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Protein

Ecdysone receptor

Gene

EcR

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Receptor for ecdysone. Binds to ecdysone response elements (ECRES) following ecdysone-binding, and recruitment of a complex containing the histone methyltransferase trr, leads to activate transcription of target genes.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi264 – 33673Nuclear receptorPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri264 – 28421NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri300 – 32425NR C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • core promoter binding Source: FlyBase
  • DNA binding Source: FlyBase
  • ecdysone binding Source: FlyBase
  • ecdysteroid hormone receptor activity Source: FlyBase
  • protein heterodimerization activity Source: FlyBase
  • repressing transcription factor binding Source: FlyBase
  • RNA polymerase II transcription coactivator binding Source: FlyBase
  • RNA polymerase II transcription factor activity, ligand-activated sequence-specific DNA binding Source: FlyBase
  • steroid binding Source: FlyBase
  • transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: FlyBase
  • transcription regulatory region sequence-specific DNA binding Source: FlyBase
  • zinc ion binding Source: InterPro

GO - Biological processi

  • autophagy Source: FlyBase
  • border follicle cell migration Source: FlyBase
  • cardiac muscle tissue development Source: FlyBase
  • cardioblast differentiation Source: FlyBase
  • cell adhesion Source: FlyBase
  • chitin-based embryonic cuticle biosynthetic process Source: FlyBase
  • dendrite morphogenesis Source: FlyBase
  • determination of adult lifespan Source: FlyBase
  • dorsal vessel heart proper cell fate commitment Source: FlyBase
  • ecdysis, chitin-based cuticle Source: FlyBase
  • ecdysone-mediated induction of salivary gland cell autophagic cell death Source: FlyBase
  • ecdysone receptor-mediated signaling pathway Source: FlyBase
  • epidermis development Source: FlyBase
  • germ-band shortening Source: FlyBase
  • germ cell development Source: FlyBase
  • hatching Source: FlyBase
  • head involution Source: FlyBase
  • histoblast morphogenesis Source: FlyBase
  • imaginal disc-derived wing morphogenesis Source: FlyBase
  • imaginal disc eversion Source: FlyBase
  • larval central nervous system remodeling Source: FlyBase
  • larval wandering behavior Source: FlyBase
  • long-term memory Source: FlyBase
  • Malpighian tubule morphogenesis Source: FlyBase
  • metamorphosis Source: FlyBase
  • muscle organ development Source: FlyBase
  • mushroom body development Source: FlyBase
  • negative regulation of growth of symbiont in host Source: FlyBase
  • negative regulation of neuroblast proliferation Source: FlyBase
  • negative regulation of transcription, DNA-templated Source: FlyBase
  • neuron development Source: FlyBase
  • neuron remodeling Source: FlyBase
  • oogenesis Source: FlyBase
  • peripheral nervous system development Source: FlyBase
  • phagocytosis, engulfment Source: FlyBase
  • positive regulation of apoptotic process Source: FlyBase
  • positive regulation of circadian sleep/wake cycle, sleep Source: FlyBase
  • positive regulation of transcription, DNA-templated Source: FlyBase
  • positive regulation of transcription from RNA polymerase II promoter Source: FlyBase
  • pupariation Source: FlyBase
  • regulation of autophagy Source: FlyBase
  • regulation of cellular respiration Source: FlyBase
  • regulation of development, heterochronic Source: FlyBase
  • regulation of glucose metabolic process Source: FlyBase
  • regulation of hemocyte proliferation Source: FlyBase
  • regulation of Malpighian tubule diameter Source: FlyBase
  • regulation of neuron remodeling Source: FlyBase
  • regulation of rhodopsin gene expression Source: FlyBase
  • regulation of transcription from RNA polymerase II promoter Source: FlyBase
  • response to cocaine Source: FlyBase
  • response to ecdysone Source: FlyBase
  • salivary gland cell autophagic cell death Source: FlyBase
  • spermatid development Source: FlyBase
  • sperm individualization Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-DME-159418. Recycling of bile acids and salts.
R-DME-383280. Nuclear Receptor transcription pathway.
SignaLinkiP34021.

Names & Taxonomyi

Protein namesi
Recommended name:
Ecdysone receptor
Alternative name(s):
20-hydroxy-ecdysone receptor
Short name:
20E receptor
EcRH
Ecdysteroid receptor
Nuclear receptor subfamily 1 group H member 1
Gene namesi
Name:EcR
Synonyms:NR1H1
ORF Names:CG1765
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0000546. EcR.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation1 Publication

GO - Cellular componenti

  • activator ecdysone receptor complex Source: FlyBase
  • cytoplasm Source: FlyBase
  • dendrite Source: FlyBase
  • ecdysone receptor holocomplex Source: FlyBase
  • nucleus Source: FlyBase
  • polytene chromosome Source: UniProtKB
  • repressor ecdysone receptor complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2366581.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 878878Ecdysone receptorPRO_0000053524Add
BLAST

Proteomic databases

PaxDbiP34021.
PRIDEiP34021.

