefjes J.,
RA Hoeijmakers J.H.J., Vermeulen W., Dantuma N.P.;
RT "DNA damage triggers nucleotide excision repair-dependent
RT monoubiquitylation of histone H2A.";
RL Genes Dev. 20:1343-1352(2006).
RN [16]
RP MASS SPECTROMETRY, AND ACETYLATION AT SER-2.
RX PubMed=16457589; DOI=10.1021/pr050269n;
RA Boyne M.T. II, Pesavento J.J., Mizzen C.A., Kelleher N.L.;
RT "Precise characterization of human histones in the H2A gene family by top
RT down mass spectrometry.";
RL J. Proteome Res. 5:248-253(2006).
RN [17]
RP UBIQUITINATION.
RX PubMed=18001824; DOI=10.1016/j.cell.2007.09.040;
RA Mailand N., Bekker-Jensen S., Faustrup H., Melander F., Bartek J.,
RA Lukas C., Lukas J.;
RT "RNF8 ubiquitylates histones at DNA double-strand breaks and promotes
RT assembly of repair proteins.";
RL Cell 131:887-900(2007).
RN [18]
RP UBIQUITINATION.
RX PubMed=18001825; DOI=10.1016/j.cell.2007.09.041;
RA Huen M.S.Y., Grant R., Manke I., Minn K., Yu X., Yaffe M.B., Chen J.;
RT "RNF8 transduces the DNA-damage signal via histone ubiquitylation and
RT checkpoint protein assembly.";
RL Cell 131:901-914(2007).
RN [19]
RP UBIQUITINATION.
RX PubMed=19203578; DOI=10.1016/j.cell.2008.12.042;
RA Stewart G.S., Panier S., Townsend K., Al-Hakim A.K., Kolas N.K.,
RA Miller E.S., Nakada S., Ylanko J., Olivarius S., Mendez M., Oldreive C.,
RA Wildenhain J., Tagliaferro A., Pelletier L., Taubenheim N., Durandy A.,
RA Byrd P.J., Stankovic T., Taylor A.M.R., Durocher D.;
RT "The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling
RT cascade at sites of DNA damage.";
RL Cell 136:420-434(2009).
RN [20]
RP UBIQUITINATION.
RX PubMed=19203579; DOI=10.1016/j.cell.2008.12.041;
RA Doil C., Mailand N., Bekker-Jensen S., Menard P., Larsen D.H.,
RA Pepperkok R., Ellenberg J., Panier S., Durocher D., Bartek J., Lukas J.,
RA Lukas C.;
RT "RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to
RT allow accumulation of repair proteins.";
RL Cell 136:435-446(2009).
RN [21]
RP CROTONYLATION AT LYS-37; LYS-119; LYS-120 AND LYS-126.
RX PubMed=21925322; DOI=10.1016/j.cell.2011.08.008;
RA Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T.,
RA Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q., Wysocka J.,
RA Ye Y., Khochbin S., Ren B., Zhao Y.;
RT "Identification of 67 histone marks and histone lysine crotonylation as a
RT new type of histone modification.";
RL Cell 146:1016-1028(2011).
RN [22]
RP UBIQUITINATION AT LYS-14 AND LYS-16 BY RNF168.
RX PubMed=22980979; DOI=10.1016/j.cell.2012.08.005;
RA Mattiroli F., Vissers J.H., van Dijk W.J., Ikpa P., Citterio E.,
RA Vermeulen W., Marteijn J.A., Sixma T.K.;
RT "RNF168 ubiquitinates K13-15 on H2A/H2AX to drive DNA Damage signaling.";
RL Cell 150:1182-1195(2012).
RN [23]
RP UBIQUITINATION AT LYS-14 AND LYS-16 BY RNF168.
RX PubMed=22713238; DOI=10.4161/cc.20919;
RA Gatti M., Pinato S., Maspero E., Soffientini P., Polo S., Penengo L.;
RT "A novel ubiquitin mark at the N-terminal tail of histone H2As targeted by
RT RNF168 ubiquitin ligase.";
RL Cell Cycle 11:2538-2544(2012).
RN [24]
RP SUCCINYLATION AT LYS-10 AND LYS-96.
