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Histone H2A type 1 (H2A.1) (Histone H2A/ptl)

 H2A1_HUMAN              Reviewed;         130 AA.
P0C0S8; P02261; Q2M1R2; Q76PA6;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
22-NOV-2017, entry version 132.
RecName: Full=Histone H2A type 1;
Short=H2A.1;
AltName: Full=Histone H2A/ptl;
Name=HIST1H2AG; Synonyms=H2AFP;
and
Name=HIST1H2AI; Synonyms=H2AFC;
and
Name=HIST1H2AK; Synonyms=H2AFD;
and
Name=HIST1H2AL; Synonyms=H2AFI;
and
Name=HIST1H2AM; Synonyms=H2AFN;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H2AI; HIST1H2AK AND
HIST1H2AL).
PubMed=9439656; DOI=10.1007/s004390050630;
Albig W., Doenecke D.;
"The human histone gene cluster at the D6S105 locus.";
Hum. Genet. 101:284-294(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H2AI; HIST1H2AK AND
HIST1H2AL).
PubMed=10064132; DOI=10.1515/BC.1999.002;
Albig W., Trappe R., Kardalinou E., Eick S., Doenecke D.;
"The human H2A and H2B histone gene complement.";
Biol. Chem. 380:7-18(1999).
[3]
NUCLEOTIDE SEQUENCE (HIST1H2AM).
PubMed=1768865; DOI=10.3109/10425179109020799;
Dobner T., Wolf I., Mai B., Lipp M.;
"A novel divergently transcribed human histone H2A/H2B gene pair.";
DNA Seq. 1:409-413(1991).
[4]
NUCLEOTIDE SEQUENCE (HIST1H2AG).
PubMed=8179821; DOI=10.1089/dna.1994.13.161;
Mannironi C., Orr A., Hatch C., Pilch D., Ivanova V., Bonner W.;
"The relative expression of human histone H2A genes is similar in
different types of proliferating cells.";
DNA Cell Biol. 13:161-170(1994).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H2AG; HIST1H2AI; HIST1H2AK;
HIST1H2AL AND HIST1H2AM).
PubMed=12408966; DOI=10.1006/geno.2002.6850;
Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.;
"The human and mouse replication-dependent histone genes.";
Genomics 80:487-498(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HIST1H2AI; HIST1H2AK;
HIST1H2AL AND HIST1H2AM).
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon, and Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
AMINO-ACID COMPOSITION OF TRYPTIC PEPTIDES.
TISSUE=Spleen;
PubMed=7410338;
Hayashi T., Ohe Y., Hayashi H., Iwai K.;
"Human spleen histone H2A. Isolation and four variant sequences.";
J. Biochem. 88:27-34(1980).
[9]
IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-2, AND
ACETYLATION AT SER-2.
PubMed=11709551; DOI=10.1074/jbc.M107894200;
Galasinski S.C., Louie D.F., Gloor K.K., Resing K.A., Ahn N.G.;
"Global regulation of post-translational modifications on core
histones.";
J. Biol. Chem. 277:2579-2588(2002).
[10]
PHOSPHORYLATION AT THR-121.
PubMed=15078818; DOI=10.1101/gad.1184604;
Aihara H., Nakagawa T., Yasui K., Ohta T., Hirose S., Dhomae N.,
Takio K., Kaneko M., Takeshima Y., Muramatsu M., Ito T.;
"Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 during
mitosis in the early Drosophila embryo.";
Genes Dev. 18:877-888(2004).
[11]
PHOSPHORYLATION AT SER-2, AND MUTAGENESIS OF SER-2.
PubMed=15010469; DOI=10.1074/jbc.M400099200;
Zhang Y., Griffin K., Mondal N., Parvin J.D.;
"Phosphorylation of histone H2A inhibits transcription on chromatin
templates.";
J. Biol. Chem. 279:21866-21872(2004).
[12]
UBIQUITINATION AT LYS-120.
