H2AX_HUMAN
ID H2AX_HUMAN Reviewed; 143 AA.
AC P16104; Q4ZGJ7; Q6IAS5;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 220.
DE RecName: Full=Histone H2AX;
DE Short=H2a/x;
DE AltName: Full=Histone H2A.X;
GN Name=H2AX {ECO:0000312|HGNC:HGNC:4739};
GN Synonyms=H2AFX {ECO:0000312|HGNC:HGNC:4739};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2587254; DOI=10.1093/nar/17.22.9113;
RA Mannironi C., Bonner W.M., Hatch C.L.;
RT "H2A.X. a histone isoprotein with a conserved C-terminal sequence, is
RT encoded by a novel mRNA with both DNA replication type and polyA 3'
RT processing signals.";
RL Nucleic Acids Res. 17:9113-9126(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Placenta;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION AT SER-140, AND MUTAGENESIS OF GLN-141.
RX PubMed=9488723; DOI=10.1074/jbc.273.10.5858;
RA Rogakou E.P., Pilch D.R., Orr A.H., Ivanova V.S., Bonner W.M.;
RT "DNA double-stranded breaks induce histone H2AX phosphorylation on serine
RT 139.";
RL J. Biol. Chem. 273:5858-5868(1998).
RN [6]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-140.
RX PubMed=10477747; DOI=10.1083/jcb.146.5.905;
RA Rogakou E.P., Boon C., Redon C., Bonner W.M.;
RT "Megabase chromatin domains involved in DNA double-strand breaks in vivo.";
RL J. Cell Biol. 146:905-916(1999).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-140.
RX PubMed=10959836; DOI=10.1016/s0960-9822(00)00610-2;
RA Paull T.T., Rogakou E.P., Yamazaki V., Kirchgessner C.U., Gellert M.,
RA Bonner W.M.;
RT "A critical role for histone H2AX in recruitment of repair factors to
RT nuclear foci after DNA damage.";
RL Curr. Biol. 10:886-895(2000).
RN [8]
RP PHOSPHORYLATION AT SER-140.
RX PubMed=10734083; DOI=10.1074/jbc.275.13.9390;
RA Rogakou E.P., Nieves-Neira W., Boon C., Pommier Y., Bonner W.M.;
RT "Initiation of DNA fragmentation during apoptosis induces phosphorylation
RT of H2AX histone at serine 139.";
RL J. Biol. Chem. 275:9390-9395(2000).
RN [9]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-140.
RX PubMed=11673449; DOI=10.1074/jbc.c100569200;
RA Ward I.M., Chen J.;
RT "Histone H2AX is phosphorylated in an ATR-dependent manner in response to
RT replicational stress.";
RL J. Biol. Chem. 276:47759-47762(2001).
RN [10]
RP FUNCTION, INTERACTION WITH NBN AND BRCA1, SUBCELLULAR LOCATION, AND
RP PHOSPHORYLATION AT SER-140.
RX PubMed=12419185; DOI=10.1016/s0960-9822(02)01259-9;
RA Kobayashi J., Tauchi H., Sakamoto S., Nakamura A., Morishima K.,
RA Matsuura S., Kobayashi T., Tamai K., Tanimoto K., Komatsu K.;
RT "NBS1 localizes to gamma-H2AX foci through interaction with the FHA/BRCT
RT domain.";
RL Curr. Biol. 12:1846-1851(2002).
RN [11]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-140.
RX PubMed=12697768; DOI=10.1074/jbc.c300117200;
RA Ward I.M., Minn K., Jorda K.G., Chen J.;
RT "Accumulation of checkpoint protein 53BP1 at DNA breaks involves its
RT binding to phosphorylated histone H2AX.";
RL J. Biol. Chem. 278:19579-19582(2003).
RN [12]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-140.
RX PubMed=12660252; DOI=10.1074/jbc.m300198200;
RA Furuta T., Takemura H., Liao Z.-Y., Aune G.J., Redon C., Sedelnikova O.A.,
RA Pilch D.R., Rogakou E.P., Celeste A., Chen H.T., Nussenzweig A.,
RA Aladjem M.I., Bonner W.M., Pommier Y.;
RT "Phosphorylation of histone H2AX and activation of Mre11, Rad50, and Nbs1
RT in response to replication-dependent DNA double-strand breaks induced by
RT mammalian DNA topoisomerase I cleavage complexes.";
RL J. Biol. Chem. 278:20303-20312(2003).
