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Q5T0N5 (FBP1L_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Formin-binding protein 1-like
Alternative name(s):
Transducer of Cdc42-dependent actin assembly protein 1
Short name=Toca-1
Gene names
Name:FNBP1L
Synonyms:C1orf39, TOCA1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length605 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1 Ref.5 Ref.11

Subunit structure

Homodimerizes, the dimers can polymerize end-to-end to form filamentous structures By similarity. Interacts with GTP-bound CDC42. Interacts with DAAM1, DIAPH1, DIAPH2, DNM1, DNM2 and WASL/N-WASP. Interacts with ATG3. Ref.1 Ref.5 Ref.6 Ref.7 Ref.11

Subcellular location

Cytoplasm. Cytoplasmcytoskeleton By similarity. Cytoplasmcell cortex By similarity. Cytoplasmic vesicle By similarity. Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity Ref.8.

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 BAA91051.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAI18954.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI18981.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DAAM1Q9Y4D12EBI-714058,EBI-2817289

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: 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.
Note: Gene prediction based on EST data.
Isoform 2 (identifier: Q5T0N5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     384-388: Missing.
Note: Gene prediction based on EST data.
Isoform 3 (identifier: Q5T0N5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     331-388: Missing.
Isoform 4 (identifier: Q5T0N5-4)

The sequence of this isoform differs from the canonical sequence as follows:
     331-388: Missing.
     605-605: S → AVTYI
Note: Gene prediction based on EST data.
Isoform 5 (identifier: Q5T0N5-5)

The sequence of this isoform differs from the canonical sequence as follows:
     384-388: Missing.
     605-605: S → AVTYI
Note: Gene prediction based on EST data. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 605605Formin-binding protein 1-like
PRO_0000261434

Regions

Domain1 – 6565FCH
Repeat409 – 48476REM
Domain538 – 59962SH3
Region1 – 287287F-BAR domain By similarity
Region245 – 535291Interaction with CDC42
Region522 – 60584Interaction with DNM1
Region541 – 60565Interaction with DAAM1, DIAPH1 and DIAPH2
Region541 – 59757Interaction with DNM2 and WASL
Coiled coil66 – 258193 By similarity
Coiled coil392 – 48493 By similarity

Sites

Site1651Mediates end-to-end attachment of dimers By similarity

Amino acid modifications

Modified residue2951Phosphoserine Ref.9 Ref.12 Ref.14
Modified residue4881Phosphoserine Ref.9 Ref.12 Ref.14
Modified residue5011Phosphoserine Ref.9 Ref.12 Ref.14

Natural variations

Alternative sequence331 – 38858Missing in isoform 3 and isoform 4.
VSP_021709
Alternative sequence384 – 3885Missing in isoform 2 and isoform 5.
VSP_021710
Alternative sequence6051S → AVTYI in isoform 4 and isoform 5.
VSP_021711

Experimental info

Mutagenesis441 – 4433MGD → IST: Impairs interaction with CDC42 and reduces CDC42-induced actin assembly. Ref.1
Mutagenesis5761W → K: Impairs interaction with WASL and reduces CDC42-induced actin assembly. Ref.1

Sequences

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

Last modified November 28, 2006. Version 2.
Checksum: 9C8576E8FAA3B626

FASTA60569,977
        10         20         30         40         50         60 
MSWGTELWDQ FDSLDKHTQW GIDFLERYAK FVKERIEIEQ NYAKQLRNLV KKYCPKRSSK 

        70         80         90        100        110        120 
DEEPRFTSCV AFFNILNELN DYAGQREVVA EEMAHRVYGE LMRYAHDLKT ERKMHLQEGR 

       130        140        150        160        170        180 
KAQQYLDMCW KQMDNSKKKF ERECREAEKA QQSYERLDND TNATKADVEK AKQQLNLRTH 

       190        200        210        220        230        240 
MADENKNEYA AQLQNFNGEQ HKHFYVVIPQ IYKQLQEMDE RRTIKLSECY RGFADSERKV 

       250        260        270        280        290        300 
IPIISKCLEG MILAAKSVDE RRDSQMVVDS FKSGFEPPGD FPFEDYSQHI YRTISDGTIS 

       310        320        330        340        350        360 
ASKQESGKMD AKTTVGKAKG KLWLFGKKPK PQSPPLTPTS LFTSSTPNGS QFLTFSIEPV 

       370        380        390        400        410        420 
HYCMNEIKTG KPRIPSFRSL KRGVSLIMGP ALEDFSHLPP EQRRKKLQQR IDELNRELQK 

       430        440        450        460        470        480 
ESDQKDALNK MKDVYEKNPQ MGDPGSLQPK LAETMNNIDR LRMEIHKNEA WLSEVEGKTG 

       490        500        510        520        530        540 
GRGDRRHSSD INHLVTQGRE SPEGSYTDDA NQEVRGPPQQ HGHHNEFDDE FEDDDPLPAI 

       550        560        570        580        590        600 
GHCKAIYPFD GHNEGTLAMK EGEVLYIIEE DKGDGWTRAR RQNGEEGYVP TSYIDVTLEK 


NSKGS 

« Hide

Isoform 2 [UniParc].

Checksum: 1C2DDFB3A3A5F0B3
Show »

FASTA60069,434
Isoform 3 [UniParc].

Checksum: 416101498FF99567
Show »

FASTA54763,572
Isoform 4 [UniParc].

