ID H2A1J_HUMAN Reviewed; 128 AA. AC Q99878; Q5JXQ5; DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 06-FEB-2007, entry version 65. DE Histone H2A type 1-J. GN Name=HIST1H2AJ; Synonyms=H2AFE; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=98102829; 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]. RX MEDLINE=22296985; PubMed=12408966; DOI=10.1016/S0888-7543(02)96850-3; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22935763; 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., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA 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., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] 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., RA Takio K., Kaneko M., Takeshima Y., Muramatsu M., Ito T.; RT "Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 during RT mitosis in the early Drosophila embryo."; RL Genes Dev. 18:877-888(2004). RN [6] 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 [7] RP UBIQUITINATION AT LYS-120. RX PubMed=15386022; DOI=10.1038/nature02985; RA Wang H., Wang L., Erdjument-Bromage H., Vidal M., Tempst P., RA Jones R.S., Zhang Y.; RT "Role of histone H2A ubiquitination in Polycomb silencing."; RL Nature 431:873-878(2004). RN [8] RP ACETYLATION AT SER-2, CITRULLINATION AT ARG-4, AND MASS 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 RT granulocytes."; RL Biochemistry 44:5827-5834(2005). RN [9] 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 RT silencing."; RL Mol. Cell 20:845-854(2005). RN [10] 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., RA de Waard H., Wu J., Yuan L., Citterio E., Houtsmuller A.B., RA Neefjes J., 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 [11] RP IDENTIFICATION BY MASS SPECTROMETRY, AND PHOSPHORYLATION AT SER-2. RX PubMed=16319397; DOI=10.1074/mcp.M500288-MCP200; RA Bonenfant D., Coulot M., Towbin H., Schindler P., van Oostrum J.; RT "Characterization of histones H2A and H2B variants and their post- RT translational modifications by mass spectrometry."; RL Mol. Cell. Proteomics 5:541-552(2006). RN [12] 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 RT top down mass spectrometry."; RL J. Proteome Res. 5:248-253(2006). CC -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and CC compact DNA into chromatin, limiting DNA accessibility to the CC cellular machineries which require DNA as a template. Histones CC thereby play a central role in transcription regulation, DNA CC repair, DNA replication and chromosomal stability. DNA CC accessibility is regulated via a complex set of post-translational CC modifications of histones, also called histone code, and CC nucleosome remodelling. CC -!- SUBUNIT: The nucleosome is a histone octamer containing two CC molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 CC heterotetramer and two H2A-H2B heterodimers. The octamer wraps CC approximately 147 bp of DNA. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- PTM: The chromatin-associated form is phosphorylated on Thr-121 CC during mitosis (Probable). CC -!- PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. CC -!- PTM: Monoubiquitination of Lys-120 by RING1 and RNF2/RING2 complex CC gives a specific tag for epigenetic transcriptional repression and CC participates in X chromosome inactivation of female mammals. It is CC involved in the initiation of both imprinted and random X CC inactivation. Ubiquitinated H2A is enriched in inactive X CC chromosome chromatin. Ubiquitination of H2A functions downstream CC of methylation of 'Lys-27' of histone H3. Monoubiquitination of CC Lys-120 by RNF2/RING2 can also be induced by ultraviolet and may CC be involved in DNA repair. CC -!- PTM: Phosphorylation on Ser-2 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. CC -!- PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex CC may play a crucial role in the germ-cell lineage (By similarity). CC -!- MASS SPECTROMETRY: MW=13838.7; METHOD=Electrospray; RANGE=2-128; CC NOTE=Monoisotopic, with N-acetylserine (Ref.12). CC -!- SIMILARITY: Belongs to the histone H2A family. 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; Z83736; CAB06031.1; -; Genomic_DNA. DR EMBL; AY131990; AAN59971.1; -; Genomic_DNA. DR EMBL; AL049822; CAB81656.1; -; Genomic_DNA. DR EMBL; BC066232; AAH66232.1; -; mRNA. DR EMBL; BC066233; AAH66233.1; -; mRNA. DR EMBL; BC066234; AAH66234.1; -; mRNA. DR EMBL; BC066235; AAH66235.1; -; mRNA. DR EMBL; BC066236; AAH66236.1; -; mRNA. DR EMBL; BC066237; AAH66237.1; -; mRNA. DR UniGene; Hs.406691; -. DR HSSP; P06897; 1AOI. DR SMR; Q99878; 2-124. DR Ensembl; ENSG00000182611; Homo sapiens. DR KEGG; hsa:8330; -. DR KEGG; hsa:8331; -. DR HGNC; HGNC:4727; HIST1H2AJ. DR MIM; 602791; gene. DR Reactome; REACT_7970.1; Maintenance of Telomeres. DR GermOnline; ENSG00000182611; Homo sapiens. DR RZPD-ProtExp; T1265; -. DR GO; GO:0000786; C:nucleosome; NAS:UniProtKB. DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB. DR GO; GO:0006334; P:nucleosome assembly; NAS:UniProtKB. DR InterPro; IPR009072; Histone-fold. DR InterPro; IPR007125; Histone_core_D. DR InterPro; IPR002119; Histone_H2A. DR Gene3D; G3DSA:1.10.20.10; Histone-fold; 1. DR Pfam; PF00125; Histone; 1. DR PRINTS; PR00620; HISTONEH2A. DR ProDom; PD000522; Histone_H2A; 1. DR SMART; SM00414; H2A; 1. DR PROSITE; PS00046; HISTONE_H2A; 1. KW Acetylation; Chromosomal protein; Citrullination; DNA-binding; KW Methylation; Nuclear protein; Nucleosome core; Phosphorylation; KW Ubl conjugation. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 128 Histone H2A type 1-J. FT /FTId=PRO_0000055239. FT MOD_RES 2 2 N-acetylserine. FT MOD_RES 2 2 Phosphoserine. FT MOD_RES 4 4 Citrulline (alternate). FT MOD_RES 4 4 Symmetric dimethylarginine (alternate) FT (By similarity). FT MOD_RES 6 6 N6-acetyllysine (By similarity). FT MOD_RES 121 121 Phosphothreonine (Probable). FT CROSSLNK 120 120 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT MUTAGEN 2 2 S->A: Blocks the inhibition of FT transcription by RPS6KA5/MSK1. SQ SEQUENCE 128 AA; 13936 MW; 638BE3FE8256343E CRC64; MSGRGKQGGK ARAKAKTRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGK VTIAQGGVLP NIQAVLLPKK TESHHKTK //