RN [13]
RP FUNCTION, INTERACTION WITH MDC1 AND TP53BP1, SUBCELLULAR LOCATION, AND
RP PHOSPHORYLATION AT SER-140.
RX PubMed=12607005; DOI=10.1038/nature01446;
RA Stewart G.S., Wang B., Bignell C.R., Taylor A.M.R., Elledge S.J.;
RT "MDC1 is a mediator of the mammalian DNA damage checkpoint.";
RL Nature 421:961-966(2003).
RN [14]
RP PHOSPHORYLATION AT SER-140.
RX PubMed=14627815; DOI=10.1093/nar/gkg921;
RA Park E.-J., Chan D.W., Park J.-H., Oettinger M.A., Kwon J.;
RT "DNA-PK is activated by nucleosomes and phosphorylates H2AX within the
RT nucleosomes in an acetylation-dependent manner.";
RL Nucleic Acids Res. 31:6819-6827(2003).
RN [15]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-140.
RX PubMed=15059890; DOI=10.1158/0008-5472.can-03-3207;
RA Stiff T., O'Driscoll M., Rief N., Iwabuchi K., Loebrich M., Jeggo P.A.;
RT "ATM and DNA-PK function redundantly to phosphorylate H2AX after exposure
RT to ionizing radiation.";
RL Cancer Res. 64:2390-2396(2004).
RN [16]
RP FUNCTION, INTERACTION WITH MDC1 AND NBN, AND SUBCELLULAR LOCATION.
RX PubMed=15201865; DOI=10.1038/sj.emboj.7600269;
RA Lukas C., Melander F., Stucki M., Falck J., Bekker-Jensen S., Goldberg M.,
RA Lerenthal Y., Jackson S.P., Bartek J., Lukas J.;
RT "Mdc1 couples DNA double-strand break recognition by Nbs1 with its H2AX-
RT dependent chromatin retention.";
RL EMBO J. 23:2674-2683(2004).
RN [17]
RP PHOSPHORYLATION AT SER-140.
RX PubMed=15489221; DOI=10.1074/jbc.m406879200;
RA Kurz E.U., Douglas P., Lees-Miller S.P.;
RT "Doxorubicin activates ATM-dependent phosphorylation of multiple downstream
RT targets in part through the generation of reactive oxygen species.";
RL J. Biol. Chem. 279:53272-53281(2004).
RN [18]
RP INTERACTION WITH DHX9, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT
RP SER-140.
RX PubMed=15613478; DOI=10.1074/jbc.m411444200;
RA Mischo H.E., Hemmerich P., Grosse F., Zhang S.;
RT "Actinomycin D induces histone gamma-H2AX foci and complex formation of
RT gamma-H2AX with Ku70 and nuclear DNA helicase II.";
RL J. Biol. Chem. 280:9586-9594(2005).
RN [19]
RP DEPHOSPHORYLATION.
RX PubMed=16310392; DOI=10.1016/j.molcel.2005.10.003;
RA Chowdhury D., Keogh M.-C., Ishii H., Peterson C.L., Buratowski S.,
RA Lieberman J.;
RT "gamma-H2AX dephosphorylation by protein phosphatase 2A facilitates DNA
RT double-strand break repair.";
RL Mol. Cell 20:801-809(2005).
RN [20]
RP INTERACTION WITH ARRB2.
RX PubMed=16820410; DOI=10.1242/jcs.03046;
RA Neuhaus E.M., Mashukova A., Barbour J., Wolters D., Hatt H.;
RT "Novel function of beta-arrestin2 in the nucleus of mature spermatozoa.";
RL J. Cell Sci. 119:3047-3056(2006).
RN [21]
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 [22]
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 [23]
RP FUNCTION, ACETYLATION AT LYS-6, UBIQUITINATION AT LYS-120, PHOSPHORYLATION
RP AT SER-140, AND MUTAGENESIS OF LYS-6 AND SER-140.
