ECD_HUMAN
ID ECD_HUMAN Reviewed; 644 AA.
AC O95905; C9JX46; E9PAW8;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Protein ecdysoneless homolog {ECO:0000250|UniProtKB:Q9W032};
DE AltName: Full=Human suppressor of GCR two {ECO:0000303|PubMed:9928932};
DE Short=hSGT1 {ECO:0000303|PubMed:9928932};
GN Name=ECD;
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] (ISOFORM 1), AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=9928932; DOI=10.1007/s004380050926;
RA Sato T., Jigami Y., Suzuki T., Uemura H.;
RT "A human gene, hSGT1, can substitute for GCR2, which encodes a general
RT regulatory factor of glycolytic gene expression in Saccharomyces
RT cerevisiae.";
RL Mol. Gen. Genet. 260:535-540(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
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 MRNA] (ISOFORM 2).
RC TISSUE=Signet-ring cell carcinoma;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [6]
RP FUNCTION, INTERACTION WITH TP53 AND MDM2, AND SUBCELLULAR LOCATION.
RX PubMed=16849563; DOI=10.1158/0008-5472.can-06-0722;
RA Zhang Y., Chen J., Gurumurthy C.B., Kim J., Bhat I., Gao Q., Dimri G.,
RA Lee S.W., Band H., Band V.;
RT "The human orthologue of Drosophila ecdysoneless protein interacts with p53
RT and regulates its function.";
RL Cancer Res. 66:7167-7175(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503; SER-505 AND SER-518, 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 [9]
RP FUNCTION, AND INTERACTION WITH RB1; RBL1 AND RBL2.
RX PubMed=19640839; DOI=10.1074/jbc.m109.030551;
RA Kim J.H., Gurumurthy C.B., Naramura M., Zhang Y., Dudley A.T., Doglio L.,
RA Band H., Band V.;
RT "Role of mammalian Ecdysoneless in cell cycle regulation.";
RL J. Biol. Chem. 284:26402-26410(2009).
RN [10]
RP FUNCTION, INTERACTION WITH EP300, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ILE-481; ASP-484; LEU-489; ASP-510; ASP-512 AND ASP-520.
RX PubMed=19919181; DOI=10.1515/bc.2010.004;
RA Kim J.H., Gurumurthy C.B., Band H., Band V.;
RT "Biochemical characterization of human Ecdysoneless reveals a role in
RT transcriptional regulation.";
RL Biol. Chem. 391:9-19(2010).
RN [11]
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 [12]
RP IDENTIFICATION BY 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 [13]
RP TISSUE SPECIFICITY.
RX PubMed=22270930; DOI=10.1007/s10549-011-1946-8;
RA Zhao X., Mirza S., Alshareeda A., Zhang Y., Gurumurthy C.B., Bele A.,
RA Kim J.H., Mohibi S., Goswami M., Lele S.M., West W., Qiu F., Ellis I.O.,
RA Rakha E.A., Green A.R., Band H., Band V.;
RT "Overexpression of a novel cell cycle regulator ecdysoneless in breast
RT cancer: a marker of poor prognosis in HER2/neu-overexpressing breast cancer
RT patients.";
RL Breast Cancer Res. Treat. 134:171-180(2012).
RN [14]
RP TISSUE SPECIFICITY.
RX PubMed=22977192; DOI=10.1158/1078-0432.ccr-12-1789;
RA Dey P., Rachagani S., Chakraborty S., Singh P.K., Zhao X., Gurumurthy C.B.,
RA Anderson J.M., Lele S., Hollingsworth M.A., Band V., Batra S.K.;
RT "Overexpression of ecdysoneless in pancreatic cancer and its role in
RT oncogenesis by regulating glycolysis.";
RL Clin. Cancer Res. 18:6188-6198(2012).
RN [15]
RP FUNCTION, AND INTERACTION WITH TXNIP.
RX PubMed=23880345; DOI=10.1016/j.bbrc.2013.07.036;
RA Suh H.W., Yun S., Song H., Jung H., Park Y.J., Kim T.D., Yoon S.R.,
RA Choi I.;
RT "TXNIP interacts with hEcd to increase p53 stability and activity.";
RL Biochem. Biophys. Res. Commun. 438:264-269(2013).
RN [16]
RP INTERACTION WITH PIH1D1.
RX PubMed=24656813; DOI=10.1016/j.celrep.2014.03.013;
RA Horejsi Z., Stach L., Flower T.G., Joshi D., Flynn H., Skehel J.M.,
RA O'Reilly N.J., Ogrodowicz R.W., Smerdon S.J., Boulton S.J.;
RT "Phosphorylation-dependent PIH1D1 interactions define substrate specificity
RT of the R2TP cochaperone complex.";
RL Cell Rep. 7:19-26(2014).
RN [17]
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 [18]
RP FUNCTION.
RX PubMed=24722212; DOI=10.1371/journal.pgen.1004287;
RA Claudius A.K., Romani P., Lamkemeyer T., Jindra M., Uhlirova M.;
RT "Unexpected role of the steroid-deficiency protein ecdysoneless in pre-mRNA
RT splicing.";
RL PLoS Genet. 10:E1004287-E1004287(2014).
RN [19]
RP PHOSPHORYLATION, SUBCELLULAR LOCATION, INTERACTION WITH RUVBL1, ASSOCIATION
RP WITH THE R2TP COMPLEX, AND MUTAGENESIS OF SER-503; SER-505; SER-518;
RP SER-572; SER-579 AND SER-584.
RX PubMed=26711270; DOI=10.1128/mcb.00594-15;
RA Mir R.A., Bele A., Mirza S., Srivastava S., Olou A.A., Ammons S.A.,
RA Kim J.H., Gurumurthy C.B., Qiu F., Band H., Band V.;
RT "A novel interaction of ecdysoneless (ECD) protein with R2TP complex
RT component RUVBL1 is required for the functional role of ECD in cell cycle
RT progression.";
RL Mol. Cell. Biol. 36:886-899(2015).
RN [20]
RP VARIANT GLY-281.
RX PubMed=11090341; DOI=10.1086/316954;
RA Bork J.M., Peters L.M., Riazuddin S., Bernstein S.L., Ahmed Z.M.,
RA Ness S.L., Polomeno R., Ramesh A., Schloss M., Srisailpathy C.R.S.,
RA Wayne S., Bellman S., Desmukh D., Ahmed Z., Khan S.N., Kaloustian V.M.D.,
RA Li X.C., Lalwani A., Riazuddin S., Bitner-Glindzicz M., Nance W.E.,
RA Liu X.-Z., Wistow G., Smith R.J.H., Griffith A.J., Wilcox E.R.,
RA Friedman T.B., Morell R.J.;
RT "Usher syndrome 1D and nonsyndromic autosomal recessive deafness DFNB12 are
RT caused by allelic mutations of the novel cadherin-like gene CDH23.";
RL Am. J. Hum. Genet. 68:26-37(2001).
CC -!- FUNCTION: Regulator of p53/TP53 stability and function. Inhibits MDM2-
CC mediated degradation of p53/TP53 possibly by cooperating in part with
CC TXNIP (PubMed:16849563, PubMed:23880345). May be involved
CC transcriptional regulation. In vitro has intrinsic transactivation
CC activity enhanced by EP300. May be a transcriptional activator required
CC for the expression of glycolytic genes (PubMed:19919181,
CC PubMed:9928932). Involved in regulation of cell cycle progression.
CC Proposed to disrupt Rb-E2F binding leading to transcriptional
CC activation of E2F proteins (PubMed:19640839). The cell cycle
CC -regulating function may depend on its RUVBL1-mediated association with
CC the R2TP complex (PubMed:26711270). May play a role in regulation of
CC pre-mRNA splicing (PubMed:24722212). {ECO:0000269|PubMed:16849563,
CC ECO:0000269|PubMed:19640839, ECO:0000269|PubMed:19919181,
CC ECO:0000269|PubMed:23880345, ECO:0000269|PubMed:26711270,
CC ECO:0000305|PubMed:24722212, ECO:0000305|PubMed:9928932}.