RX PubMed=22389435; DOI=10.1074/mcp.m111.015875;
RA Xie Z., Dai J., Dai L., Tan M., Cheng Z., Wu Y., Boeke J.D., Zhao Y.;
RT "Lysine succinylation and lysine malonylation in histones.";
RL Mol. Cell. Proteomics 11:100-107(2012).
RN [25]
RP PHOSPHORYLATION AT THR-121.
RX PubMed=24140421; DOI=10.1016/j.molcel.2013.09.017;
RA Kim K., Kim J.M., Kim J.S., Choi J., Lee Y.S., Neamati N., Song J.S.,
RA Heo K., An W.;
RT "VprBP has intrinsic kinase activity targeting histone H2A and represses
RT gene transcription.";
RL Mol. Cell 52:459-467(2013).
RN [26]
RP HYDROXYBUTYRYLATION AT LYS-6; LYS-10; LYS-37; LYS-75; LYS-76; LYS-96 AND
RP LYS-119.
RX PubMed=24681537; DOI=10.1038/nchembio.1497;
RA Dai L., Peng C., Montellier E., Lu Z., Chen Y., Ishii H., Debernardi A.,
RA Buchou T., Rousseaux S., Jin F., Sabari B.R., Deng Z., Allis C.D., Ren B.,
RA Khochbin S., Zhao Y.;
RT "Lysine 2-hydroxyisobutyrylation is a widely distributed active histone
RT mark.";
RL Nat. Chem. Biol. 10:365-370(2014).
RN [27]
RP METHYLATION AT GLN-105.
RX PubMed=24352239; DOI=10.1038/nature12819;
RA Tessarz P., Santos-Rosa H., Robson S.C., Sylvestersen K.B., Nelson C.J.,
RA Nielsen M.L., Kouzarides T.;
RT "Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated
RT modification.";
RL Nature 505:564-568(2014).
RN [28]
RP UBIQUITINATION AT LYS-120.
RX PubMed=25470042; DOI=10.1038/nature13955;
RA Bhatnagar S., Gazin C., Chamberlain L., Ou J., Zhu X., Tushir J.S.,
RA Virbasius C.M., Lin L., Zhu L.J., Wajapeyee N., Green M.R.;
RT "TRIM37 is a new histone H2A ubiquitin ligase and breast cancer
RT oncoprotein.";
RL Nature 516:116-120(2014).
RN [29]
RP DEUBIQUITINATION AT LYS-14 AND LYS-16 BY USP51.
RX PubMed=27083998; DOI=10.1101/gad.271841.115;
RA Wang Z., Zhang H., Liu J., Cheruiyot A., Lee J.H., Ordog T., Lou Z.,
RA You Z., Zhang Z.;
RT "USP51 deubiquitylates H2AK13,15ub and regulates DNA damage response.";
RL Genes Dev. 30:946-959(2016).
RN [30]
RP HYDROXYBUTYRYLATION AT LYS-10; LYS-14; LYS-37; LYS-96 AND LYS-119.
RX PubMed=27105115; DOI=10.1016/j.molcel.2016.03.036;
RA Xie Z., Zhang D., Chung D., Tang Z., Huang H., Dai L., Qi S., Li J.,
RA Colak G., Chen Y., Xia C., Peng C., Ruan H., Kirkey M., Wang D.,
RA Jensen L.M., Kwon O.K., Lee S., Pletcher S.D., Tan M., Lombard D.B.,
RA White K.P., Zhao H., Li J., Roeder R.G., Yang X., Zhao Y.;
RT "Metabolic regulation of gene expression by histone lysine beta-
RT hydroxybutyrylation.";
RL Mol. Cell 62:194-206(2016).
RN [31]
RP GLUTARYLATION AT LYS-96; LYS-100; LYS-119; LYS-120 AND LYS-126.
RX PubMed=31542297; DOI=10.1016/j.molcel.2019.08.018;
RA Bao X., Liu Z., Zhang W., Gladysz K., Fung Y.M.E., Tian G., Xiong Y.,
RA Wong J.W.H., Yuen K.W.Y., Li X.D.;
RT "Glutarylation of histone H4 lysine 91 regulates chromatin dynamics.";
RL Mol. Cell 0:0-0(2019).
RN [32] {ECO:0007744|PDB:6X59, ECO:0007744|PDB:6X5A, ECO:0007744|PDB:6XJD}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.98 ANGSTROMS) OF 2-130 IN COMPLEX WITH
RP NUCLEOSOME CORE AND CGAS.