RX PubMed=17709392; DOI=10.1128/mcb.00579-07;
RA Ikura T., Tashiro S., Kakino A., Shima H., Jacob N., Amunugama R.,
RA Yoder K., Izumi S., Kuraoka I., Tanaka K., Kimura H., Ikura M.,
RA Nishikubo S., Ito T., Muto A., Miyagawa K., Takeda S., Fishel R.,
RA Igarashi K., Kamiya K.;
RT "DNA damage-dependent acetylation and ubiquitination of H2AX enhances
RT chromatin dynamics.";
RL Mol. Cell. Biol. 27:7028-7040(2007).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [25]
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., Oldreive C.,
RA Wildenhain J., Tagliaferro A., Pelletier L., Taubenheim N., Durandy A.,
RA Byrd P.J., Stankovic T., Taylor A.M.R., 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 [26]
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., Lukas J.,
RA Lukas C.;
RT "RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to
RT allow accumulation of repair proteins.";
RL Cell 136:435-446(2009).
RN [27]
RP PHOSPHORYLATION AT TYR-143, AND MUTAGENESIS OF TYR-143.
RX PubMed=19092802; DOI=10.1038/nature07668;
RA Xiao A., Li H., Shechter D., Ahn S.H., Fabrizio L.A., Erdjument-Bromage H.,
RA Ishibe-Murakami S., Wang B., Tempst P., Hofmann K., Patel D.J.,
RA Elledge S.J., Allis C.D.;
RT "WSTF regulates the H2A.X DNA damage response via a novel tyrosine kinase
RT activity.";
RL Nature 457:57-62(2009).
RN [28]
RP PHOSPHORYLATION AT TYR-143, AND MUTAGENESIS OF TYR-143.
RX PubMed=19234442; DOI=10.1038/nature07849;
RA Cook P.J., Ju B.G., Telese F., Wang X., Glass C.K., Rosenfeld M.G.;
RT "Tyrosine dephosphorylation of H2AX modulates apoptosis and survival
RT decisions.";
RL Nature 458:591-596(2009).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [31]
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 signaling.";
RL Cell 150:1182-1195(2012).
RN [32]
RP INTERACTION WITH EPSTEIN-BARR VIRUS PROTEIN EBNA6 (MICROBIAL INFECTION),
RP AND SUBCELLULAR LOCATION.
RX PubMed=24429368; DOI=10.1128/jvi.03568-13;
RA Jha H.C., Aj M.P., Saha A., Banerjee S., Lu J., Robertson E.S.;
RT "Epstein-Barr virus essential antigen EBNA3C attenuates H2AX expression.";
RL J. Virol. 88:3776-3788(2014).
RN [33]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-135, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [34]
RP FUNCTION, AND ACETYLATION AT LYS-6.
RX PubMed=26438602; DOI=10.1128/mcb.00757-15;
RA Ikura M., Furuya K., Matsuda S., Matsuda R., Shima H., Adachi J.,
RA Matsuda T., Shiraki T., Ikura T.;
RT "Acetylation of histone H2AX at Lys 5 by the TIP60 histone
RT acetyltransferase complex is essential for the dynamic binding of NBS1 to
RT damaged chromatin.";
RL Mol. Cell. Biol. 35:4147-4157(2015).
RN [35]
RP INTERACTION WITH WRAP53.
RX PubMed=26734725; DOI=10.1080/19491034.2015.1106675;
RA Rassoolzadeh H., Coucoravas C., Farnebo M.;
RT "The proximity ligation assay reveals that at DNA double-strand breaks
RT WRAP53beta associates with gammaH2AX and controls interactions between RNF8
RT and MDC1.";
RL Nucleus 6:417-424(2015).
RN [36]
RP INTERACTION WITH HDGFL2.
RX PubMed=26721387; DOI=10.1093/nar/gkv1526;
RA Baude A., Aaes T.L., Zhai B., Al-Nakouzi N., Oo H.Z., Daugaard M.,
RA Rohde M., Jaeaettelae M.;
RT "Hepatoma-derived growth factor-related protein 2 promotes DNA repair by
RT homologous recombination.";
RL Nucleic Acids Res. 44:2214-2226(2016).
RN [37]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-128 AND LYS-135, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [38]
RP INTERACTION WITH WRAP53.
RX PubMed=27715493; DOI=10.1080/15476286.2016.1243647;
RA Coucoravas C., Dhanjal S., Henriksson S., Boehm S., Farnebo M.;
RT "Phosphorylation of the Cajal body protein WRAP53beta by ATM promotes its
RT involvement in the DNA damage response.";
RL RNA Biol. 14:804-813(2017).
