ID DIDO1_HUMAN Reviewed; 2240 AA. AC Q9BTC0; A8MY65; B9EH82; E1P5I1; O15043; Q3ZTL7; Q3ZTL8; Q4VXS1; Q4VXS2; AC Q4VXV8; Q4VXV9; Q96D72; Q9BQW0; Q9BW03; Q9H4G6; Q9H4G7; Q9NTU8; Q9NUM8; AC Q9UFB6; DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 5. DT 27-MAR-2024, entry version 206. DE RecName: Full=Death-inducer obliterator 1; DE Short=DIO-1; DE Short=hDido1; DE AltName: Full=Death-associated transcription factor 1; DE Short=DATF-1; GN Name=DIDO1; Synonyms=C20orf158, DATF1, KIAA0333; 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] (ISOFORMS 1 AND 4), FUNCTION, ROLE IN MYELOID RP NEOPLASMS, AND VARIANTS THR-544 AND THR-556. RX PubMed=16127461; DOI=10.1172/jci24177; RA Futterer A., Campanero M.R., Leonardo E., Criado L.M., Flores J.M., RA Hernandez J.M., San Miguel J.F., Martinez-A C.; RT "Dido gene expression alterations are implicated in the induction of RT hematological myeloid neoplasms."; RL J. Clin. Invest. 115:2351-2362(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=9205841; DOI=10.1093/dnares/4.2.141; RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. VII. The RT complete sequences of 100 new cDNA clones from brain which can code for RT large proteins in vitro."; RL DNA Res. 4:141-150(1997). RN [3] RP SEQUENCE REVISION. RA Ohara O., Nagase T., Kikuno R., Nomura N.; RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Placenta; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [6] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 2). RC TISSUE=Brain, Colon, Kidney, Muscle, 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 [8] RP PROTEIN SEQUENCE OF 1-14; 74-82; 519-529; 613-626; 1218-1230; 1334-1347; RP 1439-1447 AND 1743-1754, ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Ovarian carcinoma; RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.; RL Submitted (DEC-2008) to UniProtKB. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1623-2240 (ISOFORM 4). RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-898 AND SER-1456, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-805 AND SER-809, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1040 AND SER-1456, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-151; SER-152; SER-154; RP SER-805; SER-809; SER-898; SER-1019; SER-1030; SER-1260; SER-1456; THR-1469 RP AND SER-1714, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-805 AND SER-809, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-151; SER-152; SER-154; RP SER-805; SER-809; SER-1030; SER-1040; SER-1312; SER-1456 AND SER-1522, AND RP IDENTIFICATION BY 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 [17] 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-154; SER-805; RP SER-898; SER-1040; SER-1260 AND SER-1456, AND IDENTIFICATION BY MASS RP 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 [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; SER-523; SER-805; RP SER-809; SER-898; SER-1019; SER-1040; SER-1456 AND THR-1469, 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 [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1244 AND SER-1456, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [21] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1835; ARG-1893; ARG-1894; RP ARG-1977; ARG-1982; ARG-1993; ARG-2008 AND