Expressioni

Tissue specificityi

Isoform B1 predominates over isoform A in larval tissues, imaginal histoblast nests and midgut islands. Isoform A predominates over B1 in imaginal disks, and the larval prothoracic gland.1 Publication

Developmental stagei

In the salivary glands of mid instar larvae levels increase during puff stage 1 at 86-94 hours of development then remain relatively constant until the premetamorphic pulse of ecdysone in late larvae. Levels diminish dramatically from puff stage 7 onwards. Levels increase in the prepupal period during puff stage 13-14, the level remains stable until stage 21. A decrease in levels at puff stage 7 is also seen in the Malpighian tubules and less dramatically in the fat body and gut. In the wing disk the relatively low level remains unchanged.2 Publications

Gene expression databases

BgeeiP34021.
ExpressionAtlasiP34021. differential.
GenevisibleiP34021. DM.

Interactioni

Subunit structurei

Heterodimer of USP and ECR. Only the heterodimer is capable of high-affinity binding to ecdysone. Interacts with trr in an ecdysone-dependent manner.2 Publications

GO - Molecular functioni

  • protein heterodimerization activity Source: FlyBase
  • repressing transcription factor binding Source: FlyBase
  • RNA polymerase II transcription coactivator binding Source: FlyBase

Protein-protein interaction databases

BioGridi61444. 39 interactions.
DIPiDIP-158N.
IntActiP34021. 34 interactions.
MINTiMINT-294442.
STRINGi7227.FBpp0291631.

Chemistry

BindingDBiP34021.

Structurei

Secondary structure

1
878
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni265 – 2673Combined sources
Beta strandi268 – 2703Combined sources
Beta strandi273 – 2753Combined sources
Beta strandi278 – 2803Combined sources
Helixi282 – 29312Combined sources
Helixi312 – 3143Combined sources
Helixi317 – 32610Combined sources
Helixi331 – 3333Combined sources
Helixi339 – 3435Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1R0NX-ray2.60B256-364[»]
1R0OX-ray2.24B256-364[»]
2HANX-ray1.95B256-365[»]
ProteinModelPortaliP34021.
SMRiP34021. Positions 258-679.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP34021.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 263263ModulatingAdd
BLAST
Regioni431 – 651221Hormone-bindingAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi165 – 21147Gly-richAdd
BLAST
Compositional biasi193 – 1975Poly-Gly
Compositional biasi700 – 7056Poly-Ala
Compositional biasi706 – 78176Gln/Pro-richAdd
BLAST

Sequence similaritiesi

Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri264 – 28421NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri300 – 32425NR C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
GeneTreeiENSGT00840000129681.
HOGENOMiHOG000244965.
InParanoidiP34021.
KOiK14034.
OMAiNGGFNGM.
OrthoDBiEOG7DC25S.

Family and domain databases

Gene3Di1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProiIPR003069. Ecdystd_rcpt.
IPR000536. Nucl_hrmn_rcpt_lig-bd.
IPR001723. Nuclear_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamiPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR01283. ECDYSTEROIDR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 1 hit.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform ECR-B1 (identifier: P34021-1) [UniParc]FASTAAdd to basket