RN [39]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 134-143, AND PHOSPHORYLATION AT
RP SER-140.
RX PubMed=22154951; DOI=10.1016/j.jsb.2011.11.022;
RA Shao Z., Li F., Sy S.M., Yan W., Zhang Z., Gong D., Wen B., Huen M.S.,
RA Gong Q., Wu J., Shi Y.;
RT "Specific recognition of phosphorylated tail of H2AX by the tandem BRCT
RT domains of MCPH1 revealed by complex structure.";
RL J. Struct. Biol. 177:459-468(2012).
CC -!- FUNCTION: Variant histone H2A which replaces conventional H2A in a
CC subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin,
CC limiting DNA accessibility to the cellular machineries which require
CC DNA as a template. Histones thereby play a central role in
CC transcription regulation, DNA repair, DNA replication and chromosomal
CC stability. DNA accessibility is regulated via a complex set of post-
CC translational modifications of histones, also called histone code, and
CC nucleosome remodeling. Required for checkpoint-mediated arrest of cell
CC cycle progression in response to low doses of ionizing radiation and
CC for efficient repair of DNA double strand breaks (DSBs) specifically
CC when modified by C-terminal phosphorylation.
CC {ECO:0000269|PubMed:10959836, ECO:0000269|PubMed:12419185,
CC ECO:0000269|PubMed:12607005, ECO:0000269|PubMed:15201865,
CC ECO:0000269|PubMed:17709392, ECO:0000269|PubMed:26438602}.
CC -!- SUBUNIT: The nucleosome is a histone octamer containing two molecules
CC each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and
CC two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA
CC (Probable). Interacts with numerous proteins required for DNA damage
CC signaling and repair when phosphorylated on Ser-140 (PubMed:12419185,
CC PubMed:12607005, PubMed:15201865). These include MDC1, TP53BP1, BRCA1
CC and the MRN complex, composed of MRE11, RAD50, and NBN
CC (PubMed:12419185, PubMed:12607005, PubMed:15201865). Interaction with
CC the MRN complex is mediated at least in part by NBN (PubMed:12419185).
CC Also interacts with DHX9/NDHII when phosphorylated on Ser-140 and MCPH1
CC when phosphorylated at Ser-140 or Tyr-143 (PubMed:15613478). Interacts
CC with ARRB2; the interaction is detected in the nucleus upon OR1D2
CC stimulation (PubMed:16820410). Interacts with WRAP53/TCAB1
CC (PubMed:26734725, PubMed:27715493). Interacts with HDGFL2
CC (PubMed:26721387). {ECO:0000269|PubMed:12419185,
CC ECO:0000269|PubMed:12607005, ECO:0000269|PubMed:15201865,
CC ECO:0000269|PubMed:15613478, ECO:0000269|PubMed:16820410,
CC ECO:0000269|PubMed:26721387, ECO:0000269|PubMed:26734725,
CC ECO:0000269|PubMed:27715493, ECO:0000305}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus
CC protein EBNA6. {ECO:0000269|PubMed:24429368}.
