1433E_RAT
ID 1433E_RAT Reviewed; 255 AA.
AC P62260; P29360; P42655; Q63631;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=14-3-3 protein epsilon;
DE Short=14-3-3E;
DE AltName: Full=Mitochondrial import stimulation factor L subunit;
DE Short=MSF L;
GN Name=Ywhae;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC TISSUE=Pineal gland;
RX PubMed=8024705; DOI=10.1089/dna.1994.13.629;
RA Roseboom P.H., Weller J.L., Babila T., Aitken A., Sellers L.A.,
RA Moffet J.R., Namboodiri M.A., Klein D.C.;
RT "Cloning and characterization of the epsilon and zeta isoforms of the 14-3-
RT 3 proteins.";
RL DNA Cell Biol. 13:629-640(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=7822263; DOI=10.1093/oxfordjournals.jbchem.a124541;
RA Alam R., Hachiya N., Sakaguchi M., Shun-Ichiro K., Iwanaga S., Kitajima M.,
RA Mihara K., Omura T.;
RT "cDNA cloning and characterization of mitochondrial import stimulation
RT factor (MSF) purified from rat liver cytosol.";
RL J. Biochem. 116:416-425(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8694795; DOI=10.1006/bbrc.1996.0991;
RA Gao L., Gu X.B., Yu D.S., Yu R.K., Zeng G.;
RT "Association of a 14-3-3 protein with CMP-NeuAc:GM1 alpha 2,3-
RT sialyltransferase.";
RL Biochem. Biophys. Res. Commun. 224:103-107(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 1-12; 30-42; 95-106; 143-153 AND 216-225, ACETYLATION
RP AT MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fibroblast;
RA Bienvenut W.V., von Kriegsheim A., Kolch W.;
RL Submitted (JUN-2009) to UniProtKB.
RN [6]
RP PROTEIN SEQUENCE OF 20-50; 62-73; 87-94; 107-123; 131-170 AND 197-225, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA Lubec G., Diao W., Afjehi-Sadat L., Chen W.-Q., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 131-142 AND 154-170, INTERACTION WITH AANAT, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11427721; DOI=10.1073/pnas.141118798;
RA Ganguly S., Gastel J.A., Weller J.L., Schwartz C., Jaffe H.,
RA Namboodiri M.A., Coon S.L., Hickman A.B., Rollag M., Obsil T.,
RA Beauverger P., Ferry G., Boutin J.A., Klein D.C.;
RT "Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14-3-3-
RT binding switch in melatonin synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:8083-8088(2001).
RN [8]
RP INTERACTION WITH SOS1.
RX PubMed=22827337; DOI=10.1042/bj20120938;
RA Saha M., Carriere A., Cheerathodi M., Zhang X., Lavoie G., Rush J.,
RA Roux P.P., Ballif B.A.;
RT "RSK phosphorylates SOS1 creating 14-3-3-docking sites and negatively
RT regulating MAPK activation.";
RL Biochem. J. 447:159-166(2012).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; TYR-131; THR-137 AND
RP SER-210, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Adapter protein implicated in the regulation of a large
CC spectrum of both general and specialized signaling pathways. Binds to a
CC large number of partners, usually by recognition of a phosphoserine or
CC phosphothreonine motif. Binding generally results in the modulation of
CC the activity of the binding partner. Positively regulates
CC phosphorylated protein HSF1 nuclear export to the cytoplasm.
CC {ECO:0000250|UniProtKB:P62258, ECO:0000250|UniProtKB:P62261}.
CC -!- SUBUNIT: Homodimer (By similarity). Heterodimerizes with YWHAZ (By
CC similarity). Interacts with PKA-phosphorylated AANAT (PubMed:11427721).
CC Interacts with ABL1 (phosphorylated form); the interaction retains it
CC in the cytoplasm (By similarity). Interacts with ARHGEF28 (By
CC similarity). Interacts with BEX3 (By similarity). Weakly interacts with
CC CDKN1B (By similarity). Interacts with the 'Thr-369' phosphorylated
CC form of DAPK2 (By similarity). Interacts with DENND1A (By similarity).
