DIDO1_HUMAN
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 03-AUG-2022, entry version 197.
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};
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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. [Q9BTC0-4]
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; 132.
DR IntAct; Q9BTC0; 33.
DR MINT; Q9BTC0; -.
DR STRING; 9606.ENSP00000266070; -.
DR CarbonylDB; Q9BTC0; -.
DR GlyGen; Q9BTC0; 12 sites, 2 O-linked glycans (12 sites).
DR iPTMnet; Q9BTC0; -.
DR MetOSite; Q9BTC0; -.
DR PhosphoSitePlus; Q9BTC0; -.
DR BioMuta; DIDO1; -.
DR DMDM; 116241332; -.
DR EPD; Q9BTC0; -.
DR jPOST; Q9BTC0; -.
DR MassIVE; Q9BTC0; -.
DR MaxQB; Q9BTC0; -.
DR PaxDb; Q9BTC0; -.
DR PeptideAtlas; Q9BTC0; -.
DR PRIDE; Q9BTC0; -.
DR ProteomicsDB; 78967; -. [Q9BTC0-4]
DR ProteomicsDB; 78968; -. [Q9BTC0-1]
DR ProteomicsDB; 78969; -. [Q9BTC0-2]
DR ProteomicsDB; 78970; -. [Q9BTC0-3]
DR Antibodypedia; 3820; 270 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 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; FPANRGP; -.
DR OrthoDB; 174961at2759; -.
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; 260 hits in 1086 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 195 other tissues.
DR Genevisible; Q9BTC0; HS.
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:transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 1.10.472.30; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR033082; DIDO1.
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; PTHR11477:SF13; 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; SSF46942; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51321; TFIIS_CENTRAL; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
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