Checksum: B14EB59CE9010149
Show »

FASTA55164,033
Isoform 5 [UniParc].

Checksum: 8C72A845744DDFB3
Show »

FASTA60469,894

References

« Hide 'large scale' references
[1]"Toca-1 mediates Cdc42-dependent actin nucleation by activating the N-WASP-WIP complex."
Ho H.-Y.H., Rohatgi R., Lebensohn A.M., Ma L., Li J., Gygi S.P., Kirschner M.W.
Cell 118:203-216(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, INTERACTION WITH CDC42 AND WASL, MUTAGENESIS OF 441-MET--ASP-443 AND TRP-576.
Tissue: Fetal brain.
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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] OF 134-605 (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 208-605 (ISOFORM 3).
Tissue: Lung and Pituitary.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 200-605 (ISOFORM 3).
Tissue: Hepatoma.
[5]"Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins."
Itoh T., Erdmann K.S., Roux A., Habermann B., Werner H., De Camilli P.
Dev. Cell 9:791-804(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DNM1 AND WASL.
[6]"The diaphanous-related formin DAAM1 collaborates with the Rho GTPases RhoA and Cdc42, CIP4 and Src in regulating cell morphogenesis and actin dynamics."
Aspenstroem P., Richnau N., Johansson A.-S.
Exp. Cell Res. 312:2180-2194(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DAAM1; DIAPH1 AND DIAPH2.
[7]"Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis."
Tsujita K., Suetsugu S., Sasaki N., Furutani M., Oikawa T., Takenawa T.
J. Cell Biol. 172:269-279(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DNM2 AND WASL.
[8]"Tuba stimulates intracellular N-WASP-dependent actin assembly."
Kovacs E.M., Makar R.S., Gertler F.B.
J. Cell Sci. 119:2715-2726(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-488 AND SER-501, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"A novel hybrid yeast-human network analysis reveals an essential role for FNBP1L in antibacterial autophagy."
Huett A., Ng A., Cao Z., Kuballa P., Komatsu M., Daly M.J., Podolsky D.K., Xavier R.J.
J. Immunol. 182:4917-4930(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN AUTOPHAGY, INTERACTION WITH ATG3.
[12]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-488 AND SER-501, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-488 AND SER-501, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY514449 mRNA. Translation: AAR98814.1.
AL109613, AC095034, AL512651 Genomic DNA. Translation: CAI18952.1.
AL109613, AC095034, AL512651 Genomic DNA. Translation: CAI18953.1.
AL109613, AC095034, AL512651 Genomic DNA. Translation: CAI18954.1. Sequence problems.
AL512651, AC095034, AL109613 Genomic DNA. Translation: CAI18979.1.
AL512651, AC095034, AL109613 Genomic DNA. Translation: CAI18980.1.
AL512651, AC095034, AL109613 Genomic DNA. Translation: CAI18981.1. Sequence problems.
BC062477 mRNA. Translation: AAH62477.1.
BC074891 mRNA. Translation: AAH74891.1.
BC074892 mRNA. Translation: AAH74892.1.
AK000282 mRNA. Translation: BAA91051.1. Different initiation.
RefSeqNP_001020119.1. NM_001024948.2.
NP_001157945.1. NM_001164473.2.
NP_060207.2. NM_017737.4.
UniGeneHs.134060.

3D structure databases

ProteinModelPortalQ5T0N5.
SMRQ5T0N5. Positions 10-287, 393-484, 542-597.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120222. 9 interactions.
IntActQ5T0N5. 6 interactions.
MINTMINT-1424364.
STRING9606.ENSP00000271234.

PTM databases

PhosphoSiteQ5T0N5.

Polymorphism databases

DMDM118572313.

Proteomic databases

PaxDbQ5T0N5.
PRIDEQ5T0N5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000260506; ENSP00000260506; ENSG00000137942. [Q5T0N5-4]
ENST00000370253; ENSP00000359275; ENSG00000137942. [Q5T0N5-3]
ENST00000370256; ENSP00000359278; ENSG00000137942. [Q5T0N5-2]
GeneID54874.
KEGGhsa:54874.
UCSCuc001dpv.3. human. [Q5T0N5-3]
uc001dpw.3. human. [Q5T0N5-4]

Organism-specific databases

CTD54874.
GeneCardsGC01P093913.
HGNCHGNC:20851. FNBP1L.
MIM608848. gene.
neXtProtNX_Q5T0N5.
PharmGKBPA128394675.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG323796.
HOGENOMHOG000231767.
HOVERGENHBG002489.
OrthoDBEOG780RQK.
PhylomeDBQ5T0N5.

Gene expression databases

ArrayExpressQ5T0N5.
BgeeQ5T0N5.
CleanExHS_FNBP1L.
GenevestigatorQ5T0N5.

Family and domain databases

InterProIPR001060. FCH_dom.
IPR001452. SH3_domain.
[Graphical view]
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

GeneWikiFNBP1L.
GenomeRNAi54874.
NextBio57799.
PROQ5T0N5.
SOURCESearch...

Entry information

Entry nameFBP1L_HUMAN
AccessionPrimary (citable) accession number: Q5T0N5
Secondary accession number(s): Q5T0N6 expand/collapse secondary AC list , Q6B097, Q6P653, Q6R4Q4, Q9NXG1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 28, 2006
Last modified: April 16, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM