Q80TY0 · FNBP1_MOUSE
- ProteinFormin-binding protein 1
- GeneFnbp1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids616 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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 act as a link between RND2 signaling and regulation of the actin cytoskeleton. May be required for the lysosomal retention of FASLG/FASL (By similarity).
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 166 | Mediates end-to-end attachment of dimers | ||||
Sequence: K |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cell cortex | |
Cellular Component | clathrin-coated pit | |
Cellular Component | cytoplasmic vesicle | |
Cellular Component | cytoskeleton | |
Cellular Component | lysosome | |
Cellular Component | plasma membrane | |
Molecular Function | identical protein binding | |
Molecular Function | lipid binding | |
Biological Process | endocytosis | |
Biological Process | nervous system development | |
Biological Process | signal transduction |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFormin-binding protein 1
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ80TY0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Note: Enriched in cortical regions coincident with F-actin. Also localizes to endocytic vesicles and lysosomes.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000261431 | 1-616 | Formin-binding protein 1 | |||
Sequence: MSWGTELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTACKAFLSTLNEMNDYAGQHEVISENMTSQITVDLMRYVQELKQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINVTKADVEKARQQAQIRQQMAEDSKADYSLILQRFNQEQWEYYHTHIPNIFQKIQEMEERRIVRIGESMKTYAEVDRQVIPIIGKCLDGIVKAAESIDQKNDSQLVVEAYKSGFEPPGDIEFEDYTQPMKRTVSDNSLSSSKEGKPELRFGGKSRGKLWPFIKKNKLMSLLTSPHQPPPPPPASASPSAVPNGPQSPKQPKEPLSHRFNEFMTSKPKIHCFRSLKRGLSLKLGVTPEDFSNFPPEQRRKKLQQKVDDLNREIQKETDQRDAITKMKDVYLKNPQMGDPASLDQKLTEVTQNIEKLRLEAQKFEAWLAEVEGRLPARSEQARRQSGLYDGQTHQTVTNCAQDRESPDGSYTEEQSQESEHKVLAPDFDDEFDDEEPLPAIGTCKALYTFEGQNEGTISVVEGETLSVIEEDKGDGWTRIRRNEDEEGYVPTSYVEVYLDKNAKGS | ||||||
Modified residue | 66 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 110 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 296 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 299 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 348 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 358 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 496 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 499 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 520 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Homodimerizes, the dimers can polymerize end-to-end to form filamentous structures. Interacts specifically with GTP-bound RND2 and CDC42. Interacts with AKAP9, ARHGAP17, DAAM1, DIAPH1, DIAPH2, DNM1, DNM2, DNM3, FASLG/FASL, microtubules, PDE6G, SNX2 and WASL/N-WASP. May interact with TNKS (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, coiled coil, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-79 | Required for self-association and induction of membrane tubulation | ||||
Sequence: MSWGTELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTACKAFLSTLNE | ||||||
Domain | 1-264 | F-BAR | ||||
Sequence: MSWGTELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTACKAFLSTLNEMNDYAGQHEVISENMTSQITVDLMRYVQELKQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINVTKADVEKARQQAQIRQQMAEDSKADYSLILQRFNQEQWEYYHTHIPNIFQKIQEMEERRIVRIGESMKTYAEVDRQVIPIIGKCLDGIVKAAESIDQKND | ||||||
Region | 1-334 | Interaction with microtubules | ||||
Sequence: MSWGTELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTACKAFLSTLNEMNDYAGQHEVISENMTSQITVDLMRYVQELKQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINVTKADVEKARQQAQIRQQMAEDSKADYSLILQRFNQEQWEYYHTHIPNIFQKIQEMEERRIVRIGESMKTYAEVDRQVIPIIGKCLDGIVKAAESIDQKNDSQLVVEAYKSGFEPPGDIEFEDYTQPMKRTVSDNSLSSSKEGKPELRFGGKSRGKLWPFIKKNKLMSLLT | ||||||
Coiled coil | 67-259 | |||||
Sequence: YTACKAFLSTLNEMNDYAGQHEVISENMTSQITVDLMRYVQELKQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINVTKADVEKARQQAQIRQQMAEDSKADYSLILQRFNQEQWEYYHTHIPNIFQKIQEMEERRIVRIGESMKTYAEVDRQVIPIIGKCLDGIVKAAESI | ||||||
Region | 251-616 | Required for self-association and induction of membrane tubulation | ||||
Sequence: GIVKAAESIDQKNDSQLVVEAYKSGFEPPGDIEFEDYTQPMKRTVSDNSLSSSKEGKPELRFGGKSRGKLWPFIKKNKLMSLLTSPHQPPPPPPASASPSAVPNGPQSPKQPKEPLSHRFNEFMTSKPKIHCFRSLKRGLSLKLGVTPEDFSNFPPEQRRKKLQQKVDDLNREIQKETDQRDAITKMKDVYLKNPQMGDPASLDQKLTEVTQNIEKLRLEAQKFEAWLAEVEGRLPARSEQARRQSGLYDGQTHQTVTNCAQDRESPDGSYTEEQSQESEHKVLAPDFDDEFDDEEPLPAIGTCKALYTFEGQNEGTISVVEGETLSVIEEDKGDGWTRIRRNEDEEGYVPTSYVEVYLDKNAKGS | ||||||
Region | 280-314 | Disordered | ||||
Sequence: GDIEFEDYTQPMKRTVSDNSLSSSKEGKPELRFGG | ||||||
Compositional bias | 291-305 | Polar residues | ||||
Sequence: MKRTVSDNSLSSSKE | ||||||
Region | 332-366 | Disordered | ||||
Sequence: LLTSPHQPPPPPPASASPSAVPNGPQSPKQPKEPL | ||||||
Compositional bias | 335-360 | Pro residues | ||||
Sequence: SPHQPPPPPPASASPSAVPNGPQSPK | ||||||
Coiled coil | 398-490 | |||||
Sequence: PEDFSNFPPEQRRKKLQQKVDDLNREIQKETDQRDAITKMKDVYLKNPQMGDPASLDQKLTEVTQNIEKLRLEAQKFEAWLAEVEGRLPARSE | ||||||
Region | 399-551 | Interaction with RND2 | ||||
Sequence: EDFSNFPPEQRRKKLQQKVDDLNREIQKETDQRDAITKMKDVYLKNPQMGDPASLDQKLTEVTQNIEKLRLEAQKFEAWLAEVEGRLPARSEQARRQSGLYDGQTHQTVTNCAQDRESPDGSYTEEQSQESEHKVLAPDFDDEFDDEEPLPAI | ||||||
Domain | 403-480 | REM-1 | ||||
Sequence: NFPPEQRRKKLQQKVDDLNREIQKETDQRDAITKMKDVYLKNPQMGDPASLDQKLTEVTQNIEKLRLEAQKFEAWLAE | ||||||
Region | 487-531 | Disordered | ||||
Sequence: ARSEQARRQSGLYDGQTHQTVTNCAQDRESPDGSYTEEQSQESEH | ||||||
Region | 494-616 | Interaction with PDE6G | ||||
Sequence: RQSGLYDGQTHQTVTNCAQDRESPDGSYTEEQSQESEHKVLAPDFDDEFDDEEPLPAIGTCKALYTFEGQNEGTISVVEGETLSVIEEDKGDGWTRIRRNEDEEGYVPTSYVEVYLDKNAKGS | ||||||
Compositional bias | 495-516 | Polar residues | ||||
Sequence: QSGLYDGQTHQTVTNCAQDRES | ||||||
Region | 513-616 | Required for interaction with TNKS | ||||
Sequence: DRESPDGSYTEEQSQESEHKVLAPDFDDEFDDEEPLPAIGTCKALYTFEGQNEGTISVVEGETLSVIEEDKGDGWTRIRRNEDEEGYVPTSYVEVYLDKNAKGS | ||||||
