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Protein

Formin-binding protein 1

Gene

Fnbp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei166Mediates end-to-end attachment of dimersBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiR-MMU-8856828. Clathrin-mediated endocytosis.

Names & Taxonomyi

Protein namesi
Recommended name:
Formin-binding protein 1
Alternative name(s):
Formin-binding protein 17
Gene namesi
Name:Fnbp1
Synonyms:Fbp17, Kiaa0554
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:109606. Fnbp1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Coated pit, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Lysosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002614311 – 616Formin-binding protein 1Add BLAST616

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei66N6-acetyllysineBy similarity1
Modified residuei110N6-acetyllysineBy similarity1
Modified residuei296PhosphoserineCombined sources1
Modified residuei299PhosphoserineBy similarity1
Modified residuei348PhosphoserineBy similarity1
Modified residuei358PhosphoserineBy similarity1
Modified residuei496PhosphoserineCombined sources1
Modified residuei499PhosphotyrosineCombined sources1
Modified residuei520PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ80TY0.
PeptideAtlasiQ80TY0.
PRIDEiQ80TY0.

PTM databases

iPTMnetiQ80TY0.
PhosphoSitePlusiQ80TY0.

Expressioni

Tissue specificityi

Expressed in brain and testis.1 Publication

Gene expression databases

BgeeiENSMUSG00000075415.
CleanExiMM_FNBP1.
ExpressionAtlasiQ80TY0. baseline and differential.
GenevisibleiQ80TY0. MM.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

BioGridi199720. 1 interactor.
IntActiQ80TY0. 2 interactors.
MINTiMINT-4123990.
STRINGi10090.ENSMUSP00000109190.

Structurei

3D structure databases

ProteinModelPortaliQ80TY0.
SMRiQ80TY0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 264F-BARPROSITE-ProRule annotationAdd BLAST264
Repeati415 – 490REMAdd BLAST76
Domaini549 – 610SH3PROSITE-ProRule annotationAdd BLAST62

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 334Interaction with microtubulesBy similarityAdd BLAST334
Regioni1 – 79Required for self-association and induction of membrane tubulationBy similarityAdd BLAST79
Regioni251 – 616Required for self-association and induction of membrane tubulationBy similarityAdd BLAST366
Regioni399 – 551Interaction with RND2By similarityAdd BLAST153
Regioni494 – 616Interaction with PDE6GBy similarityAdd BLAST123
Regioni513 – 616Required for interaction with TNKSBy similarityAdd BLAST104
Regioni534 – 616Interaction with DNM1 and DNM3By similarityAdd BLAST83
Regioni549 – 616Interaction with ARHGAP17, DAAM1, DIAPH1 and DIAPH2By similarityAdd BLAST68
Regioni552 – 609Interaction with FASLGBy similarityAdd BLAST58
Regioni552 – 608Interaction with DNM2 and WASLBy similarityAdd BLAST57

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili67 – 259By similarityAdd BLAST193
Coiled coili398 – 490By similarityAdd BLAST93

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi336 – 365Pro-richAdd BLAST30

Domaini

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).By similarity

Sequence similaritiesi

Belongs to the FNBP1 family.Curated
Contains 1 F-BAR domain.PROSITE-ProRule annotation
Contains 1 REM (Hr1) repeat.Curated
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

eggNOGiENOG410INNY. Eukaryota.
ENOG410ZU0I. LUCA.
GeneTreeiENSGT00510000046403.
HOVERGENiHBG002489.
InParanoidiQ80TY0.
KOiK20121.
OMAiNQEQHEY.
OrthoDBiEOG091G038P.
PhylomeDBiQ80TY0.
TreeFamiTF351162.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
InterProiIPR031160. F_BAR.
IPR001060. FCH_dom.
IPR028532. FNBP1/FBP17.
IPR014729. Rossmann-like_a/b/a_fold.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR10663:SF157. PTHR10663:SF157. 1 hit.
PfamiPF00611. FCH. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
SMARTiSM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS51741. F_BAR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q80TY0-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSWGTELWDQ FDNLEKHTQW GIDILEKYIK FVKERTEIEL SYAKQLRNLS
60 70 80 90 100
KKYQPKKNSK EEEEYKYTAC KAFLSTLNEM NDYAGQHEVI SENMTSQITV
110 120 130 140 150
DLMRYVQELK QERKSNFHDG RKAQQHIETC WKQLESSKRR FERDCKEADR
160 170 180 190 200
AQQYFEKMDA DINVTKADVE KARQQAQIRQ QMAEDSKADY SLILQRFNQE
210 220 230 240 250
QWEYYHTHIP NIFQKIQEME ERRIVRIGES MKTYAEVDRQ VIPIIGKCLD
260 270 280 290 300
GIVKAAESID QKNDSQLVVE AYKSGFEPPG DIEFEDYTQP MKRTVSDNSL
310 320 330 340 350
SSSKEGKPEL RFGGKSRGKL WPFIKKNKLM SLLTSPHQPP PPPPASASPS
360 370 380 390 400
AVPNGPQSPK QPKEPLSHRF NEFMTSKPKI HCFRSLKRGL SLKLGVTPED
410 420 430 440 450
FSNFPPEQRR KKLQQKVDDL NREIQKETDQ RDAITKMKDV YLKNPQMGDP
460 470 480 490 500
ASLDQKLTEV TQNIEKLRLE AQKFEAWLAE VEGRLPARSE QARRQSGLYD
510 520 530 540 550
GQTHQTVTNC AQDRESPDGS YTEEQSQESE HKVLAPDFDD EFDDEEPLPA
560 570 580 590 600
IGTCKALYTF EGQNEGTISV VEGETLSVIE EDKGDGWTRI RRNEDEEGYV
610
PTSYVEVYLD KNAKGS
Length:616
Mass (Da):71,344
Last modified:November 28, 2006 - v2
Checksum:i947BFCFCCA4BD1E2
GO
Isoform 2 (identifier: Q80TY0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     329-394: Missing.

