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Q80TY0 (FNBP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Formin-binding protein 1
Alternative name(s):
Formin-binding protein 17
Gene names
Name:Fnbp1
Synonyms:Fbp17, Kiaa0554
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length616 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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.

Subcellular location

Cytoplasm By similarity. Cytoplasmcytoskeleton By similarity. Cytoplasmcell cortex By similarity. Lysosome By similarity. Cytoplasmic vesicle By similarity. Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Membraneclathrin-coated pit By similarity. Note: Enriched in cortical regions coincident with F-actin By similarity. Also localizes to endocytic vesicles and lysosomes By similarity.

Tissue specificity

Expressed in brain and testis. Ref.5

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.

Contains 1 FCH domain.

Contains 1 REM (Hr1) repeat.

Contains 1 SH3 domain.

Sequence caution

The sequence BAC65590.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAE33974.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processEndocytosis
   Cellular componentCell membrane
Coated pit
Cytoplasm
Cytoplasmic vesicle
Cytoskeleton
Lysosome
Membrane
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
SH3 domain
   LigandLipid-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processendocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcell cortex

Inferred from electronic annotation. Source: UniProtKB-SubCell

coated pit

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

lysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionlipid binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q80TY0-1)

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.
Isoform 2 (identifier: Q80TY0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     329-394: Missing.
Isoform 3 (identifier: Q80TY0-3)

The sequence of this isoform differs from the canonical sequence as follows:
     329-394: Missing.
     515-515: E → ES
Isoform 4 (identifier: Q80TY0-4)

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.
Isoform 5 (identifier: Q80TY0-5)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 616616Formin-binding protein 1
PRO_0000261431

Regions

Domain1 – 6565FCH
Repeat415 – 49076REM
Domain549 – 61062SH3
Region1 – 334334Interaction with microtubules By similarity
Region1 – 288288F-BAR domain By similarity
Region1 – 7979Required for self-association and induction of membrane tubulation By similarity
Region251 – 616366Required for self-association and induction of membrane tubulation By similarity
Region399 – 551153Interaction with RND2 By similarity
Region494 – 616123Interaction with PDE6G By similarity
Region513 – 616104Required for interaction with TNKS By similarity
Region534 – 61683Interaction with DNM1 and DNM3 By similarity
Region549 – 61668Interaction with ARHGAP17, DAAM1, DIAPH1 and DIAPH2 By similarity
Region552 – 60958Interaction with FASLG By similarity
Region552 – 60857Interaction with DNM2 and WASL By similarity
Coiled coil67 – 259193 By similarity
Coiled coil398 – 49093 By similarity
Compositional bias336 – 36530Pro-rich

Sites

Site1661Mediates end-to-end attachment of dimers By similarity

Amino acid modifications

Modified residue661N6-acetyllysine By similarity
Modified residue1101N6-acetyllysine By similarity
Modified residue2961Phosphoserine Ref.7
Modified residue2991Phosphoserine By similarity
Modified residue3481Phosphoserine By similarity
Modified residue3581Phosphoserine By similarity
Modified residue4961Phosphoserine Ref.6
Modified residue4991Phosphotyrosine Ref.6

Natural variations

Alternative sequence1 – 7979Missing in isoform 4.
VSP_021697
Alternative sequence329 – 39466Missing in isoform 2 and isoform 3.
VSP_021698
Alternative sequence329 – 33810Missing in isoform 4.
VSP_021699
Alternative sequence329 – 33810LMSLLTSPHQ → VLAIWTLRGL in isoform 5.
VSP_021700
Alternative sequence339 – 616278Missing in isoform 5.
VSP_021701
Alternative sequence390 – 3945Missing in isoform 4.
VSP_021702
Alternative sequence5151E → ES in isoform 3.
VSP_021703

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 28, 2006. Version 2.
Checksum: 947BFCFCCA4BD1E2

FASTA61671,344
        10         20         30         40         50         60 
MSWGTELWDQ FDNLEKHTQW GIDILEKYIK FVKERTEIEL SYAKQLRNLS KKYQPKKNSK 

        70         80         90        100        110        120 
EEEEYKYTAC KAFLSTLNEM NDYAGQHEVI SENMTSQITV DLMRYVQELK QERKSNFHDG 

       130        140        150        160        170        180 
RKAQQHIETC WKQLESSKRR FERDCKEADR AQQYFEKMDA DINVTKADVE KARQQAQIRQ 

       190        200        210        220        230        240 
QMAEDSKADY SLILQRFNQE QWEYYHTHIP NIFQKIQEME ERRIVRIGES MKTYAEVDRQ 

       250        260        270        280        290        300 
VIPIIGKCLD GIVKAAESID QKNDSQLVVE AYKSGFEPPG DIEFEDYTQP MKRTVSDNSL 

