ID EIF1A_HUMAN Reviewed; 165 AA.
AC Q8N9N8; B2R4N5; Q9BSC1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 24-JAN-2024, entry version 157.
DE RecName: Full=Probable RNA-binding protein EIF1AD;
DE AltName: Full=Eukaryotic translation initiation factor 1A domain-containing protein;
DE AltName: Full=Haponin;
GN Name=EIF1AD;
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 PROTEIN SEQUENCE, FUNCTION, INTERACTION WITH GAPDH, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=20644585; DOI=10.1134/s1068162010030027;
RA Rakitina T.V., Bogatova O.V., Smirnova E.V., Pozdeev V.I., Kostanian I.A.,
RA Lipkin V.M.;
RT "Haponin (eIF1AD) interacts with glyceraldehyde 3-phosphate dehydrogenase
RT in the CHO-K1 cell line.";
RL Bioorg. Khim. 36:312-318(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-23.
RC TISSUE=Skin;
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 INTERACTION WITH STAT1.
RX PubMed=16189514; DOI=10.1038/nature04209;
RA Rual J.F., Venkatesan K., Hao T., Hirozane-Kishikawa T., Dricot A., Li N.,
RA Berriz G.F., Gibbons F.D., Dreze M., Ayivi-Guedehoussou N., Klitgord N.,
RA Simon C., Boxem M., Milstein S., Rosenberg J., Goldberg D.S., Zhang L.V.,
RA Wong S.L., Franklin G., Li S., Albala J.S., Lim J., Fraughton C.,
RA Llamosas E., Cevik S., Bex C., Lamesch P., Sikorski R.S., Vandenhaute J.,
RA Zoghbi H.Y., Smolyar A., Bosak S., Sequerra R., Doucette-Stamm L.,
RA Cusick M.E., Hill D.E., Roth F.P., Vidal M.;
RT "Towards a proteome-scale map of the human protein-protein interaction
RT network.";
RL Nature 437:1173-1178(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-159, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-33, 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22095125; DOI=10.1134/s1607672911050097;
RA Smirnova E.V., Rakitina T.V., Bogatova O.V., Ivanova D.L., Vorobyeva E.E.,
RA Lipkin A.V., Kostanyan I.A., Lipkin V.M.;
RT "Novel protein haponin regulates cellular response to oxidative stress.";
RL Dokl. Biochem. Biophys. 440:225-227(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-159, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP STRUCTURE BY NMR OF 16-114.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the eukaryotic initiation factor 1A in MGC11102
RT protein.";
RL Submitted (SEP-2006) to the PDB data bank.
CC -!- FUNCTION: Plays a role into cellular response to oxidative stress.
CC Decreases cell proliferation. {ECO:0000269|PubMed:20644585,
CC ECO:0000269|PubMed:22095125}.
CC -!- SUBUNIT: Interacts with GAPDH and STAT1. {ECO:0000269|PubMed:16189514,
CC ECO:0000269|PubMed:20644585}.
CC -!- INTERACTION:
CC Q8N9N8; Q96CW1: AP2M1; NbExp=3; IntAct=EBI-750700, EBI-297683;
CC Q8N9N8; Q8N7W2-2: BEND7; NbExp=6; IntAct=EBI-750700, EBI-10181188;
CC Q8N9N8; Q9BWC9: CCDC106; NbExp=3; IntAct=EBI-750700, EBI-711501;
CC Q8N9N8; Q53EZ4: CEP55; NbExp=5; IntAct=EBI-750700, EBI-747776;
CC Q8N9N8; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-750700, EBI-742887;
CC Q8N9N8; O95995: GAS8; NbExp=3; IntAct=EBI-750700, EBI-1052570;
CC Q8N9N8; Q5JQS6: GCSAML; NbExp=3; IntAct=EBI-750700, EBI-17857617;
CC Q8N9N8; Q49A26: GLYR1; NbExp=4; IntAct=EBI-750700, EBI-2804292;
CC Q8N9N8; Q92759: GTF2H4; NbExp=3; IntAct=EBI-750700, EBI-6380495;
CC Q8N9N8; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-750700, EBI-739832;