RX PubMed=32911481; DOI=10.1038/s41586-020-2749-z;
RA Zhao B., Xu P., Rowlett C.M., Jing T., Shinde O., Lei Y., West A.P.,
RA Liu W.R., Li P.;
RT "The molecular basis of tight nuclear tethering and inactivation of cGAS.";
RL Nature 587:673-677(2020).
RN [33] {ECO:0007744|PDB:7JO9, ECO:0007744|PDB:7JOA}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) OF 2-130 IN COMPLEX WITH
RP NUCLEOSOME CORE AND CGAS.
RX PubMed=32913000; DOI=10.1126/science.abd0609;
RA Boyer J.A., Spangler C.J., Strauss J.D., Cesmat A.P., Liu P., McGinty R.K.,
RA Zhang Q.;
RT "Structural basis of nucleosome-dependent cGAS inhibition.";
RL Science 370:450-454(2020).
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 -!- INTERACTION:
CC P0C0S8; P55201: BRPF1; NbExp=8; IntAct=EBI-1390628, EBI-2837428;
CC P0C0S8; Q99543: DNAJC2; NbExp=2; IntAct=EBI-1390628, EBI-11017224;
CC P0C0S8; O95760: IL33; NbExp=3; IntAct=EBI-1390628, EBI-724057;
CC P0C0S8; Q99496: RNF2; NbExp=5; IntAct=EBI-1390628, EBI-722416;
CC P0C0S8; P63104: YWHAZ; NbExp=2; IntAct=EBI-1390628, EBI-347088;
CC P0C0S8; Q9DUM3; Xeno; NbExp=3; IntAct=EBI-1390628, EBI-7971837;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- PTM: Deiminated on Arg-4 in granulocytes upon calcium entry.
CC {ECO:0000269|PubMed:15823041}.
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.
CC Monoubiquitination of Lys-120 (H2AK119Ub) by TRIM37 may promote
CC transformation of cells in a number of breast cancers
CC (PubMed:25470042). Following DNA double-strand breaks (DSBs), it is
CC ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2
CC ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the
CC recruitment of repair proteins to sites of DNA damage. Ubiquitination
CC at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response
CC to DNA damage is initiated by RNF168 that mediates monoubiquitination
CC at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to
CC monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains
CC in vitro. Deubiquitinated by USP51 at Lys-14 and Lys-16 (H2AK13Ub and
CC H2AK15Ub, respectively) after damaged DNA is repaired
CC (PubMed:27083998). H2AK119Ub and ionizing radiation-induced 'Lys-63'-
CC linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events.
CC {ECO:0000269|PubMed:15386022, ECO:0000269|PubMed:16359901,
CC ECO:0000269|PubMed:16702407, ECO:0000269|PubMed:18001824,
CC ECO:0000269|PubMed:18001825, ECO:0000269|PubMed:19203578,
CC ECO:0000269|PubMed:19203579, ECO:0000269|PubMed:22713238,
CC ECO:0000269|PubMed:22980979, ECO:0000269|PubMed:24352239,
CC ECO:0000269|PubMed:25470042, ECO:0000269|PubMed:27083998}.
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:0000269|PubMed:11709551,
CC ECO:0000269|PubMed:15010469, ECO:0000269|PubMed:15078818,
CC ECO:0000269|PubMed:15823041, ECO:0000269|PubMed:16457589,
CC ECO:0000269|PubMed:24140421}.
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 (PubMed:24352239).
CC {ECO:0000269|PubMed:24352239}.
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:0000269|PubMed:21925322}.
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 -!- MASS SPECTROMETRY: Mass=13993.9; Method=Electrospray; Note=Monoisotopic
CC with N-acetylserine.; Evidence={ECO:0000269|PubMed:16457589};
CC -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR EMBL; Z83742; CAB06037.1; -; Genomic_DNA.
DR EMBL; Z83739; CAB06034.1; -; Genomic_DNA.
DR EMBL; X83549; CAA58539.1; -; Genomic_DNA.
DR EMBL; X57138; CAA40417.1; -; Genomic_DNA.
DR EMBL; L19778; AAC24466.1; -; mRNA.
DR EMBL; AY131987; AAN59968.1; -; Genomic_DNA.
