Q5T0N5 · FBP1L_HUMAN
- ProteinFormin-binding protein 1-like
- GeneFNBP1L
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids605 (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 endocytosis. May bind to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promote membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by activating the WASL/N-WASP-WASPIP/WIP complex, the predominant form of WASL/N-WASP in cells. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. Essential for autophagy of intracellular bacterial pathogens.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 165 | 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 | cytoplasm | |
Cellular Component | cytoplasmic vesicle | |
Cellular Component | cytoskeleton | |
Cellular Component | cytosol | |
Cellular Component | plasma membrane | |
Molecular Function | cadherin binding | |
Molecular Function | GTPase binding | |
Molecular Function | lipid binding | |
Biological Process | autophagy | |
Biological Process | cilium assembly | |
Biological Process | clathrin-dependent endocytosis | |
Biological Process | membrane invagination | |
Biological Process | plasma membrane tubulation | |
Biological Process | positive regulation of filopodium assembly | |
Biological Process | signal transduction | |
Biological Process | vesicle budding from membrane | |
Biological Process | vesicle organization | |
Biological Process | vesicle transport along actin filament |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFormin-binding protein 1-like
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ5T0N5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 441-443 | Impairs interaction with CDC42 and reduces CDC42-induced actin assembly. | ||||
Sequence: MGD → IST | ||||||
Mutagenesis | 576 | Impairs interaction with WASL and reduces CDC42-induced actin assembly. | ||||
Sequence: W → K |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 508 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000261434 | 1-605 | UniProt | Formin-binding protein 1-like | |||
Sequence: MSWGTELWDQFDSLDKHTQWGIDFLERYAKFVKERIEIEQNYAKQLRNLVKKYCPKRSSKDEEPRFTSCVAFFNILNELNDYAGQREVVAEEMAHRVYGELMRYAHDLKTERKMHLQEGRKAQQYLDMCWKQMDNSKKKFERECREAEKAQQSYERLDNDTNATKADVEKAKQQLNLRTHMADENKNEYAAQLQNFNGEQHKHFYVVIPQIYKQLQEMDERRTIKLSECYRGFADSERKVIPIISKCLEGMILAAKSVDERRDSQMVVDSFKSGFEPPGDFPFEDYSQHIYRTISDGTISASKQESGKMDAKTTVGKAKGKLWLFGKKPKPQSPPLTPTSLFTSSTPNGSQFLTFSIEPVHYCMNEIKTGKPRIPSFRSLKRGWSVKMGPALEDFSHLPPEQRRKKLQQRIDELNRELQKESDQKDALNKMKDVYEKNPQMGDPGSLQPKLAETMNNIDRLRMEIHKNEAWLSEVEGKTGGRGDRRHSSDINHLVTQGRESPEGSYTDDANQEVRGPPQQHGHHNEFDDEFEDDDPLPAIGHCKAIYPFDGHNEGTLAMKEGEVLYIIEEDKGDGWTRARRQNGEEGYVPTSYIDVTLEKNSKGS | |||||||
Modified residue (large scale data) | 2 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 291 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 293 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 295 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 295 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 300 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 488 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 488 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 489 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 496 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 501 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 501 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 505 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 505 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 506 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 507 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Homodimerizes, the dimers can polymerize end-to-end to form filamentous structures (By similarity).
Interacts with GTP-bound CDC42 (PubMed:15260990).
Interacts with DAAM1, DIAPH1, DIAPH2, DNM1, DNM2 and WASL/N-WASP (PubMed:16326391, PubMed:16418535, PubMed:16630611).
Interacts with ATG3 (PubMed:19342671).
Interacts (via SH3 domain) with ABI1, WASF2, CDC42 and WIPF1 (PubMed:19798448).
Interacts with GTP-bound CDC42 (PubMed:15260990).
Interacts with DAAM1, DIAPH1, DIAPH2, DNM1, DNM2 and WASL/N-WASP (PubMed:16326391, PubMed:16418535, PubMed:16630611).
Interacts with ATG3 (PubMed:19342671).