Also known as: B

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKRRWSNNGG FMRLPEESSS EVTSSSNGLV LPSGVNMSPS SLDSHDYCDQ
60 70 80 90 100
DLWLCGNESG SFGGSNGHGL SQQQQSVITL AMHGCSSTLP AQTTIIPING
110 120 130 140 150
NANGNGGSTN GQYVPGATNL GALANGMLNG GFNGMQQQIQ NGHGLINSTT
160 170 180 190 200
PSTPTTPLHL QQNLGGAGGG GIGGMGILHH ANGTPNGLIG VVGGGGGVGL
210 220 230 240 250
GVGGGGVGGL GMQHTPRSDS VNSISSGRDD LSPSSSLNGY SANESCDAKK
260 270 280 290 300
SKKGPAPRVQ EELCLVCGDR ASGYHYNALT CEGCKGFFRR SVTKSAVYCC
310 320 330 340 350
KFGRACEMDM YMRRKCQECR LKKCLAVGMR PECVVPENQC AMKRREKKAQ
360 370 380 390 400
KEKDKMTTSP SSQHGGNGSL ASGGGQDFVK KEILDLMTCE PPQHATIPLL
410 420 430 440 450
PDEILAKCQA RNIPSLTYNQ LAVIYKLIWY QDGYEQPSEE DLRRIMSQPD
460 470 480 490 500
ENESQTDVSF RHITEITILT VQLIVEFAKG LPAFTKIPQE DQITLLKACS
510 520 530 540 550
SEVMMLRMAR RYDHSSDSIF FANNRSYTRD SYKMAGMADN IEDLLHFCRQ
560 570 580 590 600
MFSMKVDNVE YALLTAIVIF SDRPGLEKAQ LVEAIQSYYI DTLRIYILNR
610 620 630 640 650
HCGDSMSLVF YAKLLSILTE LRTLGNQNAE MCFSLKLKNR KLPKFLEEIW
660 670 680 690 700
DVHAIPPSVQ SHLQITQEEN ERLERAERMR ASVGGAITAG IDCDSASTSA
710 720 730 740 750
AAAAAQHQPQ PQPQPQPSSL TQNDSQHQTQ PQLQPQLPPQ LQGQLQPQLQ
760 770 780 790 800
PQLQTQLQPQ IQPQPQLLPV SAPVPASVTA PGSLSAVSTS SEYMGGSAAI
810 820 830 840 850
GPITPATTSS ITAAVTASST TSAVPMGNGV GVGVGVGGNV SMYANAQTAM
860 870
ALMGVALHSH QEQLIGGVAV KSEHSTTA
Length:878
Mass (Da):93,853
Last modified:February 1, 1994 - v1
Checksum:iB48D610D722F014F
GO
Isoform ECR-A (identifier: P34021-2) [UniParc]FASTAAdd to basket

Also known as: A, D

The sequence of this isoform differs from the canonical sequence as follows:
     1-226: MKRRWSNNGG...RSDSVNSISS → MLTTSGQQQS...YDPYSPTGKT

Show »
Length:849
Mass (Da):91,182
Checksum:iE93D93A38236AD58
GO
Isoform ECR-B2 (identifier: P34021-3) [UniParc]FASTAAdd to basket

Also known as: C

The sequence of this isoform differs from the canonical sequence as follows:
     1-226: MKRRWSNNGG...RSDSVNSISS → MDTCGLVAELAHYIDAY

Show »
Length:669
Mass (Da):73,348
Checksum:iA9DE3D365161A34E
GO

Sequence cautioni

The sequence AAL13804.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti867 – 87812GVAVK…HSTTA → EWRLSRSTRRLHSRRRVSST NITTTTSTSCWSRKRS in AAL68274 (PubMed:12537569).CuratedAdd
BLAST

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 226226MKRRW…NSISS → MLTTSGQQQSKQKLSTLPSH ILLQQQLAASAGPSSSVSLS PSSSAALTLHVASANGGARE TTSAAAVKDKLRPTPTAIKI EPMPDVISVGTVAGGSSVAT VVAPAATTTSNKPNSTAAPS TSAAAANGHLVLVPNKRPRL DVTEDWMSTPSPGSVPSSAP PLSPSPGSQNHSYNMSNGYA SPMSAGSYDPYSPTGKT in isoform ECR-A. 1 PublicationVSP_003661Add
BLAST
Alternative sequencei1 – 226226MKRRW…NSISS → MDTCGLVAELAHYIDAY in isoform ECR-B2. CuratedVSP_003662Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74078 mRNA. Translation: AAA28498.1.
S63761 mRNA. Translation: AAB27496.2.
AE013599 Genomic DNA. Translation: AAF57278.3.
AE013599 Genomic DNA. Translation: AAF57280.2.
AE013599 Genomic DNA. Translation: AAM68347.1.
AY075461 mRNA. Translation: AAL68274.1.
AY058575 mRNA. Translation: AAL13804.1. Different initiation.
BT012469 mRNA. Translation: AAS93740.1.
BT015234 mRNA. Translation: AAT94463.1.
PIRiA40709.
A41055.
RefSeqiNP_001163061.1. NM_001169590.2. [P34021-1]
NP_724456.1. NM_165461.3. [P34021-2]
NP_724457.1. NM_165462.2. [P34021-2]
NP_724458.1. NM_165463.2. [P34021-2]
NP_724459.1. NM_165464.3. [P34021-3]
NP_724460.1. NM_165465.3. [P34021-1]
UniGeneiDm.4159.

