ID H2A2A_HUMAN Reviewed; 130 AA. AC Q6FI13; B2R5F0; P20670; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 16-JAN-2019, entry version 155. DE RecName: Full=Histone H2A type 2-A; DE AltName: Full=Histone H2A.2; DE AltName: Full=Histone H2A/o; GN Name=HIST2H2AA3; Synonyms=H2AFO, HIST2H2AA; GN and GN Name=HIST2H2AA4; 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 [MRNA]. RX PubMed=8179821; DOI=10.1089/dna.1994.13.161; 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 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Tongue; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] 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 [8] 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 [9] 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 [10] 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 [11] RP ACETYLATION AT SER-2, CITRULLINATION AT ARG-4, AND IDENTIFICATION BY RP 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 [12] 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 [13] 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 [14] RP MASS SPECTROMETRY, ACETYLATION AT SER-2 AND LYS-6, AND UBIQUITINATION RP AT LYS-120. 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). RN [15] 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 [16] 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 [17] 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., RA Oldreive C., Wildenhain J., Tagliaferro A., Pelletier L., RA Taubenheim N., Durandy A., Byrd P.J., Stankovic T., Taylor A.M.R., RA 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 [18] 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., RA Lukas J., Lukas C.; RT "RNF168 binds and amplifies ubiquitin conjugates on damaged RT chromosomes to allow accumulation of repair proteins."; RL Cell 136:435-446(2009). RN [19] 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., RA Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y.; RT "Identification of 67 histone marks and histone lysine crotonylation RT as a new type of histone modification."; RL Cell 146:1016-1028(2011). RN [20] 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 RT signaling."; RL Cell 150:1182-1195(2012). RN [21] 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 RT targeted by RNF168 ubiquitin ligase."; RL Cell Cycle 11:2538-2544(2012). RN [22] 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 [23] 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 RT represses gene transcription."; RL Mol. Cell 52:459-467(2013). RN [24] RP HYDROXYBUTYRYLATION AT LYS-6; LYS-10; LYS-37; LYS-75; LYS-76; LYS-96 RP AND LYS-119. RX PubMed=24681537; DOI=10.1038/nchembio.1497; RA Dai L., Peng C., Montellier E., Lu Z., Chen Y., Ishii H., RA Debernardi A., Buchou T., Rousseaux S., Jin F., Sabari B.R., Deng Z., RA Allis C.D., Ren B., Khochbin S., Zhao Y.; RT "Lysine 2-hydroxyisobutyrylation is a widely distributed active RT histone mark."; RL Nat. Chem. Biol. 10:365-370(2014). RN [25] RP METHYLATION AT GLN-105. RX PubMed=24352239; DOI=10.1038/nature12819; RA Tessarz P., Santos-Rosa H., Robson S.C., Sylvestersen K.B., RA Nelson C.J., 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 [26] 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 [27] 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 RT response."; RL Genes Dev. 30:946-959(2016). RN [28] 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). 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 remodeling. 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. 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, TRIM27 CC and RNF2/RING2 complex gives a specific tag for epigenetic CC transcriptional repression and participates in X chromosome CC inactivation of female mammals. It is involved in the initiation CC of both imprinted and random X inactivation. Ubiquitinated H2A is CC enriched in inactive X chromosome chromatin. Ubiquitination of H2A CC functions downstream of methylation of 'Lys-27' of histone H3 CC (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by CC ultraviolet and may be involved in DNA repair. Monoubiquitination CC of Lys-120 (H2AK119Ub) by TRIM27 may promote transformation of CC cells in a number of breast cancers (PubMed:25470042). Following CC DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys- CC 63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the CC E3 ligases RNF8 and RNF168, leading to the recruitment of repair CC proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys- CC 16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage CC is initiated by RNF168 that mediates monoubiquitination at these 2 CC sites, and 'Lys-63'-linked ubiquitin are then conjugated to CC monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin CC