Interacts (via SH3 domain) with ABI1, WASF2, CDC42 and WIPF1 (PubMed:19798448).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q5T0N5 | ADAM8 P78325 | 2 | EBI-714058, EBI-2625954 | |
BINARY | Q5T0N5 | DAAM1 Q9Y4D1 | 2 | EBI-714058, EBI-2817289 | |
BINARY | Q5T0N5 | FNBP1 Q96RU3 | 2 | EBI-714058, EBI-1111248 | |
XENO | Q5T0N5-3 | espF(U) Q8X482 | 3 | EBI-4403262, EBI-22229752 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, coiled coil, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-263 | F-BAR | ||||
Sequence: MSWGTELWDQFDSLDKHTQWGIDFLERYAKFVKERIEIEQNYAKQLRNLVKKYCPKRSSKDEEPRFTSCVAFFNILNELNDYAGQREVVAEEMAHRVYGELMRYAHDLKTERKMHLQEGRKAQQYLDMCWKQMDNSKKKFERECREAEKAQQSYERLDNDTNATKADVEKAKQQLNLRTHMADENKNEYAAQLQNFNGEQHKHFYVVIPQIYKQLQEMDERRTIKLSECYRGFADSERKVIPIISKCLEGMILAAKSVDERRD | ||||||
Coiled coil | 66-258 | |||||
Sequence: FTSCVAFFNILNELNDYAGQREVVAEEMAHRVYGELMRYAHDLKTERKMHLQEGRKAQQYLDMCWKQMDNSKKKFERECREAEKAQQSYERLDNDTNATKADVEKAKQQLNLRTHMADENKNEYAAQLQNFNGEQHKHFYVVIPQIYKQLQEMDERRTIKLSECYRGFADSERKVIPIISKCLEGMILAAKSV | ||||||
Region | 245-535 | Interaction with CDC42 | ||||
Sequence: SKCLEGMILAAKSVDERRDSQMVVDSFKSGFEPPGDFPFEDYSQHIYRTISDGTISASKQESGKMDAKTTVGKAKGKLWLFGKKPKPQSPPLTPTSLFTSSTPNGSQFLTFSIEPVHYCMNEIKTGKPRIPSFRSLKRGWSVKMGPALEDFSHLPPEQRRKKLQQRIDELNRELQKESDQKDALNKMKDVYEKNPQMGDPGSLQPKLAETMNNIDRLRMEIHKNEAWLSEVEGKTGGRGDRRHSSDINHLVTQGRESPEGSYTDDANQEVRGPPQQHGHHNEFDDEFEDDD | ||||||
Coiled coil | 392-484 | |||||
Sequence: LEDFSHLPPEQRRKKLQQRIDELNRELQKESDQKDALNKMKDVYEKNPQMGDPGSLQPKLAETMNNIDRLRMEIHKNEAWLSEVEGKTGGRGD | ||||||
Domain | 397-474 | REM-1 | ||||
Sequence: HLPPEQRRKKLQQRIDELNRELQKESDQKDALNKMKDVYEKNPQMGDPGSLQPKLAETMNNIDRLRMEIHKNEAWLSE | ||||||
Compositional bias | 476-493 | Basic and acidic residues | ||||
Sequence: EGKTGGRGDRRHSSDINH | ||||||
Region | 476-539 | Disordered | ||||
Sequence: EGKTGGRGDRRHSSDINHLVTQGRESPEGSYTDDANQEVRGPPQQHGHHNEFDDEFEDDDPLPA | ||||||
Compositional bias | 494-514 | Polar residues | ||||
Sequence: LVTQGRESPEGSYTDDANQEV | ||||||
Region | 522-605 | Interaction with DNM1 | ||||
Sequence: GHHNEFDDEFEDDDPLPAIGHCKAIYPFDGHNEGTLAMKEGEVLYIIEEDKGDGWTRARRQNGEEGYVPTSYIDVTLEKNSKGS | ||||||
Domain | 538-599 | SH3 | ||||
Sequence: PAIGHCKAIYPFDGHNEGTLAMKEGEVLYIIEEDKGDGWTRARRQNGEEGYVPTSYIDVTLE | ||||||
Region | 541-597 | Interaction with DNM2 and WASL | ||||
Sequence: GHCKAIYPFDGHNEGTLAMKEGEVLYIIEEDKGDGWTRARRQNGEEGYVPTSYIDVT | ||||||
Region | 541-605 | Interaction with DAAM1, DIAPH1 and DIAPH2 | ||||
Sequence: GHCKAIYPFDGHNEGTLAMKEGEVLYIIEEDKGDGWTRARRQNGEEGYVPTSYIDVTLEKNSKGS |
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.
Q5T0N5-1
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
- Length605
- Mass (Da)70,065
- Last updated2014-07-09 v3
- Checksum1D9237185C3006ED
Q5T0N5-2
- Name2
- Differences from canonical
- 384-388: Missing
Q5T0N5-3
- Name3
- Differences from canonical
- 331-388: Missing
Q5T0N5-4
- Name4
Q5T0N5-5
- Name5
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A075B6Q2 | A0A075B6Q2_HUMAN | FNBP1L | 451 |
Sequence caution
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_021709 | 331-388 | in isoform 3 and isoform 4 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_021710 | 384-388 | in isoform 2 and isoform 5 | |||
Sequence: Missing | ||||||
Compositional bias | 476-493 | Basic and acidic residues | ||||
Sequence: EGKTGGRGDRRHSSDINH | ||||||
Compositional bias | 494-514 | Polar residues | ||||
Sequence: LVTQGRESPEGSYTDDANQEV | ||||||
Alternative sequence | VSP_021711 | 605 | in isoform 4 and isoform 5 | |||
Sequence: S → AVTYI |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY514449 EMBL· GenBank· DDBJ | AAR98814.1 EMBL· GenBank· DDBJ | mRNA | ||
AC095034 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL109613 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL512651 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC062477 EMBL· GenBank· DDBJ | AAH62477.1 EMBL· GenBank· DDBJ | mRNA | ||
BC074891 EMBL· GenBank· DDBJ | AAH74891.1 EMBL· GenBank· DDBJ | mRNA | ||
BC074892 EMBL· GenBank· DDBJ | AAH74892.1 EMBL· GenBank· DDBJ | mRNA | ||
AK000282 EMBL· GenBank· DDBJ | BAA91051.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |