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Protein

14-3-3 protein epsilon

Gene

14-3-3epsilon

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

Functioni

Positively regulates Ras-mediated pathways. Acts downstream or parallel to Raf, but upstream of nuclear factors in Ras signaling. Three mutants have been isolated, that suppress the rough eye phenotype caused by mutated Ras1 (sev-Ras1 v12). Inhibits yki activity by restricting its nuclear localization.1 Publication

GO - Molecular functioni

  1. protein heterodimerization activity Source: FlyBase

GO - Biological processi

  1. axon guidance Source: FlyBase
  2. determination of adult lifespan Source: FlyBase
  3. DNA damage checkpoint Source: FlyBase
  4. germarium-derived oocyte fate determination Source: FlyBase
  5. imaginal disc development Source: FlyBase
  6. mitotic cell cycle checkpoint Source: FlyBase
  7. mitotic G2 DNA damage checkpoint Source: FlyBase
  8. oocyte microtubule cytoskeleton polarization Source: FlyBase
  9. pole cell migration Source: FlyBase
  10. positive regulation of ERK1 and ERK2 cascade Source: FlyBase
  11. positive regulation of growth Source: FlyBase
  12. positive regulation of Ras protein signal transduction Source: FlyBase
  13. regulation of growth Source: FlyBase
  14. regulation of mitosis Source: FlyBase
  15. response to radiation Source: FlyBase
  16. response to UV Source: FlyBase
  17. wing disc dorsal/ventral pattern formation Source: FlyBase
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_180852. Translocation of GLUT4 to the plasma membrane.
REACT_180985. Signaling by Hippo.
REACT_210254. Regulation of HSF1-mediated heat shock response.
REACT_227922. HSF1 activation.
SignaLinkiP92177.

Names & Taxonomyi

Protein namesi
Recommended name:
14-3-3 protein epsilon
Alternative name(s):
Suppressor of Ras1 3-9
Gene namesi
Name:14-3-3epsilon
Synonyms:14-3-3e, SR3-9
ORF Names:CG31196
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0020238. 14-3-3epsilon.

Subcellular locationi

GO - Cellular componenti

  1. chromosome Source: FlyBase
  2. cytoplasm Source: FlyBase
  3. germline ring canal Source: FlyBase
  4. microtubule associated complex Source: FlyBase
  5. nucleus Source: FlyBase
  6. plasma membrane Source: FlyBase
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi183 – 1831E → K: Suppressor of sev-Ras1 V12; subviable. 1 Publication
Mutagenesisi199 – 1991F → Y: Suppressor of sev-Ras1 V12. 1 Publication
Mutagenesisi214 – 2141Y → F: Suppressor of sev-Ras1 V12. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 26226214-3-3 protein epsilonPRO_0000058650Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei262 – 2621Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP92177.
PRIDEiP92177.

Expressioni

Gene expression databases

BgeeiP92177.
ExpressionAtlasiP92177. differential.

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with phosphorylated yki.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
bazQ9VX755EBI-204478,EBI-2295779

Protein-protein interaction databases

BioGridi67207. 28 interactions.
DIPiDIP-18498N.
IntActiP92177. 234 interactions.
MINTiMINT-277717.
STRINGi7227.FBpp0082987.

Structurei

3D structure databases

ProteinModelPortaliP92177.
SMRiP92177. Positions 3-232.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the 14-3-3 family.Curated

Phylogenomic databases

eggNOGiCOG5040.
GeneTreeiENSGT00760000119116.
InParanoidiP92177.
KOiK06630.
OMAiKESALIM.
OrthoDBiEOG7HHWT3.
PhylomeDBiP92177.

Family and domain databases

InterProiIPR000308. 14-3-3.
IPR023409. 14-3-3_CS.
IPR023410. 14-3-3_domain.
[Graphical view]
PANTHERiPTHR18860. PTHR18860. 1 hit.
PfamiPF00244. 14-3-3. 1 hit.
[Graphical view]
PIRSFiPIRSF000868. 14-3-3. 1 hit.
PRINTSiPR00305. 1433ZETA.
SMARTiSM00101. 14_3_3. 1 hit.
[Graphical view]
SUPFAMiSSF48445. SSF48445. 1 hit.
PROSITEiPS00796. 1433_1. 1 hit.
PS00797. 1433_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms may exist.

Isoform A (identifier: P92177-3) [UniParc]FASTAAdd to basket

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
MTERENNVYK AKLAEQAERY DEMVEAMKKV ASMDVELTVE ERNLLSVAYK
60 70 80 90 100
NVIGARRASW RIITSIEQKE ENKGAEEKLE MIKTYRGQVE KELRDICSDI
110 120 130 140 150
LNVLEKHLIP CATSGESKVF YYKMKGDYHR YLAEFATGSD RKDAAENSLI
160 170 180 190 200
AYKAASDIAM NDLPPTHPIR LGLALNFSVF YYEILNSPDR ACRLAKAAFD
210 220 230 240 250
DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQAEEV DPNAGDGEPK
260
EQIQDVEDQD VS

Note: No experimental confirmation available.

Length:262
Mass (Da):29,799
Last modified:September 19, 2003 - v2
Checksum:i2C1562208547DA9C
GO
Isoform B (identifier: P92177-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     239-239: Missing.

Note: No experimental confirmation available.

