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Protein

Formin-binding protein 1

Gene

Fnbp1

Organism
Rattus norvegicus (Rat)
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 be required for the lysosomal retention of FASLG/FASL (By similarity). May act as a link between RND2 signaling and regulation of the actin cytoskeleton. Isoform 1 and isoform 2 promote RND2-induced neurite branching in neuronal cells.By similarity2 Publications

Sites

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

GO - Molecular functioni

GO - Biological processi

  • cell differentiation Source: UniProtKB-KW
  • endocytosis Source: UniProtKB-KW
  • nervous system development Source: RGD
  • vesicle-mediated transport Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Endocytosis, Neurogenesis

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Formin-binding protein 1
Alternative name(s):
Formin-binding protein 17
Rapostlin
Gene namesi
Name:Fnbp1
Synonyms:Fbp17
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621350. Fnbp1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi587W → A: Abrogates interaction with PDE6G. 1 Publication1
Mutagenesisi601P → L: Abrogates interaction with PDE6G. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002614321 – 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 residuei299PhosphoserineCombined sources1
Modified residuei348PhosphoserineBy similarity1
Modified residuei358PhosphoserineBy similarity1
Modified residuei496PhosphoserineBy similarity1
Modified residuei499PhosphotyrosineBy similarity1
Modified residuei520PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ8R511.
PRIDEiQ8R511.

PTM databases

iPTMnetiQ8R511.
PhosphoSitePlusiQ8R511.

Expressioni

Tissue specificityi

Highly expressed in brain and lung. Expressed at lower levels in colon, heart, kidney, liver, small intestine, spleen, testis and thymus. Isoform 1 and isoform 2 are the major isoforms in brain while isoform 5 and isoform 6 are the major isoforms in lung, spleen, testis and thymus.2 Publications

Interactioni

Subunit structurei

Homodimerizes, the dimers can polymerize end-to-end to form filamentous structures. Interacts with AKAP9, ARHGAP17, DAAM1, DIAPH1, DIAPH2, DNM1, DNM2, DNM3, FASLG/FASL, and SNX2. May interact with TNKS (By similarity). Interacts specifically with GTP-bound RND2 and CDC42. Interacts with PDE6G, WASL/N-WASP and microtubules.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PDE6GP185452EBI-1111424,EBI-2622029From a different organism.
RND2P521982EBI-1111424,EBI-1111436From a different organism.
WASLO004012EBI-1111424,EBI-957615From a different organism.

Protein-protein interaction databases

BioGridi251405. 3 interactors.
IntActiQ8R511. 3 interactors.
MINTiMINT-4608929.
STRINGi10116.ENSRNOP00000049838.

Structurei

3D structure databases

ProteinModelPortaliQ8R511.
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 microtubulesAdd 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 RND2Add BLAST153
Regioni494 – 616Interaction with PDE6GAdd 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

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.
HOGENOMiHOG000231767.
HOVERGENiHBG002489.
InParanoidiQ8R511.
KOiK20121.
PhylomeDBiQ8R511.
TreeFamiTF351162.

Family and domain databases

InterProiIPR031160. F_BAR.
IPR001060. FCH_dom.
IPR028532. FNBP1/FBP17.
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 (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8R511-1) [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 KAFLSTLNEL NDYAGQHEVI SENMTSQITV
110 120 130 140 150
DLVRYVQELK QERKSNFHDG RKAQQHIETC WKQLESSKRR FERDCKEADR
160 170 180 190 200
AQQYFEKMDA DINVTKADVE KARQQAQMRQ 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 KFGGKSRGKL WPFIKKNKLM TLLTSPHQPP PPPPASASPS
360 370 380 390 400
AVPNGPQSPK QQKEPLSHRF NEFMTSKPKI HCFRSLKRGL SLKLGVTPED
410 420 430 440 450
FSNFPPEQRR KKLQQKVDDL NKEIQKETDQ RDAITKMKDV YLKNPQMGDP
460 470 480 490 500
ASLDHKLAEV TQNIEKLRLE AHKFEAWLAE VEGRLPARSE QARRQSGLYD
510 520 530 540 550
GQTHQTVTNC AQDRESPDGS YTEEQSQESE HKVLATDFDD EFDDEEPLPA
560 570 580 590 600
IGTCKALYTF EGQNEGTISV VEGETLSVIE EDKGDGWTRI RRNEDEEGYV
610
PTSYVEVYLD KNAKGS
Length:616
Mass (Da):71,293
Last modified:November 28, 2006 - v2
Checksum:i3F62F30C7AEC674E
GO
Isoform 2 (identifier: Q8R511-2) [UniParc]FASTAAdd to basket
Also known as: L

The sequence of this isoform differs from the canonical sequence as follows:
     616-616: S → AKTYI

Note: Major isoform in brain.
Show »
Length:620
Mass (Da):71,782
Checksum:i2F225FD75702F30C
GO
Isoform 3 (identifier: Q8R511-3) [UniParc]FASTAAdd to basket
Also known as: Ld

The sequence of this isoform differs from the canonical sequence as follows:
     390-394: Missing.
     616-616: S → AKTYI

Show »
Length:615
Mass (Da):71,228
Checksum:iC5F2F64E68E5B6AC
GO
Isoform 4 (identifier: Q8R511-4) [UniParc]FASTAAdd to basket
Also known as: M

The sequence of this isoform differs from the canonical sequence as follows:
     329-357: Missing.
     616-616: S → AKTYI

Show »
Length:591
Mass (Da):68,913
Checksum:i7C2758DD397671C9
GO
Isoform 5 (identifier: Q8R511-5) [UniParc]FASTAAdd to basket
Also known as: Md

The sequence of this isoform differs from the canonical sequence as follows:
     329-357: Missing.
     390-394: Missing.
     616-616: S → AKTYI

Show »
Length:586
Mass (Da):68,358
Checksum:i8170332191C47C45
GO
Isoform 6 (identifier: Q8R511-6) [UniParc]FASTAAdd to basket
Also known as: S

The sequence of this isoform differs from the canonical sequence as follows:
     329-389: Missing.
     616-616: S → AKTYI

Show »
Length:559
Mass (Da):65,088
Checksum:iB3F130FA3BE64709
GO
Isoform 7 (identifier: Q8R511-7) [UniParc]FASTAAdd to basket
Also known as: Sd

The sequence of this isoform differs from the canonical sequence as follows:
     329-394: Missing.
     616-616: S → AKTYI

Show »
Length:554
Mass (Da):64,533
Checksum:iF146F3B83FBBBE0F
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_021704329 – 394Missing in isoform 7. 1 PublicationAdd BLAST66
Alternative sequenceiVSP_021705329 – 389Missing in isoform 6. 1 PublicationAdd BLAST61
Alternative sequenceiVSP_021706329 – 357Missing in isoform 4 and isoform 5. 1 PublicationAdd BLAST29
Alternative sequenceiVSP_021707390 – 394Missing in isoform 3 and isoform 5. 1 Publication5
Alternative sequenceiVSP_021708616S → AKTYI in isoform 2, isoform 3, isoform 4, isoform 5, isoform 6 and isoform 7. 2 Publications1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB073208 mRNA. Translation: BAB90845.1.
AB126168 mRNA. Translation: BAD13422.1.
AB126169 mRNA. Translation: BAD13423.1.
AB126170 mRNA. Translation: BAD13424.1.
AB126171 mRNA. Translation: BAD13425.1.
AB126172 mRNA. Translation: BAD13426.1.
AABR03024172 Genomic DNA. No translation available.
AABR03024739 Genomic DNA. No translation available.
RefSeqiNP_620269.1. NM_138914.1. [Q8R511-2]
UniGeneiRn.20445.

Genome annotation databases

GeneIDi192348.
KEGGirno:192348.
UCSCiRGD:621350. rat. [Q8R511-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB073208 mRNA. Translation: BAB90845.1.
AB126168 mRNA. Translation: BAD13422.1.
AB126169 mRNA. Translation: BAD13423.1.
AB126170 mRNA. Translation: BAD13424.1.
AB126171 mRNA. Translation: BAD13425.1.
AB126172 mRNA. Translation: BAD13426.1.
AABR03024172 Genomic DNA. No translation available.
AABR03024739 Genomic DNA. No translation available.
RefSeqiNP_620269.1. NM_138914.1. [Q8R511-2]
UniGeneiRn.20445.

3D structure databases

ProteinModelPortaliQ8R511.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi251405. 3 interactors.
IntActiQ8R511. 3 interactors.
MINTiMINT-4608929.
STRINGi10116.ENSRNOP00000049838.

PTM databases

iPTMnetiQ8R511.
PhosphoSitePlusiQ8R511.

Proteomic databases

PaxDbiQ8R511.
PRIDEiQ8R511.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi192348.
KEGGirno:192348.
UCSCiRGD:621350. rat. [Q8R511-1]

Organism-specific databases

CTDi23048.
RGDi621350. Fnbp1.

Phylogenomic databases

eggNOGiENOG410INNY. Eukaryota.
ENOG410ZU0I. LUCA.
HOGENOMiHOG000231767.
HOVERGENiHBG002489.
InParanoidiQ8R511.
KOiK20121.
PhylomeDBiQ8R511.
TreeFamiTF351162.

Miscellaneous databases

PROiQ8R511.

Family and domain databases

InterProiIPR031160. F_BAR.
IPR001060. FCH_dom.
IPR028532. FNBP1/FBP17.
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_RAT
AccessioniPrimary (citable) accession number: Q8R511
Secondary accession number(s): Q75UE2
, Q75UE3, Q75UE4, Q75UE5, Q75UE6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 28, 2006
Last modified: November 2, 2016
This is version 106 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. 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.