GenomeNet

Database: UniProt
Entry: P62259
LinkDB: P62259
Original site: P62259 
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   03-SEP-2014, entry version 105.
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 IDENTIFICATION
RP   BY MASS 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).
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       Q8C2B3:Hdac7; NbExp=6; IntAct=EBI-356480, EBI-643830;
CC       P68433:Hist1h3i (xeno); NbExp=11; IntAct=EBI-356480, EBI-1179609;
CC       Q5S006:Lrrk2; NbExp=3; IntAct=EBI-356480, EBI-2693710;
CC       O35244:Prdx6 (xeno); NbExp=2; IntAct=EBI-356480, EBI-915490;
CC       Q8BYJ6:Tbc1d4; NbExp=6; IntAct=EBI-356480, EBI-7920707;
CC       Q64163-4:Tfdp2; NbExp=6; IntAct=EBI-356480, EBI-8077763;
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   CCDS; CCDS25056.1; -.
DR   PIR; I48337; S31975.
DR   RefSeq; NP_033562.3; NM_009536.4.
DR   UniGene; Mm.234700; -.
DR   UniGene; Mm.471625; -.
DR   ProteinModelPortal; P62259; -.
DR   SMR; P62259; 3-232.
DR   BioGrid; 204619; 267.
DR   IntAct; P62259; 4024.
DR   MINT; MINT-209058; -.
DR   PhosphoSite; P62259; -.
DR   REPRODUCTION-2DPAGE; P62259; -.
DR   MaxQB; P62259; -.
DR   PaxDb; P62259; -.
DR   PRIDE; P62259; -.
DR   Ensembl; ENSMUST00000067664; ENSMUSP00000070993; ENSMUSG00000020849.
DR   GeneID; 22627; -.
DR   KEGG; mmu:22627; -.
DR   UCSC; uc007ket.2; mouse.
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; MQESDKP; -.
DR   OrthoDB; EOG7HHWT3; -.
DR   PhylomeDB; P62259; -.
DR   TreeFam; TF102003; -.
DR   Reactome; REACT_196537; Signaling by Hippo.
DR   Reactome; REACT_196635; Regulation of PLK1 Activity at G2/M Transition.
DR   Reactome; REACT_199054; Translocation of GLUT4 to the plasma membrane.
DR   Reactome; REACT_210754; NADE modulates death signalling.
DR   Reactome; REACT_222185; Regulation of HSF1-mediated heat shock response.
DR   Reactome; REACT_225256; HSF1 activation.
DR   ChiTaRS; YWHAE; mouse.
DR   NextBio; 302987; -.
DR   PRO; PR:P62259; -.
DR   ArrayExpress; P62259; -.
DR   Bgee; P62259; -.
DR   Genevestigator; P62259; -.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl.
DR   GO; GO:0005871; C:kinesin complex; IEA:Ensembl.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:Ensembl.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
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:1902309; P:negative regulation of peptidyl-serine dephosphorylation; IEA:Ensembl.
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   GO; GO:0060306; P:regulation of membrane repolarization; IEA:Ensembl.
DR   GO; GO:1901016; P:regulation of potassium ion transmembrane transporter activity; IEA:Ensembl.
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; SSF48445; 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 (By similarity).
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
//
DBGET integrated database retrieval system