Human Gene FNBP1 (ENST00000446176.7) from GENCODE V44
Description: Homo sapiens formin binding protein 1 (FNBP1), transcript variant 1, mRNA. (from RefSeq NM_015033) RefSeq Summary (NM_015033): 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. [provided by RefSeq, Jul 2008]. Gencode Transcript: ENST00000446176.7 Gencode Gene: ENSG00000187239.19 Transcript (Including UTRs) Position: hg38 chr9:129,887,187-130,043,189 Size: 156,003 Total Exon Count: 17 Strand: - Coding Region Position: hg38 chr9:129,890,539-130,042,975 Size: 152,437 Coding Exon Count: 17
ID:FNBP1_HUMAN DESCRIPTION: RecName: Full=Formin-binding protein 1; AltName: Full=Formin-binding protein 17; Short=hFBP17; FUNCTION: May act as a link between RND2 signaling and regulation of the actin cytoskeleton (By similarity). Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during the late stage of clathrin-mediated endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also enhances actin polymerization via the recruitment of WASL/N-WASP, which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. May be required for the lysosomal retention of FASLG/FASL. SUBUNIT: Interacts specifically with GTP-bound RND2 and CDC42. Interacts with PDE6G and microtubules (By similarity). Homodimerizes, the dimers can polymerize end-to-end to form filamentous structures. Interacts with AKAP9, ARHGAP17, DAAM1, DIAPH1, DIAPH2, DNM1, DNM2, DNM3, FASLG/FASL, SNX2 and WASL/N- WASP. May interact with TNKS. INTERACTION: Self; NbExp=3; IntAct=EBI-1111248, EBI-1111248; Q05193:DNM1; NbExp=5; IntAct=EBI-1111248, EBI-713135; O95166:GABARAP; NbExp=2; IntAct=EBI-1111248, EBI-712001; O60749:SNX2; NbExp=4; IntAct=EBI-1111248, EBI-1046690; O95271:TNKS; NbExp=4; IntAct=EBI-1111248, EBI-1105254; SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. Lysosome. Cytoplasmic vesicle. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Membrane, clathrin-coated pit. Note=Enriched in cortical regions coincident with F-actin. Also localizes to endocytic vesicles and lysosomes. TISSUE SPECIFICITY: 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. DOMAIN: The F-BAR domain binds the phospholipid membrane with its concave surface. The end-to-end polymerization of dimers of these domains provides a curved surface that fits best membranes with around 600 A diameter, and may drive tubulation. DISEASE: Note=A chromosomal aberration involving FNBP1 is found in acute leukemias. Translocation t(9;11)(q34;q23) with MLL. The relatively low incidence of the MLL-FNBP1 fusion protein in acute leukemia may reflect the marginal capacity of this fusion protein to induce cellular transformation. SIMILARITY: Belongs to the FNBP1 family. SIMILARITY: Contains 1 FCH domain. SIMILARITY: Contains 1 REM (Hr1) repeat. SIMILARITY: Contains 1 SH3 domain. SEQUENCE CAUTION: Sequence=AAH62463.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence; Sequence=AAK49824.1; Type=Erroneous initiation; Sequence=BAA25480.1; Type=Erroneous initiation; Sequence=BAA91451.1; Type=Erroneous initiation; Sequence=CAI12149.1; Type=Erroneous gene model prediction; Sequence=CAI12150.1; Type=Erroneous gene model prediction; Sequence=CAI13910.1; Type=Erroneous gene model prediction; Sequence=CAI13911.1; Type=Erroneous gene model prediction; WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/FBP17ID353.html";
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q96RU3
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.