CC -!- INTERACTION:
CC P16104; P38398: BRCA1; NbExp=4; IntAct=EBI-494830, EBI-349905;
CC P16104; P58876: H2BC5; NbExp=2; IntAct=EBI-494830, EBI-4409942;
CC P16104; Q16695: H3-4; NbExp=12; IntAct=EBI-494830, EBI-358900;
CC P16104; P62805: H4C9; NbExp=5; IntAct=EBI-494830, EBI-302023;
CC P16104; P02545: LMNA; NbExp=3; IntAct=EBI-494830, EBI-351935;
CC P16104; P45983: MAPK8; NbExp=3; IntAct=EBI-494830, EBI-286483;
CC P16104; Q14676: MDC1; NbExp=21; IntAct=EBI-494830, EBI-495644;
CC P16104; P49959: MRE11; NbExp=7; IntAct=EBI-494830, EBI-396513;
CC P16104; O60934: NBN; NbExp=14; IntAct=EBI-494830, EBI-494844;
CC P16104; Q6ZW49-1: PAXIP1; NbExp=7; IntAct=EBI-494830, EBI-7521368;
CC P16104; O15297: PPM1D; NbExp=3; IntAct=EBI-494830, EBI-1551512;
CC P16104; P51532: SMARCA4; NbExp=9; IntAct=EBI-494830, EBI-302489;
CC P16104; Q15554: TERF2; NbExp=4; IntAct=EBI-494830, EBI-706637;
CC P16104; Q12888: TP53BP1; NbExp=6; IntAct=EBI-494830, EBI-396540;
CC P16104; Q99986: VRK1; NbExp=3; IntAct=EBI-494830, EBI-1769146;
CC P16104; PRO_0000022031 [Q9Z0X1]: Aifm1; Xeno; NbExp=2; IntAct=EBI-494830, EBI-5326677;
CC P16104; P46933-1: Apbb1; Xeno; NbExp=2; IntAct=EBI-494830, EBI-15759525;
CC P16104; Q6P4T3: Eya3; Xeno; NbExp=2; IntAct=EBI-494830, EBI-15759383;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12419185,
CC ECO:0000269|PubMed:12660252, ECO:0000269|PubMed:12697768,
CC ECO:0000269|PubMed:15613478, ECO:0000269|PubMed:24429368}. Chromosome
CC {ECO:0000269|PubMed:10959836, ECO:0000269|PubMed:11673449,
CC ECO:0000269|PubMed:12607005, ECO:0000269|PubMed:12660252,
CC ECO:0000269|PubMed:15059890, ECO:0000269|PubMed:15201865,
CC ECO:0000269|PubMed:15613478}.
CC -!- DEVELOPMENTAL STAGE: Synthesized in G1 as well as in S-phase.
CC -!- DOMAIN: The [ST]-Q motif constitutes a recognition sequence for kinases
CC from the PI3/PI4-kinase family.
CC -!- PTM: Phosphorylated on Ser-140 (to form gamma-H2AX or H2AX139ph) in
CC response to DNA double strand breaks (DSBs) generated by exogenous
CC genotoxic agents and by stalled replication forks, and may also occur
CC during meiotic recombination events and immunoglobulin class switching
CC in lymphocytes. Phosphorylation can extend up to several thousand
CC nucleosomes from the actual site of the DSB and may mark the
CC surrounding chromatin for recruitment of proteins required for DNA
CC damage signaling and repair. Widespread phosphorylation may also serve
CC to amplify the damage signal or aid repair of persistent lesions.
CC Phosphorylation of Ser-140 (H2AX139ph) in response to ionizing
CC radiation is mediated by both ATM and PRKDC while defects in DNA
CC replication induce Ser-140 phosphorylation (H2AX139ph) subsequent to
CC activation of ATR and PRKDC. Dephosphorylation of Ser-140 by PP2A is
CC required for DNA DSB repair. In meiosis, Ser-140 phosphorylation
CC (H2AX139ph) may occur at synaptonemal complexes during leptotene as an
CC ATM-dependent response to the formation of programmed DSBs by SPO11.
CC Ser-140 phosphorylation (H2AX139ph) may subsequently occurs at
CC unsynapsed regions of both autosomes and the XY bivalent during
CC zygotene, downstream of ATR and BRCA1 activation. Ser-140
CC phosphorylation (H2AX139ph) may also be required for transcriptional
CC repression of unsynapsed chromatin and meiotic sex chromosome
CC inactivation (MSCI), whereby the X and Y chromosomes condense in
CC pachytene to form the heterochromatic XY-body. During immunoglobulin
CC class switch recombination in lymphocytes, Ser-140 phosphorylation
CC (H2AX139ph) may occur at sites of DNA-recombination subsequent to
CC activation of the activation-induced cytidine deaminase AICDA.
CC Phosphorylation at Tyr-143 (H2AXY142ph) by BAZ1B/WSTF determines the
CC relative recruitment of either DNA repair or pro-apoptotic factors.
CC Phosphorylation at Tyr-143 (H2AXY142ph) favors the recruitment of
CC APBB1/FE65 and pro-apoptosis factors such as MAPK8/JNK1, triggering
CC apoptosis. In contrast, dephosphorylation of Tyr-143 by EYA proteins
CC (EYA1, EYA2, EYA3 or EYA4) favors the recruitment of MDC1-containing
CC DNA repair complexes to the tail of phosphorylated Ser-140 (H2AX139ph).
CC {ECO:0000269|PubMed:10477747, ECO:0000269|PubMed:10734083,
CC ECO:0000269|PubMed:10959836, ECO:0000269|PubMed:11673449,
CC ECO:0000269|PubMed:12419185, ECO:0000269|PubMed:12607005,
CC ECO:0000269|PubMed:12660252, ECO:0000269|PubMed:12697768,
CC ECO:0000269|PubMed:14627815, ECO:0000269|PubMed:15059890,
CC ECO:0000269|PubMed:15489221, ECO:0000269|PubMed:15613478,
CC ECO:0000269|PubMed:17709392, ECO:0000269|PubMed:19092802,
CC ECO:0000269|PubMed:19234442, ECO:0000269|PubMed:22154951,
CC ECO:0000269|PubMed:9488723}.
CC -!- PTM: Monoubiquitination of Lys-120 (H2AXK119ub) by RING1 and RNF2/RING2
CC complex gives a specific tag for epigenetic transcriptional repression
CC (By similarity). Following DNA double-strand breaks (DSBs), it is
CC ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2
CC ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the
CC recruitment of repair proteins to sites of DNA damage. Ubiquitination
CC at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response
CC to DNA damage is initiated by RNF168 that mediates monoubiquitination
CC at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to
CC monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains
CC in vitro. H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked
CC ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events.
CC {ECO:0000250|UniProtKB:P27661, ECO:0000269|PubMed:18001824,
CC ECO:0000269|PubMed:18001825, ECO:0000269|PubMed:19203578,
CC ECO:0000269|PubMed:19203579, ECO:0000269|PubMed:22980979}.
CC -!- PTM: Acetylation at Lys-6 (H2AXK5ac) by KAT5 component of the NuA4
CC histone acetyltransferase complex promotes NBN/NBS1 assembly at the
CC sites of DNA damage (PubMed:17709392, PubMed:26438602). Acetylation at
CC Lys-37 increases in S and G2 phases. This modification has been
CC proposed to play a role in DNA double-strand break repair (By
CC similarity). {ECO:0000250|UniProtKB:P27661,
CC ECO:0000269|PubMed:17709392, ECO:0000269|PubMed:26438602}.
CC -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/h2afx/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/H2AFXID40783ch11q23.html";
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DR EMBL; X14850; CAA32968.1; -; mRNA.
DR EMBL; CR457079; CAG33360.1; -; mRNA.
DR EMBL; DQ015918; AAY22178.1; -; Genomic_DNA.
DR EMBL; BC004915; AAH04915.1; -; mRNA.
DR EMBL; BC011694; AAH11694.1; -; mRNA.
DR EMBL; BC013416; AAH13416.1; -; mRNA.
DR CCDS; CCDS8410.1; -.
DR PIR; S07631; S07631.
DR RefSeq; NP_002096.1; NM_002105.2.
DR PDB; 1YDP; X-ray; 1.90 A; P=78-86.
DR PDB; 2AZM; X-ray; 2.41 A; C/D=134-143.
DR PDB; 2D31; X-ray; 3.20 A; C/F=78-86.
DR PDB; 2DYP; X-ray; 2.50 A; C=78-86.
DR PDB; 3SHV; X-ray; 2.10 A; C/D=134-143.
DR PDB; 3SQD; X-ray; 2.15 A; C/D=134-143.
DR PDB; 3SZM; X-ray; 2.63 A; I/J/K/L/M/N/O/P=134-143.
DR PDB; 3U3Z; X-ray; 1.50 A; B=140-143.
DR PDB; 6K1I; X-ray; 2.75 A; C/G=1-143.
DR PDB; 6K1J; X-ray; 2.85 A; C/G=1-143.
DR PDB; 6K1K; X-ray; 2.20 A; C/G=1-143.
DR PDB; 6ZWK; X-ray; 1.55 A; G/H/I/J/K/L=134-143.
DR PDBsum; 1YDP; -.
DR PDBsum; 2AZM; -.
DR PDBsum; 2D31; -.
DR PDBsum; 2DYP; -.
DR PDBsum; 3SHV; -.
DR PDBsum; 3SQD; -.
DR PDBsum; 3SZM; -.
DR PDBsum; 3U3Z; -.
DR PDBsum; 6K1I; -.
DR PDBsum; 6K1J; -.
DR PDBsum; 6K1K; -.
DR PDBsum; 6ZWK; -.
DR AlphaFoldDB; P16104; -.