ARG-2024, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [22] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-247 AND LYS-879, 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 [23] RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 266-325 IN COMPLEX WITH RP METHYLATED HISTONE H3 PEPTIDE, FUNCTION (ISOFORMS 2 AND 4), SUBUNIT, RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF TRP-291. RX PubMed=23831028; DOI=10.1016/j.celrep.2013.06.014; RA Gatchalian J., Futterer A., Rothbart S.B., Tong Q., Rincon-Arano H., RA Sanchez de Diego A., Groudine M., Strahl B.D., Martinez-A C., RA van Wely K.H., Kutateladze T.G.; RT "Dido3 PHD modulates cell differentiation and division."; RL Cell Rep. 4:148-158(2013). CC -!- FUNCTION: Putative transcription factor, weakly pro-apoptotic when CC overexpressed (By similarity). Tumor suppressor. Required for early CC embryonic stem cell development. {ECO:0000250, CC ECO:0000269|PubMed:16127461}. CC -!- FUNCTION: [Isoform 2]: Displaces isoform 4 at the onset of CC differentiation, required for repression of stemness genes. CC {ECO:0000269|PubMed:16127461}. CC -!- SUBUNIT: Interacts specifically (via PHD-type zinc finger) with histone CC H3 that is trimethylated at 'Lys-4' (H3K4me3), histone phosphorylation CC at 'Thr-3' or 'Thr-6' disrupts this binding and promotes translocation CC of DIDO1 from chromatin to the mitotic spindle during mitosis. CC {ECO:0000269|PubMed:23831028}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus CC {ECO:0000255|PROSITE-ProRule:PRU00651}. Cytoplasm, cytoskeleton, CC spindle {ECO:0000269|PubMed:23831028}. Note=Translocates to the nucleus CC after pro-apoptotic stimuli (By similarity). Translocates to the CC mitotic spindle upon loss of interaction with H3K4me3 during early CC mitosis. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=4; Synonyms=DIDO3; CC IsoId=Q9BTC0-4; Sequence=Displayed; CC Name=1; Synonyms=DIDO2; CC IsoId=Q9BTC0-1; Sequence=VSP_017225, VSP_017226; CC Name=2; Synonyms=DIDO1; CC IsoId=Q9BTC0-2; Sequence=VSP_007209, VSP_007210; CC Name=3; Synonyms=a; CC IsoId=Q9BTC0-3; Sequence=VSP_007211, VSP_007212; CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- DOMAIN: The PHD-type zinc finger forms an aromatic cage around H3K4me3. CC -!- MISCELLANEOUS: Defects in DIDO1 may be a cause of myeloid neoplasms. CC -!- SEQUENCE CAUTION: CC Sequence=BAA20791.2; Type=Erroneous initiation; Evidence={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; AY481571; AAS49898.1; -; mRNA. DR EMBL; AY481572; AAS49899.1; -; mRNA. DR EMBL; AB002331; BAA20791.2; ALT_INIT; mRNA. DR EMBL; AK002127; BAA92094.1; -; mRNA. DR EMBL; AL117379; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL035669; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471077; EAW75322.1; -; Genomic_DNA. DR EMBL; CH471077; EAW75323.1; -; Genomic_DNA. DR EMBL; BC000770; AAH00770.1; -; mRNA. DR EMBL; BC004237; AAH04237.1; -; mRNA. DR EMBL; BC012757; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC014489; AAH14489.1; -; mRNA. DR EMBL; BC137177; AAI37178.1; -; mRNA. DR EMBL; AL133063; CAB61387.1; -; mRNA. DR CCDS; CCDS13508.2; -. [Q9BTC0-1] DR CCDS; CCDS13509.1; -. [Q9BTC0-3] DR CCDS; CCDS33506.1; -. [Q9BTC0-4] DR RefSeq; NP_001180298.1; NM_001193369.1. [Q9BTC0-4] DR RefSeq; NP_001180299.1; NM_001193370.1. [Q9BTC0-1] DR