Q5T0N5 · FBP1L_HUMAN

  • Protein
    Formin-binding protein 1-like
  • Gene
    FNBP1L
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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.

160550100150200250300350400450500550600
TypeIDPosition(s)Description
Site165Mediates end-to-end attachment of dimers

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcell cortex
Cellular Componentcytoplasm
Cellular Componentcytoplasmic vesicle
Cellular Componentcytoskeleton
Cellular Componentcytosol
Cellular Componentplasma membrane
Molecular Functioncadherin binding
Molecular FunctionGTPase binding
Molecular Functionlipid binding
Biological Processautophagy
Biological Processcilium assembly
Biological Processclathrin-dependent endocytosis
Biological Processmembrane invagination
Biological Processplasma membrane tubulation
Biological Processpositive regulation of filopodium assembly
Biological Processsignal transduction
Biological Processvesicle budding from membrane
Biological Processvesicle organization
Biological Processvesicle transport along actin filament

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Formin-binding protein 1-like
  • Alternative names
    • Transducer of Cdc42-dependent actin assembly protein 1 (Toca-1)

Gene names

    • Name
      FNBP1L
    • Synonyms
      C1orf39, TOCA1

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q5T0N5
  • Secondary accessions
    • J3QSS4
    • Q5T0N6
    • Q6B097
    • Q6P653
    • Q6R4Q4
    • Q9NXG1

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Disease & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis441-443Impairs interaction with CDC42 and reduces CDC42-induced actin assembly.
Mutagenesis576Impairs interaction with WASL and reduces CDC42-induced actin assembly.

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.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue (large scale data), modified residue.

TypeIDPosition(s)SourceDescription
ChainPRO_00002614341-605UniProtFormin-binding protein 1-like
Modified residue (large scale data)2PRIDEPhosphoserine
Modified residue (large scale data)291PRIDEPhosphotyrosine
Modified residue (large scale data)293PRIDEPhosphothreonine
Modified residue295UniProtPhosphoserine
Modified residue (large scale data)295PRIDEPhosphoserine
Modified residue (large scale data)300PRIDEPhosphoserine
Modified residue488UniProtPhosphoserine
Modified residue (large scale data)488PRIDEPhosphoserine
Modified residue (large scale data)489PRIDEPhosphoserine
Modified residue (large scale data)496PRIDEPhosphothreonine
Modified residue501UniProtPhosphoserine
Modified residue (large scale data)501PRIDEPhosphoserine
Modified residue505UniProtPhosphoserine
Modified residue (large scale data)505PRIDEPhosphoserine
Modified residue (large scale data)506PRIDEPhosphotyrosine
Modified residue (large scale data)507PRIDEPhosphothreonine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

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).

Binary interactions

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain, coiled coil, region, compositional bias.

TypeIDPosition(s)Description
Domain1-263F-BAR
Coiled coil66-258
Region245-535Interaction with CDC42
Coiled coil392-484
Domain397-474REM-1
Compositional bias476-493Basic and acidic residues
Region476-539Disordered
Compositional bias494-514Polar residues
Region522-605Interaction with DNM1
Domain538-599SH3
Region541-597Interaction with DNM2 and WASL
Region541-605Interaction with DAAM1, DIAPH1 and DIAPH2

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

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (5)
  • Sequence status
    Complete

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.

  • Length
    605
  • Mass (Da)
    70,065
  • Last updated
    2014-07-09 v3
  • Checksum
    1D9237185C3006ED
MSWGTELWDQFDSLDKHTQWGIDFLERYAKFVKERIEIEQNYAKQLRNLVKKYCPKRSSKDEEPRFTSCVAFFNILNELNDYAGQREVVAEEMAHRVYGELMRYAHDLKTERKMHLQEGRKAQQYLDMCWKQMDNSKKKFERECREAEKAQQSYERLDNDTNATKADVEKAKQQLNLRTHMADENKNEYAAQLQNFNGEQHKHFYVVIPQIYKQLQEMDERRTIKLSECYRGFADSERKVIPIISKCLEGMILAAKSVDERRDSQMVVDSFKSGFEPPGDFPFEDYSQHIYRTISDGTISASKQESGKMDAKTTVGKAKGKLWLFGKKPKPQSPPLTPTSLFTSSTPNGSQFLTFSIEPVHYCMNEIKTGKPRIPSFRSLKRGWSVKMGPALEDFSHLPPEQRRKKLQQRIDELNRELQKESDQKDALNKMKDVYEKNPQMGDPGSLQPKLAETMNNIDRLRMEIHKNEAWLSEVEGKTGGRGDRRHSSDINHLVTQGRESPEGSYTDDANQEVRGPPQQHGHHNEFDDEFEDDDPLPAIGHCKAIYPFDGHNEGTLAMKEGEVLYIIEEDKGDGWTRARRQNGEEGYVPTSYIDVTLEKNSKGS

Q5T0N5-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q5T0N5-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q5T0N5-4

Q5T0N5-5

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A075B6Q2A0A075B6Q2_HUMANFNBP1L451

Sequence caution

The sequence BAA91051.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

Showing features for alternative sequence, compositional bias.

TypeIDPosition(s)Description
Alternative sequenceVSP_021709331-388in isoform 3 and isoform 4
Alternative sequenceVSP_021710384-388in isoform 2 and isoform 5
Compositional bias476-493Basic and acidic residues
Compositional bias494-514Polar residues
Alternative sequenceVSP_021711605in isoform 4 and isoform 5

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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