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| Motif | Protein | Start | End | Switch Type | Switch Subtype | Switch description | Information | Evidence |
Negative regulator of sexual conjugation and meiosis - RAN1 - Schizosaccharomyces pombe (strain 972 / ATCC 24843) | ||||||||
| LIG_14-3-3_1 | MEI2_SCHPO | 435 | 440 | Avidity‑sensing | Phosphorylation of two 14-3-3-binding motifs in Meiosis protein mei2 (mei2) by Negative regulator of sexual conjugation and meiosis (ran1) induces high-avidity binding to dimeric DNA damage checkpoint protein rad24 (rad24), with pT527 being the high-affinity interaction site. | Curated | ||
RAC-alpha serine/threonine-protein kinase - AKT1 - Rattus norvegicus | ||||||||
| 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). | Curated | |
RAC-alpha serine/threonine-protein kinase - AKT1 - Homo sapiens | ||||||||
| LIG_14-3-3_1 | ATX1_HUMAN | 772 | 777 | Binary | Physicochemical compatibility | Phosphorylation of S775 by RAC-alpha serine/threonine-protein kinase (AKT1) in the 14-3-3-binding motif of Ataxin-1 (ATXN1) induces binding to the 14-3-3 protein zeta/delta (YWHAZ) protein. | Curated | |
| 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. | Curated | ||
| LIG_14-3-3_1 | FOXO4_HUMAN | 29 | 34 | Avidity‑sensing | Phosphorylation of two 14-3-3-binding motifs in Foxo4 by PKB induces binding of 14-3-3 dimer. In the nucleus, this blocks binding to DNA, while in the cytoplasm it blocks reimport of Foxo4 into the nucleus by blocking its Nuclear Localisation Signal (NLS). Since binding of 14-3-3 to a single motif occurs with an affinity similar to the affinity of Foxo4 for DNA, multivalent binding of 14-3-3 dimer is required for efficient inhibition of DNA binding. | Curated | ||
RAC-alpha serine/threonine-protein kinase - AKT1 - Mus musculus | ||||||||
| 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). | Curated | |
Serine/threonine-protein kinase Chk2 - CHEK2 - Homo sapiens | ||||||||
| LIG_14-3-3_1 | MDM4_HUMAN | 364 | 369 | Avidity‑sensing | Optimal binding of 14-3-3 dimer to Hdmx in response to DNA damage requires phosphorylation of two 14-3-3-binding motifs by Chk2 kinase. Binding of 14-3-3 dimer is involved in inactivation of Hdmx, a negative regulator of p53, in response to DNA damage. | Curated | ||
Serine/threonine-protein kinase Sgk1 - SGK1 - Homo sapiens | ||||||||
| 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. | Curated | |