RefSeq; NP_071388.2; NM_022105.4. [Q9BTC0-3] DR RefSeq; NP_149072.2; NM_033081.2. [Q9BTC0-4] DR RefSeq; NP_542986.1; NM_080796.3. [Q9BTC0-3] DR RefSeq; NP_542987.2; NM_080797.3. [Q9BTC0-1] DR RefSeq; XP_011526811.1; XM_011528509.2. DR PDB; 2M3H; NMR; -; A=265-322. DR PDB; 4L7X; X-ray; 1.35 A; A=266-325. DR PDBsum; 2M3H; -. DR PDBsum; 4L7X; -. DR AlphaFoldDB; Q9BTC0; -. DR BMRB; Q9BTC0; -. DR SMR; Q9BTC0; -. DR BioGRID; 116266; 172. DR IntAct; Q9BTC0; 36. DR MINT; Q9BTC0; -. DR STRING; 9606.ENSP00000266070; -. DR CarbonylDB; Q9BTC0; -. DR GlyCosmos; Q9BTC0; 12 sites, 2 glycans. DR GlyGen; Q9BTC0; 26 sites, 2 O-linked glycans (26 sites). DR iPTMnet; Q9BTC0; -. DR MetOSite; Q9BTC0; -. DR PhosphoSitePlus; Q9BTC0; -. DR SwissPalm; Q9BTC0; -. DR BioMuta; DIDO1; -. DR DMDM; 116241332; -. DR EPD; Q9BTC0; -. DR jPOST; Q9BTC0; -. DR MassIVE; Q9BTC0; -. DR MaxQB; Q9BTC0; -. DR PaxDb; 9606-ENSP00000266070; -. DR PeptideAtlas; Q9BTC0; -. DR ProteomicsDB; 78967; -. [Q9BTC0-4] DR ProteomicsDB; 78968; -. [Q9BTC0-1] DR ProteomicsDB; 78969; -. [Q9BTC0-2] DR ProteomicsDB; 78970; -. [Q9BTC0-3] DR Pumba; Q9BTC0; -. DR Antibodypedia; 3820; 311 antibodies from 37 providers. DR DNASU; 11083; -. DR Ensembl; ENST00000266070.8; ENSP00000266070.4; ENSG00000101191.17. [Q9BTC0-4] DR Ensembl; ENST00000354665.8; ENSP00000346692.4; ENSG00000101191.17. [Q9BTC0-3] DR Ensembl; ENST00000370366.1; ENSP00000359391.1; ENSG00000101191.17. [Q9BTC0-2] DR Ensembl; ENST00000370368.5; ENSP00000359394.1; ENSG00000101191.17. [Q9BTC0-3] DR Ensembl; ENST00000370371.8; ENSP00000359397.4; ENSG00000101191.17. [Q9BTC0-3] DR Ensembl; ENST00000395340.5; ENSP00000378749.1; ENSG00000101191.17. [Q9BTC0-1] DR Ensembl; ENST00000395343.6; ENSP00000378752.1; ENSG00000101191.17. [Q9BTC0-4] DR GeneID; 11083; -. DR KEGG; hsa:11083; -. DR MANE-Select; ENST00000395343.6; ENSP00000378752.1; NM_001193369.2; NP_001180298.1. DR UCSC; uc002ydr.3; human. [Q9BTC0-4] DR AGR; HGNC:2680; -. DR CTD; 11083; -. DR DisGeNET; 11083; -. DR GeneCards; DIDO1; -. DR HGNC; HGNC:2680; DIDO1. DR HPA; ENSG00000101191; Low tissue specificity. DR MIM; 604140; gene. DR neXtProt; NX_Q9BTC0; -. DR OpenTargets; ENSG00000101191; -. DR PharmGKB; PA27147; -. DR VEuPathDB; HostDB:ENSG00000101191; -. DR eggNOG; KOG1632; Eukaryota. DR eggNOG; KOG1634; Eukaryota. DR GeneTree; ENSGT00940000155532; -. DR HOGENOM; CLU_000673_1_0_1; -. DR InParanoid; Q9BTC0; -. DR OMA; HPNQFDG; -. DR OrthoDB; 5406765at2759; -. DR PhylomeDB; Q9BTC0; -. DR TreeFam; TF350578; -. DR PathwayCommons; Q9BTC0; -. DR Reactome; R-HSA-1221632; Meiotic synapsis. [Q9BTC0-1] DR SignaLink; Q9BTC0; -. DR SIGNOR; Q9BTC0; -. DR BioGRID-ORCS; 11083; 285 hits in 1165 CRISPR screens. DR ChiTaRS; DIDO1; human. DR GeneWiki; DIDO1; -. DR GenomeRNAi; 11083; -. DR Pharos; Q9BTC0; Tbio. DR PRO; PR:Q9BTC0; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; Q9BTC0; Protein. DR Bgee; ENSG00000101191; Expressed in buccal mucosa cell and 197 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0097190; P:apoptotic signaling pathway; IEA:Ensembl. DR GO; GO:0006351; P:DNA-templated transcription; IBA:GO_Central. DR CDD; cd15639; PHD_DIDO1_like; 1. DR CDD; cd21547; SPOC_DIDO1-like; 1. DR Gene3D; 1.10.472.30; Transcription elongation factor S-II, central domain; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR033082; DIDO1_PHD. DR InterPro; IPR012921; SPOC_C. DR InterPro; IPR003618; TFIIS_cen_dom. DR InterPro; IPR036575; TFIIS_cen_dom_sf. DR InterPro; IPR019786; Zinc_finger_PHD-type_CS. DR InterPro; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR001965; Znf_PHD. DR InterPro; IPR019787; Znf_PHD-finger. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR11477:SF13; DEATH-INDUCER OBLITERATOR 1; 1. DR PANTHER; PTHR11477; TRANSCRIPTION FACTOR S-II ZINC FINGER DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF00628; PHD; 1. DR Pfam; PF07744; SPOC; 1. DR Pfam; PF07500; TFIIS_M; 1. DR SMART; SM00249; PHD; 1. DR SMART; SM00510; TFS2M; 1. DR SUPFAM; SSF46942; Elongation factor TFIIS domain 2; 1. DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1. DR PROSITE; PS51321; TFIIS_CENTRAL; 1. DR PROSITE; PS01359; ZF_PHD_1; 1. DR PROSITE; PS50016; ZF_PHD_2; 1. DR Genevisible; Q9BTC0; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; Cytoplasm; KW Cytoskeleton; Direct protein sequencing; Isopeptide bond; Metal-binding; KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation; KW Zinc; Zinc-finger. FT CHAIN 1..2240 FT /note="Death-inducer obliterator 1" FT /id="PRO_0000059324" FT DOMAIN 670..790 FT /note="TFIIS central" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00651" FT ZN_FING 268..322 FT /note="PHD-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146" FT REGION 1..259 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 431..456 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 501..567 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 584..618 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 773..826 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 860..947 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1013..1045 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1206..1427 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1453..1472 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1517..2240 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 165..173 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT MOTIF 185..193 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 1..44 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 65..91 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 94..134 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 136..200 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 227..259 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 433..449 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 529..543 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 773..798 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 866..894 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1028..1045 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1206..1221 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1256..1272 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1290..1315 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1394..1423 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1532..1557 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1840..1858 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1998..2012 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2067..2229 