Protein detail

FNBP1

Formin-binding protein 1 (Formin-binding protein 17) (hFBP17)

Entry name
FNBP1
UniProt ID
EVMP confidence score
0.63
Supporting publications (n)
9
Transmembrane count
Protein classification
Disease related genesPlasma proteinsPredicted intracellular proteins
EVMP confidence score

Annotation confidence score; open for threshold definitions.

Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information11
Protein Names
Formin-binding protein 1 (Formin-binding protein 17) (hFBP17)
Protein Class (3)
Disease related genesPlasma proteinsPredicted intracellular proteins
Protein Function (2)
  • Disease related genes
  • Predicted intracellular proteins
Entrez Gene Symbol
Gene Synonym (2)
FBP17KIAA0554
Gene Description
Formin binding protein 1
Chromosome
9
Position
129887187-130043189
Supporting publications (n)
9
EVMP confidence score
0.63
Fluorescence & Localization6
FNBP1 fluorescence
Tissue Specificbone marrowCell SpecificNK-cellsSingle-Nuclei Brain SpecificleukocyteBlood Cell SpecificgdT-cellBlood Lineage SpecificNK-cells
Function & Pathway8
Relations & Evidence15

Ligand-Receptor Signaling (8)

8 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
intracellularintracellularComPPINoNoNoNoNo
intracellularintracellularGO_IntercellNoNoNoNoNo
intracellularintracellularUniProt_locationNoNoNoNoNo
intracellularintracellularOmniPathNoNoNoNoNo
fbar_actin_dynamics_endocytosisintracellular_intercellular_relatedHGNCYesNoNoNoNo
intracellular_intercellular_relatedintracellular_intercellular_relatedOmniPathYesNoNoNoNo
plasma_membraneplasma_membraneUniProt_locationNoNoNoNoNo
plasma_membraneplasma_membraneOmniPathNoNoNoNoNo

Isolation & Detection Technology (1)

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationMass spectrometry140326690
Sequence, Structure & Domains15

Sequences

Length
617
Mass
71,307
Sequence
MSWGTELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTSCKAFISNLNEMNDYAGQHEVISENMASQIIVDLARYVQELKQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINVTKADVEKARQQAQIRHQMAEDSKADYSSILQKFNHEQHEYYHTHIPNIFQKIQEMEERRIVRMGESMKTYAEVDRQVIPIIGKCLDGIVKAAESIDQKNDSQLVIEAYKSGFEPPGDIEFEDYTQPMKRTVSDNSLSNSRGEGKPDLKFGGKSKGKLWPFIKKNKLMSLLTSPHQPPPPPPASASPSAVPNGPQSPKQQKEPLSHRFNEFMTSKPKIHCFRSLKRGLSLKLGATPEDFSNLPPEQRRKKLQQKVDELNKEIQKEMDQRDAITKMKDVYLKNPQMGDPASLDHKLAEVSQNIEKLRVETQKFEAWLAEVEGRLPARSEQARRQSGLYDSQNPPTVNNCAQDRESPDGSYTEEQSQESEMKVLATDFDDEFDDEEPLPAIGTCKALYTFEGQNEGTISVVEGETLYVIEEDKGDGWTRIRRNEDEEGYVPTSYVEVCLDKNAKDS
Alternative Products
Event=Alternative splicing; Named isoforms=5; Name=1; IsoId=Q96RU3-1; Sequence=Displayed; Name=2; IsoId=Q96RU3-2; Sequence=VSP_021695, VSP_021696; Name=3; IsoId=Q96RU3-3; Sequence=VSP_021694, VSP_021696; Name=4; IsoId=Q96RU3-4; Sequence=VSP_021693; Name=5; IsoId=Q96RU3-5; Sequence=VSP_021695
Alternative Sequence
329..394; Missing (in isoform 4); 330..358; Missing (in isoform 3); 391..395; Missing (in isoform 2 and isoform 5); 616..617; DS -> GAKTYI (in isoform 2 and isoform 3)

3D Structural Models

Turn
7..9
Helix
3..6; 11..52; 68..160; 166..206; 208..238; 241..257; 261..272
3D Structure
X-ray crystallography (1)

Domain & Motif Annotations

Compositional Bias
338..347; Pro residues; 499..512; Polar residues
Coiled Coil
67..259; 398..490
Domain (CC)
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.
Domain (FT)
1..264; F-BAR; 404..481; REM-1; 550..611; SH3
Region
1..335; Interaction with microtubules; 1..79; Required for self-association and induction of membrane tubulation; 251..617; Required for self-association and induction of membrane tubulation; 280..315; Disordered; 333..366; Disordered; 400..552; Interaction with RND2; 486..531; Disordered; 495..617; Interaction with PDE6G; 514..617; Required for interaction with TNKS; 535..617; Interaction with DNM1 and DNM3; 550..617; Interaction with ARHGAP17, DAAM1, DIAPH1 and DIAPH2; 553..610; Interaction with FASLG; 553..609; Interaction with DNM2 and WASL
Protein Families
FNBP1 family
Sequence Similarities
Belongs to the FNBP1 family.
Clinical Relevance4
Interaction Protein (6)
ENSG00000079805ENSG00000106976ENSG00000117560ENSG00000137942ENSG00000173273ENSG00000205302
Interaction Count
6
Interaction Dataset (2)
intact_biogridintact_biogrid_opencell
Supporting Publications9
PMIDTitleAbstract
29242380Insights into the Proteome of Gastrointestinal Stromal Tumors-Derived Exosomes Reveals New Potential Diagnostic Biomarkers.No abstract available
30760538Microvesicle Proteomic Profiling of Uterine Liquid Biopsy for Ovarian Cancer Early Detection.No abstract available
32795414Extracellular Vesicle and Particle Biomarkers Define Multiple Human Cancers.Among traditional exosome markers, CD9, HSPA8, ALIX, and HSP90AB1 represent pan-EVP markers, while ACTB, MSN, and RAP1B are novel pan-EVP markers.
37862381Surfaceome analysis of extracellular vesicles from senescent cells uncovers uptake repressor DPP4.No abstract available
38731868The Deep Proteomics Approach Identified Extracellular Vesicular Proteins Correlated to Extracellular Matrix in Type One and Two Endometrial Cancer.No abstract available
40091455Potential Role of Menstrual Fluid-Derived Small Extracellular Vesicle Proteins in Endometriosis Pathogenesiss.No abstract available
40311616Integrative proteomic profiling of tumor and plasma extracellular vesicles identifies a diagnostic biomarker panel for colorectal cancer.No abstract available
40619995A 96-Well Ultrafiltration Approach for the High-Throughput Proteome Analysis of Extracellular Vesicles Isolated From Conditioned Medium.No abstract available
40784529Serum-derived exosome proteomics unveils the distinct and adjustable nature of the dampness constitution in traditional Chinese medicine.No abstract available