CC Q8N9N8; P50222: MEOX2; NbExp=3; IntAct=EBI-750700, EBI-748397;
CC Q8N9N8; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-750700, EBI-10172526;
CC Q8N9N8; Q8N565: MREG; NbExp=3; IntAct=EBI-750700, EBI-10978787;
CC Q8N9N8; P26367: PAX6; NbExp=3; IntAct=EBI-750700, EBI-747278;
CC Q8N9N8; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-750700, EBI-10302990;
CC Q8N9N8; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-750700, EBI-79165;
CC Q8N9N8; Q96BK5: PINX1; NbExp=3; IntAct=EBI-750700, EBI-721782;
CC Q8N9N8; A6NK89: RASSF10; NbExp=3; IntAct=EBI-750700, EBI-6912267;
CC Q8N9N8; Q9NYW8: RBAK; NbExp=3; IntAct=EBI-750700, EBI-1210429;
CC Q8N9N8; Q5RL73: RBM48; NbExp=3; IntAct=EBI-750700, EBI-473821;
CC Q8N9N8; O00560: SDCBP; NbExp=6; IntAct=EBI-750700, EBI-727004;
CC Q8N9N8; Q9H190: SDCBP2; NbExp=7; IntAct=EBI-750700, EBI-742426;
CC Q8N9N8; P42224: STAT1; NbExp=4; IntAct=EBI-750700, EBI-1057697;
CC Q8N9N8; O75558: STX11; NbExp=6; IntAct=EBI-750700, EBI-714135;
CC Q8N9N8; B9A6K1: TBC1D5; NbExp=3; IntAct=EBI-750700, EBI-10217641;
CC Q8N9N8; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-750700, EBI-11139477;
CC Q8N9N8; Q08117-2: TLE5; NbExp=3; IntAct=EBI-750700, EBI-11741437;
CC Q8N9N8; P19237: TNNI1; NbExp=3; IntAct=EBI-750700, EBI-746692;
CC Q8N9N8; O43829: ZBTB14; NbExp=3; IntAct=EBI-750700, EBI-10176632;
CC Q8N9N8; Q96BR9: ZBTB8A; NbExp=6; IntAct=EBI-750700, EBI-742740;
CC Q8N9N8; P59817: ZNF280A; NbExp=3; IntAct=EBI-750700, EBI-8489342;
CC Q8N9N8; Q96K83: ZNF521; NbExp=3; IntAct=EBI-750700, EBI-6597673;
CC Q8N9N8; Q96NG5: ZNF558; NbExp=3; IntAct=EBI-750700, EBI-373363;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20644585,
CC ECO:0000269|PubMed:22095125}.
CC -!- TISSUE SPECIFICITY: Expressed in the glioblastoma cell line U-87MG, the
CC embryonic kidney cell line HEK293, the pancreatic carcinoma cell line
CC PANC-1, the breast carcinoma cell line MCF-7, the lung cancer cell line
CC NCI-H460, and the chronic myelogenous leukemia cell line K-562.
CC {ECO:0000269|PubMed:20644585}.
CC -!- SIMILARITY: Belongs to the EIF1AD family. {ECO:0000305}.
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DR EMBL; AK094129; BAC04293.1; -; mRNA.
DR EMBL; AK311891; BAG34832.1; -; mRNA.
DR EMBL; CH471076; EAW74478.1; -; Genomic_DNA.
DR EMBL; BC005131; AAH05131.1; -; mRNA.
DR CCDS; CCDS8124.1; -.
DR RefSeq; NP_001229410.1; NM_001242481.1.
DR RefSeq; NP_001229411.1; NM_001242482.1.
DR RefSeq; NP_001229412.1; NM_001242483.1.
DR RefSeq; NP_001229413.1; NM_001242484.1.
DR RefSeq; NP_001229414.1; NM_001242485.1.
DR RefSeq; NP_001229415.1; NM_001242486.1.
DR RefSeq; NP_115701.2; NM_032325.3.
DR RefSeq; XP_016873901.1; XM_017018412.1.
DR PDB; 2DGY; NMR; -; A=17-114.
DR PDB; 6ZXF; EM; 3.70 A; j=1-165.
DR PDB; 6ZXG; EM; 2.60 A; j=1-165.
DR PDB; 6ZXH; EM; 2.70 A; j=1-165.
DR PDBsum; 2DGY; -.
DR PDBsum; 6ZXF; -.
DR PDBsum; 6ZXG; -.
DR PDBsum; 6ZXH; -.
DR AlphaFoldDB; Q8N9N8; -.
DR EMDB; EMD-11519; -.
DR EMDB; EMD-11520; -.
DR EMDB; EMD-11521; -.
DR SMR; Q8N9N8; -.
DR BioGRID; 124012; 97.
DR IntAct; Q8N9N8; 38.
DR MINT; Q8N9N8; -.
DR STRING; 9606.ENSP00000434056; -.
DR GlyGen; Q8N9N8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8N9N8; -.
DR PhosphoSitePlus; Q8N9N8; -.
DR BioMuta; EIF1AD; -.
DR DMDM; 74729733; -.
DR EPD; Q8N9N8; -.
DR jPOST; Q8N9N8; -.
DR MassIVE; Q8N9N8; -.
DR MaxQB; Q8N9N8; -.