PubMed=15386022; DOI=10.1038/nature02985;
Wang H., Wang L., Erdjument-Bromage H., Vidal M., Tempst P.,
Jones R.S., Zhang Y.;
"Role of histone H2A ubiquitination in Polycomb silencing.";
Nature 431:873-878(2004).
[13]
ACETYLATION AT SER-2, CITRULLINATION AT ARG-4, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=15823041; DOI=10.1021/bi047505c;
Hagiwara T., Hidaka Y., Yamada M.;
"Deimination of histone H2A and H4 at arginine 3 in HL-60
granulocytes.";
Biochemistry 44:5827-5834(2005).
[14]
UBIQUITINATION AT LYS-120.
PubMed=16359901; DOI=10.1016/j.molcel.2005.12.002;
Cao R., Tsukada Y., Zhang Y.;
"Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene
silencing.";
Mol. Cell 20:845-854(2005).
[15]
UBIQUITINATION AT LYS-120.
PubMed=16702407; DOI=10.1101/gad.373706;
Bergink S., Salomons F.A., Hoogstraten D., Groothuis T.A.M.,
de Waard H., Wu J., Yuan L., Citterio E., Houtsmuller A.B.,
Neefjes J., Hoeijmakers J.H.J., Vermeulen W., Dantuma N.P.;
"DNA damage triggers nucleotide excision repair-dependent
monoubiquitylation of histone H2A.";
Genes Dev. 20:1343-1352(2006).
[16]
MASS SPECTROMETRY, AND ACETYLATION AT SER-2.
PubMed=16457589; DOI=10.1021/pr050269n;
Boyne M.T. II, Pesavento J.J., Mizzen C.A., Kelleher N.L.;
"Precise characterization of human histones in the H2A gene family by
top down mass spectrometry.";
J. Proteome Res. 5:248-253(2006).
[17]
UBIQUITINATION.
PubMed=18001824; DOI=10.1016/j.cell.2007.09.040;
Mailand N., Bekker-Jensen S., Faustrup H., Melander F., Bartek J.,
Lukas C., Lukas J.;
"RNF8 ubiquitylates histones at DNA double-strand breaks and promotes
assembly of repair proteins.";
Cell 131:887-900(2007).
[18]
UBIQUITINATION.
PubMed=18001825; DOI=10.1016/j.cell.2007.09.041;
Huen M.S.Y., Grant R., Manke I., Minn K., Yu X., Yaffe M.B., Chen J.;
"RNF8 transduces the DNA-damage signal via histone ubiquitylation and
checkpoint protein assembly.";
Cell 131:901-914(2007).
[19]
UBIQUITINATION.
PubMed=19203578; DOI=10.1016/j.cell.2008.12.042;
Stewart G.S., Panier S., Townsend K., Al-Hakim A.K., Kolas N.K.,
Miller E.S., Nakada S., Ylanko J., Olivarius S., Mendez M.,
Oldreive C., Wildenhain J., Tagliaferro A., Pelletier L.,
Taubenheim N., Durandy A., Byrd P.J., Stankovic T., Taylor A.M.R.,
Durocher D.;
"The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling
cascade at sites of DNA damage.";
Cell 136:420-434(2009).
[20]
UBIQUITINATION.
PubMed=19203579; DOI=10.1016/j.cell.2008.12.041;
Doil C., Mailand N., Bekker-Jensen S., Menard P., Larsen D.H.,
Pepperkok R., Ellenberg J., Panier S., Durocher D., Bartek J.,
Lukas J., Lukas C.;
"RNF168 binds and amplifies ubiquitin conjugates on damaged
chromosomes to allow accumulation of repair proteins.";
Cell 136:435-446(2009).
[21]
CROTONYLATION AT LYS-37; LYS-119; LYS-120 AND LYS-126.
PubMed=21925322; DOI=10.1016/j.cell.2011.08.008;
Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T.,
Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q.,
Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y.;
"Identification of 67 histone marks and histone lysine crotonylation
as a new type of histone modification.";
Cell 146:1016-1028(2011).
