Biology:FNBP1
From HandWiki
Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
Formin-binding protein 1 is a protein that in humans is encoded by the FNBP1 gene.[1][2][3]
Function
The protein encoded by this gene is a member of the formin-binding-protein family. The protein contains an N-terminal Fer/Cdc42-interacting protein 4 (CIP4) homology (FCH) domain followed by a coiled-coil domain, a proline-rich motif, a second coiled-coil domain, a Rho family protein-binding domain (RBD), and a C-terminal SH3 domain. This protein binds sorting nexin 2 (SNX2), tankyrase (TNKS), and dynamin; an interaction between this protein and formin has not been demonstrated yet in human.[3]
Interactions
FNBP1 has been shown to interact with:
References
- ↑ "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro". DNA Res 5 (1): 31–9. Aug 1998. doi:10.1093/dnares/5.1.31. PMID 9628581.
- ↑ 2.0 2.1 "The human formin-binding protein 17 (FBP17) interacts with sorting nexin, SNX2, and is an MLL-fusion partner in acute myelogeneous leukemia". Proc Natl Acad Sci U S A 98 (15): 8756–61. Jul 2001. doi:10.1073/pnas.121433898. PMID 11438682. Bibcode: 2001PNAS...98.8756F.
- ↑ 3.0 3.1 "Entrez Gene: FNBP1 formin binding protein 1". https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=23048.
- ↑ "AKAP350 interaction with cdc42 interacting protein 4 at the Golgi apparatus". Mol. Biol. Cell 15 (6): 2771–81. Jun 2004. doi:10.1091/mbc.E03-10-0757. PMID 15047863.
- ↑ "A novel dynamin-associating molecule, formin-binding protein 17, induces tubular membrane invaginations and participates in endocytosis". J. Biol. Chem. 279 (38): 40091–9. Sep 2004. doi:10.1074/jbc.M404899200. PMID 15252009.
- ↑ "Identification of interaction partners of the cytosolic polyproline region of CD95 ligand (CD178)". FEBS Lett. 519 (1–3): 50–8. May 2002. doi:10.1016/s0014-5793(02)02709-6. PMID 12023017.
- ↑ 7.0 7.1 "The formin-binding protein 17, FBP17, binds via a TNKS binding motif to tankyrase, a protein involved in telomere maintenance". FEBS Lett. 554 (1–2): 10–6. Nov 2003. doi:10.1016/s0014-5793(03)01063-9. PMID 14596906.
Further reading
- "Rich, a rho GTPase-activating protein domain-containing protein involved in signaling by Cdc42 and Rac1". J. Biol. Chem. 276 (37): 35060–70. 2001. doi:10.1074/jbc.M103540200. PMID 11431473.
- "Identification of interaction partners of the cytosolic polyproline region of CD95 ligand (CD178)". FEBS Lett. 519 (1–3): 50–8. 2002. doi:10.1016/S0014-5793(02)02709-6. PMID 12023017.
- "Rapostlin is a novel effector of Rnd2 GTPase inducing neurite branching". J. Biol. Chem. 277 (47): 45428–34. 2003. doi:10.1074/jbc.M208090200. PMID 12244061.
- "FNBP2 gene on human chromosome 1q32.1 encodes ARHGAP family protein with FCH, FBH, RhoGAP and SH3 domains". Int. J. Mol. Med. 11 (6): 791–7. 2004. doi:10.3892/ijmm.11.6.791. PMID 12736724.
- "The formin-binding protein 17, FBP17, binds via a TNKS binding motif to tankyrase, a protein involved in telomere maintenance". FEBS Lett. 554 (1–2): 10–6. 2003. doi:10.1016/S0014-5793(03)01063-9. PMID 14596906.
- "AKAP350 Interaction with cdc42 Interacting Protein 4 at the Golgi Apparatus". Mol. Biol. Cell 15 (6): 2771–81. 2004. doi:10.1091/mbc.E03-10-0757. PMID 15047863.
- "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry". Anal. Chem. 76 (10): 2763–72. 2004. doi:10.1021/ac035352d. PMID 15144186.
- "A novel dynamin-associating molecule, formin-binding protein 17, induces tubular membrane invaginations and participates in endocytosis". J. Biol. Chem. 279 (38): 40091–9. 2004. doi:10.1074/jbc.M404899200. PMID 15252009.
- "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. 2004. doi:10.1073/pnas.0404720101. PMID 15302935. Bibcode: 2004PNAS..10112130B.
- "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nat. Biotechnol. 23 (1): 94–101. 2005. doi:10.1038/nbt1046. PMID 15592455.
- "Serological identification and bioinformatics analysis of immunogenic antigens in multiple myeloma". Cancer Immunol. Immunother. 55 (8): 910–7. 2006. doi:10.1007/s00262-005-0074-x. PMID 16193335.
- "Regulation of FasL expression: a SH3 domain containing protein family involved in the lysosomal association of FasL". Cell. Signal. 18 (8): 1327–37. 2006. doi:10.1016/j.cellsig.2005.10.015. PMID 16318909.
- "Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins". Dev. Cell 9 (6): 791–804. 2006. doi:10.1016/j.devcel.2005.11.005. PMID 16326391.
- "Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis". J. Cell Biol. 172 (2): 269–79. 2006. doi:10.1083/jcb.200508091. PMID 16418535.
 |  |
