Aliases for YWHAB Gene
- Tyrosine 3-Monooxygenase/Tryptophan 5-Monooxygenase Activation Protein, Beta 2 3
- Tyrosine 3-Monooxygenase/Tryptophan 5-Monooxygenase Activation Protein, Alpha Polypeptide 2 3
- Tyrosine 3-Monooxygenase/Tryptophan 5-Monooxygenase Activation Protein, Beta Polypeptide 2 3
- Protein Kinase C Inhibitor Protein 1 3 4
- 14-3-3 Alpha 2 3
- Protein 1054 3 4
- KCIP-1 3 4
- Protein Kinase C Inhibitor Protein-1 3
- Brain Protein 14-3-3, Beta Isoform 3
External Ids for YWHAB Gene
Previous Symbols for YWHAB Gene
This gene encodes a protein belonging to the 14-3-3 family of proteins, members of which mediate signal transduction by binding to phosphoserine-containing proteins. This highly conserved protein family is found in both plants and mammals. The encoded protein has been shown to interact with RAF1 and CDC25 phosphatases, suggesting that it may play a role in linking mitogenic signaling and the cell cycle machinery. Two transcript variants, which encode the same protein, have been identified for this gene. [provided by RefSeq, Jul 2008]
GeneCards Summary for YWHAB Gene
YWHAB (Tyrosine 3-Monooxygenase/Tryptophan 5-Monooxygenase Activation Protein, Beta) is a Protein Coding gene. Among its related pathways are PI3K-Akt signaling pathway and PI-3K cascade. GO annotations related to this gene include enzyme binding and protein C-terminus binding. An important paralog of this gene is YWHAZ.
UniProtKB/Swiss-Prot for YWHAB Gene
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. Negative regulator of osteogenesis. Blocks the nuclear translocation of the phosphorylated form (by AKT1) of SRPK2 and antagonizes its stimulatory effect on cyclin D1 expression resulting in blockage of neuronal apoptosis elicited by SRPK2.
14.3.3 proteins are a group of highly conserved proteins that are involved in many vital cellular processes such as metabolism, protein trafficking, signal transduction, apoptosis and cell cycle regulation. 14.3.3 proteins are phospho-serine/phospho-threonine binding proteins that have a diverse array of partners including transcription factors, biosynthetic enzymes, cytoskeletal proteins, signalling molecules, apoptosis factors and tumour suppressors. The 14.3.3 family consists of 7 isoforms; beta, gamma, epsilon, sigma, zeta, tau and eta. 14.3.3 proteins are ubiquitously expressed and self assemble into homo- and heterodimers, with the exception of 14.3.3sigma, which exclusively forms homodimers and is found in cells of epithelial origin only. Each monomer contains an independent ligand-binding site, thus the 14.3.3 dimer can interact with two target proteins simultaneously. 14.3.3 proteins are highly rigid structures and ligand binding can induce conformational changes that alter the stability and/or catalytic activity of the ligand. Furthermore, 14.3.3 protein binding can physically occlude sequence-specific or structural motifs on the target that prevent molecular interactions and/or modulate the accessibility of a target protein to modifying enzymes such as kinases, phosphatases and proteases. In addition, 14.3.3 proteins can act as a scaffold molecule to anchor target proteins within close proximity of one another. 14.3.3 proteins represent an integration point for proliferative, survival, apoptotic and stress signalling pathways. Members of the 14.3.3 protein family enhance the activity of many proteins with proliferative and/or survival functions, such as Raf kinases, and antagonise the activity of proteins that promote cell death and senescence, such as Bad, Bim and Bax. In contrast, 14.3.3sigma acts as a tumour suppressor and its expression is upregulated coordinately with p53 and BRAC1. This isoform sequesters cdk1-cyclin B complexes in the cytoplasm, and thus delays cell cycle progression. 14.3.3sigma is also a crucial regulator of translation during mitosis. Because many 14.3.3 interactions are phosphorylation dependent, 14.3.3 proteins have been integrated into the core regulatory pathways that are crucial for normal growth and development. 14.3.3 proteins are directly involved in cellular processes such as cytokinesis, cell-contact inhibition, anchorage-independent growth and cell adhesion, and it is these pathways that often become dysregulated in disease states such as cancer.