       310        320        330        340        350        360 
SSSKEGKPEL RFGGKSRGKL WPFIKKNKLM SLLTSPHQPP PPPPASASPS AVPNGPQSPK 

       370        380        390        400        410        420 
QPKEPLSHRF NEFMTSKPKI HCFRSLKRGL SLKLGVTPED FSNFPPEQRR KKLQQKVDDL 

       430        440        450        460        470        480 
NREIQKETDQ RDAITKMKDV YLKNPQMGDP ASLDQKLTEV TQNIEKLRLE AQKFEAWLAE 

       490        500        510        520        530        540 
VEGRLPARSE QARRQSGLYD GQTHQTVTNC AQDRESPDGS YTEEQSQESE HKVLAPDFDD 

       550        560        570        580        590        600 
EFDDEEPLPA IGTCKALYTF EGQNEGTISV VEGETLSVIE EDKGDGWTRI RRNEDEEGYV 

       610 
PTSYVEVYLD KNAKGS 

« Hide

Isoform 2 [UniParc].

Checksum: AA80F83DEBE4AC5B
Show »

FASTA55064,139
Isoform 3 [UniParc].

Checksum: E73927365F88D8C2
Show »

FASTA55164,226
Isoform 4 [UniParc].

Checksum: 482B1709BE440057
Show »

FASTA52260,086
Isoform 5 [UniParc].

Checksum: F83CA4FE103657D2
Show »

FASTA33839,972

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 169-616 (ISOFORM 5).
Strain: C57BL/6J and NOD.
Tissue: Dendritic cell, Embryo, Kidney and Spleen.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
Strain: FVB/N.
Tissue: Mammary gland.
[5]"A novel dynamin-associating molecule, formin-binding protein 17, induces tubular membrane invaginations and participates in endocytosis."
Kamioka Y., Fukuhara S., Sawa H., Nagashima K., Masuda M., Matsuda M., Mochizuki N.
J. Biol. Chem. 279:40091-40099(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[6]"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-496 AND TYR-499, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Mast cell.
[7]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001033789.1. NM_001038700.2.
NP_001171119.1. NM_001177648.1.
NP_001171120.1. NM_001177649.1.
NP_001171121.1. NM_001177650.1.
NP_062279.1. NM_019406.3.
UniGeneMm.440993.
Mm.52297.

3D structure databases

ProteinModelPortalQ80TY0.
SMRQ80TY0. Positions 1-288, 399-485, 554-607.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199720. 1 interaction.
IntActQ80TY0. 2 interactions.
MINTMINT-4123990.
STRING10090.ENSMUSP00000109183.

PTM databases

PhosphoSiteQ80TY0.

Proteomic databases

PaxDbQ80TY0.
PRIDEQ80TY0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000113552; ENSMUSP00000109181; ENSMUSG00000075415. [Q80TY0-5]
ENSMUST00000113559; ENSMUSP00000109189; ENSMUSG00000075415. [Q80TY0-4]
ENSMUST00000113560; ENSMUSP00000109190; ENSMUSG00000075415. [Q80TY0-1]
ENSMUST00000113562; ENSMUSP00000109192; ENSMUSG00000075415. [Q80TY0-2]
ENSMUST00000113564; ENSMUSP00000109194; ENSMUSG00000075415. [Q80TY0-3]
GeneID14269.
KEGGmmu:14269.
UCSCuc008jdh.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

CTD23048.
MGIMGI:109606. Fnbp1.
RougeSearch...

Phylogenomic databases

eggNOGNOG323796.
GeneTreeENSGT00510000046403.
HOVERGENHBG002489.
OMALDKNAKG.
PhylomeDBQ80TY0.
TreeFamTF351162.

Gene expression databases

ArrayExpressQ80TY0.
BgeeQ80TY0.
CleanExMM_FNBP1.
GenevestigatorQ80TY0.

Family and domain databases

InterProIPR001060. FCH_dom.
IPR028532. FNBP1.
IPR001452. SH3_domain.
[Graphical view]
PANTHERPTHR12602:SF23. PTHR12602:SF23. 1 hit.
PfamPF00611. FCH. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
SMARTSM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS50133. FCH. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFNBP1. mouse.
NextBio285633.
PROQ80TY0.
SOURCESearch...

Entry information

Entry nameFNBP1_MOUSE
AccessionPrimary (citable) accession number: Q80TY0
Secondary accession number(s): A2AQ40 expand/collapse secondary AC list , A2AQ46, Q3TA45, Q3TCW9, Q3U081, Q3UPI7, Q8C727, Q99L37
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 28, 2006
Last modified: April 16, 2014
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot