ATG9A	protein	Q7Z3C6	UNIPROT	YWHAE	protein	P62258	UNIPROT	up-regulates activity	binding			9606									25266655	t		miannu	Our data suggest that the localization of mammalian Atg9A to autophagosomes requires phosphorylation on the C terminus of Atg9A at S761, which creates a 14-3-3ζ docking site. Under basal conditions, this phosphorylation is maintained at a low level and is dependent on both ULK1 and AMPK.	SIGNOR-266368	0.2	
YWHAE	protein	P62258	UNIPROT	TBP	protein	P20226	UNIPROT	up-regulates activity	binding												10449590	t		lperfetto	The in vitro binding with general transcription factors TBP and TFIIB together with its nuclear location provide evidence supporting a role for 14-3-3 proteins as transcriptional activators or coactivators when part of a DNA binding complex.	SIGNOR-262834	0.354	
YWHAE	protein	P62258	UNIPROT	NDEL1	protein	Q9GZM8	UNIPROT	up-regulates activity	binding			9606	BTO:0000938								17202468	t		miannu	14-3-3epsilon is involved in the proper localization of NUDEL and LIS1 in axons. 14-3-3ε binds to NUDEL phosphorylated by cyclin-dependent kinase (cdk5) and maintains NUDEL phosphorylation. Deficiency of 14-3-3ε causes mislocalization of the NUDEL/LIS1 complex from axons, suggesting that 14-3-3ε regulates the axonal targeting of the NUDEL/LIS1 complex by sustaining NUDEL phosphorylation	SIGNOR-252160	0.649	
YWHAE	protein	P62258	UNIPROT	NEFL	protein	P07196	UNIPROT	down-regulates activity	binding			9606									23230147	t		miannu	These results suggest the important role of 14-3-3 in the dynamic regulation of NF-L assembly, and in the capacity to prevent the formation of NF-L aggregates. all seven isoforms specifically interacted with NF-L, but not NF-M or NF-H. specific interaction of 14-3-3 proteins with phosphorylated NF-L subunits also indicated the role of 14-3-3 and NF-L phosphorylation in the disassembly of neurofilaments. What is more, binding of 14-3-3 to phosphorylated NF-L subunits may prevent the dephosphorylation of these subunits by phosphatases, maintaining the hyperphosphorylation state of the subunits, which facilitates the disassembly of neurofilaments.	SIGNOR-252398	0.281	
YWHAE	protein	P62258	UNIPROT	CDKN1B	protein	P46527	UNIPROT	down-regulates	binding			9606									12042314	t		miannu	14-3-3_, 14-3-3_, and 14-3-3_ (but not 14-3-3_ and 14-3-3_) could form a complex with p27kip1 / we discovered that akt-mediated p27kip1phosphorylation directly induces p27kip1binding to 14-3-3 and cytoplasmic localization through phosphorylating the newly identified thr198residue.	SIGNOR-88297	0.513	
YWHAE	protein	P62258	UNIPROT	GRIN2C	protein	Q14957	UNIPROT	up-regulates quantity by stabilization	binding			10090									19477150	t		miannu	Here, we demonstrate that PKB/Akt directly phosphorylates NR2C on serine 1096 (S1096). In addition, we identify 14-3-3epsilon as an NR2C interactor, whose binding is dependent on S1096 phosphorylation. These data are all consistent with a model in which NR1 and NR2C oligomerize, PKB phosphorylates S1096, and 14-3-3ε binds to phosphorylated NR2C thereby promoting NR2C-containing NMDA receptor surface expression in cerebellar granule cells. 	SIGNOR-262622	0.323