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Gene Review

PEBP1  -  phosphatidylethanolamine binding protein 1

Homo sapiens

Synonyms: HCNP, HCNPpp, HEL-210, HEL-S-34, Neuropolypeptide h3, ...
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Disease relevance of PEBP1


Psychiatry related information on PEBP1


High impact information on PEBP1


Chemical compound and disease context of PEBP1


Biological context of PEBP1


Anatomical context of PEBP1


Associations of PEBP1 with chemical compounds


Physical interactions of PEBP1


Enzymatic interactions of PEBP1

  • RKIP was than identified as a protein that bound Raf and blocked its ability to phosphorylate MEK, thus earning its new name of RKIP [22].

Regulatory relationships of PEBP1

  • Immunofluorescent double staining revealed that RKIP was expressed in most beta cells and a subset of pancreatic polypeptide-expressing cells [14].
  • RKIP blocks Raf-induced phosphorylation of MEK [23].
  • Finally, these results raise the possibility that RKIP status in tumors could influence the efficacy of treatments such as poisons that stimulate the Aurora B-dependent spindle assembly checkpoint [24].
  • Subsequent to identification of its role in the Raf:MEK pathway, RKIP has been demonstrated to regulate several other signaling pathways including G-protein signaling and NF-kappaB signaling [22].
  • These findings demonstrate that RKIP overexpression regulates tumor cell sensitivity to TRAIL via inhibition of YY1, up-regulation of DR5, and modulation of apoptotic pathways [25].

Other interactions of PEBP1

  • We showed that the effects of RKIP on B-Raf functions were independent of its known inhibitory action on Raf-1 [2].
  • Previous findings implicated a negative regulatory role of the Raf-1 kinase inhibitor protein (RKIP) on the ERK1/2 pathway [13].
  • No significant correlations were observed between RKIP expression and histologic type, tumor differentiation grade, size, or estrogen receptor status [4].
  • Remarkably, RKIP, which was shown to interfere with the activation of MEK by Raf, was highly expressed in primary as well as in metastatic MCC [26].
  • Analytical solutions, relating the steady-state values of the fast varying protein concentrations and the slow varying ones, are derived and interpreted as restrictions on the regulatory role of RKIP on ERK-pathway [27].

