Search by BoMiProt ID - Bomi34

Primary Information

BoMiProt ID Bomi34
Protein Name 14-3-3 protein beta/alpha
Organism Bos taurus
Uniprot IdP68250
Milk FractionExosome
Ref Sequence Id NP_777219.2
Amino Acid Lenth 246
Molecular Weight 28081
Fasta Sequence
Gene Name YWHAB
Gene Id 286863
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondry Information

Presence in other biological fluids/tissue/cells abundant in the brain, comprising approximately 1% of its total soluble protein ; also present in almost all tissues, including testes, liver, and heart
Protein Function are highly conserved dimeric proteins; involvement in vital cellular processes, such as metabolism, protein trafficking, signal transduction, apoptosis and cell-cycle regulation; 14–3–3sigma is a putative tumor suppressor that is transactivated by p53 in response to DNA damage; when up-regulated, 14–3–3s induces S–G1 and G2–M cell cycle arrests; 14-3-3γ is critical for maintaining cellular homeostasis and signal transduction; 14-3-3γ is also an important factor for intracellular phosphorylation, which participates in various pathophysiological processes; 14-3-3 maintains Raf-1 in an inactive state in the absence of activation signals but promotes Raf-1 activation and stabilizes its active conformation when such signals are received; 14- 3-3 isoforms may ensure DNA damage-induced cell cycle arrest
Biochemical Properties acidic isoelectric point of 4–5; primarily binds phosphorylated ligands; also capable of interacting with unphosphorylated ligands; activation of the ExoS ADP-ribosyltransferase (12, 13) and of tryptophan hydroxylase; activator of the 43-kDa inositol polyphosphate 5-phosphatase
Significance in milk 14-3-3 sigma regulates epithelial polarity in mammary gland as found in humans; 14-3-3γ Regulates Lipopolysaccharide-Induced Inflammatory Responses and Lactation in Dairy Cow Mammary Epithelial Cells
PTMs Phosphorylation of 14-3-3 appears to modulate the function of 14-3-3 isoforms. Three phosphorylation sites have been determined in 14-3-3eta: S58, S184, and T232; in mammalian isoforms, only 14-3-3sigma and 14-3-3eta have a phosphorylation site at the corresponding 232 position
Significance of PTMs regulate ligand binding activity; phosphorylated forms of beta and eta show increased potency in the inhibition of PKC in vitro
Linking IDs Bomi391 Bomi392 Bomi393 Bomi394 Bomi395
Bibliography 1. Liu, L., Lin, Y., Liu, L., Bian, Y., Zhang, L., Gao, X., & Li, Q. (2015). 14-3-3γ Regulates Lipopolysaccharide-Induced Inflammatory Responses and Lactation in Dairy Cow Mammary Epithelial Cells by Inhibiting NF-κB and MAPKs and Up-Regulating mTOR Signaling. International Journal of Molecular Sciences, 16(7), 16622–16641.
2. Danes, C. G., Wyszomierski, S. L., Lu, J., Neal, C. L., Yang, W., & Yu, D. (2008). 14-3-3 zeta down-regulates p53 in mammary epithelial cells and confers luminal filling. Cancer Research, 68(6), 1760–1767.
3. Ling, C., Zuo, D., Xue, B., Muthuswamy, S., & Muller, W. J. (2010). A novel role for 14-3-3sigma in regulating epithelial cell polarity. Genes & Development, 24(9), 947–956.
4. Megidish, T., Cooper, J., Zhang, L., Fu, H., & Hakomori, S. (1998). A novel sphingosine-dependent protein kinase (SDK1) specifically phosphorylates certain isoforms of 14-3-3 protein. The Journal of Biological Chemistry, 273(34), 21834–21845.
5. Michaud, N. R., Fabian, J. R., Mathes, K. D., & Morrison, D. K. (1995). 14-3-3 is not essential for Raf-1 function: identification of Raf-1 proteins that are biologically activated in a 14-3-3- and Ras-independent manner. Molecular and Cellular Biology, 15(6), 3390–3397.
6. Campbell, J. K., Gurung, R., Romero, S., Speed, C. J., Andrews, R. K., Berndt, M. C., & Mitchell, C. A. (1997). Activation of the 43 kDa inositol polyphosphate 5-phosphatase by 14-3-3zeta. Biochemistry, 36(49), 15363–15370.
7. Celis, J. E., Gesser, B., Rasmussen, H. H., Madsen, P., Leffers, H., Dejgaard, K., … Vandekerckhove, J. (1990). Comprehensive two‐dimensional gel protein databases offer a global approach to the analysis of human cells: The transformed amnion cells (AMA) master database and its link to genome DNA sequence data. ELECTROPHORESIS, 11(12), 989–1071.
8. Isobe, T., Ichimura, T., Sunaya, T., Okuyama, T., Takahashi, N., Kuwano, R., & Takahashi, Y. (1991). Distinct forms of the protein kinase-dependent activator of tyrosine and tryptophan hydroxylases. Journal of Molecular Biology, 217(1), 125–132.
9. Wang, W., & Shakes, D. C. (1996). Molecular evolution of the 14-3-3 protein family. Journal of Molecular Evolution, 43(4), 384–398.