ECD_MOUSE
ID ECD_MOUSE Reviewed; 641 AA.
AC Q9CS74;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Protein ecdysoneless homolog {ECO:0000250|UniProtKB:Q9W032};
GN Name=Ecd;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION.
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).
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. May be involved transcriptional regulation. In vitro has
CC intrinsic transactivation activity enhanced by EP300. May be a
CC transcriptional activator required for the expression of glycolytic
CC genes (By similarity). Involved in regulation of cell cycle progression
CC (PubMed:26711270). Proposed to disrupt Rb-E2F binding leading to
CC transcriptional activation of E2F proteins (PubMed:19640839). The cell
CC cycle -regulating function may depend on its RUVBL1-mediated
CC association with the R2TP complex. May play a role in regulation of
CC pre-mRNA splicing (By similarity). {ECO:0000250|UniProtKB:O95905}.
CC -!- SUBUNIT: Interacts with TP53, MDM2, TXNIP. Interacts (phosphorylated)
CC with PIH1D1. Interacts with RUVBL1 mediating the PIH1D1-independent
CC association with the R2TP complex. Interacts with RB1, RBL1 and RBL2;
CC ECD competes with E2F1 for binding to hypophospshorylated RB1.
CC Interacts with EP300. {ECO:0000250|UniProtKB:O95905}.
CC -!- INTERACTION:
CC Q9CS74; Q9R000: Itgb1bp2; NbExp=2; IntAct=EBI-7922565, EBI-7922331;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus
CC {ECO:0000250|UniProtKB:O95905}.
CC -!- PTM: Phosphorylated predominantly by CK2 on two serine-containing
CC clusters; involved in cell cycle regulation activity.
CC {ECO:0000250|UniProtKB:O95905}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal. {ECO:0000269|PubMed:19640839}.
CC -!- SIMILARITY: Belongs to the ECD family. {ECO:0000305}.
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DR EMBL; AK028664; BAC26054.1; -; mRNA.
DR EMBL; BC013470; AAH13470.1; -; mRNA.
DR CCDS; CCDS26842.1; -.
DR RefSeq; NP_081751.1; NM_027475.3.
DR AlphaFoldDB; Q9CS74; -.
DR SMR; Q9CS74; -.
DR BioGRID; 214157; 10.
DR IntAct; Q9CS74; 13.
DR MINT; Q9CS74; -.
DR STRING; 10090.ENSMUSP00000022344; -.
DR iPTMnet; Q9CS74; -.
DR PhosphoSitePlus; Q9CS74; -.
DR EPD; Q9CS74; -.
DR MaxQB; Q9CS74; -.
DR PaxDb; Q9CS74; -.
DR PeptideAtlas; Q9CS74; -.
DR PRIDE; Q9CS74; -.
DR ProteomicsDB; 277668; -.
DR Antibodypedia; 29316; 175 antibodies from 25 providers.
DR DNASU; 70601; -.
DR Ensembl; ENSMUST00000022344; ENSMUSP00000022344; ENSMUSG00000021810.
DR GeneID; 70601; -.
DR KEGG; mmu:70601; -.
DR UCSC; uc011zgo.1; mouse.
DR CTD; 11319; -.
DR MGI; MGI:1917851; Ecd.
DR VEuPathDB; HostDB:ENSMUSG00000021810; -.
DR eggNOG; KOG2406; Eukaryota.
DR GeneTree; ENSGT00390000015361; -.
DR HOGENOM; CLU_006241_2_0_1; -.
DR InParanoid; Q9CS74; -.
DR OMA; TKDYIWQ; -.
DR OrthoDB; 603336at2759; -.
DR PhylomeDB; Q9CS74; -.
DR TreeFam; TF324229; -.
DR BioGRID-ORCS; 70601; 21 hits in 72 CRISPR screens.
DR ChiTaRS; Ecd; mouse.
DR PRO; PR:Q9CS74; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9CS74; protein.
DR Bgee; ENSMUSG00000021810; Expressed in internal carotid artery and 251 other tissues.
DR ExpressionAtlas; Q9CS74; baseline and differential.
DR Genevisible; Q9CS74; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0035035; F:histone acetyltransferase binding; ISO:MGI.
DR GO; GO:0048144; P:fibroblast proliferation; IMP:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IMP:MGI.
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; Cytoplasm; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..641
FT /note="Protein ecdysoneless homolog"
FT /id="PRO_0000220845"
FT REGION 439..641
FT /note="Transcription activation"
FT /evidence="ECO:0000250|UniProtKB:O95905"
FT REGION 481..497
FT /note="Involved in nuclear export"
FT /evidence="ECO:0000250|UniProtKB:O95905"
FT REGION 499..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..531
FT /note="Acidic region required for transactivation activity"
FT /evidence="ECO:0000250|UniProtKB:O95905"
FT REGION 554..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..521
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95905"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95905"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95905"
SQ SEQUENCE 641 AA; 71710 MW; 679C6E2EE6404357 CRC64;
MEGSGKLAMV EDAVEYHLFL IPDKARGTEE HREILQKYIE RIMTQFAPIL VPYIWQNQPF
NLKYKPAKGG VPAHMYGMTK FGDNIEDEWF IVYVIKQITK EFPELVARVE DNDGEFLLIE
AADFLPKWLD PDNSANRVFF HHGELCIIPV PRKSERIPWL PMTPPTIQQA LSIISAHPEA
VLASESIQAA VDRRVSGYPE RVEASLHRAH CFLPAGIVAV LKQQPRLLSA AVQAFYLRDP
IDLRACRVFK TFLPETRIMA SVTFTKCLYA QLVQQKFVPD RRSGYGLPPP SHPQYRAYEL
GMKLAHGFEI LCSKCSPHFS DSRKSLVTAS PLWASFLESL KRNDYFKGLM DGSAQYQERL
EMAKNYFQLS IHRPESSLAM SPGEEILTVL QTQPFDVAEL KTEEADLPPE DDDQWLDLSP
DQLDQLLQDA AGRKESQPGP QKEELQNYDV AQVSDSMKAF ISKVSSHKGA ELPRDPSEAP
ITFDADSFLN YFDKILGAKP QESDSEDDPG EEDVEGVDSD DDVGFEAQES ESLKGALGSL
KSYMARMDQE LAHTSMGRSF TTRERLNKDP PSHTANDNSD EEDSGAGDCA VEAVDVDLNL
ISNILESYSS QAGLAGPASN LLHSMGVRLP DNADHNPQVS Q
