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14-3-3 protein epsilon (14-3-3E)

 1433E_CHICK             Reviewed;         255 AA.
Q5ZMT0; P84171;
21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
23-NOV-2004, sequence version 1.
23-MAY-2018, entry version 84.
RecName: Full=14-3-3 protein epsilon;
Short=14-3-3E;
Name=YWHAE {ECO:0000250|UniProtKB:P62262}; ORFNames=RCJMB04_1e8;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1] {ECO:0000305, ECO:0000312|EMBL:CAG30963.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=CB {ECO:0000312|EMBL:CAG30963.1};
TISSUE=Bursa of Fabricius {ECO:0000312|EMBL:CAG30963.1};
PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J.,
Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M.,
Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.-M.;
"Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
function analysis.";
Genome Biol. 6:R6.1-R6.9(2005).
[2] {ECO:0000305}
IDENTIFICATION, AND MASS SPECTROMETRY.
TISSUE=Embryo {ECO:0000269|PubMed:16287166};
PubMed=16287166; DOI=10.1002/pmic.200402056;
Agudo D., Gomez-Esquer F., Diaz-Gil G., Martinez-Arribas F.,
Delcan J., Schneider J., Palomar M.A., Linares R.;
"Proteomic analysis of the Gallus gallus embryo at stage-29 of
development.";
Proteomics 5:4946-4957(2005).
-!- 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.
{ECO:0000250|UniProtKB:P62261}.
-!- SUBUNIT: Homodimer, and heterodimer with other family members.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P62258}.
Cytoplasm {ECO:0000250|UniProtKB:P62258}.
-!- MASS SPECTROMETRY: Mass=29440; Mass_error=2; Method=MALDI;
Range=1-255; Evidence={ECO:0000269|PubMed:16287166};
-!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000255}.
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EMBL; AJ719304; CAG30963.1; -; mRNA.
RefSeq; NP_001006219.1; NM_001006219.1.
UniGene; Gga.4550; -.
ProteinModelPortal; Q5ZMT0; -.
SMR; Q5ZMT0; -.
BioGrid; 678887; 2.
IntAct; Q5ZMT0; 1.
STRING; 9031.ENSGALP00000004182; -.
PaxDb; Q5ZMT0; -.
PRIDE; Q5ZMT0; -.
Ensembl; ENSGALT00000039926; ENSGALP00000039133; ENSGALG00000002661.
GeneID; 417554; -.
KEGG; gga:417554; -.
CTD; 7531; -.
eggNOG; KOG0841; Eukaryota.
eggNOG; COG5040; LUCA.
GeneTree; ENSGT00760000119116; -.
HOGENOM; HOG000240379; -.
HOVERGEN; HBG050423; -.
InParanoid; Q5ZMT0; -.
KO; K06630; -.
OrthoDB; EOG091G0VKY; -.
PhylomeDB; Q5ZMT0; -.
Reactome; R-GGA-1445148; Translocation of GLUT4 to the plasma membrane.
Reactome; R-GGA-2028269; Signaling by Hippo.
Reactome; R-GGA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-GGA-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-GGA-3371511; HSF1 activation.
Reactome; R-GGA-380259; Loss of Nlp from mitotic centrosomes.
Reactome; R-GGA-380270; Recruitment of mitotic centrosome proteins and complexes.
Reactome; R-GGA-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-GGA-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-GGA-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-GGA-8854518; AURKA Activation by TPX2.
Reactome; R-GGA-8876198; RAB GEFs exchange GTP for GDP on RABs.
PRO; PR:Q5ZMT0; -.
Proteomes; UP000000539; Chromosome 19.
Bgee; ENSGALG00000002661; -.
ExpressionAtlas; Q5ZMT0; baseline and differential.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0005246; F:calcium channel regulator activity; IEA:Ensembl.
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: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: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:1901016; P:regulation of potassium ion transmembrane transporter activity; IEA:Ensembl.
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;
Acetylation; Complete proteome; Cytoplasm; Nucleus;
Reference proteome.
CHAIN 1 255 14-3-3 protein epsilon. {ECO:0000305}.
/FTId=PRO_0000223506.
SITE 57 57 Interaction with phosphoserine on
interacting protein. {ECO:0000250}.
SITE 130 130 Interaction with phosphoserine on
interacting protein. {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P62262}.
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


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