DR EMBL; AY131989; AAN59970.1; -; Genomic_DNA.
DR EMBL; AY131991; AAN59972.1; -; Genomic_DNA.
DR EMBL; AY131992; AAN59973.1; -; Genomic_DNA.
DR EMBL; AY131993; AAN59974.1; -; Genomic_DNA.
DR EMBL; Z98744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL009179; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL021807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016677; AAH16677.1; -; mRNA.
DR EMBL; BC069306; AAH69306.1; -; mRNA.
DR EMBL; BC104199; AAI04200.1; -; mRNA.
DR EMBL; BC104198; AAI04199.1; -; mRNA.
DR EMBL; BC105129; AAI05130.1; -; mRNA.
DR EMBL; BC112072; AAI12073.1; -; mRNA.
DR EMBL; BC112254; AAI12255.1; -; mRNA.
DR EMBL; BC112256; AAI12257.1; -; mRNA.
DR CCDS; CCDS4619.1; -.
DR CCDS; CCDS4626.1; -.
DR CCDS; CCDS4632.1; -.
DR CCDS; CCDS4634.1; -.
DR CCDS; CCDS4639.1; -.
DR PIR; B56624; HSHUA1.
DR RefSeq; NP_003500.1; NM_003509.2.
DR RefSeq; NP_003501.1; NM_003510.2.
DR RefSeq; NP_003502.1; NM_003511.2.
DR RefSeq; NP_003505.1; NM_003514.2.
DR RefSeq; NP_066408.1; NM_021064.4.
DR PDB; 4QYL; X-ray; 1.80 A; E/F/G/H=2-13.
DR PDB; 5KGF; EM; 4.54 A; C/G=1-130.
DR PDB; 6R0C; EM; 4.20 A; C/G=1-130.
DR PDB; 6RNY; EM; 3.90 A; C/G=1-130.
DR PDB; 6X59; EM; 2.98 A; C/G=2-130.
DR PDB; 6X5A; EM; 4.36 A; C/G=2-130.
DR PDB; 6XJD; EM; 6.80 A; C/G=2-130.
DR PDB; 7BG9; EM; 3.80 A; L=1-130.
DR PDB; 7E8D; EM; 2.80 A; C/G=2-130.
DR PDB; 7JO9; EM; 3.30 A; C/G=2-130.
DR PDB; 7JOA; EM; 3.30 A; C/G=2-130.
DR PDBsum; 4QYL; -.
DR PDBsum; 5KGF; -.
DR PDBsum; 6R0C; -.
DR PDBsum; 6RNY; -.
DR PDBsum; 6X59; -.
DR PDBsum; 6X5A; -.
DR PDBsum; 6XJD; -.
DR PDBsum; 7BG9; -.
DR PDBsum; 7E8D; -.
DR PDBsum; 7JO9; -.
DR PDBsum; 7JOA; -.
DR AlphaFoldDB; P0C0S8; -.
DR SMR; P0C0S8; -.
DR BioGRID; 113925; 37.
DR BioGRID; 113926; 13.
DR BioGRID; 113928; 74.
DR BioGRID; 113932; 248.
DR BioGRID; 114459; 184.
DR DIP; DIP-39638N; -.
DR IntAct; P0C0S8; 76.
DR MINT; P0C0S8; -.
DR STRING; 9606.ENSP00000351589; -.
DR GlyGen; P0C0S8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P0C0S8; -.
DR PhosphoSitePlus; P0C0S8; -.
DR SwissPalm; P0C0S8; -.
DR BioMuta; HIST1H2AI; -.
DR DMDM; 83288406; -.
DR EPD; P0C0S8; -.
DR jPOST; P0C0S8; -.
DR MassIVE; P0C0S8; -.
DR MaxQB; P0C0S8; -.
DR PaxDb; P0C0S8; -.
DR PeptideAtlas; P0C0S8; -.
DR PRIDE; P0C0S8; -.
DR TopDownProteomics; P0C0S8; -.
DR Antibodypedia; 44633; 381 antibodies from 22 providers.
DR Antibodypedia; 64494; 152 antibodies from 5 providers.
DR Antibodypedia; 72665; 31 antibodies from 3 providers.
DR Antibodypedia; 74550; 32 antibodies from 4 providers.