Show »
Length:550
Mass (Da):64,139
Checksum:iAA80F83DEBE4AC5B
GO
Isoform 3 (identifier: Q80TY0-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     329-394: Missing.
     515-515: E → ES

Show »
Length:551
Mass (Da):64,226
Checksum:iE73927365F88D8C2
GO
Isoform 4 (identifier: Q80TY0-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-79: Missing.
     329-338: Missing.
     390-394: Missing.

Note: No experimental confirmation available.
Show »
Length:522
Mass (Da):60,086
Checksum:i482B1709BE440057
GO
Isoform 5 (identifier: Q80TY0-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     329-338: LMSLLTSPHQ → VLAIWTLRGL
     339-616: Missing.

Show »
Length:338
Mass (Da):39,972
Checksum:iF83CA4FE103657D2
GO

Sequence cautioni

The sequence BAC65590 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAE33974 differs from that shown. Reason: Erroneous initiation.Curated

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0216971 – 79Missing in isoform 4. 1 PublicationAdd BLAST79
Alternative sequenceiVSP_021698329 – 394Missing in isoform 2 and isoform 3. 1 PublicationAdd BLAST66
Alternative sequenceiVSP_021699329 – 338Missing in isoform 4. 1 Publication10
Alternative sequenceiVSP_021700329 – 338LMSLLTSPHQ → VLAIWTLRGL in isoform 5. 2 Publications10
Alternative sequenceiVSP_021701339 – 616Missing in isoform 5. 2 PublicationsAdd BLAST278
Alternative sequenceiVSP_021702390 – 394Missing in isoform 4. 1 Publication5
Alternative sequenceiVSP_021703515E → ES in isoform 3. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK122308 mRNA. Translation: BAC65590.1. Different initiation.
AK052652 mRNA. Translation: BAC35082.1.
AK143512 mRNA. Translation: BAE25408.1.
AK157135 mRNA. Translation: BAE33974.1. Different initiation.
AK170497 mRNA. Translation: BAE41836.1.
AK172100 mRNA. Translation: BAE42825.1.
AL844546 Genomic DNA. Translation: CAM18436.1.
AL844546 Genomic DNA. Translation: CAM18442.1.
BC003867 mRNA. Translation: AAH03867.1.
CCDSiCCDS15894.1. [Q80TY0-5]
CCDS38097.1. [Q80TY0-2]
CCDS50560.1. [Q80TY0-4]
CCDS50561.1. [Q80TY0-1]
CCDS57165.1. [Q80TY0-3]
RefSeqiNP_001033789.1. NM_001038700.2. [Q80TY0-2]
NP_001171119.1. NM_001177648.1. [Q80TY0-1]
NP_001171120.1. NM_001177649.1. [Q80TY0-3]
NP_001171121.1. NM_001177650.1. [Q80TY0-4]
NP_062279.1. NM_019406.3. [Q80TY0-5]
UniGeneiMm.440993.
Mm.52297.

Genome annotation databases

EnsembliENSMUST00000113552; ENSMUSP00000109181; ENSMUSG00000075415. [Q80TY0-5]
ENSMUST00000113559; ENSMUSP00000109189; ENSMUSG00000075415. [Q80TY0-4]
ENSMUST00000113560; ENSMUSP00000109190; ENSMUSG00000075415. [Q80TY0-1]
ENSMUST00000113562; ENSMUSP00000109192; ENSMUSG00000075415. [Q80TY0-2]
ENSMUST00000113564; ENSMUSP00000109194; ENSMUSG00000075415. [Q80TY0-3]
GeneIDi14269.
KEGGimmu:14269.
UCSCiuc008jdh.1. mouse. [Q80TY0-4]
uc008jdi.2. mouse. [Q80TY0-2]
uc008jdj.2. mouse. [Q80TY0-1]
uc008jdk.2. mouse. [Q80TY0-3]
uc008jdm.2. mouse. [Q80TY0-5]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK122308 mRNA. Translation: BAC65590.1. Different initiation.
AK052652 mRNA. Translation: BAC35082.1.
AK143512 mRNA. Translation: BAE25408.1.
AK157135 mRNA. Translation: BAE33974.1. Different initiation.
AK170497 mRNA. Translation: BAE41836.1.
AK172100 mRNA. Translation: BAE42825.1.
AL844546 Genomic DNA. Translation: CAM18436.1.
AL844546 Genomic DNA. Translation: CAM18442.1.
BC003867 mRNA. Translation: AAH03867.1.
CCDSiCCDS15894.1. [Q80TY0-5]
CCDS38097.1. [Q80TY0-2]
CCDS50560.1. [Q80TY0-4]
CCDS50561.1. [Q80TY0-1]
CCDS57165.1. [Q80TY0-3]
RefSeqiNP_001033789.1. NM_001038700.2. [Q80TY0-2]
NP_001171119.1. NM_001177648.1. [Q80TY0-1]
NP_001171120.1. NM_001177649.1. [Q80TY0-3]
NP_001171121.1. NM_001177650.1. [Q80TY0-4]
NP_062279.1. NM_019406.3. [Q80TY0-5]
UniGeneiMm.440993.
Mm.52297.

3D structure databases

ProteinModelPortaliQ80TY0.
SMRiQ80TY0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199720. 1 interactor.
IntActiQ80TY0. 2 interactors.
MINTiMINT-4123990.
STRINGi10090.ENSMUSP00000109190.

PTM databases

iPTMnetiQ80TY0.
PhosphoSitePlusiQ80TY0.

Proteomic databases

PaxDbiQ80TY0.
PeptideAtlasiQ80TY0.
PRIDEiQ80TY0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000113552; ENSMUSP00000109181; ENSMUSG00000075415. [Q80TY0-5]
ENSMUST00000113559; ENSMUSP00000109189; ENSMUSG00000075415. [Q80TY0-4]
ENSMUST00000113560; ENSMUSP00000109190; ENSMUSG00000075415. [Q80TY0-1]
ENSMUST00000113562; ENSMUSP00000109192; ENSMUSG00000075415. [Q80TY0-2]
ENSMUST00000113564; ENSMUSP00000109194; ENSMUSG00000075415. [Q80TY0-3]
GeneIDi14269.
KEGGimmu:14269.
UCSCiuc008jdh.1. mouse. [Q80TY0-4]
uc008jdi.2. mouse. [Q80TY0-2]
uc008jdj.2. mouse. [Q80TY0-1]
uc008jdk.2. mouse. [Q80TY0-3]
uc008jdm.2. mouse. [Q80TY0-5]

Organism-specific databases

CTDi23048.
MGIiMGI:109606. Fnbp1.
RougeiSearch...

Phylogenomic databases

eggNOGiENOG410INNY. Eukaryota.
ENOG410ZU0I. LUCA.
GeneTreeiENSGT00510000046403.
HOVERGENiHBG002489.
InParanoidiQ80TY0.
KOiK20121.
OMAiNQEQHEY.
OrthoDBiEOG091G038P.
PhylomeDBiQ80TY0.
TreeFamiTF351162.

Enzyme and pathway databases

ReactomeiR-MMU-8856828. Clathrin-mediated endocytosis.

Miscellaneous databases

ChiTaRSiFnbp1. mouse.
PROiQ80TY0.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000075415.
CleanExiMM_FNBP1.
ExpressionAtlasiQ80TY0. baseline and differential.
GenevisibleiQ80TY0. MM.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
InterProiIPR031160. F_BAR.
IPR001060. FCH_dom.
IPR028532. FNBP1/FBP17.
IPR014729. Rossmann-like_a/b/a_fold.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR10663:SF157. PTHR10663:SF157. 1 hit.
PfamiPF00611. FCH. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
SMARTiSM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS51741. F_BAR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFNBP1_MOUSE
AccessioniPrimary (citable) accession number: Q80TY0
Secondary accession number(s): A2AQ40
, A2AQ46, Q3TA45, Q3TCW9, Q3U081, Q3UPI7, Q8C727, Q99L37
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 28, 2006
Last modified: November 30, 2016
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.