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330" FT MOD_RES 60 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 114 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8C9B9" FT MOD_RES 151 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 152 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT MOD_RES 154 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT MOD_RES 523 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 805 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 809 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 889 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8C9B9" FT MOD_RES 898 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1019 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1030 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 1040 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1244 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 1256 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q8C9B9" FT MOD_RES 1260 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692" FT MOD_RES 1312 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 1456 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 1469 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1522 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 1714 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1835 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 1893 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 1894 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 1977 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 1982 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 1993 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 2008 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 2024 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT CROSSLNK 247 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 879 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 530..562 FT /note="STKEDRRSEEKAAAMAASKKTAPPGSAVGKQPA -> CMYHLGVGLLDPSRS FT FWIAIPWACPGLGVAALC (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_007211" FT VAR_SEQ 530..544 FT /note="STKEDRRSEEKAAAM -> CSGKYSYSLHPSLIA (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_007209" FT VAR_SEQ 545..2240 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_007210" FT VAR_SEQ 563..2240 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_007212" FT VAR_SEQ 1182..1189 FT /note="LESPRPNI -> KRRLSGWR (in isoform 1)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16127461, ECO:0000303|PubMed:9205841" FT /id="VSP_017225" FT VAR_SEQ 1190..2240 FT /note="Missing (in isoform 1)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16127461, ECO:0000303|PubMed:9205841" FT /id="VSP_017226" FT VARIANT 13 FT /note="P -> L (in dbSNP:rs6090161)" FT /id="VAR_028310" FT VARIANT 276 FT /note="P -> L (in dbSNP:rs6090160)" FT /id="VAR_028311" FT VARIANT 544 FT /note="M -> T (in dbSNP:rs1883848)" FT /evidence="ECO:0000269|PubMed:16127461" FT /id="VAR_057093" FT VARIANT 556 FT /note="A -> T (in dbSNP:rs1883847)" FT /evidence="ECO:0000269|PubMed:16127461" FT /id="VAR_057094" FT VARIANT 793 FT /note="A -> G (in dbSNP:rs750077)" FT /id="VAR_057095" FT VARIANT 1220 FT /note="P -> Q (in dbSNP:rs6011441)" FT /id="VAR_057096" FT VARIANT 