CC -!- SUBUNIT: Interacts with TP53, MDM2, TXNIP (PubMed:16849563,
CC PubMed:23880345). Interacts (phosphorylated) with PIH1D1. Interacts
CC with RUVBL1 mediating the PIH1D1-independent association with the R2TP
CC complex (PubMed:24656813, PubMed:26711270). Interacts with RB1, RBL1
CC and RBL2; ECD competes with E2F1 for binding to hypophospshorylated RB1
CC (PubMed:19640839). Interacts with EP300 (PubMed:19919181).
CC {ECO:0000269|PubMed:16849563, ECO:0000269|PubMed:19640839,
CC ECO:0000269|PubMed:19919181, ECO:0000269|PubMed:23880345,
CC ECO:0000269|PubMed:24656813, ECO:0000269|PubMed:26711270}.
CC -!- INTERACTION:
CC O95905; Q9NWS0: PIH1D1; NbExp=11; IntAct=EBI-2557598, EBI-357318;
CC O95905; Q6P2Q9: PRPF8; NbExp=3; IntAct=EBI-2557598, EBI-538479;
CC O95905; Q9Y265: RUVBL1; NbExp=7; IntAct=EBI-2557598, EBI-353675;
CC O95905; Q9H3M7: TXNIP; NbExp=5; IntAct=EBI-2557598, EBI-1369170;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16849563,
CC ECO:0000269|PubMed:19919181, ECO:0000269|PubMed:26711270}. Nucleus
CC {ECO:0000269|PubMed:16849563, ECO:0000269|PubMed:19919181,
CC ECO:0000269|PubMed:26711270}. Note=Predominantly is located in the
CC cytoplasm. {ECO:0000269|PubMed:16849563, ECO:0000269|PubMed:19919181,
CC ECO:0000269|PubMed:26711270}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O95905-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95905-2; Sequence=VSP_045670;
CC Name=3;
CC IsoId=O95905-3; Sequence=VSP_045671;
CC -!- TISSUE SPECIFICITY: Highly expressed in muscle and heart. Over-
CC expressed in pancreatic and breast cancers.
CC {ECO:0000269|PubMed:22270930, ECO:0000269|PubMed:22977192}.
CC -!- PTM: Phosphorylated predominantly by CK2 on two serine-containing
CC clusters; involved in cell cycle regulation activity.
CC {ECO:0000269|PubMed:26711270}.
CC -!- SIMILARITY: Belongs to the ECD family. {ECO:0000305}.
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DR EMBL; D88208; BAA75199.1; -; mRNA.
DR EMBL; AK315711; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK225519; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC016394; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000721; AAH00721.1; -; mRNA.
DR CCDS; CCDS44433.1; -. [O95905-2]
DR CCDS; CCDS44434.1; -. [O95905-3]
DR CCDS; CCDS7321.1; -. [O95905-1]
DR RefSeq; NP_001129224.1; NM_001135752.1. [O95905-3]
DR RefSeq; NP_001129225.1; NM_001135753.1. [O95905-2]
DR RefSeq; NP_009196.1; NM_007265.2. [O95905-1]
DR AlphaFoldDB; O95905; -.
DR BioGRID; 116450; 110.
DR IntAct; O95905; 60.
DR MINT; O95905; -.
DR STRING; 9606.ENSP00000401566; -.
DR GlyGen; O95905; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O95905; -.
DR PhosphoSitePlus; O95905; -.
DR BioMuta; ECD; -.
DR EPD; O95905; -.
DR jPOST; O95905; -.
DR MassIVE; O95905; -.
DR MaxQB; O95905; -.
DR PaxDb; O95905; -.
DR PeptideAtlas; O95905; -.
DR PRIDE; O95905; -.
DR ProteomicsDB; 12074; -.
DR ProteomicsDB; 19095; -.
DR ProteomicsDB; 51121; -. [O95905-1]
DR Antibodypedia; 29316; 175 antibodies from 25 providers.
DR DNASU; 11319; -.