chains in vitro. Deubiquitinated by USP51 at Lys-14 and Lys-16 CC (H2AK13Ub and H2AK15Ub, respectively) after damaged DNA is CC repaired (PubMed:27083998). H2AK119Ub and ionizing radiation- CC induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are CC distinct events. {ECO:0000269|PubMed:15386022, CC ECO:0000269|PubMed:16359901, ECO:0000269|PubMed:16457589, 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 CC mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly CC represses transcription. Acetylation of H3 inhibits Ser-2 CC phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 CC (H2AT120ph) by DCAF1 is present in the regulatory region of many CC tumor suppresor genes and down-regulates their transcription. CC {ECO:0000269|PubMed:15010469, ECO:0000269|PubMed:15078818, CC ECO:0000269|PubMed:15823041, ECO:0000269|PubMed:16457589, 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 CC ribosomal DNA locus and impairs binding of the FACT complex CC (PubMed:24352239). {ECO:0000269|PubMed:24352239}. CC -!- PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex CC may play a crucial role in the germ-cell lineage. CC {ECO:0000250|UniProtKB:P22752}. CC -!- PTM: Crotonylation (Kcr) is specifically present in male germ CC cells and marks testis-specific genes in post-meiotic cells, CC including X-linked genes that escape sex chromosome inactivation CC in haploid cells. Crotonylation marks active promoters and CC enhancers and confers resistance to transcriptional repressors. It CC is also associated with post-meiotically activated genes on CC autosomes. {ECO:0000269|PubMed:21925322}. CC -!- MASS SPECTROMETRY: Mass=13997.9; Method=Electrospray; Range=2-130; CC Note=Monoisotopic with N-acetylserine.; CC Evidence={ECO:0000269|PubMed:16457589}; CC -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}. 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; AK312163; BAG35097.1; -; mRNA. 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; CH878687; EAW50859.1; -; Genomic_DNA. DR EMBL; BC096705; AAH96705.1; -; mRNA. DR EMBL; BC096739; AAH96739.1; -; mRNA. DR EMBL; BC098171; AAH98171.1; -; mRNA. DR CCDS; CCDS30849.1; -. DR CCDS; CCDS934.1; -. DR PIR; S06742; S06742. DR RefSeq; NP_001035807.1; NM_001040874.1. DR RefSeq; NP_003507.1; NM_003516.2. DR UniGene; Hs.530461; -. DR UniGene; Hs.745563; -. DR ProteinModelPortal; Q6FI13; -. DR SMR; Q6FI13; -. DR BioGrid; 113933; 35. DR BioGrid; 593221; 8. DR CORUM; Q6FI13; -. DR DIP; DIP-33167N; -. DR IntAct; Q6FI13; 23. DR STRING; 9606.ENSP00000358158; -. DR iPTMnet; Q6FI13; -. DR PhosphoSitePlus; Q6FI13; -. DR SwissPalm; Q6FI13; -. DR BioMuta; HIST2H2AA4; -. DR DMDM; 74757558; -. DR EPD; Q6FI13; -. DR jPOST; Q6FI13; -. DR MaxQB; Q6FI13; -. DR PaxDb; Q6FI13; -. DR PeptideAtlas; Q6FI13; -. DR PRIDE; Q6FI13; -. DR ProteomicsDB; 66294; -. DR TopDownProteomics; Q6FI13; -. DR DNASU; 723790; -. DR DNASU; 8337; -. DR Ensembl; ENST00000369159; ENSP00000358155; ENSG00000203812. DR Ensembl; ENST00000607355; ENSP00000475814; ENSG00000272196. DR GeneID; 723790; -. DR GeneID; 8337; -. DR KEGG; hsa:723790; -. DR KEGG; hsa:8337; -. DR UCSC; uc001esw.4; human. DR CTD; 723790; -. DR CTD; 8337; -. DR DisGeNET; 723790; -. DR DisGeNET; 8337; -. DR EuPathDB; HostDB:ENSG00000203812.2; -. DR EuPathDB; HostDB:ENSG00000272196.2; -. DR GeneCards; HIST2H2AA3; -. DR GeneCards; HIST2H2AA4; -. DR HGNC; HGNC:4736; HIST2H2AA3. DR HGNC; HGNC:29668; HIST2H2AA4. DR HPA; HPA041189; -. DR MIM; 142720; gene. DR neXtProt; NX_Q6FI13; -. DR OpenTargets; ENSG00000272196; -. DR PharmGKB; PA29113; -. DR eggNOG; KOG1756; Eukaryota. DR eggNOG; COG5262; LUCA. DR GeneTree; ENSGT00940000156302; -. DR HOGENOM; HOG000234652; -. DR HOVERGEN; HBG009342; -. DR InParanoid; Q6FI13; -. DR KO; K11251; -. DR OMA; AGCKAGG; -. DR OrthoDB; 1504122at2759; -. DR PhylomeDB; Q6FI13; -. DR TreeFam; TF300137; -. DR Reactome; R-HSA-1221632; Meiotic synapsis. DR Reactome; R-HSA-171306; Packaging Of Telomere Ends. DR Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation. DR Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex. DR Reactome; R-HSA-212300; PRC2 methylates histones and DNA. DR Reactome; R-HSA-2299718; Condensation of Prophase Chromosomes. DR Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence. DR Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP). DR Reactome; R-HSA-2559586; DNA Damage/Telomere Stress Induced Senescence. 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-427359; SIRT1 negatively regulates rRNA expression. DR Reactome; R-HSA-427389; ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression. DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression. DR Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression. DR Reactome; R-HSA-5334118; DNA methylation. DR Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs. DR Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis. DR Reactome; R-HSA-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3. 