[22]
UBIQUITINATION AT LYS-14 AND LYS-16 BY RNF168.
PubMed=22980979; DOI=10.1016/j.cell.2012.08.005;
Mattiroli F., Vissers J.H., van Dijk W.J., Ikpa P., Citterio E.,
Vermeulen W., Marteijn J.A., Sixma T.K.;
"RNF168 ubiquitinates K13-15 on H2A/H2AX to drive DNA Damage
signaling.";
Cell 150:1182-1195(2012).
[23]
UBIQUITINATION AT LYS-14 AND LYS-16 BY RNF168.
PubMed=22713238; DOI=10.4161/cc.20919;
Gatti M., Pinato S., Maspero E., Soffientini P., Polo S., Penengo L.;
"A novel ubiquitin mark at the N-terminal tail of histone H2As
targeted by RNF168 ubiquitin ligase.";
Cell Cycle 11:2538-2544(2012).
[24]
SUCCINYLATION AT LYS-10 AND LYS-96.
PubMed=22389435; DOI=10.1074/mcp.M111.015875;
Xie Z., Dai J., Dai L., Tan M., Cheng Z., Wu Y., Boeke J.D., Zhao Y.;
"Lysine succinylation and lysine malonylation in histones.";
Mol. Cell. Proteomics 11:100-107(2012).
[25]
PHOSPHORYLATION AT THR-121.
PubMed=24140421; DOI=10.1016/j.molcel.2013.09.017;
Kim K., Kim J.M., Kim J.S., Choi J., Lee Y.S., Neamati N., Song J.S.,
Heo K., An W.;
"VprBP has intrinsic kinase activity targeting histone H2A and
represses gene transcription.";
Mol. Cell 52:459-467(2013).
[26]
HYDROXYBUTYRYLATION AT LYS-6; LYS-10; LYS-37; LYS-75; LYS-76; LYS-96
AND LYS-119.
PubMed=24681537; DOI=10.1038/nchembio.1497;
Dai L., Peng C., Montellier E., Lu Z., Chen Y., Ishii H.,
Debernardi A., Buchou T., Rousseaux S., Jin F., Sabari B.R., Deng Z.,
Allis C.D., Ren B., Khochbin S., Zhao Y.;
"Lysine 2-hydroxyisobutyrylation is a widely distributed active
histone mark.";
Nat. Chem. Biol. 10:365-370(2014).
[27]
METHYLATION AT GLN-105.
PubMed=24352239; DOI=10.1038/nature12819;
Tessarz P., Santos-Rosa H., Robson S.C., Sylvestersen K.B.,
Nelson C.J., Nielsen M.L., Kouzarides T.;
"Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated
modification.";
Nature 505:564-568(2014).
[28]
UBIQUITINATION AT LYS-120.
PubMed=25470042; DOI=10.1038/nature13955;
Bhatnagar S., Gazin C., Chamberlain L., Ou J., Zhu X., Tushir J.S.,
Virbasius C.M., Lin L., Zhu L.J., Wajapeyee N., Green M.R.;
"TRIM37 is a new histone H2A ubiquitin ligase and breast cancer
oncoprotein.";
Nature 516:116-120(2014).
[29]
DEUBIQUITINATION AT LYS-14 AND LYS-16 BY USP51.
PubMed=27083998; DOI=10.1101/gad.271841.115;
Wang Z., Zhang H., Liu J., Cheruiyot A., Lee J.H., Ordog T., Lou Z.,
You Z., Zhang Z.;
"USP51 deubiquitylates H2AK13,15ub and regulates DNA damage
response.";
Genes Dev. 30:946-959(2016).
[30]
HYDROXYBUTYRYLATION AT LYS-10; LYS-14; LYS-37; LYS-96 AND LYS-119.