DR Ensembl; ENST00000372979.9; ENSP00000362070.4; ENSG00000122882.11. [O95905-1]
DR Ensembl; ENST00000430082.6; ENSP00000401566.1; ENSG00000122882.11. [O95905-3]
DR Ensembl; ENST00000454759.6; ENSP00000395786.1; ENSG00000122882.11. [O95905-2]
DR GeneID; 11319; -.
DR KEGG; hsa:11319; -.
DR MANE-Select; ENST00000372979.9; ENSP00000362070.4; NM_007265.3; NP_009196.1.
DR UCSC; uc001jtn.4; human. [O95905-1]
DR CTD; 11319; -.
DR DisGeNET; 11319; -.
DR GeneCards; ECD; -.
DR HGNC; HGNC:17029; ECD.
DR HPA; ENSG00000122882; Low tissue specificity.
DR MIM; 616464; gene.
DR neXtProt; NX_O95905; -.
DR OpenTargets; ENSG00000122882; -.
DR PharmGKB; PA143485450; -.
DR VEuPathDB; HostDB:ENSG00000122882; -.
DR eggNOG; KOG2406; Eukaryota.
DR GeneTree; ENSGT00390000015361; -.
DR HOGENOM; CLU_006241_2_0_1; -.
DR InParanoid; O95905; -.
DR OMA; TKDYIWQ; -.
DR OrthoDB; 603336at2759; -.
DR PhylomeDB; O95905; -.
DR TreeFam; TF324229; -.
DR PathwayCommons; O95905; -.
DR SignaLink; O95905; -.
DR BioGRID-ORCS; 11319; 779 hits in 1087 CRISPR screens.
DR ChiTaRS; ECD; human.
DR GeneWiki; ECD_(gene); -.
DR GenomeRNAi; 11319; -.
DR Pharos; O95905; Tbio.
DR PRO; PR:O95905; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; O95905; protein.
DR Bgee; ENSG00000122882; Expressed in sural nerve and 188 other tissues.
DR ExpressionAtlas; O95905; baseline and differential.
DR Genevisible; O95905; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0035035; F:histone acetyltransferase binding; IDA:UniProtKB.
DR GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR010770; Ecd.
DR PANTHER; PTHR13060; PTHR13060; 1.
DR Pfam; PF07093; SGT1; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Cytoplasm; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..644
FT /note="Protein ecdysoneless homolog"
FT /id="PRO_0000220844"
FT REGION 430..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..644
FT /note="Transcription activation"
FT /evidence="ECO:0000269|PubMed:19919181"
FT REGION 481..497
FT /note="Involved in nuclear export"
FT /evidence="ECO:0000269|PubMed:19919181"
FT REGION 496..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..532
FT /note="Acidic region required for transactivation activity"
FT /evidence="ECO:0000269|PubMed:19919181"
FT REGION 567..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..527
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648"
FT VAR_SEQ 262..304
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_045670"
FT VAR_SEQ 375
FT /note="E -> ERLEVQWRDPGLLQAPPPGFTPFICLSLLSTWDN (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045671"
FT VARIANT 45
FT /note="R -> Q (in dbSNP:rs3812619)"
FT /id="VAR_051970"
FT VARIANT 281
FT /note="R -> G (in dbSNP:rs151023501)"
FT /evidence="ECO:0000269|PubMed:11090341"
FT /id="VAR_012191"
FT VARIANT 452
FT /note="E -> Q (in dbSNP:rs3736518)"
FT /id="VAR_051971"
FT VARIANT 501
FT /note="N -> S (in dbSNP:rs36152134)"
FT /id="VAR_051972"
FT VARIANT 634
FT /note="D -> G (in dbSNP:rs2271904)"
FT /id="VAR_051973"
FT MUTAGEN 481
FT /note="I->A: Decreases transactivation activity."
FT /evidence="ECO:0000269|PubMed:19919181"
FT MUTAGEN 484
FT /note="D->F: Decreases transactivation activity."
FT /evidence="ECO:0000269|PubMed:19919181"
FT MUTAGEN 489
FT /note="L->A: Decreases transactivation activity."
