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14-3-3 protein epsilon (14-3-3E) (Mitochondrial import stimulation factor L subunit) (MSF L)

 1433E_RAT               Reviewed;         255 AA.
P62260; P29360; P42655; Q63631;
05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
03-JUL-2019, entry version 148.
RecName: Full=14-3-3 protein epsilon;
Short=14-3-3E;
AltName: Full=Mitochondrial import stimulation factor L subunit;
Short=MSF L;
Name=Ywhae;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
TISSUE=Pineal gland;
PubMed=8024705; DOI=10.1089/dna.1994.13.629;
Roseboom P.H., Weller J.L., Babila T., Aitken A., Sellers L.A.,
Moffet J.R., Namboodiri M.A., Klein D.C.;
"Cloning and characterization of the epsilon and zeta isoforms of the
14-3-3 proteins.";
DNA Cell Biol. 13:629-640(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=7822263;
Alam R., Hachiya N., Sakaguchi M., Shun-Ichiro K., Iwanaga S.,
Kitajima M., Mihara K., Omura T.;
"cDNA cloning and characterization of mitochondrial import stimulation
factor (MSF) purified from rat liver cytosol.";
J. Biochem. 116:416-425(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=8694795; DOI=10.1006/bbrc.1996.0991;
Gao L., Gu X.B., Yu D.S., Yu R.K., Zeng G.;
"Association of a 14-3-3 protein with CMP-NeuAc:GM1 alpha 2,3-
sialyltransferase.";
Biochem. Biophys. Res. Commun. 224:103-107(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pituitary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 1-12; 30-42; 95-106; 143-153 AND 216-225,
ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Fibroblast;
Bienvenut W.V., von Kriegsheim A., Kolch W.;
Submitted (JUN-2009) to UniProtKB.
[6]
PROTEIN SEQUENCE OF 20-50; 62-73; 87-94; 107-123; 131-170 AND 197-225,
AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
Lubec G., Diao W., Afjehi-Sadat L., Chen W.-Q., Kang S.U., Lubec S.;
Submitted (SEP-2007) to UniProtKB.
[7]
PROTEIN SEQUENCE OF 131-142 AND 154-170, INTERACTION WITH AANAT, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=11427721; DOI=10.1073/pnas.141118798;
Ganguly S., Gastel J.A., Weller J.L., Schwartz C., Jaffe H.,
Namboodiri M.A., Coon S.L., Hickman A.B., Rollag M., Obsil T.,
Beauverger P., Ferry G., Boutin J.A., Klein D.C.;
"Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14-
3-3-binding switch in melatonin synthesis.";
Proc. Natl. Acad. Sci. U.S.A. 98:8083-8088(2001).
[8]
INTERACTION WITH SOS1.
PubMed=22827337; DOI=10.1042/BJ20120938;
Saha M., Carriere A., Cheerathodi M., Zhang X., Lavoie G., Rush J.,
Roux P.P., Ballif B.A.;
"RSK phosphorylates SOS1 creating 14-3-3-docking sites and negatively
regulating MAPK activation.";
Biochem. J. 447:159-166(2012).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; TYR-131; THR-137 AND
SER-210, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Adapter protein implicated in the regulation of a large
spectrum of both general and specialized signaling pathways. Binds
to a large number of partners, usually by recognition of a
phosphoserine or phosphothreonine motif. Binding generally results
in the modulation of the activity of the binding partner.
Positively regulates phosphorylated protein HSF1 nuclear export to
the cytoplasm. {ECO:0000250|UniProtKB:P62258,
ECO:0000250|UniProtKB:P62261}.
-!- SUBUNIT: Homodimer (By similarity). Heterodimerizes with YWHAZ (By
similarity). Interacts with PKA-phosphorylated AANAT
(PubMed:11427721). Interacts with ABL1 (phosphorylated form); the
interaction retains it in the cytoplasm (By similarity). Interacts
with ARHGEF28 (By similarity). Interacts with BEX3 (By
similarity). Weakly interacts with CDKN1B (By similarity).
Interacts with the 'Thr-369' phosphorylated form of DAPK2 (By
similarity). Interacts with DENND1A (By similarity). Interacts
with GAB2 (By similarity). Interacts with phosphorylated GRB10 (By
similarity). Interacts with KSR1 (By similarity). Interacts with
NDEL1 (By similarity). Interacts with PI4KB, TBC1D22A and TBC1D22B
(By similarity). Interacts with the phosphorylated (by AKT1) form
of SRPK2 (By similarity). Interacts with TIAM2 (By similarity).
Interacts with the 'Ser-1134' and 'Ser-1161' phosphorylated form
of SOS1 (PubMed:22827337). Interacts with ZFP36 (via
phosphorylated form) (By similarity). Interacts with SLITRK1 (By
similarity). Interacts with HSF1 (via phosphorylated form); this
interaction promotes HSF1 sequestration in the cytoplasm in a ERK-
dependent manner (By similarity). Interacts with RIPOR2 (By
similarity). Interacts with KLHL22; required for the nuclear
localization of KLHL22 upon amino acid starvation (By similarity).
Interacts with CRTC1 (By similarity). Interacts with CRTC2
(probably when phosphorylated at 'Ser-171') (By similarity).