PubMed=27105115; DOI=10.1016/j.molcel.2016.03.036;
Xie Z., Zhang D., Chung D., Tang Z., Huang H., Dai L., Qi S., Li J.,
Colak G., Chen Y., Xia C., Peng C., Ruan H., Kirkey M., Wang D.,
Jensen L.M., Kwon O.K., Lee S., Pletcher S.D., Tan M., Lombard D.B.,
White K.P., Zhao H., Li J., Roeder R.G., Yang X., Zhao Y.;
"Metabolic regulation of gene expression by histone lysine beta-
hydroxybutyrylation.";
Mol. Cell 62:194-206(2016).
-!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and
compact DNA into chromatin, limiting DNA accessibility to the
cellular machineries which require DNA as a template. Histones
thereby play a central role in transcription regulation, DNA
repair, DNA replication and chromosomal stability. DNA
accessibility is regulated via a complex set of post-translational
modifications of histones, also called histone code, and
nucleosome remodeling.
-!- SUBUNIT: The nucleosome is a histone octamer containing two
molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4
heterotetramer and two H2A-H2B heterodimers. The octamer wraps
approximately 147 bp of DNA.
-!- INTERACTION:
Q9DUM3:- (xeno); NbExp=3; IntAct=EBI-1390628, EBI-7971837;
P55201:BRPF1; NbExp=8; IntAct=EBI-1390628, EBI-2837428;
Q99543:DNAJC2; NbExp=2; IntAct=EBI-1390628, EBI-11017224;
O95760:IL33; NbExp=3; IntAct=EBI-1390628, EBI-724057;
Q99496:RNF2; NbExp=5; IntAct=EBI-1390628, EBI-722416;
P63104:YWHAZ; NbExp=2; IntAct=EBI-1390628, EBI-347088;
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
-!- PTM: Deiminated on Arg-4 in granulocytes upon calcium entry.
{ECO:0000269|PubMed:15823041}.
-!- PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM27
and RNF2/RING2 complex gives a specific tag for epigenetic
transcriptional repression and participates in X chromosome
inactivation of female mammals. It is involved in the initiation
of both imprinted and random X inactivation. Ubiquitinated H2A is
enriched in inactive X chromosome chromatin. Ubiquitination of H2A
functions downstream of methylation of 'Lys-27' of histone H3
(H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by
ultraviolet and may be involved in DNA repair. Monoubiquitination
of Lys-120 (H2AK119Ub) by TRIM27 may promote transformation of
cells in a number of breast cancers (PubMed:25470042). Following
DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-
63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the
E3 ligases RNF8 and RNF168, leading to the recruitment of repair
proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-
16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage
is initiated by RNF168 that mediates monoubiquitination at these 2
sites, and 'Lys-63'-linked ubiquitin are then conjugated to
monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin
chains in vitro. Deubiquitinated by USP51 at Lys-14 and Lys-16
(H2AK13Ub and H2AK15Ub, respectively) after damaged DNA is
repaired (PubMed:27083998). H2AK119Ub and ionizing radiation-
induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are
distinct events. {ECO:0000269|PubMed:15386022,
ECO:0000269|PubMed:16359901, ECO:0000269|PubMed:16702407,
ECO:0000269|PubMed:18001824, ECO:0000269|PubMed:18001825,
ECO:0000269|PubMed:19203578, ECO:0000269|PubMed:19203579,
ECO:0000269|PubMed:22713238, ECO:0000269|PubMed:22980979,
ECO:0000269|PubMed:24352239, ECO:0000269|PubMed:25470042,
ECO:0000269|PubMed:27083998}.
-!- PTM: Phosphorylation on Ser-2 (H2AS1ph) is enhanced during
mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly
represses transcription. Acetylation of H3 inhibits Ser-2
phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121
(H2AT120ph) by DCAF1 is present in the regulatory region of many
tumor suppresor genes and down-regulates their transcription.
{ECO:0000269|PubMed:11709551, ECO:0000269|PubMed:15010469,
ECO:0000269|PubMed:15078818, ECO:0000269|PubMed:15823041,
ECO:0000269|PubMed:16457589, ECO:0000269|PubMed:24140421}.
-!- PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex
may play a crucial role in the germ-cell lineage.
