Formin Binding Protein 1 (FNBP1)

FBP17

SPN	U365
HGNC	17069
MGI	109606
PubMed	14596906
RGD	621350
UniProt	Q96RU3
Wiki	FNBP1

Formin-binding protein 1 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. Very highly expressed in the epithelial cells of the gastrointestinal tract, respiratory, reproductive and urinary systems. Also highly expressed in brown adipose tissue, cardiomyocytes, enteric ganglia and glucagon producing cells of the pancreas. Expressed in germ cells of the testis and all regions of the brain.

Reference

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FEBS Lett. 519:50-58(2002) [PubMed] [Europe PMC] [Abstract]

"The formin-binding protein 17, FBP17, binds via a TNKS binding motif to tankyrase, a protein involved in telomere maintenance."
FEBS Lett. 554:10-16(2003) [PubMed] [Europe PMC] [Abstract]

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Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]

"A novel dynamin-associating molecule, formin-binding protein 17, induces tubular membrane invaginations and participates in endocytosis."
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Mol. Biol. Cell 15:2771-2781(2004) [PubMed] [Europe PMC] [Abstract]

"Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins."
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"Regulation of FasL expression: a SH3 domain containing protein family involved in the lysosomal association of FasL."
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"The diaphanous-related formin DAAM1 collaborates with the Rho GTPases RhoA and Cdc42, CIP4 and Src in regulating cell morphogenesis and actin dynamics."
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"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
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"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
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"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]

"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]

"Initial characterization of the human central proteome."
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]

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Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]

"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]

"Curved EFC/F-BAR-domain dimers are joined end to end into a filament for membrane invagination in endocytosis."
Cell 129:761-772(2007) [PubMed] [Europe PMC] [Abstract]