DR Antibodypedia; 76502; 7 antibodies from 4 providers.
DR DNASU; 8329; -.
DR Ensembl; ENST00000358739.5; ENSP00000351589.3; ENSG00000196747.5.
DR Ensembl; ENST00000359193.4; ENSP00000352119.2; ENSG00000196787.4.
DR Ensembl; ENST00000359611.4; ENSP00000352627.3; ENSG00000278677.2.
DR Ensembl; ENST00000613174.2; ENSP00000482538.2; ENSG00000276903.2.
DR Ensembl; ENST00000618958.2; ENSP00000482431.2; ENSG00000275221.2.
DR GeneID; 8329; -.
DR GeneID; 8330; -.
DR GeneID; 8332; -.
DR GeneID; 8336; -.
DR GeneID; 8969; -.
DR KEGG; hsa:8329; -.
DR KEGG; hsa:8330; -.
DR KEGG; hsa:8332; -.
DR KEGG; hsa:8336; -.
DR KEGG; hsa:8969; -.
DR MANE-Select; ENST00000358739.5; ENSP00000351589.3; NM_003509.3; NP_003500.1.
DR MANE-Select; ENST00000359193.4; ENSP00000352119.2; NM_021064.5; NP_066408.1.
DR MANE-Select; ENST00000359611.4; ENSP00000352627.3; NM_003514.2; NP_003505.1.
DR MANE-Select; ENST00000613174.2; ENSP00000482538.2; NM_003511.3; NP_003502.1.
DR MANE-Select; ENST00000618958.2; ENSP00000482431.2; NM_003510.3; NP_003501.1.
DR UCSC; uc003niw.4; human.
DR CTD; 8329; -.
DR CTD; 8330; -.
DR CTD; 8332; -.
DR CTD; 8336; -.
DR CTD; 8969; -.
DR DisGeNET; 8329; -.
DR DisGeNET; 8330; -.
DR DisGeNET; 8332; -.
DR DisGeNET; 8336; -.
DR DisGeNET; 8969; -.
DR GeneCards; H2AC11; -.
DR GeneCards; H2AC13; -.
DR GeneCards; H2AC15; -.
DR GeneCards; H2AC16; -.
DR GeneCards; H2AC17; -.
DR HGNC; HGNC:4737; H2AC11.
DR HGNC; HGNC:4725; H2AC13.
DR HGNC; HGNC:4726; H2AC15.
DR HGNC; HGNC:4730; H2AC16.
DR HGNC; HGNC:4735; H2AC17.
DR HPA; ENSG00000196747; Tissue enhanced (bone marrow, brain).
DR HPA; ENSG00000196787; Tissue enhanced (breast, testis).
DR HPA; ENSG00000275221; Low tissue specificity.
DR HPA; ENSG00000276903; Tissue enhanced (bone marrow, brain).
DR HPA; ENSG00000278677; Tissue enhanced (bone marrow, brain).
DR MIM; 602787; gene.
DR MIM; 602788; gene.
DR MIM; 602793; gene.
DR MIM; 602796; gene.
DR MIM; 615012; gene.
DR neXtProt; NX_P0C0S8; -.
DR OpenTargets; ENSG00000196747; -.
DR OpenTargets; ENSG00000196787; -.
DR OpenTargets; ENSG00000275221; -.
DR OpenTargets; ENSG00000276903; -.
DR OpenTargets; ENSG00000278677; -.
DR VEuPathDB; HostDB:ENSG00000196747; -.
DR VEuPathDB; HostDB:ENSG00000196787; -.
DR VEuPathDB; HostDB:ENSG00000275221; -.
DR VEuPathDB; HostDB:ENSG00000276903; -.
DR VEuPathDB; HostDB:ENSG00000278677; -.
DR eggNOG; KOG1756; Eukaryota.
DR GeneTree; ENSGT00940000153125; -.
DR HOGENOM; CLU_062828_3_1_1; -.
DR InParanoid; P0C0S8; -.
DR OMA; MPNIHQT; -.
DR OrthoDB; 1504122at2759; -.
DR PhylomeDB; P0C0S8; -.
DR TreeFam; TF300137; -.
DR PathwayCommons; P0C0S8; -.
