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Protein

Density-regulated protein homolog

Gene

DENR

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Regulates translation as part of a complex with MCTS1. Specifically required for translational re-initiation in mRNAs containing upstream open reading frames (uORFs). Not required for standard translational initiation. Regulates expression of a subset of gene products including mbc, InR and EcR.1 Publication

GO - Molecular functioni

  • mRNA binding Source: FlyBase
  • translation initiation factor activity Source: InterPro

GO - Biological processi

  • ecdysone receptor-mediated signaling pathway Source: FlyBase
  • positive regulation of cell proliferation Source: FlyBase
  • positive regulation of insulin receptor signaling pathway Source: FlyBase
  • positive regulation of translational initiation Source: FlyBase
  • translation reinitiation Source: FlyBase
Complete GO annotation...

Keywords - Biological processi

Translation regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Density-regulated protein homolog1 Publication
Gene namesi
Name:DENRImported
ORF Names:CG9099Imported
OrganismiDrosophila melanogaster (Fruit fly)Imported
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0030802. DENR.

Pathology & Biotechi

Disruption phenotypei

Animals die as pharate adults with crooked legs, abnormal genitalia and a larval-like epidermis. Proliferation of histoblast cells is impaired.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 189189Density-regulated protein homologCuratedPRO_0000432074Add
BLAST

Proteomic databases

PRIDEiQ9VX98.

Interactioni

Subunit structurei

Interacts with MCTS1.1 Publication

Protein-protein interaction databases

IntActiQ9VX98. 3 interactions.
MINTiMINT-280600.

Structurei

3D structure databases

ProteinModelPortaliQ9VX98.
SMRiQ9VX98. Positions 102-182.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini105 – 17268SUI1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the DENR family.Curated
Contains 1 SUI1 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0023.
GeneTreeiENSGT00390000014349.
OMAiVIPEKWA.
OrthoDBiEOG7T4MMN.
PhylomeDBiQ9VX98.

Family and domain databases

Gene3Di3.30.780.10. 1 hit.
InterProiIPR005873. Drp1.
IPR001950. TIF_SUI1.
[Graphical view]
PfamiPF01253. SUI1. 1 hit.
[Graphical view]
SUPFAMiSSF55159. SSF55159. 1 hit.
TIGRFAMsiTIGR01159. DRP1. 1 hit.
PROSITEiPS50296. SUI1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VX98-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTNEDVGTNS VADRLQLGPR EGVTYPIQMK YCGHCTMPIE YCEYYPEYEK
60 70 80 90 100
CKEWLELHMP DDFERLKIEE EAAAADGTDD DKKRQKRGGK GLLRVKKKED
110 120 130 140 150
VPKRICVSRA ARGKKKSVTV VTGLSTFDID LKVAAKFFGT KFACGSSVTG
160 170 180
DDEIVIQGDV KDDLFDVIPE KWAEIDEDVI EDLGDQKRT
Length:189
Mass (Da):21,349
Last modified:October 1, 2002 - v3
Checksum:i8FD869D637727C62
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014298 Genomic DNA. Translation: AAF48679.3.
AE014298 Genomic DNA. Translation: AGB95472.1.
AY060757 mRNA. Translation: AAL28305.1.
RefSeqiNP_001259630.1. NM_001272701.1.
NP_573176.1. NM_132948.4.
UniGeneiDm.19728.

Genome annotation databases

EnsemblMetazoaiFBtr0074347; FBpp0074121; FBgn0030802.
FBtr0310520; FBpp0302657; FBgn0030802.
GeneIDi32679.
KEGGidme:Dmel_CG9099.
UCSCiCG9099-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014298 Genomic DNA. Translation: AAF48679.3.
AE014298 Genomic DNA. Translation: AGB95472.1.
AY060757 mRNA. Translation: AAL28305.1.
RefSeqiNP_001259630.1. NM_001272701.1.
NP_573176.1. NM_132948.4.
UniGeneiDm.19728.

3D structure databases

ProteinModelPortaliQ9VX98.
SMRiQ9VX98. Positions 102-182.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9VX98. 3 interactions.
MINTiMINT-280600.

Proteomic databases

PRIDEiQ9VX98.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0074347; FBpp0074121; FBgn0030802.
FBtr0310520; FBpp0302657; FBgn0030802.
GeneIDi32679.
KEGGidme:Dmel_CG9099.
UCSCiCG9099-RA. d. melanogaster.

Organism-specific databases

FlyBaseiFBgn0030802. DENR.

Phylogenomic databases

eggNOGiCOG0023.
GeneTreeiENSGT00390000014349.
OMAiVIPEKWA.
OrthoDBiEOG7T4MMN.
PhylomeDBiQ9VX98.

Miscellaneous databases

GenomeRNAii32679.
NextBioi779800.
PROiQ9VX98.

Family and domain databases

Gene3Di3.30.780.10. 1 hit.
InterProiIPR005873. Drp1.
IPR001950. TIF_SUI1.
[Graphical view]
PfamiPF01253. SUI1. 1 hit.
[Graphical view]
SUPFAMiSSF55159. SSF55159. 1 hit.
TIGRFAMsiTIGR01159. DRP1. 1 hit.
PROSITEiPS50296. SUI1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
  2. Cited for: GENOME REANNOTATION.
    Strain: BerkeleyImported.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BerkeleyImported.
    Tissue: HeadImported.
  4. "DENR-MCT-1 promotes translation re-initiation downstream of uORFs to control tissue growth."
    Schleich S., Strassburger K., Janiesch P.C., Koledachkina T., Miller K.K., Haneke K., Cheng Y.S., Kuchler K., Stoecklin G., Duncan K.E., Teleman A.A.
    Nature 512:208-212(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MCTS1, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiDENR_DROME
AccessioniPrimary (citable) accession number: Q9VX98
Secondary accession number(s): Q95SJ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 4, 2015
Last sequence update: October 1, 2002
Last modified: April 29, 2015
This is version 114 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.