FNBP1

From Wikipedia, the free encyclopedia

Formin binding protein 1

PDB rendering based on 2efl.

Available structures: 2efl

Identifiers

Symbol(s)

FNBP1; KIAA0554; FBP17; MGC126804

External IDs

OMIM: 606191 MGI: 109606 HomoloGene: 10445

Gene ontology
Molecular Function:	• RNA binding • structural constituent of ribosome • lipid binding • identical protein binding
Cellular Component:	• intracellular • lysosome • ribosome • cytoskeleton • membrane
Biological Process:	• translation • endocytosis

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_015033 (mRNA)
NP_055848 (protein)

NM_001038700 (mRNA)
NP_001033789 (protein)

Location

Chr 9: 131.69 - 131.85 Mb

Chr 2: 30.86 - 30.96 Mb

Pubmed search

[1]

[2]

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]

[edit] References

^ ^a ^b Entrez Gene: FNBP1 formin binding protein 1.

[edit] 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.