ID 1433E_MOUSE Reviewed; 255 AA.
AC P62259; P29360; P42655; Q63631;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 01-MAY-2013, entry version 92.
DE RecName: Full=14-3-3 protein epsilon;
DE Short=14-3-3E;
GN Name=Ywhae;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=Swiss; TISSUE=Kidney;
RX PubMed=7750640; DOI=10.1006/dbio.1995.1139;
RA McConnell J.E., Armstrong J.F., Bard J.B.;
RT "The mouse 14-3-3 epsilon isoform, a kinase regulator whose expression
RT pattern is modulated in mesenchyme and neuronal differentiation.";
RL Dev. Biol. 169:218-228(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129/Sv;
RA Takihara Y., Irie K., Nomura M., Motaleb M., Matsumoto K., Shimada K.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ILS, and ISS;
RX PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT "High-throughput sequence identification of gene coding variants
RT within alcohol-related QTLs.";
RL Mamm. Genome 12:657-663(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6; TISSUE=Brain;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 131-141; 154-170 AND 197-215, AND MASS
RP SPECTROMETRY.
RC TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Friebe K., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [6]
RP INTERACTION WITH ARHGEF28.
RX PubMed=11533041; DOI=10.1074/jbc.M107709200;
RA Zhai J., Lin H., Shamim M., Schlaepfer W.W., Canete-Soler R.;
RT "Identification of a novel interaction of 14-3-3 with p190RhoGEF.";
RL J. Biol. Chem. 276:41318-41324(2001).
RN [7]
RP INTERACTION WITH NDEL1.
RX PubMed=12796778; DOI=10.1038/ng1169;
RA Toyo-oka K., Shionoya A., Gambello M.J., Cardoso C., Leventer R.,
RA Ward H.L., Ayala R., Tsai L.-H., Dobyns W., Ledbetter D.,
RA Hirotsune S., Wynshaw-Boris A.;
RT "14-3-3epsilon is important for neuronal migration by binding to
RT NUDEL: a molecular explanation for Miller-Dieker syndrome.";
RL Nat. Genet. 34:274-285(2003).
RN [8]
RP INTERACTION WITH GRB10.
RX PubMed=15722337; DOI=10.1074/jbc.M501477200;
RA Urschel S., Bassermann F., Bai R.Y., Munch S., Peschel C., Duyster J.;
RT "Phosphorylation of grb10 regulates its interaction with 14-3-3.";
RL J. Biol. Chem. 280:16987-16993(2005).
RN [9]
RP INTERACTION WITH TIAM2.
RX PubMed=17320046; DOI=10.1016/j.bbrc.2007.02.028;
RA Takefuji M., Mori K., Morita Y., Arimura N., Nishimura T.,
RA Nakayama M., Hoshino M., Iwamatsu A., Murohara T., Kaibuchi K.,
RA Amano M.;
RT "Rho-kinase modulates the function of STEF, a Rac GEF, through its
RT phosphorylation.";
RL Biochem. Biophys. Res. Commun. 355:788-794(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=17203969; DOI=10.1021/pr0604155;
RA Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT "Protein phosphorylation and expression profiling by Yin-yang
RT multidimensional liquid chromatography (Yin-yang MDLC) mass
RT spectrometry.";
RL J. Proteome Res. 6:250-262(2007).
CC -!- FUNCTION: Adapter protein implicated in the regulation of a large
CC spectrum of both general and specialized signaling pathways. Binds
CC to a large number of partners, usually by recognition of a
CC phosphoserine or phosphothreonine motif. Binding generally results
CC in the modulation of the activity of the binding partner.
CC -!- SUBUNIT: Homodimer. Heterodimerizes with YWHAZ (By similarity).
CC Interacts with NDEL1, ARHGEF28 and TIAM2. Interacts with ABL1
CC (phosphorylated form); the interaction retains it in the
CC cytoplasm. Weakly interacts with CDKN1B. Interacts with GAB2 (By
CC similarity). Interacts with PKA-phosphorylated AANAT (By
CC similarity). Interacts with phosphorylated GRB10. Interacts with
CC the phosphorylated (by AKT1) form of SRPK2 (By similarity).
