ID H2A2A_HUMAN STANDARD; PRT; 129 AA. AC Q6FI13; P20670; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 2. DT 21-MAR-2006, entry version 18. DE Histone H2A type 2-A (H2A.2). GN Name=HIST2H2AA; Synonyms=H2AFO; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=94235160; PubMed=8179821; 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 RT different types of proliferating cells."; RL DNA Cell Biol. 13:161-170(1994). 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 MRNA]. RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., RA Korn B., Zuo D., Hu Y., LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG Human chromosome 1 international sequencing consortium; RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; 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 [6] 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 [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, ACETYLATION SITE LYS-5, AND RP 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 histones H2A and H2B variants and their post- RT translational modifications by mass spectrometry."; RL Mol. Cell. Proteomics 0:0-0(2005). RN [11] RP MASS SPECTROMETRY, ACETYLATION SITES SER-1 AND LYS-5, AND RP UBIQUITINATION SITE LYS-119. 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 -!- MASS SPECTROMETRY: MW=13997.9; METHOD=Electrospray; RANGE=1-129; CC NOTE=Monoisotopic, with N-acetylserine (Ref.9). 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; L19779; AAC24465.1; -; mRNA. DR EMBL; AY131971; AAN59957.1; -; Genomic_DNA. DR EMBL; CR536525; CAG38762.1; -; mRNA. DR EMBL; CR541872; CAG46670.1; -; mRNA. DR EMBL; AL591493; CAI12562.1; -; Genomic_DNA. DR EMBL; AL591493; CAI12565.1; -; Genomic_DNA. DR EMBL; BC001629; AAH01629.1; -; mRNA. DR EMBL; BC019308; AAH19308.1; -; mRNA. DR EMBL; BC096705; AAH96705.1; -; mRNA. DR EMBL; BC096739; AAH96739.1; -; mRNA. DR EMBL; BC098171; AAH98171.1; -; mRNA. DR PIR; S06742; S06742. DR HSSP; P06897; 1AOI. DR SMR; Q6FI13; 2-124. DR Ensembl; ENSG00000183558; Homo sapiens. DR H-InvDB; HIX0001003; -. DR HGNC; HGNC:4736; HIST2H2AA. DR MIM; 142720; gene. 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 1 129 Histone H2A type 2-A. FT /FTId=PRO_0000055232. 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. FT MOD_RES 120 120 Phosphothreonine (Probable). FT CROSSLNK 119 119 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). SQ SEQUENCE 129 AA; 13964 MW; CA97150A13FE8371 CRC64; SGRGKQGGKA RAKAKSRSSR AGLQFPVGRV HRLLRKGNYA ERVGAGAPVY MAAVLEYLTA EILELAGNAA RDNKKTRIIP RHLQLAIRND EELNKLLGKV TIAQGGVLPN IQAVLLPKKT ESHHKAKGK //