CC Interacts with GAB2 (By similarity). Interacts with phosphorylated
CC GRB10 (By similarity). Interacts with KSR1 (By similarity). Interacts
CC with NDEL1 (By similarity). Interacts with PI4KB, TBC1D22A and TBC1D22B
CC (By similarity). Interacts with the phosphorylated (by AKT1) form of
CC SRPK2 (By similarity). Interacts with TIAM2 (By similarity). Interacts
CC with the 'Ser-1134' and 'Ser-1161' phosphorylated form of SOS1
CC (PubMed:22827337). Interacts with ZFP36 (via phosphorylated form) (By
CC similarity). Interacts with SLITRK1 (By similarity). Interacts with
CC HSF1 (via phosphorylated form); this interaction promotes HSF1
CC sequestration in the cytoplasm in a ERK-dependent manner (By
CC similarity). Interacts with RIPOR2 (By similarity). Interacts with
CC KLHL22; required for the nuclear localization of KLHL22 upon amino acid
CC starvation (By similarity). Interacts with CRTC1 (By similarity).
CC Interacts with CRTC2 (probably when phosphorylated at 'Ser-171') (By
CC similarity). Interacts with CRTC3 (probably when phosphorylated at
CC 'Ser-162' and/or 'Ser-273') (By similarity). Interacts with ATP2B1 and
CC ATP2B3; this interaction inhibits calcium-transporting ATPase activity
CC (By similarity). Interacts with MEFV (By similarity).
CC {ECO:0000250|UniProtKB:P62258, ECO:0000250|UniProtKB:P62259,
CC ECO:0000269|PubMed:11427721, ECO:0000269|PubMed:22827337}.
CC -!- INTERACTION:
CC P62260; P67828: CSNK1A1; Xeno; NbExp=2; IntAct=EBI-356462, EBI-7540603;
CC P62260; Q9UKT5: FBXO4; Xeno; NbExp=2; IntAct=EBI-356462, EBI-960409;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P62258}. Cytoplasm
CC {ECO:0000250|UniProtKB:P62258}. Melanosome
CC {ECO:0000250|UniProtKB:P62258}.
CC -!- DEVELOPMENTAL STAGE: Present at high levels in the pineal gland early
CC in development and decreased steadily thereafter.
CC {ECO:0000269|PubMed:8024705}.
CC -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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DR EMBL; M84416; AAC37659.1; -; mRNA.
DR EMBL; D30739; BAA06401.1; -; mRNA.
DR EMBL; U53882; AAC52676.1; -; mRNA.
DR EMBL; BC063163; AAH63163.1; -; mRNA.
DR PIR; JX0341; JX0341.
DR RefSeq; NP_113791.1; NM_031603.1.
DR AlphaFoldDB; P62260; -.
DR SMR; P62260; -.
DR BioGRID; 248364; 17.
DR CORUM; P62260; -.
DR DIP; DIP-37260N; -.
DR IntAct; P62260; 14.
DR MINT; P62260; -.
DR STRING; 10116.ENSRNOP00000007100; -.
DR CarbonylDB; P62260; -.
DR iPTMnet; P62260; -.
DR PhosphoSitePlus; P62260; -.
DR World-2DPAGE; 0004:P62260; -.
DR jPOST; P62260; -.
DR PaxDb; P62260; -.
DR PRIDE; P62260; -.
DR Ensembl; ENSRNOT00000007100; ENSRNOP00000007100; ENSRNOG00000005290.
DR GeneID; 29753; -.
DR KEGG; rno:29753; -.
DR CTD; 7531; -.
DR RGD; 62000; Ywhae.
DR eggNOG; KOG0841; Eukaryota.
DR GeneTree; ENSGT01050000244964; -.
DR HOGENOM; CLU_058290_0_0_1; -.
DR InParanoid; P62260; -.
DR OMA; IPCATTG; -.
DR OrthoDB; 1176818at2759; -.
DR PhylomeDB; P62260; -.
DR TreeFam; TF102003; -.
DR Reactome; R-RNO-111447; Activation of BAD and translocation to mitochondria.
DR Reactome; R-RNO-2028269; Signaling by Hippo.
DR Reactome; R-RNO-205025; NADE modulates death signalling.
