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H2A1H_HUMAN
ID   H2A1H_HUMAN             Reviewed;         128 AA.
AC   Q96KK5;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 163.
DE   RecName: Full=Histone H2A type 1-H;
DE   AltName: Full=H2A-clustered histone 12 {ECO:0000312|HGNC:HGNC:13671};
DE   AltName: Full=Histone H2A/s;
GN   Name=H2AC12 {ECO:0000312|HGNC:HGNC:13671};
GN   Synonyms=HIST1H2AH {ECO:0000312|HGNC:HGNC:13671}, HIST1H2AI;
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].
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
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   [4]
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   [5]
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   [6]
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   [7]
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   [8]
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   [9]
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   [10]
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   [11]
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   [12]
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   [13]
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   [14]
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   [15]
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   [16]
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   [17]
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   [18]
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   [19]
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   [20]
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   [21]
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   [22]
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   [23]
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   [24]
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).
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: 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:15010469,
CC       ECO:0000269|PubMed:15078818, ECO:0000269|PubMed:15823041,
CC       ECO:0000269|PubMed:24140421}.
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: 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: 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   -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR   EMBL; AY131988; AAN59969.1; -; Genomic_DNA.
DR   EMBL; AL021807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC093851; AAH93851.1; -; mRNA.
DR   EMBL; BC093849; AAH93849.1; -; mRNA.
DR   CCDS; CCDS4622.1; -.
DR   RefSeq; NP_542163.1; NM_080596.2.
DR   AlphaFoldDB; Q96KK5; -.
DR   SMR; Q96KK5; -.
DR   BioGRID; 124438; 75.
DR   DIP; DIP-61699N; -.
DR   IntAct; Q96KK5; 56.
DR   MINT; Q96KK5; -.
DR   iPTMnet; Q96KK5; -.
DR   PhosphoSitePlus; Q96KK5; -.
DR   SwissPalm; Q96KK5; -.
DR   BioMuta; HIST1H2AH; -.
DR   DMDM; 74751984; -.
DR   jPOST; Q96KK5; -.
DR   MassIVE; Q96KK5; -.
DR   MaxQB; Q96KK5; -.
DR   PaxDb; Q96KK5; -.
DR   PeptideAtlas; Q96KK5; -.
DR   PRIDE; Q96KK5; -.
DR   TopDownProteomics; Q96KK5; -.
DR   Antibodypedia; 72981; 121 antibodies from 17 providers.
DR   DNASU; 85235; -.
DR   Ensembl; ENST00000377459.3; ENSP00000366679.2; ENSG00000274997.2.
DR   GeneID; 85235; -.
DR   KEGG; hsa:85235; -.
DR   MANE-Select; ENST00000377459.3; ENSP00000366679.2; NM_080596.3; NP_542163.1.
DR   UCSC; uc003niz.5; human.
DR   CTD; 85235; -.
DR   DisGeNET; 85235; -.
DR   GeneCards; H2AC12; -.
DR   HGNC; HGNC:13671; H2AC12.
DR   HPA; ENSG00000274997; Tissue enhanced (bone marrow, brain).
DR   MIM; 615013; gene.
DR   neXtProt; NX_Q96KK5; -.
DR   OpenTargets; ENSG00000274997; -.
DR   VEuPathDB; HostDB:ENSG00000274997; -.
DR   eggNOG; KOG1756; Eukaryota.
DR   GeneTree; ENSGT00940000153125; -.
DR   HOGENOM; CLU_062828_3_3_1; -.
DR   InParanoid; Q96KK5; -.
DR   OMA; ANEMFIN; -.
DR   OrthoDB; 1504122at2759; -.
DR   PhylomeDB; Q96KK5; -.
DR   TreeFam; TF300137; -.
DR   PathwayCommons; Q96KK5; -.
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; Q96KK5; -.
DR   SIGNOR; Q96KK5; -.
DR   BioGRID-ORCS; 85235; 449 hits in 1027 CRISPR screens.
DR   ChiTaRS; HIST1H2AH; human.
DR   GeneWiki; HIST1H2AH; -.
DR   GenomeRNAi; 85235; -.
DR   Pharos; Q96KK5; Tbio.
DR   PRO; PR:Q96KK5; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q96KK5; protein.
DR   Bgee; ENSG00000274997; Expressed in bone marrow cell and 91 other tissues.
DR   ExpressionAtlas; Q96KK5; baseline and differential.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
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   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   Acetylation; Chromosome; Citrullination; DNA-binding; Hydroxylation;
KW   Isopeptide bond; Methylation; Nucleosome core; Nucleus; Phosphoprotein;
KW   Reference proteome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:15823041"
FT   CHAIN           2..128
FT                   /note="Histone H2A type 1-H"
FT                   /id="PRO_0000230200"
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:15823041"
FT   MOD_RES         2
FT                   /note="Phosphoserine; by RPS6KA5"
FT                   /evidence="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:Q8CGP6"
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"
SQ   SEQUENCE   128 AA;  13906 MW;  639793FE8256343E CRC64;
     MSGRGKQGGK ARAKAKTRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YLAAVLEYLT
     AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGK VTIAQGGVLP NIQAVLLPKK
     TESHHKAK
 
 
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