DR Reactome; R-HSA-3214815; HDACs deacetylate histones.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR Reactome; R-HSA-3214858; RMTs methylate histone arginines.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-5689901; Metalloprotease DUBs.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR SignaLink; P0C0S8; -.
DR SIGNOR; P0C0S8; -.
DR BioGRID-ORCS; 8329; 275 hits in 637 CRISPR screens.
DR BioGRID-ORCS; 8330; 223 hits in 1059 CRISPR screens.
DR BioGRID-ORCS; 8332; 254 hits in 993 CRISPR screens.
DR BioGRID-ORCS; 8336; 318 hits in 995 CRISPR screens.
DR BioGRID-ORCS; 8969; 44 hits in 1034 CRISPR screens.
DR ChiTaRS; HIST1H2AI; human.
DR ChiTaRS; HIST1H2AM; human.
DR GeneWiki; HIST1H2AG; -.
DR GeneWiki; HIST1H2AI; -.
DR GeneWiki; HIST1H2AK; -.
DR GeneWiki; HIST1H2AL; -.
DR GeneWiki; HIST1H2AM; -.
DR Pharos; P0C0S8; Tbio.
DR PRO; PR:P0C0S8; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P0C0S8; protein.
DR Bgee; ENSG00000196747; Expressed in bone marrow cell and 93 other tissues.
DR ExpressionAtlas; P0C0S8; baseline and differential.
DR Genevisible; P0C0S8; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
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; DNA-binding;
KW Hydroxylation; Isopeptide bond; Methylation; Nucleosome core; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P0C0S9"
FT CHAIN 2..130
FT /note="Histone H2A type 1"
FT /id="PRO_0000055235"
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:11709551,
FT ECO:0000269|PubMed:15823041, ECO:0000269|PubMed:16457589"
FT MOD_RES 2
FT /note="Phosphoserine; by RPS6KA5"
FT /evidence="ECO:0000269|PubMed:11709551,
FT ECO:0000269|PubMed:15010469"
FT MOD_RES 4
FT /note="Citrulline; alternate"
FT /evidence="ECO:0000269|PubMed:15823041"
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:0000269|PubMed:24681537"
FT MOD_RES 10
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 10
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
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:0000269|PubMed:22389435"
FT MOD_RES 14
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 37
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 37
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 37
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 75
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 76
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 96
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 96
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 96
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31542297"
FT MOD_RES 96
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:22389435"
FT MOD_RES 100
FT /note="N6-glutaryllysine"
FT /evidence="ECO:0000269|PubMed:31542297"
FT MOD_RES 105
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000269|PubMed:24352239"
FT MOD_RES 119
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 119
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 119
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 119
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31542297"
FT MOD_RES 120
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 120
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31542297"
FT MOD_RES 121
FT /note="Phosphothreonine; by DCAF1"
FT /evidence="ECO:0000269|PubMed:15078818,
FT ECO:0000269|PubMed:24140421"
FT MOD_RES 126
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 126
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31542297"
FT CROSSLNK 14
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:22713238,
FT ECO:0000269|PubMed:22980979"
FT CROSSLNK 16
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:22713238,
FT ECO:0000269|PubMed:22980979"
FT CROSSLNK 120
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:15386022,
FT ECO:0000269|PubMed:16359901, ECO:0000269|PubMed:16702407,
FT ECO:0000269|PubMed:25470042"
FT MUTAGEN 2
FT /note="S->A: Blocks the inhibition of transcription by
FT RPS6KA5/MSK1."
FT /evidence="ECO:0000269|PubMed:15010469"
FT HELIX 18..22
FT /evidence="ECO:0007829|PDB:7E8D"
FT HELIX 28..36
FT /evidence="ECO:0007829|PDB:7E8D"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:7E8D"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:7E8D"
FT HELIX 47..73
FT /evidence="ECO:0007829|PDB:7E8D"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:7E8D"
FT HELIX 81..90
FT /evidence="ECO:0007829|PDB:7E8D"
FT HELIX 92..97
FT /evidence="ECO:0007829|PDB:7E8D"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:7E8D"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:7E8D"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:6X59"
SQ SEQUENCE 130 AA; 14091 MW; 48DD539793FE8256 CRC64;
MSGRGKQGGK ARAKAKTRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YLAAVLEYLT
AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGK VTIAQGGVLP NIQAVLLPKK
TESHHKAKGK