DR Reactome; R-RNO-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-RNO-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-RNO-3371511; HSF1 activation.
DR Reactome; R-RNO-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-RNO-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-RNO-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-RNO-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-RNO-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-RNO-5625740; RHO GTPases activate PKNs.
DR Reactome; R-RNO-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-RNO-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
DR Reactome; R-RNO-8854518; AURKA Activation by TPX2.
DR Reactome; R-RNO-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR PRO; PR:P62260; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000005290; Expressed in Ammon's horn and 20 other tissues.
DR Genevisible; P62260; RN.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0090724; C:central region of growth cone; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005871; C:kinesin complex; IDA:RGD.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0005246; F:calcium channel regulator activity; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; IPI:RGD.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0051219; F:phosphoprotein binding; ISO:RGD.
DR GO; GO:0050815; F:phosphoserine residue binding; ISO:RGD.
DR GO; GO:0015459; F:potassium channel regulator activity; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0008426; F:protein kinase C inhibitor activity; TAS:RGD.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0097110; F:scaffold protein binding; ISO:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
DR GO; GO:0021987; P:cerebral cortex development; ISO:RGD.
DR GO; GO:0021766; P:hippocampus development; ISO:RGD.
DR GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB.
DR GO; GO:1905913; P:negative regulation of calcium ion export across plasma membrane; ISO:RGD.
DR GO; GO:1901020; P:negative regulation of calcium ion transmembrane transporter activity; ISO:RGD.
DR GO; GO:1902309; P:negative regulation of peptidyl-serine dephosphorylation; ISO:RGD.
DR GO; GO:0035308; P:negative regulation of protein dephosphorylation; ISO:RGD.
DR GO; GO:0001764; P:neuron migration; ISO:RGD.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; ISS:UniProtKB.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0034504; P:protein localization to nucleus; ISS:UniProtKB.
DR GO; GO:0006605; P:protein targeting; ISO:RGD.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; ISO:RGD.
DR GO; GO:0060306; P:regulation of membrane repolarization; ISO:RGD.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0099072; P:regulation of postsynaptic membrane neurotransmitter receptor levels; IDA:SynGO.
DR GO; GO:1901016; P:regulation of potassium ion transmembrane transporter activity; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 1.20.190.20; -; 1.
DR InterPro; IPR000308; 14-3-3.
DR InterPro; IPR023409; 14-3-3_CS.
DR InterPro; IPR036815; 14-3-3_dom_sf.
DR InterPro; IPR023410; 14-3-3_domain.
DR PANTHER; PTHR18860; PTHR18860; 1.
DR Pfam; PF00244; 14-3-3; 1.
DR PIRSF; PIRSF000868; 14-3-3; 1.
DR PRINTS; PR00305; 1433ZETA.
DR SMART; SM00101; 14_3_3; 1.
DR SUPFAM; SSF48445; SSF48445; 1.
DR PROSITE; PS00796; 1433_1; 1.
DR PROSITE; PS00797; 1433_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..255
FT /note="14-3-3 protein epsilon"
FT /id="PRO_0000058620"
FT REGION 234..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 57
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000250"
FT SITE 130
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.5"
FT MOD_RES 50
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62258"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 69
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62258"
FT MOD_RES 118
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62258"
FT MOD_RES 123
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62258"
FT MOD_RES 131
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 137
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 232
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P62258"
FT CROSSLNK 50
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P62258"
FT CONFLICT 73
FT /note="K -> T (in Ref. 3; AAC52676)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="F -> S (in Ref. 3; AAC52676)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="K -> Y (in Ref. 3; AAC52676)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 255 AA; 29174 MW; 07817CCBD1F75B26 CRC64;
MDDREDLVYQ AKLAEQAERY DEMVESMKKV AGMDVELTVE ERNLLSVAYK NVIGARRASW
RIISSIEQKE ENKGGEDKLK MIREYRQMVE TELKLICCDI LDVLDKHLIP AANTGESKVF
YYKMKGDYHR YLAEFATGND RKEAAENSLV AYKAASDIAM TELPPTHPIR LGLALNFSVF
YYEILNSPDR ACRLAKAAFD DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQGDGE
EQNKEALQDV EDENQ