DR PaxDb; 9606-ENSP00000309175; -.
DR PeptideAtlas; Q8N9N8; -.
DR ProteomicsDB; 72570; -.
DR Pumba; Q8N9N8; -.
DR Antibodypedia; 44351; 81 antibodies from 14 providers.
DR DNASU; 84285; -.
DR Ensembl; ENST00000312234.6; ENSP00000309175.2; ENSG00000175376.9.
DR Ensembl; ENST00000526451.5; ENSP00000436644.1; ENSG00000175376.9.
DR Ensembl; ENST00000527249.5; ENSP00000435439.1; ENSG00000175376.9.
DR Ensembl; ENST00000529964.5; ENSP00000435942.2; ENSG00000175376.9.
DR Ensembl; ENST00000533544.6; ENSP00000434056.1; ENSG00000175376.9.
DR GeneID; 84285; -.
DR KEGG; hsa:84285; -.
DR MANE-Select; ENST00000533544.6; ENSP00000434056.1; NM_001242481.2; NP_001229410.1.
DR UCSC; uc001ogm.3; human.
DR AGR; HGNC:28147; -.
DR CTD; 84285; -.
DR DisGeNET; 84285; -.
DR GeneCards; EIF1AD; -.
DR HGNC; HGNC:28147; EIF1AD.
DR HPA; ENSG00000175376; Low tissue specificity.
DR MIM; 618473; gene.
DR neXtProt; NX_Q8N9N8; -.
DR OpenTargets; ENSG00000175376; -.
DR PharmGKB; PA162384553; -.
DR VEuPathDB; HostDB:ENSG00000175376; -.
DR eggNOG; KOG2925; Eukaryota.
DR GeneTree; ENSGT00390000011180; -.
DR HOGENOM; CLU_106477_2_1_1; -.
DR InParanoid; Q8N9N8; -.
DR OMA; GVQCDAE; -.
DR OrthoDB; 55184at2759; -.
DR PhylomeDB; Q8N9N8; -.
DR TreeFam; TF314439; -.
DR PathwayCommons; Q8N9N8; -.
DR SignaLink; Q8N9N8; -.
DR BioGRID-ORCS; 84285; 638 hits in 1159 CRISPR screens.
DR ChiTaRS; EIF1AD; human.
DR EvolutionaryTrace; Q8N9N8; -.
DR GenomeRNAi; 84285; -.
DR Pharos; Q8N9N8; Tdark.
DR PRO; PR:Q8N9N8; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q8N9N8; Protein.
DR Bgee; ENSG00000175376; Expressed in pancreatic ductal cell and 183 other cell types or tissues.
DR ExpressionAtlas; Q8N9N8; baseline and differential.
DR Genevisible; Q8N9N8; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:InterPro.
DR CDD; cd05792; S1_eIF1AD_like; 1.
DR Gene3D; 1.10.1200.180; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR InterPro; IPR039294; EIF1AD.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR006196; RNA-binding_domain_S1_IF1.
DR InterPro; IPR001253; TIF_eIF-1A.
DR PANTHER; PTHR21641:SF0; RNA-BINDING PROTEIN EIF1AD-RELATED; 1.
DR PANTHER; PTHR21641; TRANSLATION INITIATION FACTOR-RELATED; 1.
DR Pfam; PF01176; eIF-1a; 1.
DR SMART; SM00652; eIF1a; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50832; S1_IF1_TYPE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT CHAIN 1..165
FT /note="Probable RNA-binding protein EIF1AD"
FT /id="PRO_0000314151"
FT DOMAIN 5..89
FT /note="S1-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00181"
FT REGION 112..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 6..12
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 56..65
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOD_RES 33
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3THJ3"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5RKI6"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3THJ3"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5RKI6"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 23
FT /note="D -> N (in dbSNP:rs17849919)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_037851"
FT VARIANT 159
FT /note="S -> N (in dbSNP:rs2276017)"
FT /id="VAR_037852"
FT HELIX 3..14
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 26..35
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:6ZXG"
FT TURN 55..60
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 78..88
FT /evidence="ECO:0007829|PDB:6ZXG"
FT HELIX 92..98
FT /evidence="ECO:0007829|PDB:6ZXG"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:6ZXG"
SQ SEQUENCE 165 AA; 19053 MW; 33FB5ACB777084B2 CRC64;
MSQATKRKHV VKEVLGEHIV PSDQQQIVRV LRTPGNNLHE VETAQGQRFL VSMPSKYRKN
IWIKRGDFLI VDPIEEGEKV KAEISFVLCK DHVRSLQKEG FWPEAFSEVA EKHNNRNRQT
QPELPAEPQL SGEESSSEDD SDLFVNTNRR QYHESEEESE EEEAA
//