1708 FT /note="S -> C (in dbSNP:rs41282984)" FT /id="VAR_061740" FT MUTAGEN 291 FT /note="W->T: Abolishes binding to H3K4me3." FT /evidence="ECO:0000269|PubMed:23831028" FT CONFLICT 252 FT /note="G -> E (in Ref. 4; BAA92094)" FT /evidence="ECO:0000305" FT TURN 271..274 FT /evidence="ECO:0007829|PDB:4L7X" FT STRAND 277..280 FT /evidence="ECO:0007829|PDB:2M3H" FT STRAND 282..284 FT /evidence="ECO:0007829|PDB:4L7X" FT TURN 286..288 FT /evidence="ECO:0007829|PDB:4L7X" FT STRAND 291..293 FT /evidence="ECO:0007829|PDB:4L7X" FT HELIX 294..297 FT /evidence="ECO:0007829|PDB:4L7X" FT HELIX 301..310 FT /evidence="ECO:0007829|PDB:4L7X" FT TURN 317..319 FT /evidence="ECO:0007829|PDB:4L7X" FT CONFLICT Q9BTC0-2:535 FT /note="S -> L (in Ref. 7; AAH00770)" FT /evidence="ECO:0000305" SQ SEQUENCE 2240 AA; 243873 MW; 9B89361A24A72C58 CRC64; MDDKGDPSNE EAPKAIKPTS KEFRKTWGFR RTTIAKREGA GDAEADPLEP PPPQQQLGLS LRRSGRQPKR TERVEQFLTI ARRRGRRSMP VSLEDSGEPT SCPATDAETA SEGSVESASE TRSGPQSAST AVKERPASSE KVKGGDDHDD TSDSDSDGLT LKELQNRLRR KREQEPTERP LKGIQSRLRK KRREEGPAET VGSEASDTVE GVLPSKQEPE NDQGVVSQAG KDDRESKLEG KAAQDIKDEE PGDLGRPKPE CEGYDPNALY CICRQPHNNR FMICCDRCEE WFHGDCVGIS EARGRLLERN GEDYICPNCT ILQVQDETHS ETADQQEAKW RPGDADGTDC TSIGTIEQKS SEDQGIKGRI EKAANPSGKK KLKIFQPVIE APGASKCIGP GCCHVAQPDS VYCSNDCILK HAAATMKFLS SGKEQKPKPK EKMKMKPEKP SLPKCGAQAG IKISSVHKRP APEKKETTVK KAVVVPARSE ALGKEAACES STPSWASDHN YNAVKPEKTA APSPSLLYKS TKEDRRSEEK AAAMAASKKT APPGSAVGKQ PAPRNLVPKK SSFANVAAAT PAIKKPPSGF KGTIPKRPWL SATPSSGASA ARQAGPAPAA ATAASKKFPG SAALVGAVRK PVVPSVPMAS PAPGRLGAMS AAPSQPNSQI RQNIRRSLKE ILWKRVNDSD DLIMTENEVG KIALHIEKEM FNLFQVTDNR YKSKYRSIMF NLKDPKNQGL FHRVLREEIS LAKLVRLKPE ELVSKELSTW KERPARSVME SRTKLHNESK KTAPRQEAIP DLEDSPPVSD SEEQQESARA VPEKSTAPLL DVFSSMLKDT TSQHRAHLFD LNCKICTGQV PSAEDEPAPK KQKLSASVKK EDLKSKHDSS APDPAPDSAD EVMPEAVPEV ASEPGLESAS HPNVDRTYFP GPPGDGHPEP SPLEDLSPCP ASCGSGVVTT VTVSGRDPRT APSSSCTAVA SAASRPDSTH MVEARQDVPK PVLTSVMVPK SILAKPSSSP DPRYLSVPPS PNISTSESRS PPEGDTTLFL SRLSTIWKGF INMQSVAKFV TKAYPVSGCF DYLSEDLPDT IHIGGRIAPK TVWDYVGKLK SSVSKELCLI RFHPATEEEE VAYISLYSYF SSRGRFGVVA NNNRHVKDLY LIPLSAQDPV PSKLLPFEGP GLESPRPNII LGLVICQKIK RPANSGELDK MDEKRTRLQP EEADVPAYPK VATVPQSEKK PSKYPLCSAD AAVSTTPPGS PPPPPPLPEP PVLKVLSSLK PAAPSPATAA TTAAAASTAA SSTASSASKT ASPLEHILQT LFGKKKSFDP SAREPPGSTA GLPQEPKTTA EDGVPAPPLL DPIVQQFGQF SKDKALEEEE DDRPYDPEEE YDPERAFDTQ LVERGRRHEV ERAPEAAAAE REEVAYDPED ETILEEAKVT VDDLPNRMCA DVRRNSVERP AEPVAGAATP SLVEQQKMLE ELNKQIEEQK RQLEEQEEAL RQQRAAVGVS MAHFSVSDAL MSPPPKSSLP KAELFQQEQQ SADKPASLPP ASQASNHRDP RQARRLATET GEGEGEPLSR LSARGAQGAL PERDASRGGL VGQAPMPVPE EKEPASSPWA SGEKPPAGSE QDGWKAEPGE GTRPATVGDS SARPARRVLL PTPPCGALQP GFPLQHDGER DPFTCPGFAS QDKALGSAQY EDPRNLHSAG RSSSPAGETE GDREPQARPG EGTAPLPPPG QKVGGSQPPF QGQREPGPHA LGMSGLHGPN FPGPRGPAPP FPEENIASND GPRGPPPARF GAQKGPIPSL FSGQHGPPPY GDSRGPSPSY LGGPRGVAPS QFEERKDPHG EKREFQDAPY NEVTGAPAQF EGTEQAPFLG SRGGAPFQFG GQRRPLLSQL KGPRGGPPPS QFGGQRGPPP GHFVGPRGPH PSQFETARGP HPNQFEGPRG QAPNFMPGPR GIQPQQFEDQ RVHSPPRFTN QRAPAPLQFG GLRGSAPFSE KNEQTPSRFH FQGQAPQVMK PGPRPLLELP SHPPQHRKDR WEEAGPPSAL SSSAPGQGPE ADGQWASADF REGKGHEYRN QTFEGRQRER FDVGPKEKPL EEPDAQGRAS EDRRRERERG RNWSRERDWD RPREWDRHRD KDSSRDWDRN RERSANRDRE READRGKEWD RSRERSRNRE RERDRRRDRD RSRSRERDRD KARDRERGRD RKDRSKSKES ARDPKPEASR ASDAGTASQA //