{ECO:0000250|UniProtKB:P22752}.
-!- PTM: Glutamine methylation at Gln-105 (H2AQ104me) by FBL is
specifically dedicated to polymerase I. It is present at 35S
ribosomal DNA locus and impairs binding of the FACT complex
(PubMed:24352239). {ECO:0000269|PubMed:24352239}.
-!- PTM: Crotonylation (Kcr) is specifically present in male germ
cells and marks testis-specific genes in post-meiotic cells,
including X-linked genes that escape sex chromosome inactivation
in haploid cells. Crotonylation marks active promoters and
enhancers and confers resistance to transcriptional repressors. It
is also associated with post-meiotically activated genes on
autosomes. {ECO:0000269|PubMed:21925322}.
-!- MASS SPECTROMETRY: Mass=13993.9; Method=Electrospray; Range=2-130;
Note=Monoisotopic with N-acetylserine.;
Evidence={ECO:0000269|PubMed:16457589};
-!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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EMBL; Z83742; CAB06037.1; -; Genomic_DNA.
EMBL; Z83739; CAB06034.1; -; Genomic_DNA.
EMBL; X83549; CAA58539.1; -; Genomic_DNA.
EMBL; X57138; CAA40417.1; -; Genomic_DNA.
EMBL; L19778; AAC24466.1; -; mRNA.
EMBL; AY131987; AAN59968.1; -; Genomic_DNA.
EMBL; AY131989; AAN59970.1; -; Genomic_DNA.
EMBL; AY131991; AAN59972.1; -; Genomic_DNA.
EMBL; AY131992; AAN59973.1; -; Genomic_DNA.
EMBL; AY131993; AAN59974.1; -; Genomic_DNA.
EMBL; Z98744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL009179; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL021807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC016677; AAH16677.1; -; mRNA.
EMBL; BC069306; AAH69306.1; -; mRNA.
EMBL; BC104199; AAI04200.1; -; mRNA.
EMBL; BC104198; AAI04199.1; -; mRNA.
EMBL; BC105129; AAI05130.1; -; mRNA.
EMBL; BC112072; AAI12073.1; -; mRNA.
EMBL; BC112254; AAI12255.1; -; mRNA.
EMBL; BC112256; AAI12257.1; -; mRNA.
CCDS; CCDS4619.1; -.
CCDS; CCDS4626.1; -.
CCDS; CCDS4632.1; -.
CCDS; CCDS4634.1; -.
CCDS; CCDS4639.1; -.
PIR; B56624; HSHUA1.
RefSeq; NP_003500.1; NM_003509.2.
RefSeq; NP_003501.1; NM_003510.2.
RefSeq; NP_003502.1; NM_003511.2.
RefSeq; NP_003505.1; NM_003514.2.
RefSeq; NP_066408.1; NM_021064.4.
UniGene; Hs.134999; -.
UniGene; Hs.233568; -.
UniGene; Hs.51011; -.
UniGene; Hs.534035; -.
UniGene; Hs.734717; -.
PDB; 4QYL; X-ray; 1.80 A; E/F/G/H=2-13.
PDB; 5KGF; EM; 4.54 A; C/G=1-130.
PDBsum; 4QYL; -.
PDBsum; 5KGF; -.
ProteinModelPortal; P0C0S8; -.
SMR; P0C0S8; -.
BioGrid; 113925; 10.
BioGrid; 113926; 12.
BioGrid; 113928; 10.
BioGrid; 113932; 12.
BioGrid; 114459; 53.
DIP; DIP-39638N; -.
IntAct; P0C0S8; 28.
MINT; MINT-1519720; -.
STRING; 9606.ENSP00000352627; -.
iPTMnet; P0C0S8; -.
PhosphoSitePlus; P0C0S8; -.
SwissPalm; P0C0S8; -.
BioMuta; HIST1H2AG; -.
DMDM; 83288406; -.
EPD; P0C0S8; -.
MaxQB; P0C0S8; -.