DR SMR; P16104; -.
DR BioGRID; 109268; 591.
DR CORUM; P16104; -.
DR DIP; DIP-33604N; -.
DR ELM; P16104; -.
DR IntAct; P16104; 293.
DR MINT; P16104; -.
DR STRING; 9606.ENSP00000434024; -.
DR GlyGen; P16104; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P16104; -.
DR PhosphoSitePlus; P16104; -.
DR SwissPalm; P16104; -.
DR BioMuta; H2AFX; -.
DR DMDM; 121992; -.
DR EPD; P16104; -.
DR jPOST; P16104; -.
DR MassIVE; P16104; -.
DR MaxQB; P16104; -.
DR PaxDb; P16104; -.
DR PeptideAtlas; P16104; -.
DR PRIDE; P16104; -.
DR ProteomicsDB; 53286; -.
DR TopDownProteomics; P16104; -.
DR ABCD; P16104; 4 sequenced antibodies.
DR Antibodypedia; 3220; 1601 antibodies from 47 providers.
DR DNASU; 3014; -.
DR Ensembl; ENST00000375167.1; ENSP00000364310.1; ENSG00000188486.4.
DR Ensembl; ENST00000530167.2; ENSP00000434024.1; ENSG00000188486.4.
DR GeneID; 3014; -.
DR KEGG; hsa:3014; -.
DR MANE-Select; ENST00000530167.2; ENSP00000434024.1; NM_002105.3; NP_002096.1.
DR UCSC; uc001pvg.4; human.
DR CTD; 3014; -.
DR DisGeNET; 3014; -.
DR GeneCards; H2AX; -.
DR HGNC; HGNC:4739; H2AX.
DR HPA; ENSG00000188486; Low tissue specificity.
DR MIM; 601772; gene.
DR neXtProt; NX_P16104; -.
DR OpenTargets; ENSG00000188486; -.
DR PharmGKB; PA29116; -.
DR VEuPathDB; HostDB:ENSG00000188486; -.
DR eggNOG; KOG1756; Eukaryota.
DR GeneTree; ENSGT01020000230360; -.
DR HOGENOM; CLU_062828_3_1_1; -.
DR InParanoid; P16104; -.
DR OMA; FQMAGRG; -.
DR OrthoDB; 1504122at2759; -.
DR PhylomeDB; P16104; -.
DR TreeFam; TF300137; -.
DR PathwayCommons; P16104; -.
DR Reactome; R-HSA-110328; Recognition and association of DNA glycosylase with site containing an affected pyrimidine.
DR Reactome; R-HSA-110329; Cleavage of the damaged pyrimidine.
DR Reactome; R-HSA-110330; Recognition and association of DNA glycosylase with site containing an affected purine.
DR Reactome; R-HSA-110331; Cleavage of the damaged purine.
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-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-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
DR Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-HSA-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
DR Reactome; R-HSA-73728; RNA Polymerase I Promoter Opening.
DR Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape.
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-9616222; Transcriptional regulation of granulopoiesis.
DR Reactome; R-HSA-9670095; Inhibition of DNA recombination at telomere.
DR Reactome; R-HSA-9710421; Defective pyroptosis.
DR Reactome; R-HSA-977225; Amyloid fiber formation.
DR SignaLink; P16104; -.
DR SIGNOR; P16104; -.
DR BioGRID-ORCS; 3014; 307 hits in 1084 CRISPR screens.
DR ChiTaRS; H2AFX; human.
DR EvolutionaryTrace; P16104; -.
DR GeneWiki; H2AFX; -.
DR GenomeRNAi; 3014; -.
DR Pharos; P16104; Tbio.
DR PRO; PR:P16104; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P16104; protein.
DR Bgee; ENSG00000188486; Expressed in ventricular zone and 193 other tissues.
DR Genevisible; P16104; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0000794; C:condensed nuclear chromosome; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005657; C:replication fork; IEA:Ensembl.
DR GO; GO:0090734; C:site of DNA damage; IMP:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; IDA:MGI.
DR GO; GO:0001741; C:XY body; IEA:Ensembl.
DR GO; GO:0003684; F:damaged DNA binding; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0042393; F:histone binding; IPI:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:BHF-UCL.
DR GO; GO:0071480; P:cellular response to gamma radiation; IEA:Ensembl.