CC -!- INTERACTION:
CC Q8CHQ0:Fbxo4; NbExp=2; IntAct=EBI-356480, EBI-3895153;
CC Q5S006:Lrrk2; NbExp=3; IntAct=EBI-356480, EBI-2693710;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Melanosome (By
CC similarity).
CC -!- DEVELOPMENTAL STAGE: In the E8.5 embryo, expressed throughout the
CC embryo. Within a day, expression was more marked in mesenchyme
CC than elsewhere (e.g. epithelial tissue, where it was generally
CC low), although levels in neural tissue rose again by about E12.5.
CC This difference was maintained until E15.5 when expression levels
CC started to drop in most tissues, with those of the nervous system,
CC tooth, and kidney being exceptions. Strongly expressed in early
CC mesenchyme. The expression decreased as the mesenchyme
CC differentiated.
CC -!- SIMILARITY: Belongs to the 14-3-3 family.
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DR EMBL; Z19599; CAA79659.1; -; mRNA.
DR EMBL; D87663; BAA13424.1; -; mRNA.
DR EMBL; AF483478; AAL90752.1; -; mRNA.
DR EMBL; AF483479; AAL90753.1; -; mRNA.
DR EMBL; BC058686; AAH58686.1; -; mRNA.
DR IPI; IPI00118384; -.
DR PIR; I48337; S31975.
DR RefSeq; NP_033562.3; NM_009536.4.
DR UniGene; Mm.234700; -.
DR ProteinModelPortal; P62259; -.
DR IntAct; P62259; 14.
DR MINT; MINT-209058; -.
DR PhosphoSite; P62259; -.
DR REPRODUCTION-2DPAGE; P62259; -.
DR PaxDb; P62259; -.
DR PRIDE; P62259; -.
DR Ensembl; ENSMUST00000067664; ENSMUSP00000070993; ENSMUSG00000020849.
DR GeneID; 22627; -.
DR KEGG; mmu:22627; -.
DR CTD; 7531; -.
DR MGI; MGI:894689; Ywhae.
DR eggNOG; COG5040; -.
DR HOGENOM; HOG000240379; -.
DR HOVERGEN; HBG050423; -.
DR InParanoid; P62259; -.
DR KO; K06630; -.
DR OMA; KESALIM; -.
DR OrthoDB; EOG4HHP34; -.
DR Reactome; REACT_147847; Translocation of Glut4 to the Plasma Membrane.
DR ChiTaRS; YWHAE; mouse.
DR NextBio; 302987; -.
DR ArrayExpress; P62259; -.
DR Bgee; P62259; -.
DR Genevestigator; P62259; -.
DR GermOnline; ENSMUSG00000020849; Mus musculus.
DR GO; GO:0033267; C:axon part; IEA:Compara.
DR GO; GO:0005871; C:kinesin complex; IEA:Compara.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0019904; F:protein domain specific binding; IDA:MGI.
DR GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR GO; GO:0021766; P:hippocampus development; IMP:MGI.
DR GO; GO:0035308; P:negative regulation of protein dephosphorylation; IDA:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0006605; P:protein targeting; IDA:MGI.
DR Gene3D; 1.20.190.20; -; 1.
DR InterPro; IPR000308; 14-3-3.
DR InterPro; IPR023409; 14-3-3_CS.
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; 14-3-3; 1.
DR PROSITE; PS00796; 1433_1; 1.
DR PROSITE; PS00797; 1433_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1 255 14-3-3 protein epsilon.
FT /FTId=PRO_0000058619.
FT SITE 57 57 Interaction with phosphoserine on
FT interacting protein (By similarity).
FT SITE 130 130 Interaction with phosphoserine on
FT interacting protein (By similarity).
FT MOD_RES 1 1 N-acetylmethionine (By similarity).
FT MOD_RES 50 50 N6-acetyllysine (By similarity).
FT MOD_RES 69 69 N6-acetyllysine (By similarity).
FT MOD_RES 118 118 N6-acetyllysine (By similarity).
FT MOD_RES 123 123 N6-acetyllysine (By similarity).
FT MOD_RES 210 210 Phosphoserine.
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
//
