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Gene Review

FNBP1  -  formin binding protein 1

Homo sapiens

Synonyms: FBP17, Formin-binding protein 1, Formin-binding protein 17, KIAA0554, hFBP17
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Disease relevance of FNBP1

  • The t(9;11) has been described in patients with acute myeloid leukemia (AML), and two genes [AF9 (at 9p21) and FBP17 (at 9q34)] have been cloned as fusion partners of the MLL gene [1].

High impact information on FNBP1

  • The EFC domains of FBP17, CIP4, and other PCH protein family members show weak homology to the Bin-amphiphysin-Rvs (BAR) domain [2].
  • We found that FBP17 coordinated membrane deformation with actin cytoskeleton reorganization during endocytosis [2].
  • From an analysis of free-energy landscapes from atomic-level molecular dynamics simulations, the biphasic folding kinetics observed in the FBP WW domain may be traced to the ability of this WW domain to adopt two slightly different forms of packing in its hydrophobic core [3].
  • The FBP free-energy surface can be tuned between three-state and two-state kinetics by changing the temperature, by truncation of the C terminus, or by selected point mutations [4].
  • We screened a human kidney library and identified a sorting nexin, SNX2, as a protein interaction partner of FBP17 [5].

Biological context of FNBP1


Anatomical context of FNBP1


Physical interactions of FNBP1


Other interactions of FNBP1

  • TRIP10 gene encodes FNBP1 family protein with FCH, FBH, and SH3 domains [10].
  • We previously identified the formin-binding protein 17 (FBP17) as such an MLL fusion partner [9].
  • Using yeast two-hybrid and pull-down assays, we found that AKAP350 interacts with a family of structurally related proteins, including FBP17, FBP17b, and cdc42 interacting protein 4 (CIP4) [11].

Analytical, diagnostic and therapeutic context of FNBP1

  • We also detected FBP17 in the brain by immunoblotting and in situ hybridization [7].
  • We evaluated whether FBP17 and members of the Rho family interact in vivo with a yeast two-hybrid assay [5].
  • The results of the microarray analysis indicated that the increased expression of cdc42-interacting protein 4, KIAA0554 and tropomyosin 1, which are all associated with the cytoskeletal system, may be involved in the reduction of motile and invasive activity by the HOXD3-antisense gene transduction [12].
  • This protein was purified and used as antigen in ELISA and compared with other antigens, namely fibronectin-binding protein(s) (FNBP, Mr 185,000), alpha-toxin and teichoic acid [13].


  1. Identification of a novel RAS GTPase-activating protein (RASGAP) gene at 9q34 as an MLL fusion partner in a patient with de novo acute myeloid leukemia. von Bergh, A.R., Wijers, P.M., Groot, A.J., van Zelderen-Bhola, S., Falkenburg, J.H., Kluin, P.M., Schuuring, E. Genes Chromosomes Cancer (2004) [Pubmed]
  2. Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis. Tsujita, K., Suetsugu, S., Sasaki, N., Furutani, M., Oikawa, T., Takenawa, T. J. Cell Biol. (2006) [Pubmed]
  3. Integrating folding kinetics and protein function: biphasic kinetics and dual binding specificity in a WW domain. Karanicolas, J., Brooks, C.L. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  4. Tuning the free-energy landscape of a WW domain by temperature, mutation, and truncation. Nguyen, H., Jager, M., Moretto, A., Gruebele, M., Kelly, J.W. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  5. The human formin-binding protein 17 (FBP17) interacts with sorting nexin, SNX2, and is an MLL-fusion partner in acute myelogeneous leukemia. Fuchs, U., Rehkamp, G., Haas, O.A., Slany, R., Kōnig, M., Bojesen, S., Bohle, R.M., Damm-Welk, C., Ludwig, W.D., Harbott, J., Borkhardt, A. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  6. Identification and characterization of human FNBP1L gene in silico. Katoh, M., Katoh, M. Int. J. Mol. Med. (2004) [Pubmed]
  7. A novel dynamin-associating molecule, formin-binding protein 17, induces tubular membrane invaginations and participates in endocytosis. Kamioka, Y., Fukuhara, S., Sawa, H., Nagashima, K., Masuda, M., Matsuda, M., Mochizuki, N. J. Biol. Chem. (2004) [Pubmed]
  8. Identification of interaction partners of the cytosolic polyproline region of CD95 ligand (CD178). Ghadimi, M.P., Sanzenbacher, R., Thiede, B., Wenzel, J., Jing, Q., Plomann, M., Borkhardt, A., Kabelitz, D., Janssen, O. FEBS Lett. (2002) [Pubmed]
  9. The formin-binding protein 17, FBP17, binds via a TNKS binding motif to tankyrase, a protein involved in telomere maintenance. Fuchs, U., Rehkamp, G.F., Slany, R., Follo, M., Borkhardt, A. FEBS Lett. (2003) [Pubmed]
  10. Identification and characterization of TRIP8 gene in silico. Katoh, M., Katoh, M. Int. J. Mol. Med. (2003) [Pubmed]
  11. AKAP350 interaction with cdc42 interacting protein 4 at the Golgi apparatus. Larocca, M.C., Shanks, R.A., Tian, L., Nelson, D.L., Stewart, D.M., Goldenring, J.R. Mol. Biol. Cell (2004) [Pubmed]
  12. Transduction of HOXD3-antisense into human melanoma cells results in decreased invasive and motile activities. Okubo, Y., Hamada, J., Takahashi, Y., Tada, M., Tsutsumida, A., Furuuchi, K., Aoyama, T., Sugihara, T., Moriuchi, T. Clin. Exp. Metastasis (2002) [Pubmed]
  13. Detection of Staphylococcus aureus infection by enzyme-linked immunosorbent assay and immunoblotting, using high molecular weight staphylococcal proteins. Rydén, C., Yacoub, A., Kvarnström, A., Wadström, T., Maxe, I., Friman, G., Rubin, K. FEMS microbiology immunology. (1990) [Pubmed]
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