Compositional bias | 517-531 | Basic and acidic residues | ||||
Sequence: PDGSYTEEQSQESEH | ||||||
Region | 534-616 | Interaction with DNM1 and DNM3 | ||||
Sequence: LAPDFDDEFDDEEPLPAIGTCKALYTFEGQNEGTISVVEGETLSVIEEDKGDGWTRIRRNEDEEGYVPTSYVEVYLDKNAKGS | ||||||
Domain | 549-610 | SH3 | ||||
Sequence: PAIGTCKALYTFEGQNEGTISVVEGETLSVIEEDKGDGWTRIRRNEDEEGYVPTSYVEVYLD | ||||||
Region | 549-616 | Interaction with ARHGAP17, DAAM1, DIAPH1 and DIAPH2 | ||||
Sequence: PAIGTCKALYTFEGQNEGTISVVEGETLSVIEEDKGDGWTRIRRNEDEEGYVPTSYVEVYLDKNAKGS | ||||||
Region | 552-608 | Interaction with DNM2 and WASL | ||||
Sequence: GTCKALYTFEGQNEGTISVVEGETLSVIEEDKGDGWTRIRRNEDEEGYVPTSYVEVY | ||||||
Region | 552-609 | Interaction with FASLG | ||||
Sequence: GTCKALYTFEGQNEGTISVVEGETLSVIEEDKGDGWTRIRRNEDEEGYVPTSYVEVYL |
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 (By similarity).
Sequence similarities
Belongs to the FNBP1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 5 isoforms produced by Alternative splicing.
Q80TY0-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length616
- Mass (Da)71,344
- Last updated2006-11-28 v2
- Checksum947BFCFCCA4BD1E2
Q80TY0-2
- Name2
- Differences from canonical
- 329-394: Missing
Q80TY0-3
- Name3
Q80TY0-4
- Name4
Q80TY0-5
- Name5
Computationally mapped potential isoform sequences
There are 9 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_021697 | 1-79 | in isoform 4 | |||
Sequence: Missing | ||||||
Compositional bias | 291-305 | Polar residues | ||||
Sequence: MKRTVSDNSLSSSKE | ||||||
Alternative sequence | VSP_021699 | 329-338 | in isoform 4 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_021700 | 329-338 | in isoform 5 | |||
Sequence: LMSLLTSPHQ → VLAIWTLRGL | ||||||
Alternative sequence | VSP_021698 | 329-394 | in isoform 2 and isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 335-360 | Pro residues | ||||
Sequence: SPHQPPPPPPASASPSAVPNGPQSPK | ||||||
Alternative sequence | VSP_021701 | 339-616 | in isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_021702 | 390-394 | in isoform 4 | |||
Sequence: Missing | ||||||
Compositional bias | 495-516 | Polar residues | ||||
Sequence: QSGLYDGQTHQTVTNCAQDRES | ||||||
Alternative sequence | VSP_021703 | 515 | in isoform 3 | |||
Sequence: E → ES | ||||||
Compositional bias | 517-531 | Basic and acidic residues | ||||
Sequence: PDGSYTEEQSQESEH |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK122308 EMBL· GenBank· DDBJ | BAC65590.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK052652 EMBL· GenBank· DDBJ | BAC35082.1 EMBL· GenBank· DDBJ | mRNA | ||
AK143512 EMBL· GenBank· DDBJ | BAE25408.1 EMBL· GenBank· DDBJ | mRNA | ||
AK157135 EMBL· GenBank· DDBJ | BAE33974.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK170497 EMBL· GenBank· DDBJ | BAE41836.1 EMBL· GenBank· DDBJ | mRNA | ||
AK172100 EMBL· GenBank· DDBJ | BAE42825.1 EMBL· GenBank· DDBJ | mRNA | ||
AL844546 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC003867 EMBL· GenBank· DDBJ | AAH03867.1 EMBL· GenBank· DDBJ | mRNA |