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FLASH GENE

Symbol

FNBP1

contributors: npt/mct - updated : 14-01-2015

HGNC name	formin binding protein 1
HGNC id	17069

FLASH GENE DNA RNA EXPRESSION PROTEIN DISORDER ANIMAL & CELL MODELS

EXPRESSION

Type	ubiquitous

expressed in	(based on citations)
organ(s)	System Organ level 1 Organ level 2 Organ level 3 Organ level 4 Level Pubmed Species Stage Rna symbol blood / hematopoietic spleen       highly Cardiovascular heart       highly Nervous brain limbic system hippocampus   predominantly Rattus norvegicus Fetal Reproductive male system prostate     highly Urinary kidney       highly

cell lineage

cell lines

fluid/secretion

at STAGE

PROTEIN

PHYSICAL PROPERTIES

STRUCTURE

motifs/domains	N terminal region homologous to the cell division cycle protein CDC15, EFC (extended FER-CIP4 homology)/F-BAR (FER-CIP4 homology and Bin-amphiphysin-Rvs) domain previously shown to have membrane binding and deformation activities ((Tsuboi 2009)
	two coiled-coil domains
	a proline rich motif
	a FBH (FNBP1 AND 2 homology), and HR1 (PRKC related homology) domains
	an ARHN-binding domain localized between FCH and SH3 domains
	an IN, insert region
	a SH3 (Src homology 3) domain at the carboxyl terminus

HOMOLOGY

interspecies	homolog to S.pombe cdc15
	ortholog to rattus Fnbp1
	ortholog to murine Fnbp1

Homologene

FAMILY	Rho gene family
	FNBP1 family

CATEGORY

regulatory , RNA associated

SUBCELLULAR LOCALIZATION	intracellular
	intracellular,cytoplasm,organelle,lysosome
	intracellular,cytoplasm,cytosolic,vesicle
	intracellular,cytoplasm,cytoskeleton,microtubule
	intracellular,nucleus
text	FBP17/MLL fusion gene only in the nucleus
	FBP17 only in the cytoplasm (directly binds to microtubules)

basic FUNCTION	inducing neurite branching in response to ARHN
	regulating endocytosis by forming vesicotubular structures and involved in dynamin-mediated endocytosis in both a clathrin-dependent and -independent manner
	recruits WAS, WIPF1, and dynamin-2 to the plasma membrane and that this recruitment is necessary for the formation of podosomes and phagocytic cups (Tsuboi 2009)
	facilitates membrane deformation and actin polymerization to occur simultaneously at the same membrane sites, which mediates a common molecular step in the formation of podosomes and phagocytic cups (Tsuboi 2009)
	stimulating curvature-dependent actin polymerization with WAS-WIPF complex (Takano 2008)
	recruited to clathrin-coated pits in the late stage of clathrin-mediated endocytosis, indicating its physiological role (Shimada (2007)
	has a critical role in the process of bladder tumor cell invasion by mediating invadopodia formation
	FNBP1 and RND2 cooperatively regulate spine density
	plays a key role in spine formation through the regulation of membrane dynamics
	has emerged as a crucial factor linking the plasma membrane to WAS-mediated actin polymerization
	self-assembly of FNBP1 at the podosomal membrane initiates actin polymerization, whereas the clustering of PSTPIP2 has an opposite effect

CELLULAR PROCESS	protein, translation/synthesis
	cell organization/biogenesis

PHYSIOLOGICAL PROCESS

PATHWAY

metabolism

signaling

a component

forming of a complex also including DNM2, TRIP10, WAS in the early stage of endocytosis

INTERACTION

DNA

RNA

small molecule

protein	SNX2
	first effector of ARHN, regulating neurite branch formation
	coupling membrane deformation to actin cytoskeleton reorganization in various cellulkar processes
	interacting with TNKS via a special TNKS-binding motif
	binding to WAS via the SH3 Domain
	binding to AKAP9, influencing the maintenance of Golgi apparatus
	interacting with DNM1 and regulating endocytosis by forming vesicotubular structures
	bind to neural Wiskott-Aldrich syndrome protein (WAS)which links phosphatidylinositol (4,5)-bisphosphate and the Rho family GTPase CDC42 to the Arp2/3 complex (Takano 2008)
	RND2, binds to the HR1 domain of Rapostlin (FNBP1) (enhanced the Rapostlin-induced tubular membrane invagination
	assembly of FNBP1 on the plasma membranes is antagonized by PSTPIP2, another F-BAR protein implicated in auto-inflammatory disorder
	assembly of FNBP1 is dependent on WAS, and its dissociation by WAS inhibition strongly induces a self-organization of PSTPIP2 at podosomes

cell & other

REGULATION

ASSOCIATED DISORDERS

corresponding disease(s)

Other morbid association(s)

Type Gene Modification Chromosome rearrangement Protein expression Protein Function tumoral fusion     protein chimeric fused with MLL in acute myelogemous leukemia

Susceptibility

Variant & Polymorphism

Candidate gene

Marker

Therapy target

ANIMAL & CELL MODELS