Ywhaz(Msfs1);

14-3-3 protein zeta/delta;

Protein kinase C inhibitor protein 1(KCIP-1);Mitochondrial import stimulation factor S1 subunit;

Rat (Rattus norvegicus). 

Homodimer. Heterodimerizes with YWHAE (By similarity). Homo- and hetero-dimerization is inhibited by phosphorylation on Ser-58 (By similarity). Interacts with FOXO4, NOXA1, SSH1 and ARHGEF2. Interacts with CDK16 and with WEE1 (C-terminal). Interacts with MLF1 (phosphorylated form); the interaction retains it in the cytoplasm. Interacts with Thr-phosphorylated ITGB2. Interacts with Pseudomonas aeruginosa exoS (unphosphorylated form). Interacts with BAX; the interaction occurs in the cytoplasm. Under stress conditions, MAPK8-mediated phosphorylation releases BAX to mitochondria. Interacts with phosphorylated RAF1; the interaction is inhibited when YWHAZ is phosphorylated on Thr-232. Interacts with TP53; the interaction enhances p53 transcriptional acivity. The Ser-58 phosphorylated form inhibits this interaction and p53 transcriptional activity. Interacts with ABL1 (phosphorylated form); the interaction retains ABL1 in the cytoplasm. Interacts with AANAT ('Thr-31' phosphorylated form); the interaction modulates AANAT enzymatic activity through preventing dephosphorylation and/or proteolysis and stabilizing substrate binding. Subsequently, a second molecule of AANAT ('Ser-205' phosphorylated form), can bind the other YWHAZ monomer with similar effect. Interacts with AKT1; the interaction phosphorylates YWHAZ and modulates dimerization (By similarity). Interacts with GAB2 and SAMSN1 (By similarity). Interacts with BSPRY. Interacts with BCL2L11.

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.

Cytoplasm Melanosome Located to stage I to stage IV melanosomes.

245

N/A

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P63102

Rn.1292

P63102

PF00244

rno:25578