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-606279; Deposition of new CENPA-containing nucleosomes at the centromere. DR Reactome; R-HSA-73728; RNA Polymerase I Promoter Opening. DR Reactome; R-HSA-73777; RNA Polymerase I Chain Elongation. DR Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function. DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs. DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression. DR Reactome; R-HSA-912446; Meiotic recombination. DR Reactome; R-HSA-977225; Amyloid fiber formation. DR GeneWiki; HIST2H2AA3; -. DR PRO; PR:Q6FI13; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; ENSG00000203812; Expressed in 87 organ(s), highest expression level in blood. DR CleanEx; HS_HIST2H2AA3; -. DR CleanEx; HS_HIST2H2AA4; -. DR Genevisible; Q6FI13; HS. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0000790; C:nuclear chromatin; IBA:GO_Central. DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; IBA:GO_Central. DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro. DR GO; GO:0006325; P:chromatin organization; IBA:GO_Central. 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 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; Complete proteome; KW DNA-binding; Hydroxylation; Isopeptide bond; Methylation; KW Nucleosome core; Nucleus; Phosphoprotein; Reference proteome; KW Ubl conjugation. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:15823041, FT ECO:0000269|PubMed:16457589}. FT CHAIN 2 130 Histone H2A type 2-A. FT /FTId=PRO_0000055232. FT MOD_RES 2 2 N-acetylserine. FT {ECO:0000269|PubMed:15823041, FT ECO:0000269|PubMed:16457589}. FT MOD_RES 2 2 Phosphoserine; by RPS6KA5. FT {ECO:0000269|PubMed:15010469}. FT MOD_RES 4 4 Citrulline; alternate. FT {ECO:0000269|PubMed:15823041}. FT MOD_RES 4 4 Symmetric dimethylarginine; by PRMT5; FT alternate. FT {ECO:0000250|UniProtKB:Q6GSS7}. FT MOD_RES 6 6 N6-(2-hydroxyisobutyryl)lysine; FT alternate. {ECO:0000269|PubMed:24681537}. FT MOD_RES 6 6 N6-acetyllysine; alternate. FT {ECO:0000269|PubMed:16457589}. FT MOD_RES 10 10 N6-(2-hydroxyisobutyryl)lysine; FT alternate. {ECO:0000269|PubMed:24681537}. FT MOD_RES 10 10 N6-(beta-hydroxybutyryl)lysine; FT alternate. {ECO:0000269|PubMed:27105115}. FT MOD_RES 10 10 N6-succinyllysine; alternate. FT {ECO:0000269|PubMed:22389435}. FT MOD_RES 14 14 N6-(beta-hydroxybutyryl)lysine; FT alternate. {ECO:0000269|PubMed:27105115}. FT MOD_RES 37 37 N6-(2-hydroxyisobutyryl)lysine; FT alternate. {ECO:0000269|PubMed:24681537}. FT MOD_RES 37 37 N6-(beta-hydroxybutyryl)lysine; FT alternate. {ECO:0000269|PubMed:27105115}. FT MOD_RES 37 37 N6-crotonyllysine; alternate. FT {ECO:0000269|PubMed:21925322}. FT MOD_RES 75 75 N6-(2-hydroxyisobutyryl)lysine. FT {ECO:0000269|PubMed:24681537}. FT MOD_RES 76 76 N6-(2-hydroxyisobutyryl)lysine. FT {ECO:0000269|PubMed:24681537}. FT MOD_RES 96 96 N6-(2-hydroxyisobutyryl)lysine; FT alternate. {ECO:0000269|PubMed:24681537}. FT MOD_RES 96 96 N6-(beta-hydroxybutyryl)lysine; FT alternate. {ECO:0000269|PubMed:27105115}. FT MOD_RES 96 96 N6-succinyllysine; alternate. FT {ECO:0000269|PubMed:22389435}. FT MOD_RES 105 105 N5-methylglutamine. FT {ECO:0000269|PubMed:24352239}. FT MOD_RES 119 119 N6-(2-hydroxyisobutyryl)lysine; FT alternate. {ECO:0000269|PubMed:24681537}. FT MOD_RES 119 119 N6-(beta-hydroxybutyryl)lysine; FT alternate. {ECO:0000269|PubMed:27105115}. FT MOD_RES 119 119 N6-crotonyllysine; alternate. FT {ECO:0000269|PubMed:21925322}. FT MOD_RES 120 120 N6-crotonyllysine; alternate. FT {ECO:0000269|PubMed:21925322}. FT MOD_RES 121 121 Phosphothreonine; by DCAF1. FT {ECO:0000269|PubMed:15078818, FT ECO:0000269|PubMed:24140421}. FT MOD_RES 126 126 N6-crotonyllysine. FT {ECO:0000269|PubMed:21925322}. FT CROSSLNK 14 14 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin); FT alternate. {ECO:0000269|PubMed:22713238, FT ECO:0000269|PubMed:22980979}. FT CROSSLNK 16 16 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT {ECO:0000269|PubMed:22713238, FT ECO:0000269|PubMed:22980979}. FT CROSSLNK 120 120 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin); FT alternate. {ECO:0000269|PubMed:15386022, FT ECO:0000269|PubMed:16359901, FT ECO:0000269|PubMed:16457589, FT ECO:0000269|PubMed:16702407, FT ECO:0000269|PubMed:25470042}. FT MUTAGEN 2 2 S->A: Blocks the inhibition of FT transcription by RPS6KA5/MSK1. FT {ECO:0000269|PubMed:15010469}. SQ SEQUENCE 130 AA; 14095 MW; 53AEDC6CE3FE8317 CRC64; MSGRGKQGGK ARAKAKSRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YMAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGK VTIAQGGVLP NIQAVLLPKK TESHHKAKGK //