DR GO; GO:0090398; P:cellular senescence; IEA:Ensembl.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IDA:UniProtKB.
DR GO; GO:0006302; P:double-strand break repair; NAS:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:Ensembl.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006334; P:nucleosome assembly; NAS:UniProtKB.
DR GO; GO:0045739; P:positive regulation of DNA repair; NAS:UniProtKB.
DR GO; GO:0010212; P:response to ionizing radiation; NAS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR CDD; cd00074; H2A; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR IDEAL; IID00027; -.
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 PANTHER; PTHR23430; PTHR23430; 1.
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 3D-structure; Acetylation; Cell cycle; Chromosome; DNA damage;
KW DNA recombination; DNA repair; DNA-binding; Host-virus interaction;
KW Isopeptide bond; Meiosis; Nucleosome core; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P27661"
FT CHAIN 2..143
FT /note="Histone H2AX"
FT /id="PRO_0000055242"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 140..141
FT /note="[ST]-Q motif"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P27661"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27661"
FT MOD_RES 6
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:17709392,
FT ECO:0000269|PubMed:26438602"
FT MOD_RES 10
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P27661"
FT MOD_RES 10
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT MOD_RES 37
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P27661"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27661"
FT MOD_RES 140
FT /note="Phosphoserine; by ATM, ATR and PRKDC"
FT /evidence="ECO:0000269|PubMed:10477747,
FT ECO:0000269|PubMed:10734083, ECO:0000269|PubMed:10959836,
FT ECO:0000269|PubMed:11673449, ECO:0000269|PubMed:12419185,
FT ECO:0000269|PubMed:12607005, ECO:0000269|PubMed:12660252,
FT ECO:0000269|PubMed:12697768, ECO:0000269|PubMed:14627815,
FT ECO:0000269|PubMed:15059890, ECO:0000269|PubMed:15489221,
FT ECO:0000269|PubMed:15613478, ECO:0000269|PubMed:17709392,
FT ECO:0000269|PubMed:22154951, ECO:0000269|PubMed:9488723,
FT ECO:0007744|PubMed:17525332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 143
FT /note="Phosphotyrosine; by WSTF"
FT /evidence="ECO:0000269|PubMed:19092802,
FT ECO:0000269|PubMed:19234442"
FT CROSSLNK 14
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:22980979"
FT CROSSLNK 16
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:22980979"
FT CROSSLNK 120
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:17709392"
FT CROSSLNK 128
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 135
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT MUTAGEN 6
FT /note="K->R: Decreased acetylation and reduced H2AXK119ub
FT ubiquitination."
FT /evidence="ECO:0000269|PubMed:17709392"
FT MUTAGEN 140
FT /note="S->A: Impaired phosphorylation without affecting
FT H2AXK5ac acetylation."
FT /evidence="ECO:0000269|PubMed:17709392"
FT MUTAGEN 141
FT /note="Q->N: Reduced phosphorylation of S-140 in response
FT to DNA damage."
FT /evidence="ECO:0000269|PubMed:9488723"
FT MUTAGEN 143
FT /note="Y->F: Displays a reduced apoptotic response. S-140
FT phosphorylation is reduced."
FT /evidence="ECO:0000269|PubMed:19092802,
FT ECO:0000269|PubMed:19234442"
FT CONFLICT 78
FT /note="R -> L (in Ref. 2; CAG33360)"
FT /evidence="ECO:0000305"
FT HELIX 18..22
FT /evidence="ECO:0007829|PDB:6K1K"
FT HELIX 28..37
FT /evidence="ECO:0007829|PDB:6K1K"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:6K1K"
FT HELIX 47..73
FT /evidence="ECO:0007829|PDB:6K1K"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:6K1K"
FT HELIX 81..90
FT /evidence="ECO:0007829|PDB:6K1K"
FT HELIX 92..97
FT /evidence="ECO:0007829|PDB:6K1K"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:6K1K"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:6K1I"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:6K1K"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:6ZWK"
SQ SEQUENCE 143 AA; 15145 MW; D4683775C2E6C3A9 CRC64;
MSGRGKTGGK ARAKAKSRSS RAGLQFPVGR VHRLLRKGHY AERVGAGAPV YLAAVLEYLT
AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGG VTIAQGGVLP NIQAVLLPKK
TSATVGPKAP SGGKKATQAS QEY
