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

section_title =
summary_text = 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.cite web | title = Entrez Gene: FNBP1 formin binding protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23048| accessdate = ]


Further reading

citations =
*cite journal | author=Nagase T, Ishikawa K, Miyajima N, "et al." |title=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. |journal=DNA Res. |volume=5 |issue= 1 |pages= 31–9 |year= 1998 |pmid= 9628581 |doi=10.1093/dnares/5.1.31
*cite journal | author=Richnau N, Aspenström P |title=Rich, a rho GTPase-activating protein domain-containing protein involved in signaling by Cdc42 and Rac1. |journal=J. Biol. Chem. |volume=276 |issue= 37 |pages= 35060–70 |year= 2001 |pmid= 11431473 |doi= 10.1074/jbc.M103540200
*cite journal | author=Fuchs U, Rehkamp G, Haas OA, "et al." |title=The human formin-binding protein 17 (FBP17) interacts with sorting nexin, SNX2, and is an MLL-fusion partner in acute myelogeneous leukemia. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 15 |pages= 8756–61 |year= 2001 |pmid= 11438682 |doi= 10.1073/pnas.121433898
*cite journal | author=Ghadimi MP, Sanzenbacher R, Thiede B, "et al." |title=Identification of interaction partners of the cytosolic polyproline region of CD95 ligand (CD178). |journal=FEBS Lett. |volume=519 |issue= 1-3 |pages= 50–8 |year= 2002 |pmid= 12023017 |doi=10.1016/S0014-5793(02)02709-6
*cite journal | author=Fujita H, Katoh H, Ishikawa Y, "et al." |title=Rapostlin is a novel effector of Rnd2 GTPase inducing neurite branching. |journal=J. Biol. Chem. |volume=277 |issue= 47 |pages= 45428–34 |year= 2003 |pmid= 12244061 |doi= 10.1074/jbc.M208090200
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*cite journal | author=Katoh M, Katoh M |title=FNBP2 gene on human chromosome 1q32.1 encodes ARHGAP family protein with FCH, FBH, RhoGAP and SH3 domains. |journal=Int. J. Mol. Med. |volume=11 |issue= 6 |pages= 791–7 |year= 2004 |pmid= 12736724 |doi=
*cite journal | author=Fuchs U, Rehkamp GF, Slany R, "et al." |title=The formin-binding protein 17, FBP17, binds via a TNKS binding motif to tankyrase, a protein involved in telomere maintenance. |journal=FEBS Lett. |volume=554 |issue= 1-2 |pages= 10–6 |year= 2003 |pmid= 14596906 |doi=10.1016/S0014-5793(03)01063-9
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Larocca MC, Shanks RA, Tian L, "et al." |title=AKAP350 interaction with cdc42 interacting protein 4 at the Golgi apparatus. |journal=Mol. Biol. Cell |volume=15 |issue= 6 |pages= 2771–81 |year= 2004 |pmid= 15047863 |doi= 10.1091/mbc.E03-10-0757
*cite journal | author=Brill LM, Salomon AR, Ficarro SB, "et al." |title=Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry. |journal=Anal. Chem. |volume=76 |issue= 10 |pages= 2763–72 |year= 2004 |pmid= 15144186 |doi= 10.1021/ac035352d
*cite journal | author=Humphray SJ, Oliver K, Hunt AR, "et al." |title=DNA sequence and analysis of human chromosome 9. |journal=Nature |volume=429 |issue= 6990 |pages= 369–74 |year= 2004 |pmid= 15164053 |doi= 10.1038/nature02465
*cite journal | author=Kamioka Y, Fukuhara S, Sawa H, "et al." |title=A novel dynamin-associating molecule, formin-binding protein 17, induces tubular membrane invaginations and participates in endocytosis. |journal=J. Biol. Chem. |volume=279 |issue= 38 |pages= 40091–9 |year= 2004 |pmid= 15252009 |doi= 10.1074/jbc.M404899200
*cite journal | author=Beausoleil SA, Jedrychowski M, Schwartz D, "et al." |title=Large-scale characterization of HeLa cell nuclear phosphoproteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130–5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Rush J, Moritz A, Lee KA, "et al." |title=Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. |journal=Nat. Biotechnol. |volume=23 |issue= 1 |pages= 94–101 |year= 2005 |pmid= 15592455 |doi= 10.1038/nbt1046
*cite journal | author=Zhou FL, Zhang WG, Chen G, "et al." |title=Serological identification and bioinformatics analysis of immunogenic antigens in multiple myeloma. |journal=Cancer Immunol. Immunother. |volume=55 |issue= 8 |pages= 910–7 |year= 2006 |pmid= 16193335 |doi= 10.1007/s00262-005-0074-x
*cite journal | author=Qian J, Chen W, Lettau M, "et al." |title=Regulation of FasL expression: a SH3 domain containing protein family involved in the lysosomal association of FasL. |journal=Cell. Signal. |volume=18 |issue= 8 |pages= 1327–37 |year= 2006 |pmid= 16318909 |doi= 10.1016/j.cellsig.2005.10.015
*cite journal | author=Itoh T, Erdmann KS, Roux A, "et al." |title=Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins. |journal=Dev. Cell |volume=9 |issue= 6 |pages= 791–804 |year= 2006 |pmid= 16326391 |doi= 10.1016/j.devcel.2005.11.005
*cite journal | author=Tsujita K, Suetsugu S, Sasaki N, "et al." |title=Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis. |journal=J. Cell Biol. |volume=172 |issue= 2 |pages= 269–79 |year= 2006 |pmid= 16418535 |doi= 10.1083/jcb.200508091

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