PaxDb; P0C0S8; -.
PeptideAtlas; P0C0S8; -.
PRIDE; P0C0S8; -.
TopDownProteomics; P0C0S8; -.
DNASU; 8329; -.
DNASU; 8330; -.
DNASU; 8332; -.
DNASU; 8969; -.
Ensembl; ENST00000358739; ENSP00000351589; ENSG00000196747.
Ensembl; ENST00000359193; ENSP00000352119; ENSG00000196787.
Ensembl; ENST00000359611; ENSP00000352627; ENSG00000278677.
Ensembl; ENST00000613174; ENSP00000482538; ENSG00000276903.
Ensembl; ENST00000618958; ENSP00000482431; ENSG00000275221.
GeneID; 8329; -.
GeneID; 8330; -.
GeneID; 8332; -.
GeneID; 8336; -.
GeneID; 8969; -.
KEGG; hsa:8329; -.
KEGG; hsa:8330; -.
KEGG; hsa:8332; -.
KEGG; hsa:8336; -.
KEGG; hsa:8969; -.
UCSC; uc003niw.4; human.
CTD; 8329; -.
CTD; 8330; -.
CTD; 8332; -.
CTD; 8336; -.
CTD; 8969; -.
DisGeNET; 8332; -.
EuPathDB; HostDB:ENSG00000196747.4; -.
EuPathDB; HostDB:ENSG00000196787.3; -.
EuPathDB; HostDB:ENSG00000275221.1; -.
EuPathDB; HostDB:ENSG00000276903.1; -.
EuPathDB; HostDB:ENSG00000278677.1; -.
GeneCards; HIST1H2AG; -.
GeneCards; HIST1H2AI; -.
GeneCards; HIST1H2AK; -.
GeneCards; HIST1H2AL; -.
GeneCards; HIST1H2AM; -.
H-InvDB; HIX0200889; -.
HGNC; HGNC:4737; HIST1H2AG.
HGNC; HGNC:4725; HIST1H2AI.
HGNC; HGNC:4726; HIST1H2AK.
HGNC; HGNC:4730; HIST1H2AL.
HGNC; HGNC:4735; HIST1H2AM.
HPA; HPA041189; -.
MIM; 602787; gene.
MIM; 602788; gene.
MIM; 602793; gene.
MIM; 602796; gene.
MIM; 615012; gene.
neXtProt; NX_P0C0S8; -.
OpenTargets; ENSG00000196747; -.
OpenTargets; ENSG00000196787; -.
OpenTargets; ENSG00000275221; -.
OpenTargets; ENSG00000276903; -.
OpenTargets; ENSG00000278677; -.
PharmGKB; PA29114; -.
eggNOG; KOG1756; Eukaryota.
eggNOG; COG5262; LUCA.
GeneTree; ENSGT00900000140854; -.
HOGENOM; HOG000234652; -.
HOVERGEN; HBG009342; -.
InParanoid; P0C0S8; -.
KO; K11251; -.
OrthoDB; EOG091G0XGD; -.
PhylomeDB; P0C0S8; -.
TreeFam; TF300137; -.
Reactome; R-HSA-3214815; HDACs deacetylate histones.
Reactome; R-HSA-3214847; HATs acetylate histones.
Reactome; R-HSA-3214858; RMTs methylate histone arginines.
Reactome; R-HSA-5689603; UCH proteinases.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-5689901; Metalloprotease DUBs.
SIGNOR; P0C0S8; -.
ChiTaRS; HIST1H2AM; human.
GeneWiki; HIST1H2AG; -.
GeneWiki; HIST1H2AI; -.
GeneWiki; HIST1H2AK; -.
GeneWiki; HIST1H2AL; -.
GeneWiki; HIST1H2AM; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000196747; -.
CleanEx; HS_HIST1H2AG; -.
CleanEx; HS_HIST1H2AI; -.
CleanEx; HS_HIST1H2AK; -.
CleanEx; HS_HIST1H2AL; -.
CleanEx; HS_HIST1H2AM; -.
