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14-3-3 protein epsilon (Suppressor of Ras1 3-9)

 1433E_DROME             Reviewed;         262 AA.
P92177; Q8IN86; Q8IN87; Q9VEA8;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
19-SEP-2003, sequence version 2.
12-SEP-2018, entry version 160.
RecName: Full=14-3-3 protein epsilon;
AltName: Full=Suppressor of Ras1 3-9;
Name=14-3-3epsilon; Synonyms=14-3-3e, SR3-9; ORFNames=CG31196;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM D), AND MUTAGENESIS
OF GLU-183; PHE-199 AND TYR-214.
PubMed=9159394; DOI=10.1101/gad.11.9.1132;
Chang H.C., Rubin G.M.;
"14-3-3 epsilon positively regulates Ras-mediated signaling in
Drosophila.";
Genes Dev. 11:1132-1139(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=17372656; DOI=10.1039/b617545g;
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,
Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
"An integrated chemical, mass spectrometric and computational strategy
for (quantitative) phosphoproteomics: application to Drosophila
melanogaster Kc167 cells.";
Mol. Biosyst. 3:275-286(2007).
[5]
INTERACTION WITH YKI.
PubMed=18256197; DOI=10.1242/dev.015255;
Oh H., Irvine K.D.;
"In vivo regulation of Yorkie phosphorylation and localization.";
Development 135:1081-1088(2008).
[6]
FUNCTION, AND INTERACTION WITH YKI.
PubMed=19900439; DOI=10.1016/j.ydbio.2009.10.046;
Ren F., Zhang L., Jiang J.;
"Hippo signaling regulates Yorkie nuclear localization and activity
through 14-3-3 dependent and independent mechanisms.";
Dev. Biol. 337:303-312(2010).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:19900439}.
-!- SUBUNIT: Homodimer (By similarity). Interacts with phosphorylated
yki. {ECO:0000250, ECO:0000269|PubMed:18256197,
ECO:0000269|PubMed:19900439}.
-!- INTERACTION:
Q9VX75:baz; NbExp=5; IntAct=EBI-204478, EBI-2295779;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Comment=Additional isoforms may exist.;
Name=A;
IsoId=P92177-3; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=B;
IsoId=P92177-2; Sequence=VSP_008203;
Note=No experimental confirmation available.;
Name=C;
IsoId=P92177-4; Sequence=VSP_026086;
Note=No experimental confirmation available.;
Name=D;
IsoId=P92177-1; Sequence=VSP_008204;
-!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U84898; AAC47520.1; -; Genomic_DNA.
EMBL; U84897; AAC47519.1; -; mRNA.
EMBL; AE014297; AAF55519.2; -; Genomic_DNA.
EMBL; AE014297; AAN13764.1; -; Genomic_DNA.
EMBL; AE014297; AAN13765.1; -; Genomic_DNA.
EMBL; AE014297; AAN13766.1; -; Genomic_DNA.
RefSeq; NP_732309.1; NM_169796.2. [P92177-3]
RefSeq; NP_732310.1; NM_169797.3. [P92177-2]
RefSeq; NP_732311.1; NM_169798.3. [P92177-1]
RefSeq; NP_732312.1; NM_169799.2. [P92177-4]
UniGene; Dm.2357; -.
ProteinModelPortal; P92177; -.
SMR; P92177; -.
BioGrid; 67207; 54.
DIP; DIP-18498N; -.
IntAct; P92177; 235.
MINT; P92177; -.
STRING; 7227.FBpp0082987; -.
iPTMnet; P92177; -.
PaxDb; P92177; -.
PRIDE; P92177; -.
EnsemblMetazoa; FBtr0083565; FBpp0082987; FBgn0020238. [P92177-3]
EnsemblMetazoa; FBtr0083566; FBpp0082988; FBgn0020238. [P92177-2]
EnsemblMetazoa; FBtr0083567; FBpp0082989; FBgn0020238. [P92177-4]
EnsemblMetazoa; FBtr0083568; FBpp0082990; FBgn0020238. [P92177-1]
GeneID; 42186; -.
KEGG; dme:Dmel_CG31196; -.
CTD; 42186; -.
FlyBase; FBgn0020238; 14-3-3epsilon.
eggNOG; KOG0841; Eukaryota.
eggNOG; COG5040; LUCA.
GeneTree; ENSGT00760000119116; -.
InParanoid; P92177; -.
KO; K06630; -.
OMA; IPCATTG; -.
OrthoDB; EOG091G0VKY; -.
PhylomeDB; P92177; -.
Reactome; R-DME-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
Reactome; R-DME-2028269; Signaling by Hippo.
Reactome; R-DME-390098; Phosphorylation-dependent inhibition of YKI.
Reactome; R-DME-432553; Phosphorylation of PER and TIM.
Reactome; R-DME-5625740; RHO GTPases activate PKNs.