Analytical, diagnostic and therapeutic context of PEBP1


  1. Loss of raf kinase inhibitor protein promotes cell proliferation and migration of human hepatoma cells. Lee, H.C., Tian, B., Sedivy, J.M., Wands, J.R., Kim, M. Gastroenterology (2006) [Pubmed]
  2. RKIP downregulates B-Raf kinase activity in melanoma cancer cells. Park, S., Yeung, M.L., Beach, S., Shields, J.M., Yeung, K.C. Oncogene (2005) [Pubmed]
  3. The role of Raf kinase inhibitor protein (RKIP) in health and disease. Keller, E.T., Fu, Z., Brennan, M. Biochem. Pharmacol. (2004) [Pubmed]
  4. Reduction of Raf-1 kinase inhibitor protein expression correlates with breast cancer metastasis. Hagan, S., Al-Mulla, F., Mallon, E., Oien, K., Ferrier, R., Gusterson, B., García, J.J., Kolch, W. Clin. Cancer Res. (2005) [Pubmed]
  5. Identification of RKIP as an invasion suppressor protein in nasopharyngeal carcinoma by proteomic analysis. Chen, Y., Ouyang, G.L., Yi, H., Li, M.Y., Zhang, P.F., Li, C., Li, J.L., Liu, Y.F., Chen, Z.C., Xiao, Z.Q. J. Proteome Res. (2008) [Pubmed]
  6. Raf kinase inhibitory protein regulates aurora B kinase and the spindle checkpoint. Eves, E.M., Shapiro, P., Naik, K., Klein, U.R., Trakul, N., Rosner, M.R. Mol. Cell (2006) [Pubmed]
  7. Mutant V599EB-Raf regulates growth and vascular development of malignant melanoma tumors. Sharma, A., Trivedi, N.R., Zimmerman, M.A., Tuveson, D.A., Smith, C.D., Robertson, G.P. Cancer Res. (2005) [Pubmed]
  8. Interaction of the gelsolin-derived antibacterial PBP 10 peptide with lipid bilayers and cell membranes. Bucki, R., Janmey, P.A. Antimicrob. Agents Chemother. (2006) [Pubmed]
  9. Selection and cloning of poly(rC)-binding protein 2 and Raf kinase inhibitor protein RNA activators of 2',5'-oligoadenylate synthetase from prostate cancer cells. Molinaro, R.J., Jha, B.K., Malathi, K., Varambally, S., Chinnaiyan, A.M., Silverman, R.H. Nucleic Acids Res. (2006) [Pubmed]
  10. Raf-1 kinase inhibitor protein: structure, function, regulation of cell signaling, and pivotal role in apoptosis. Odabaei, G., Chatterjee, D., Jazirehi, A.R., Goodglick, L., Yeung, K., Bonavida, B. Adv. Cancer Res. (2004) [Pubmed]
  11. Raf kinase inhibitor protein interacts with NF-kappaB-inducing kinase and TAK1 and inhibits NF-kappaB activation. Yeung, K.C., Rose, D.W., Dhillon, A.S., Yaros, D., Gustafsson, M., Chatterjee, D., McFerran, B., Wyche, J., Kolch, W., Sedivy, J.M. Mol. Cell. Biol. (2001) [Pubmed]
  12. Induction of Raf kinase inhibitor protein contributes to macrophage differentiation. Schuierer, M.M., Heilmeier, U., Boettcher, A., Ugocsai, P., Bosserhoff, A.K., Schmitz, G., Langmann, T. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  13. Inhibition of the Raf-MEK1/2-ERK1/2 signaling pathway, Bcl-xL down-regulation, and chemosensitization of non-Hodgkin's lymphoma B cells by Rituximab. Jazirehi, A.R., Vega, M.I., Chatterjee, D., Goodglick, L., Bonavida, B. Cancer Res. (2004) [Pubmed]
  14. Raf kinase inhibitory protein inhibits beta-cell proliferation. Zhang, L., Fu, Z., Binkley, C., Giordano, T., Burant, C.F., Logsdon, C.D., Simeone, D.M. Surgery (2004) [Pubmed]
  15. Reduction in Raf kinase inhibitor protein expression is associated with increased Ras-extracellular signal-regulated kinase signaling in melanoma cell lines. Schuierer, M.M., Bataille, F., Hagan, S., Kolch, W., Bosserhoff, A.K. Cancer Res. (2004) [Pubmed]
  16. A novel human phosphatidylethanolamine-binding protein resists tumor necrosis factor alpha-induced apoptosis by inhibiting mitogen-activated protein kinase pathway activation and phosphatidylethanolamine externalization. Wang, X., Li, N., Liu, B., Sun, H., Chen, T., Li, H., Qiu, J., Zhang, L., Wan, T., Cao, X. J. Biol. Chem. (2004) [Pubmed]
  17. The Raf kinase inhibitor BAY 43-9006 reduces cellular uptake of platinum compounds and cytotoxicity in human colorectal carcinoma cell lines. Heim, M., Scharifi, M., Zisowsky, J., Jaehde, U., Voliotis, D., Seeber, S., Strumberg, D. Anticancer Drugs (2005) [Pubmed]
  18. Raf kinase as a target for anticancer therapeutics. Sridhar, S.S., Hedley, D., Siu, L.L. Mol. Cancer Ther. (2005) [Pubmed]
  19. Human androgen receptor expressed in HeLa cells activates transcription in vitro. De Vos, P., Schmitt, J., Verhoeven, G., Stunnenberg, H.G. Nucleic Acids Res. (1994) [Pubmed]
  20. The Crystal Structure of a Thermophilic Glucose Binding Protein Reveals Adaptations that Interconvert Mono and Di-saccharide Binding Sites. Cuneo, M.J., Changela, A., Warren, J.J., Beese, L.S., Hellinga, H.W. J. Mol. Biol. (2006) [Pubmed]
  21. Killing two birds with one RKIP. Goel, R., Baldassare, J.J. Trends Endocrinol. Metab. (2004) [Pubmed]
  22. The biology of a prostate cancer metastasis suppressor protein: Raf kinase inhibitor protein. Keller, E.T., Fu, Z., Brennan, M. J. Cell. Biochem. (2005) [Pubmed]
  23. Raf kinase inhibitor protein: a prostate cancer metastasis suppressor gene. Keller, E.T., Fu, Z., Yeung, K., Brennan, M. Cancer Lett. (2004) [Pubmed]
  24. MAP kinase meets mitosis: A role for Raf Kinase Inhibitory Protein in spindle checkpoint regulation. Rosner, M.R. Cell division (2007) [Pubmed]
  25. Regulation of tumor cell sensitivity to TRAIL-induced apoptosis by the metastatic suppressor Raf kinase inhibitor protein via Yin Yang 1 inhibition and death receptor 5 up-regulation. Baritaki, S., Katsman, A., Chatterjee, D., Yeung, K.C., Spandidos, D.A., Bonavida, B. J. Immunol. (2007) [Pubmed]
  26. Absence of classical MAP kinase pathway signalling in Merkel cell carcinoma. Houben, R., Michel, B., Vetter-Kauczok, C.S., Pföhler, C., Laetsch, B., Wolter, M.D., Leonard, J.H., Trefzer, U., Ugurel, S., Schrama, D., Becker, J.C. J. Invest. Dermatol. (2006) [Pubmed]
  27. Reduction of nonlinear dynamic systems with an application to signal transduction pathways. Petrov, V., Nikolova, E., Wolkenhauer, O. IET systems biology (2007) [Pubmed]
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