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P92177

- 1433E_DROME

UniProt

P92177 - 1433E_DROME

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Protein

14-3-3 protein epsilon

Gene
14-3-3epsilon, 14-3-3e, SR3-9, CG31196
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - 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 binding Source: UniProtKB
  2. 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 growth Source: FlyBase
  11. regulation of growth Source: FlyBase
  12. regulation of mitosis Source: FlyBase
  13. response to radiation Source: FlyBase
  14. response to UV Source: FlyBase
  15. wing disc dorsal/ventral pattern formation Source: FlyBase
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_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
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.

Interactioni

Subunit structurei

Homodimer By similarity. Interacts with phosphorylated yki.2 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.

Family & Domainsi

Sequence similaritiesi

Belongs to the 14-3-3 family.

Phylogenomic databases

eggNOGiCOG5040.
GeneTreeiENSGT00730000110613.
InParanoidiP92177.
KOiK06630.
OMAiMQESDKP.
OrthoDBiEOG7HHWT3.
PhylomeDBiP92177.

Family and domain databases

Gene3Di1.20.190.20. 1 hit.
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. Align

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

MTERENNVYK AKLAEQAERY DEMVEAMKKV ASMDVELTVE ERNLLSVAYK    50
NVIGARRASW RIITSIEQKE ENKGAEEKLE MIKTYRGQVE KELRDICSDI 100
LNVLEKHLIP CATSGESKVF YYKMKGDYHR YLAEFATGSD RKDAAENSLI 150
AYKAASDIAM NDLPPTHPIR LGLALNFSVF YYEILNSPDR ACRLAKAAFD 200
DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQAEEV DPNAGDGEPK 250
EQIQDVEDQD VS 262

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. VSP_026086
Alternative sequencei239 – 2402Missing in isoform D. VSP_008204
Alternative sequencei239 – 2391Missing in isoform B. VSP_008203

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_169797.2. [P92177-2]
NP_732311.1. NM_169798.2. [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:
EMBL
GenBank
DDBJ
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 .
RefSeqi NP_732309.1. NM_169796.2. [P92177-3 ]
NP_732310.1. NM_169797.2. [P92177-2 ]
NP_732311.1. NM_169798.2. [P92177-1 ]
NP_732312.1. NM_169799.2. [P92177-4 ]
UniGenei Dm.2357.

3D structure databases

ProteinModelPortali P92177.
SMRi P92177. Positions 3-232.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 67207. 28 interactions.
DIPi DIP-18498N.
IntActi P92177. 234 interactions.
MINTi MINT-277717.
STRINGi 7227.FBpp0082987.

Proteomic databases

PaxDbi P92177.
PRIDEi P92177.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0083565 ; FBpp0082987 ; FBgn0020238 . [P92177-3 ]
GeneIDi 42186.
KEGGi dme:Dmel_CG31196.

Organism-specific databases

CTDi 42186.
FlyBasei FBgn0020238. 14-3-3epsilon.

Phylogenomic databases

eggNOGi COG5040.
GeneTreei ENSGT00730000110613.
InParanoidi P92177.
KOi K06630.
OMAi MQESDKP.
OrthoDBi EOG7HHWT3.
PhylomeDBi P92177.

Enzyme and pathway databases

Reactomei REACT_210254. Regulation of HSF1-mediated heat shock response.
REACT_227922. HSF1 activation.
SignaLinki P92177.

Miscellaneous databases

ChiTaRSi 14-3-3epsilon. drosophila.
GenomeRNAii 42186.
NextBioi 827573.
PROi P92177.

Gene expression databases

Bgeei P92177.

Family and domain databases

Gene3Di 1.20.190.20. 1 hit.
InterProi IPR000308. 14-3-3.
IPR023409. 14-3-3_CS.
IPR023410. 14-3-3_domain.
[Graphical view ]
PANTHERi PTHR18860. PTHR18860. 1 hit.
Pfami PF00244. 14-3-3. 1 hit.
[Graphical view ]
PIRSFi PIRSF000868. 14-3-3. 1 hit.
PRINTSi PR00305. 1433ZETA.
SMARTi SM00101. 14_3_3. 1 hit.
[Graphical view ]
SUPFAMi SSF48445. SSF48445. 1 hit.
PROSITEi PS00796. 1433_1. 1 hit.
PS00797. 1433_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 120 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

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