ID H2A1J_HUMAN STANDARD; PRT; 127 AA. AC Q99878; Q5JXQ5; DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2001, sequence version 2. DT 18-APR-2006, entry version 51. 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 MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [5] RP PHOSPHORYLATION SITE THR-120. 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 SITE SER-1, AND MUTAGENESIS OF SER-1. 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 SITE LYS-119. 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 SITE SER-1, CITRULLINATION SITE ARG-3, AND 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 RT granulocytes."; RL Biochemistry 44:5827-5834(2005). RN [9] RP UBIQUITINATION SITE LYS-119. 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 IDENTIFICATION BY MASS SPECTROMETRY, AND PHOSPHORYLATION SITE SER-1. RX PubMed=16319397; DOI=10.1074/mcp.M500288-MCP200; RA Bonenfant D., Coulot M., Towbin H., Schindler P., van Oostrum J.; RT "Characterization of histone H2A and H2B variants and their post- RT translational modifications by mass spectrometry."; RL Mol. Cell. Proteomics 5:541-552(2006). RN [11] RP MASS SPECTROMETRY, AND ACETYLATION SITE SER-1. 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 -!- SUBUNIT: The nucleosome is an octamer containing two molecules CC each of H2A, H2B, H3 and H4. The octamer wraps approximately 146 CC bp of DNA. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- PTM: The chromatin-associated form is phosphorylated on Thr-120 CC during mitosis (Probable). CC -!- PTM: Deiminated on Arg-3 in granulocytes upon calcium entry. CC -!- PTM: Monoubiquitination of Lys-119 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. CC -!- PTM: Phosphorylation on Ser-1 is enhanced during mitosis. CC Phosphorylation on Ser-1 by RPS6KA5/MSK1 directly represses CC transcription. Acetylation of H3 inhibits Ser-1 phosphorylation by CC RPS6KA5/MSK1. CC -!- MASS SPECTROMETRY: MW=13838.7; METHOD=Electrospray; RANGE=1-127; CC NOTE=Monoisotopic, with N-acetylserine (Ref.11). 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.233568; -. DR UniGene; Hs.406691; -. DR UniGene; Hs.584828; -. DR HSSP; P06897; 1AOI. DR SMR; Q99878; 1-123. DR Ensembl; ENSG00000182611; Homo sapiens. DR HGNC; HGNC:4727; HIST1H2AJ. DR MIM; 602791; gene. DR GO; GO:0000786; C:nucleosome; NAS. DR GO; GO:0003677; F:DNA binding; NAS. DR GO; GO:0007001; P:chromosome organization and biogenesis (sen...; NAS. DR GO; GO:0006334; P:nucleosome assembly; NAS. DR InterPro; IPR007124; Hist_TAF. DR InterPro; IPR009072; Histone-fold. DR InterPro; IPR007125; Histone_core_D. DR InterPro; IPR002119; Histone_H2A. DR PANTHER; PTHR11611; Histone_H2A; 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 Nuclear protein; Nucleosome core; Phosphorylation; Ubl conjugation. FT INIT_MET 0 0 By similarity. FT CHAIN 1 127 Histone H2A type 1-J. FT /FTId=PRO_0000055239. FT MOD_RES 1 1 N-acetylserine. FT MOD_RES 1 1 Phosphoserine. FT MOD_RES 3 3 Citrulline. FT MOD_RES 5 5 N6-acetyllysine (By similarity). FT MOD_RES 120 120 Phosphothreonine (Probable). FT CROSSLNK 119 119 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT MUTAGEN 1 1 S->A: Blocks the inhibition of FT transcription by RPS6KA5/MSK1. SQ SEQUENCE 127 AA; 13805 MW; FAED13FE8230C415 CRC64; SGRGKQGGKA RAKAKTRSSR AGLQFPVGRV HRLLRKGNYA ERVGAGAPVY LAAVLEYLTA EILELAGNAA RDNKKTRIIP RHLQLAIRND EELNKLLGKV TIAQGGVLPN IQAVLLPKKT ESHHKTK //