14-3-3 Recombinant Rabbit Monoclonal Antibody [JJ083-6] (ET1701-2)

UNIPROT #

P31946

PROTEIN NAME

14-3-3

SYNONYMS

14 3 3 antibody;14 3 3 protein beta antibody;14 3 3 protein beta/alpha antibody;14 3 3 protein zeta antibody;14 3 3 zeta antibody;14-3-3 protein beta/alpha antibody;14-3-3 protein/cytosolic phospholipase A2 antibody;1433B_HUMAN antibody;GW128 antibody;HS1 antibody;KCIP 1 antibody;KCIP-1 antibody;MGC111427 antibody;MGC126532 antibody;MGC138156 antibody;N-terminally processed antibody;Protein 1054 antibody;Protein kinase C inhibitor protein 1 antibody;Tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, delta polypeptide antibody;Tyrosine 3/tryptophan 5 -monooxygenase activation protein, zeta polypeptide antibody;YWHAB antibody;YWHAD antibody;YWHAZ antibody

SEQUENCE SIMILARITIES

Belongs to the 14-3-3 family.

POST-TRANSLATIONAL MODIFICATION

The alpha, brain-specific form differs from the beta form in being phosphorylated. Phosphorylated on Ser-60 by protein kinase C delta type catalytic subunit in a sphingosine-dependent fashion.

SUBCELLULAR LOCATION

Cytoplasm, Melanosome, Vacuole membrane.

FUNCTION

14-3-3 proteins are a family of conserved regulatory molecules that are expressed in all eukaryotic cells. 14-3-3 proteins have the ability to bind a multitude of functionally diverse signaling proteins, including kinases, phosphatases, and transmembrane receptors. More than 200 signaling proteins have been reported as 14-3-3 ligands. 14-3-3 proteins play an isoform-specific role in class switch recombination. They are believed to interact with the protein Activation-Induced (Cytidine) Deaminase in mediating class switch recombination. Phosphorylation of Cdc25C by CDS1 and CHEK1 creates a binding site for the 14-3-3 family of phosphoserine binding proteins. Binding of 14-3-3 has little effect on Cdc25C activity, and it is believed that 14-3-3 regulates Cdc25C by sequestering it to the cytoplasm, thereby preventing the interactions with CycB-Cdk1 that are localized to the nucleus at the G2/M transition.