Show »
Length:261
Mass (Da):29,669
Checksum:i8195754CE0B089AD
GO
Isoform C (identifier: P92177-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     239-244: Missing.

Note: No experimental confirmation available.

Show »
Length:256
Mass (Da):29,173
Checksum:i0B2FEE0EA6D36219
GO
Isoform D (identifier: P92177-1) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     239-240: Missing.

Show »
Length:260
Mass (Da):29,570
Checksum:i1282192917E3A7A4
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei239 – 2446Missing in isoform C. CuratedVSP_026086
Alternative sequencei239 – 2402Missing in isoform D. 1 PublicationVSP_008204
Alternative sequencei239 – 2391Missing in isoform B. CuratedVSP_008203

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U84898 Genomic DNA. Translation: AAC47520.1.
U84897 mRNA. Translation: AAC47519.1.
AE014297 Genomic DNA. Translation: AAF55519.2.
AE014297 Genomic DNA. Translation: AAN13764.1.
AE014297 Genomic DNA. Translation: AAN13765.1.
AE014297 Genomic DNA. Translation: AAN13766.1.
RefSeqiNP_732309.1. NM_169796.2. [P92177-3]
NP_732310.1. NM_169797.3. [P92177-2]
NP_732311.1. NM_169798.3. [P92177-1]
NP_732312.1. NM_169799.2. [P92177-4]
UniGeneiDm.2357.

Genome annotation databases

EnsemblMetazoaiFBtr0083565; FBpp0082987; FBgn0020238. [P92177-3]
GeneIDi42186.
KEGGidme:Dmel_CG31196.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U84898 Genomic DNA. Translation: AAC47520.1.
U84897 mRNA. Translation: AAC47519.1.
AE014297 Genomic DNA. Translation: AAF55519.2.
AE014297 Genomic DNA. Translation: AAN13764.1.
AE014297 Genomic DNA. Translation: AAN13765.1.
AE014297 Genomic DNA. Translation: AAN13766.1.
RefSeqiNP_732309.1. NM_169796.2. [P92177-3]
NP_732310.1. NM_169797.3. [P92177-2]
NP_732311.1. NM_169798.3. [P92177-1]
NP_732312.1. NM_169799.2. [P92177-4]
UniGeneiDm.2357.

3D structure databases

ProteinModelPortaliP92177.
SMRiP92177. Positions 3-232.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi67207. 28 interactions.
DIPiDIP-18498N.
IntActiP92177. 234 interactions.
MINTiMINT-277717.
STRINGi7227.FBpp0082987.

Proteomic databases

PaxDbiP92177.
PRIDEiP92177.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0083565; FBpp0082987; FBgn0020238. [P92177-3]
GeneIDi42186.
KEGGidme:Dmel_CG31196.

Organism-specific databases

CTDi42186.
FlyBaseiFBgn0020238. 14-3-3epsilon.

Phylogenomic databases

eggNOGiCOG5040.
GeneTreeiENSGT00760000119116.
InParanoidiP92177.
KOiK06630.
OMAiKESALIM.
OrthoDBiEOG7HHWT3.
PhylomeDBiP92177.

Enzyme and pathway databases

ReactomeiREACT_180852. Translocation of GLUT4 to the plasma membrane.
REACT_180985. Signaling by Hippo.
REACT_210254. Regulation of HSF1-mediated heat shock response.
REACT_227922. HSF1 activation.
SignaLinkiP92177.

Miscellaneous databases

ChiTaRSi14-3-3epsilon. fly.
GenomeRNAii42186.
NextBioi827573.
PROiP92177.

Gene expression databases

BgeeiP92177.
ExpressionAtlasiP92177. differential.

Family and domain databases

InterProiIPR000308. 14-3-3.
IPR023409. 14-3-3_CS.
IPR023410. 14-3-3_domain.
[Graphical view]
PANTHERiPTHR18860. PTHR18860. 1 hit.
PfamiPF00244. 14-3-3. 1 hit.
[Graphical view]
PIRSFiPIRSF000868. 14-3-3. 1 hit.
PRINTSiPR00305. 1433ZETA.
SMARTiSM00101. 14_3_3. 1 hit.
[Graphical view]
SUPFAMiSSF48445. SSF48445. 1 hit.
PROSITEiPS00796. 1433_1. 1 hit.
PS00797. 1433_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "14-3-3 epsilon positively regulates Ras-mediated signaling in Drosophila."
    Chang H.C., Rubin G.M.
    Genes Dev. 11:1132-1139(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM D), MUTAGENESIS OF GLU-183; PHE-199 AND TYR-214.
  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. "An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
    Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
    Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262, IDENTIFICATION BY MASS SPECTROMETRY.
  5. "In vivo regulation of Yorkie phosphorylation and localization."
    Oh H., Irvine K.D.
    Development 135:1081-1088(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH YKI.
  6. "Hippo signaling regulates Yorkie nuclear localization and activity through 14-3-3 dependent and independent mechanisms."
    Ren F., Zhang L., Jiang J.
    Dev. Biol. 337:303-312(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH YKI.

Entry informationi

Entry namei1433E_DROME
AccessioniPrimary (citable) accession number: P92177
Secondary accession number(s): Q8IN86, Q8IN87, Q9VEA8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: September 19, 2003
Last modified: January 7, 2015
This is version 124 of the entry and version 2 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.