Interacts with CRTC3 (probably when phosphorylated at 'Ser-162'
and/or 'Ser-273') (By similarity). Interacts with ATP2B1; this
interaction inhibits calcium-transporting ATPase activity (By
similarity). {ECO:0000250|UniProtKB:P62258,
ECO:0000250|UniProtKB:P62259, ECO:0000269|PubMed:11427721,
ECO:0000269|PubMed:22827337}.
-!- INTERACTION:
P67828:CSNK1A1 (xeno); NbExp=2; IntAct=EBI-356462, EBI-7540603;
Q9UKT5:FBXO4 (xeno); NbExp=2; IntAct=EBI-356462, EBI-960409;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P62258}.
Cytoplasm {ECO:0000250|UniProtKB:P62258}. Melanosome
{ECO:0000250|UniProtKB:P62258}.
-!- DEVELOPMENTAL STAGE: Present at high levels in the pineal gland
early in development and decreased steadily thereafter.
{ECO:0000269|PubMed:8024705}.
-!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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EMBL; M84416; AAC37659.1; -; mRNA.
EMBL; D30739; BAA06401.1; -; mRNA.
EMBL; U53882; AAC52676.1; -; mRNA.
EMBL; BC063163; AAH63163.1; -; mRNA.
PIR; JX0341; JX0341.
RefSeq; NP_113791.1; NM_031603.1.
SMR; P62260; -.
BioGrid; 248364; 14.
CORUM; P62260; -.
DIP; DIP-37260N; -.
IntAct; P62260; 11.
MINT; P62260; -.
STRING; 10116.ENSRNOP00000007100; -.
CarbonylDB; P62260; -.
iPTMnet; P62260; -.
PhosphoSitePlus; P62260; -.
World-2DPAGE; 0004:P62260; -.
jPOST; P62260; -.
PaxDb; P62260; -.
PRIDE; P62260; -.
Ensembl; ENSRNOT00000007100; ENSRNOP00000007100; ENSRNOG00000005290.
GeneID; 29753; -.
KEGG; rno:29753; -.
CTD; 7531; -.
RGD; 62000; Ywhae.
eggNOG; KOG0841; Eukaryota.
eggNOG; COG5040; LUCA.
GeneTree; ENSGT00960000186603; -.
HOGENOM; HOG000240379; -.
InParanoid; P62260; -.
KO; K06630; -.
OMA; MKEHEKG; -.
OrthoDB; 1398991at2759; -.
PhylomeDB; P62260; -.
TreeFam; TF102003; -.
Reactome; R-RNO-111447; Activation of BAD and translocation to mitochondria.
Reactome; R-RNO-2028269; Signaling by Hippo.
Reactome; R-RNO-205025; NADE modulates death signalling.
Reactome; R-RNO-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-RNO-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-RNO-3371511; HSF1 activation.
Reactome; R-RNO-380259; Loss of Nlp from mitotic centrosomes.
Reactome; R-RNO-380270; Recruitment of mitotic centrosome proteins and complexes.
Reactome; R-RNO-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
Reactome; R-RNO-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-RNO-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-RNO-5625740; RHO GTPases activate PKNs.
Reactome; R-RNO-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-RNO-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
Reactome; R-RNO-8854518; AURKA Activation by TPX2.
Reactome; R-RNO-8876198; RAB GEFs exchange GTP for GDP on RABs.
PRO; PR:P62260; -.
Proteomes; UP000002494; Chromosome 10.
Bgee; ENSRNOG00000005290; Expressed in 10 organ(s), highest expression level in brain.
Genevisible; P62260; RN.
GO; GO:0030424; C:axon; IDA:RGD.
GO; GO:0090724; C:central region of growth cone; IDA:RGD.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
GO; GO:0005871; C:kinesin complex; IDA:RGD.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0045202; C:synapse; IDA:SynGO.
GO; GO:0005246; F:calcium channel regulator activity; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; IPI:RGD.
GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0044325; F:ion channel binding; IEA:Ensembl.
GO; GO:0050815; F:phosphoserine residue binding; IEA:Ensembl.
GO; GO:0015459; F:potassium channel regulator activity; IEA:Ensembl.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0008426; F:protein kinase C inhibitor activity; TAS:RGD.
GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB.
GO; GO:1905913; P:negative regulation of calcium ion export across plasma membrane; IEA:Ensembl.
GO; GO:1901020; P:negative regulation of calcium ion transmembrane transporter activity; IEA:Ensembl.
GO; GO:1902309; P:negative regulation of peptidyl-serine dephosphorylation; IEA:Ensembl.
GO; GO:0001764; P:neuron migration; IEA:Ensembl.
GO; GO:0046827; P:positive regulation of protein export from nucleus; ISS:UniProtKB.
GO; GO:0034504; P:protein localization to nucleus; ISS:UniProtKB.
GO; GO:0006605; P:protein targeting; IEA:Ensembl.
GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IEA:Ensembl.
GO; GO:0060306; P:regulation of membrane repolarization; IEA:Ensembl.
GO; GO:0099072; P:regulation of postsynaptic membrane neurotransmitter receptor levels; IDA:SynGO.
GO; GO:1901016; P:regulation of potassium ion transmembrane transporter activity; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:RGD.
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