1433E_BOVIN
ID 1433E_BOVIN Reviewed; 255 AA.
AC P62261; P29360; P42655; Q3ZC40; Q63631;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=14-3-3 protein epsilon;
DE Short=14-3-3E;
GN Name=YWHAE;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Jones J.M., Niikura T., Pinke R.M., Guo W., Molday L., Leykam J.,
RA McConnell D.G.;
RT "Expression of 14-3-3 proteins in bovine retinal photoreceptors.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RX PubMed=7931346; DOI=10.1046/j.1471-4159.1994.63051908.x;
RA Tanji M., Horwitz R., Rosenfeld G., Waymire J.C.;
RT "Activation of protein kinase C by purified bovine brain 14-3-3: comparison
RT with tyrosine hydroxylase activation.";
RL J. Neurochem. 63:1908-1916(1994).
CC -!- FUNCTION: Adapter protein implicated in the regulation of a large
CC spectrum of both general and specialized signaling pathways
CC (PubMed:7931346). Binds to a large number of partners, usually by
CC recognition of a phosphoserine or phosphothreonine motif
CC (PubMed:7931346). Binding generally results in the modulation of the
CC activity of the binding partner (PubMed:7931346). Positively regulates
CC phosphorylated protein HSF1 nuclear export to the cytoplasm (By
CC similarity). {ECO:0000250|UniProtKB:P62258,
CC ECO:0000269|PubMed:7931346}.
CC -!- SUBUNIT: Homodimer. Heterodimerizes with YWHAZ. Interacts with NDEL1,
CC ARHGEF28 and TIAM2. Interacts with ABL1 (phosphorylated form); the
CC interaction retains it in the cytoplasm. Weakly interacts with CDKN1B.
CC Interacts with GAB2. Interacts with phosphorylated GRB10. Interacts
CC with PKA-phosphorylated AANAT. Interacts with the phosphorylated (by
CC AKT1) form of SRPK2. Interacts with KSR1. Interacts with the 'Thr-369'
CC phosphorylated form of DAPK2 (By similarity). Interacts with DENND1A
CC (By similarity). Interacts with PI4KB, TBC1D22A and TBC1D22B. Interacts
CC with the phosphorylated (by AKT1) form of SRPK2. Interacts with TIAM2.
CC Interacts with the 'Ser-1134' and 'Ser-1161' phosphorylated form of
CC SOS1. Interacts with ZFP36 (via phosphorylated form) (By similarity).
CC Interacts with SLITRK1 (By similarity). Interacts with HSF1 (via
CC phosphorylated form); this interaction promotes HSF1 sequestration in
CC the cytoplasm in a ERK-dependent manner (By similarity). Interacts with
CC RIPOR2 (By similarity). Interacts with KLHL22; required for the nuclear
CC localization of KLHL22 upon amino acid starvation (By similarity).
CC Interacts with CRTC1 (By similarity). Interacts with CRTC2 (probably
CC when phosphorylated at 'Ser-171') (By similarity). Interacts with CRTC3
CC (probably when phosphorylated at 'Ser-162' and/or 'Ser-273') (By
CC similarity). Interacts with ATP2B1 and ATP2B3; this interaction
CC inhibits calcium-transporting ATPase activity (By similarity).
CC Interacts with MEFV (By similarity). {ECO:0000250|UniProtKB:P62258,
CC ECO:0000250|UniProtKB:P62259, ECO:0000250|UniProtKB:P62260}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P62258}. Cytoplasm
CC {ECO:0000250|UniProtKB:P62258}. Melanosome
CC {ECO:0000250|UniProtKB:P62258}.
CC -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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DR EMBL; AF043735; AAC61927.1; -; mRNA.
DR EMBL; BC102928; AAI02929.1; -; mRNA.
DR RefSeq; NP_776916.1; NM_174491.3.
DR AlphaFoldDB; P62261; -.
DR SMR; P62261; -.
DR BioGRID; 159403; 1.
DR MINT; P62261; -.
DR STRING; 9913.ENSBTAP00000007442; -.
DR PaxDb; P62261; -.
DR PeptideAtlas; P62261; -.
DR PRIDE; P62261; -.
DR Ensembl; ENSBTAT00000007442; ENSBTAP00000007442; ENSBTAG00000005664.
DR GeneID; 282125; -.
DR KEGG; bta:282125; -.
DR CTD; 7531; -.
DR VEuPathDB; HostDB:ENSBTAG00000005664; -.
DR VGNC; VGNC:37045; YWHAE.
DR eggNOG; KOG0841; Eukaryota.
DR GeneTree; ENSGT01050000244964; -.
DR HOGENOM; CLU_058290_0_0_1; -.
DR InParanoid; P62261; -.
DR OMA; IPCATTG; -.
DR OrthoDB; 1176818at2759; -.
DR TreeFam; TF102003; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000005664; Expressed in Ammon's horn and 104 other tissues.
DR ExpressionAtlas; P62261; baseline.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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:0050815; F:phosphoserine residue binding; IDA:UniProtKB.
DR GO; GO:0050816; F:phosphothreonine residue binding; IDA:UniProtKB.
DR GO; GO:1990051; P:activation of protein kinase C activity; IDA:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
DR GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB.
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:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..255
FT /note="14-3-3 protein epsilon"
FT /id="PRO_0000058617"
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:0000250|UniProtKB:P62258"
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:0000250|UniProtKB:P62260"
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:0000250|UniProtKB:P62260"
FT MOD_RES 137
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P62260"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62258"
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"
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