FT /evidence="ECO:0000269|PubMed:19919181"
FT MUTAGEN 503
FT /note="S->A: Greatly impairs in vitro phosphorylation by
FT CK2 and impairs cell cycle regulation activity; when
FT associated with A-505, A-518, A-572, A-579 and A-584."
FT /evidence="ECO:0000269|PubMed:26711270"
FT MUTAGEN 505
FT /note="S->A: Greatly impairs in vitro phosphorylation by
FT CK2 and impairs cell cycle regulation activity; when
FT associated with A-503, A-518, A-572, A-579 and A-584."
FT /evidence="ECO:0000269|PubMed:26711270"
FT MUTAGEN 510
FT /note="D->R: Increases transactivation activity."
FT /evidence="ECO:0000269|PubMed:19919181"
FT MUTAGEN 512
FT /note="D->R: Increases transactivation activity."
FT /evidence="ECO:0000269|PubMed:19919181"
FT MUTAGEN 518
FT /note="S->A: Greatly impairs in vitro phosphorylation by
FT CK2 and impairs cell cycle regulation activity; when
FT associated with A-503, A-505, A-572, A-579 and A-584."
FT /evidence="ECO:0000269|PubMed:26711270"
FT MUTAGEN 520
FT /note="D->P: Increases transactivation activity."
FT /evidence="ECO:0000269|PubMed:19919181"
FT MUTAGEN 572
FT /note="S->A: Greatly impairs in vitro phosphorylation by
FT CK2 and impairs cell cycle regulation activity; when
FT associated with A-503, A-505, A-518, A-579 and A-584."
FT /evidence="ECO:0000269|PubMed:26711270"
FT MUTAGEN 579
FT /note="S->A: Greatly impairs in vitro phosphorylation by
FT CK2 and impairs cell cycle regulation activity; when
FT associated with A-503, A-505, A-518, A-572 and A-584."
FT /evidence="ECO:0000269|PubMed:26711270"
FT MUTAGEN 584
FT /note="S->A: Greatly impairs in vitro phosphorylation by
FT CK2 and impairs cell cycle regulation activity; when
FT associated with A-503, A-505, A-518, A-572 and A-579."
FT /evidence="ECO:0000269|PubMed:26711270"
FT CONFLICT 28
FT /note="S -> P (in Ref. 2; AK225519)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="F -> S (in Ref. 2; AK225519)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="W -> R (in Ref. 2; AK225519)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 644 AA; 72758 MW; F9B0D2BBFDB38CAF CRC64;
MEETMKLATM EDTVEYCLFL IPDESRDSDK HKEILQKYIE RIITRFAPML VPYIWQNQPF
NLKYKPGKGG VPAHMFGVTK FGDNIEDEWF IVYVIKQITK EFPELVARIE DNDGEFLLIE
AADFLPKWLD PENSTNRVFF CHGELCIIPA PRKSGAESWL PTTPPTIPQA LNIITAHSEK
ILASESIRAA VNRRIRGYPE KIQASLHRAH CFLPAGIVAV LKQRPRLVAA AVQAFYLRDP
IDLRACRVFK TFLPETRIMT SVTFTKCLYA QLVQQRFVPD RRSGYRLPPP SDPQYRAHEL
GMKLAHGFEI LCSKCSPHFS DCKKSLVTAS PLWASFLESL KKNDYFKGLI EGSAQYRERL
EMAENYFQLS VDWPESSLAM SPGEEILTLL QTIPFDIEDL KKEAANLPPE DDDQWLDLSP
DQLDQLLQEA VGKKESESVS KEEKEQNYDL TEVSESMKAF ISKVSTHKGA ELPREPSEAP
ITFDADSFLN YFDKILGPRP NESDSDDLDD EDFECLDSDD DLDFETHEPG EEASLKGTLD
NLKSYMAQMD QELAHTCISK SFTTRNQVEP VSQTTDNNSD EEDSGTGESV MAPVDVDLNL
VSNILESYSS QAGLAGPASN LLQSMGVQLP DNTDHRPTSK PTKN