ExpressionAtlas; P0C0S8; baseline and differential.
Genevisible; P0C0S8; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; IBA:GO_Central.
GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IBA:GO_Central.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
GO; GO:0006342; P:chromatin silencing; IBA:GO_Central.
CDD; cd00074; H2A; 1.
InterPro; IPR009072; Histone-fold.
InterPro; IPR002119; Histone_H2A.
InterPro; IPR007125; Histone_H2A/H2B/H3.
InterPro; IPR032454; Histone_H2A_C.
InterPro; IPR032458; Histone_H2A_CS.
Pfam; PF00125; Histone; 1.
Pfam; PF16211; Histone_H2A_C; 1.
PRINTS; PR00620; HISTONEH2A.
SMART; SM00414; H2A; 1.
SUPFAM; SSF47113; SSF47113; 1.
PROSITE; PS00046; HISTONE_H2A; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Chromosome; Citrullination;
Complete proteome; DNA-binding; Hydroxylation; Isopeptide bond;
Methylation; Nucleosome core; Nucleus; Phosphoprotein;
Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P0C0S9}.
CHAIN 2 130 Histone H2A type 1.
/FTId=PRO_0000055235.
MOD_RES 2 2 N-acetylserine.
{ECO:0000269|PubMed:11709551,
ECO:0000269|PubMed:15823041,
ECO:0000269|PubMed:16457589}.
MOD_RES 2 2 Phosphoserine; by RPS6KA5.
{ECO:0000269|PubMed:11709551,
ECO:0000269|PubMed:15010469}.
MOD_RES 4 4 Citrulline; alternate.
{ECO:0000269|PubMed:15823041}.
MOD_RES 4 4 Symmetric dimethylarginine; by PRMT5;
alternate.
{ECO:0000250|UniProtKB:P22752}.
MOD_RES 6 6 N6-(2-hydroxyisobutyryl)lysine.
{ECO:0000269|PubMed:24681537}.
MOD_RES 10 10 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 10 10 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 10 10 N6-succinyllysine; alternate.
{ECO:0000269|PubMed:22389435}.
MOD_RES 14 14 N6-(beta-hydroxybutyryl)lysine.
{ECO:0000269|PubMed:27105115}.
MOD_RES 37 37 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 37 37 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 37 37 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 75 75 N6-(2-hydroxyisobutyryl)lysine.
{ECO:0000269|PubMed:24681537}.
MOD_RES 76 76 N6-(2-hydroxyisobutyryl)lysine.
{ECO:0000269|PubMed:24681537}.
MOD_RES 96 96 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 96 96 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 96 96 N6-succinyllysine; alternate.
{ECO:0000269|PubMed:22389435}.
MOD_RES 105 105 N5-methylglutamine.
{ECO:0000269|PubMed:24352239}.
MOD_RES 119 119 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 119 119 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 119 119 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 120 120 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 121 121 Phosphothreonine; by DCAF1.
{ECO:0000269|PubMed:15078818,
ECO:0000269|PubMed:24140421}.
MOD_RES 126 126 N6-crotonyllysine.
{ECO:0000269|PubMed:21925322}.
CROSSLNK 14 14 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:22713238,
ECO:0000269|PubMed:22980979}.
CROSSLNK 16 16 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:22713238,
ECO:0000269|PubMed:22980979}.
CROSSLNK 120 120 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate. {ECO:0000269|PubMed:15386022,
ECO:0000269|PubMed:16359901,
ECO:0000269|PubMed:16702407,
ECO:0000269|PubMed:25470042}.
MUTAGEN 2 2 S->A: Blocks the inhibition of
transcription by RPS6KA5/MSK1.
{ECO:0000269|PubMed:15010469}.
SEQUENCE 130 AA; 14091 MW; 48DD539793FE8256 CRC64;
MSGRGKQGGK ARAKAKTRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YLAAVLEYLT
AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGK VTIAQGGVLP NIQAVLLPKK
TESHHKAKGK


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