switches.ELM

Group by :Switch type Motif class Protein Enzyme Pathway Hide inferred Group Index Colouring Info Filtered: ELM:LIG_14-3-3_1 (7 hits) x

x Coloured by: Pathway evidence source
Curated inferred

x Index

	Aldosterone-regulated sodium reabsorption	PI3K-Akt signaling pathway
PI3K-Akt signaling pathway	PI3K-Akt signaling pathway

Motif

Protein

Start

End

Switch Type

Switch Subtype

Switch description

Information

Evidence

(Reactome - 2721265)
LIG_14-3-3_1	BAD_RAT	134	139	Binary	Physicochemical compatibility	Phosphorylation of S137 by RAC-alpha serine/threonine-protein kinase (Akt1) in the 14-3-3-binding motif of Bcl2 antagonist of cell death (Bad) induces binding to the 14-3-3 protein beta/alpha (YWHAB) protein. This interaction inhibits the pro-apoptotic activity of Bcl2 antagonist of cell death (Bad).	details	Curated
Aldosterone-regulated sodium reabsorption (KEGG - hsa04960)
LIG_14-3-3_1	NED4L_HUMAN	465	470	Specificity	Domain hiding	Phosphorylation of Isoform Nedd4-2a of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L) by Serine/threonine-protein kinase Sgk1 (SGK1) induces binding to 14-3-3 protein eta (YWHAH). This inhibits (whether allosterically or sterically is not known) interactions of NEDD4L via its WW domains with the PY motif in Amiloride-sensitive sodium channel subunit gamma (SCNN1G) (ENaC). As a result, ENaC does not get degraded and ENaC-mediated Na+ currents increase.	details	Inferred
PI3K-Akt signaling pathway (KEGG - hsa04151)
LIG_14-3-3_1	RAF1_HUMAN	256	261	Binary	Physicochemical compatibility	Phosphorylation of S257 in the 14-3-3-binding motif of RAF proto-oncogene serine/threonine-protein kinase (RAF1) abolishes binding of the motif, phosphorylated at S259, to 14-3-3 protein zeta/delta (YWHAZ).	details	Inferred
LIG_14-3-3_1	RAF1_HUMAN	256	261	Avidity‑sensing		Phosphorylation of two 14-3-3-binding motifs in RAF proto-oncogene serine/threonine-protein kinase (RAF1) in response to growth factors induces high-avidity binding to dimeric 14-3-3 protein zeta/delta (YWHAZ), with pS621 being the high-affinity interaction site. This interaction locks RAF proto-oncogene serine/threonine-protein kinase (RAF1) in an inhibited conformation.	details	Curated
LIG_14-3-3_1	RAF1_HUMAN	618	623	Avidity‑sensing		Phosphorylation of two 14-3-3-binding motifs in RAF proto-oncogene serine/threonine-protein kinase (RAF1) in response to growth factors induces high-avidity binding to dimeric 14-3-3 protein zeta/delta (YWHAZ), with pS621 being the high-affinity interaction site. This interaction locks RAF proto-oncogene serine/threonine-protein kinase (RAF1) in an inhibited conformation.	details	Curated
PI3K-Akt signaling pathway (KEGG - mmu04151)
LIG_14-3-3_1	BAD_MOUSE	133	138	Binary	Physicochemical compatibility	Phosphorylation of S136 in Bcl2 antagonist of cell death (Bad) by RAC-alpha serine/threonine-protein kinase (Akt1) in response to survival and growth signals such as Interleukin-3 (Il3) induces binding to 14-3-3 protein theta (Ywhaq). Binding of 14-3-3 protein theta (Ywhaq) results in dissociation of Bcl2 antagonist of cell death (Bad) from Bcl-2-like protein 1 (Bcl2l1), and thereby inhibits the pro-apoptotic activity of Bcl2 antagonist of cell death (Bad) by allowing liberated Bcl-2-like protein 1 (Bcl2l1) to exert its anti-apoptotic effect on pro-apoptotic proteins like Apoptosis regulator BAX (Bax).	details	Inferred
PI3K-Akt signaling pathway (KEGG - rno04151)
LIG_14-3-3_1	BAD_RAT	134	139	Binary	Physicochemical compatibility	Phosphorylation of S137 by RAC-alpha serine/threonine-protein kinase (Akt1) in the 14-3-3-binding motif of Bcl2 antagonist of cell death (Bad) induces binding to the 14-3-3 protein beta/alpha (YWHAB) protein. This interaction inhibits the pro-apoptotic activity of Bcl2 antagonist of cell death (Bad).	details	Curated