Reactome; R-DME-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-DME-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
Reactome; R-DME-8876198; RAB GEFs exchange GTP for GDP on RABs.
SignaLink; P92177; -.
ChiTaRS; 14-3-3epsilon; fly.
GenomeRNAi; 42186; -.
PRO; PR:P92177; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0020238; Expressed in 26 organ(s), highest expression level in embryo.
ExpressionAtlas; P92177; baseline and differential.
Genevisible; P92177; DM.
GO; GO:0005813; C:centrosome; HDA:FlyBase.
GO; GO:0005694; C:chromosome; IDA:FlyBase.
GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0045172; C:germline ring canal; IDA:FlyBase.
GO; GO:0005654; C:nucleoplasm; HDA:FlyBase.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0005886; C:plasma membrane; HDA:FlyBase.
GO; GO:0050815; F:phosphoserine residue binding; IPI:FlyBase.
GO; GO:0019904; F:protein domain specific binding; IEA:InterPro.
GO; GO:0046982; F:protein heterodimerization activity; IPI:FlyBase.
GO; GO:0008134; F:transcription factor binding; IPI:FlyBase.
GO; GO:0007411; P:axon guidance; IMP:FlyBase.
GO; GO:0042994; P:cytoplasmic sequestering of transcription factor; IMP:FlyBase.
GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
GO; GO:0000077; P:DNA damage checkpoint; IMP:FlyBase.
GO; GO:0007294; P:germarium-derived oocyte fate determination; IMP:FlyBase.
GO; GO:0007444; P:imaginal disc development; TAS:FlyBase.
GO; GO:0007093; P:mitotic cell cycle checkpoint; TAS:FlyBase.
GO; GO:0008103; P:oocyte microtubule cytoskeleton polarization; IMP:FlyBase.
GO; GO:0007280; P:pole cell migration; IMP:FlyBase.
GO; GO:0045927; P:positive regulation of growth; IMP:FlyBase.
GO; GO:0035332; P:positive regulation of hippo signaling; IGI:FlyBase.
GO; GO:0046579; P:positive regulation of Ras protein signal transduction; HGI:FlyBase.
GO; GO:0040008; P:regulation of growth; IGI:FlyBase.
GO; GO:0007088; P:regulation of mitotic nuclear division; IMP:FlyBase.
GO; GO:0009314; P:response to radiation; TAS:FlyBase.
GO; GO:0009411; P:response to UV; IMP:FlyBase.
GO; GO:0048190; P:wing disc dorsal/ventral pattern formation; IGI:FlyBase.
Gene3D; 1.20.190.20; -; 1.
InterPro; IPR000308; 14-3-3.
InterPro; IPR023409; 14-3-3_CS.
InterPro; IPR036815; 14-3-3_dom_sf.
InterPro; IPR023410; 14-3-3_domain.
PANTHER; PTHR18860; PTHR18860; 1.
Pfam; PF00244; 14-3-3; 1.
PIRSF; PIRSF000868; 14-3-3; 1.
PRINTS; PR00305; 1433ZETA.
SMART; SM00101; 14_3_3; 1.
SUPFAM; SSF48445; SSF48445; 1.
PROSITE; PS00796; 1433_1; 1.
PROSITE; PS00797; 1433_2; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Phosphoprotein;
Reference proteome.
CHAIN 1 262 14-3-3 protein epsilon.
/FTId=PRO_0000058650.
MOD_RES 262 262 Phosphoserine.
{ECO:0000269|PubMed:17372656}.
VAR_SEQ 239 244 Missing (in isoform C). {ECO:0000305}.
/FTId=VSP_026086.
VAR_SEQ 239 240 Missing (in isoform D).
{ECO:0000303|PubMed:9159394}.
/FTId=VSP_008204.
VAR_SEQ 239 239 Missing (in isoform B). {ECO:0000305}.
/FTId=VSP_008203.
MUTAGEN 183 183 E->K: Suppressor of sev-Ras1 V12;
subviable. {ECO:0000269|PubMed:9159394}.
MUTAGEN 199 199 F->Y: Suppressor of sev-Ras1 V12.
{ECO:0000269|PubMed:9159394}.
MUTAGEN 214 214 Y->F: Suppressor of sev-Ras1 V12.
{ECO:0000269|PubMed:9159394}.
SEQUENCE 262 AA; 29799 MW; 2C1562208547DA9C CRC64;
MTERENNVYK AKLAEQAERY DEMVEAMKKV ASMDVELTVE ERNLLSVAYK NVIGARRASW
RIITSIEQKE ENKGAEEKLE MIKTYRGQVE KELRDICSDI LNVLEKHLIP CATSGESKVF
YYKMKGDYHR YLAEFATGSD RKDAAENSLI AYKAASDIAM NDLPPTHPIR LGLALNFSVF
YYEILNSPDR ACRLAKAAFD DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQAEEV
DPNAGDGEPK EQIQDVEDQD VS


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