FNBP1

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Formin binding protein 1
PDB rendering based on 2efl.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols FNBP1 ; KIAA0554; FBP17; MGC126804
External IDs Template:OMIM5 Template:MGI HomoloGene10445
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Formin binding protein 1, also known as FNBP1, is a human gene.[1]

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.[1]

References

  1. 1.0 1.1 "Entrez Gene: FNBP1 formin binding protein 1".

Further reading

  • Nagase T, Ishikawa K, Miyajima N; et al. (1998). "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. PMID 9628581.
  • Richnau N, Aspenström P (2001). "Rich, a rho GTPase-activating protein domain-containing protein involved in signaling by Cdc42 and Rac1". J. Biol. Chem. 276 (37): 35060–70. doi:10.1074/jbc.M103540200. PMID 11431473.
  • Fuchs U, Rehkamp G, Haas OA; et al. (2001). "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. doi:10.1073/pnas.121433898. PMID 11438682.
  • Ghadimi MP, Sanzenbacher R, Thiede B; et al. (2002). "Identification of interaction partners of the cytosolic polyproline region of CD95 ligand (CD178)". FEBS Lett. 519 (1–3): 50–8. PMID 12023017.
  • Fujita H, Katoh H, Ishikawa Y; et al. (2003). "Rapostlin is a novel effector of Rnd2 GTPase inducing neurite branching". J. Biol. Chem. 277 (47): 45428–34. doi:10.1074/jbc.M208090200. PMID 12244061.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Katoh M, Katoh M (2004). "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. PMID 12736724.
  • Fuchs U, Rehkamp GF, Slany R; et al. (2003). "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. PMID 14596906.
  • Ota T, Suzuki Y, Nishikawa T; et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Larocca MC, Shanks RA, Tian L; et al. (2004). "AKAP350 interaction with cdc42 interacting protein 4 at the Golgi apparatus". Mol. Biol. Cell. 15 (6): 2771–81. doi:10.1091/mbc.E03-10-0757. PMID 15047863.
  • Brill LM, Salomon AR, Ficarro SB; et al. (2004). "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. doi:10.1021/ac035352d. PMID 15144186.
  • Humphray SJ, Oliver K, Hunt AR; et al. (2004). "DNA sequence and analysis of human chromosome 9". Nature. 429 (6990): 369–74. doi:10.1038/nature02465. PMID 15164053.
  • Kamioka Y, Fukuhara S, Sawa H; et al. (2004). "A novel dynamin-associating molecule, formin-binding protein 17, induces tubular membrane invaginations and participates in endocytosis". J. Biol. Chem. 279 (38): 40091–9. doi:10.1074/jbc.M404899200. PMID 15252009.
  • Beausoleil SA, Jedrychowski M, Schwartz D; et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMID 15302935.
  • Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
  • Rush J, Moritz A, Lee KA; et al. (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455.
  • Zhou FL, Zhang WG, Chen G; et al. (2006). "Serological identification and bioinformatics analysis of immunogenic antigens in multiple myeloma". Cancer Immunol. Immunother. 55 (8): 910–7. doi:10.1007/s00262-005-0074-x. PMID 16193335.
  • Qian J, Chen W, Lettau M; et al. (2006). "Regulation of FasL expression: a SH3 domain containing protein family involved in the lysosomal association of FasL". Cell. Signal. 18 (8): 1327–37. doi:10.1016/j.cellsig.2005.10.015. PMID 16318909.
  • Itoh T, Erdmann KS, Roux A; et al. (2006). "Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins". Dev. Cell. 9 (6): 791–804. doi:10.1016/j.devcel.2005.11.005. PMID 16326391.
  • Tsujita K, Suetsugu S, Sasaki N; et al. (2006). "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. doi:10.1083/jcb.200508091. PMID 16418535.

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