Genome annotation databases

EnsemblMetazoaiFBtr0086011; FBpp0085352; FBgn0000546. [P34021-1]
FBtr0302439; FBpp0291631; FBgn0000546. [P34021-1]
GeneIDi35540.
KEGGidme:Dmel_CG1765.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74078 mRNA. Translation: AAA28498.1.
S63761 mRNA. Translation: AAB27496.2.
AE013599 Genomic DNA. Translation: AAF57278.3.
AE013599 Genomic DNA. Translation: AAF57280.2.
AE013599 Genomic DNA. Translation: AAM68347.1.
AY075461 mRNA. Translation: AAL68274.1.
AY058575 mRNA. Translation: AAL13804.1. Different initiation.
BT012469 mRNA. Translation: AAS93740.1.
BT015234 mRNA. Translation: AAT94463.1.
PIRiA40709.
A41055.
RefSeqiNP_001163061.1. NM_001169590.2. [P34021-1]
NP_724456.1. NM_165461.3. [P34021-2]
NP_724457.1. NM_165462.2. [P34021-2]
NP_724458.1. NM_165463.2. [P34021-2]
NP_724459.1. NM_165464.3. [P34021-3]
NP_724460.1. NM_165465.3. [P34021-1]
UniGeneiDm.4159.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1R0NX-ray2.60B256-364[»]
1R0OX-ray2.24B256-364[»]
2HANX-ray1.95B256-365[»]
ProteinModelPortaliP34021.
SMRiP34021. Positions 258-679.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61444. 39 interactions.
DIPiDIP-158N.
IntActiP34021. 34 interactions.
MINTiMINT-294442.
STRINGi7227.FBpp0291631.

Chemistry

BindingDBiP34021.
ChEMBLiCHEMBL2366581.

Proteomic databases

PaxDbiP34021.
PRIDEiP34021.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0086011; FBpp0085352; FBgn0000546. [P34021-1]
FBtr0302439; FBpp0291631; FBgn0000546. [P34021-1]
GeneIDi35540.
KEGGidme:Dmel_CG1765.

Organism-specific databases

CTDi35540.
FlyBaseiFBgn0000546. EcR.

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
GeneTreeiENSGT00840000129681.
HOGENOMiHOG000244965.
InParanoidiP34021.
KOiK14034.
OMAiNGGFNGM.
OrthoDBiEOG7DC25S.

Enzyme and pathway databases

ReactomeiR-DME-159418. Recycling of bile acids and salts.
R-DME-383280. Nuclear Receptor transcription pathway.
SignaLinkiP34021.

Miscellaneous databases

ChiTaRSiEcR. fly.
EvolutionaryTraceiP34021.
GenomeRNAii35540.
PROiP34021.

Gene expression databases

BgeeiP34021.
ExpressionAtlasiP34021. differential.
GenevisibleiP34021. DM.

Family and domain databases

Gene3Di1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProiIPR003069. Ecdystd_rcpt.
IPR000536. Nucl_hrmn_rcpt_lig-bd.
IPR001723. Nuclear_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamiPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR01283. ECDYSTEROIDR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 1 hit.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Drosophila EcR gene encodes an ecdysone receptor, a new member of the steroid receptor superfamily."
    Koelle M.R., Talbot W.S., Segraves W.A., Bender M.T., Cherbas P., Hogness D.S.
    Cell 67:59-77(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ECR-B1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ECR-A).
    Strain: Berkeley.
    Tissue: Embryo.
  5. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
    Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ECR-B1).
    Strain: Berkeley.
    Tissue: Embryo.
  6. "Drosophila tissues with different metamorphic responses to ecdysone express different ecdysone receptor isoforms."
    Talbot W.S., Swyryd E.A., Hogness D.S.
    Cell 73:1323-1337(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING.
  7. "Functional ecdysone receptor is the product of EcR and Ultraspiracle genes."
    Yao T.-P., Froman B.M., Jiang Z., Cherbas L., Chen J.-D., McKeown M.M., Cherbas P., Evans R.M.
    Nature 366:476-479(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  8. "Puffs and PCR: the in vivo dynamics of early gene expression during ecdysone responses in Drosophila."
    Huet F., Ruiz C., Richards G.
    Development 118:613-627(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  9. "Methylation at lysine 4 of histone H3 in ecdysone-dependent development of Drosophila."
    Sedkov Y., Cho E., Petruk S., Cherbas L., Smith S.T., Jones R.S., Cherbas P., Canaani E., Jaynes J.B., Mazo A.
    Nature 426:78-83(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRR.

Entry informationi

Entry nameiECR_DROME
AccessioniPrimary (citable) accession number: P34021
Secondary accession number(s): Q0E9N8
, Q6AWL4, Q8SY10, Q95TS4, Q9V9K8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: July 6, 2016
This is version 186 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.