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Q8K012

- FBP1L_MOUSE

UniProt

Q8K012 - FBP1L_MOUSE

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Protein
Formin-binding protein 1-like
Gene
Fnbp1l, Toca1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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-WASPIP 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 By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei165 – 1651Mediates end-to-end attachment of dimers By similarity

GO - Molecular functioni

  1. lipid binding Source: UniProtKB-KW

GO - Biological processi

  1. autophagy Source: UniProtKB-KW
  2. endocytosis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Autophagy, Endocytosis

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Formin-binding protein 1-like
Alternative name(s):
Transducer of Cdc42-dependent actin assembly protein 1
Short name:
Toca-1
Gene namesi
Name:Fnbp1l
Synonyms:Toca1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:1925642. Fnbp1l.

Subcellular locationi

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

GO - Cellular componenti

  1. cell cortex Source: UniProtKB-SubCell
  2. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
  3. cytoskeleton Source: UniProtKB-SubCell
  4. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 605605Formin-binding protein 1-like
PRO_0000261435Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei295 – 2951Phosphoserine1 Publication
Modified residuei488 – 4881Phosphoserine By similarity
Modified residuei501 – 5011Phosphoserine By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8K012.
PaxDbiQ8K012.
PRIDEiQ8K012.

PTM databases

PhosphoSiteiQ8K012.

Expressioni

Gene expression databases

CleanExiMM_FNBP1L.
GenevestigatoriQ8K012.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiQ8K012. 1 interaction.
MINTiMINT-4116706.

Structurei

3D structure databases

ProteinModelPortaliQ8K012.
SMRiQ8K012. Positions 10-287, 393-478, 542-602.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 6565FCH
Add
BLAST
Repeati409 – 48476REM
Add
BLAST
Domaini538 – 59962SH3
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 287287F-BAR domain By similarity
Add
BLAST
Regioni245 – 535291Interaction with CDC42 By similarity
Add
BLAST
Regioni522 – 60584Interaction with DNM1 By similarity
Add
BLAST
Regioni541 – 60565Interaction with DAAM1, DIAPH1 and DIAPH2 By similarity
Add
BLAST
Regioni541 – 59757Interaction with DNM2 and WASL By similarity
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili66 – 258193 By similarity
Add
BLAST
Coiled coili392 – 48493 By similarity
Add
BLAST

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.

Sequence similaritiesi

Belongs to the FNBP1 family.
Contains 1 FCH domain.
Contains 1 REM (Hr1) repeat.
Contains 1 SH3 domain.

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

eggNOGiNOG323796.
HOGENOMiHOG000231767.
HOVERGENiHBG002489.
InParanoidiQ8K012.
PhylomeDBiQ8K012.

Family and domain databases

InterProiIPR001060. FCH_dom.
IPR001452. SH3_domain.
[Graphical view]
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.
PROSITEiPS50133. FCH. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8K012-1) [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

MSWGTELWDQ FDSLDKHTQW GIDFLERYAK FVKERIEIEQ NYAKQLRNLV    50
KKYCPKRSSK DEEPRFTSCI AFFNILNELN DYAGQREVVA EEMAHRVYGE 100
LMRYAHDLKT ERKMHLQEGR KAQQYLDMCW KQMDNSKKKF ERECREAEKA 150
QQSYERLDND TNATKADVEK AKQQLNLRTH MADENKNEYA AQLQNFNGEQ 200
HKHFYVVIPQ IYKQLQEMDE RRTIKLSECY RGFADSERKV IPIISKCLEG 250
MILAAKSVDE RRDSQMVVDS FKSGFEPPGD FPFEDYSQHI YRTISDGTIS 300
AAKQESGKMD SKSTVGKAKG KLWLFGKKPK PQSPPLTPTS LFTSSTPNGS 350
QFLTLSIEPV HYCMNEIKTG KPRIPSFRSL KRGVSLIMGP ALEDFSHLPP 400
EQRRKKLQQR IDELNRGLQK EADQKEALNK MKDVYEKNPQ MGDPGSLQPK 450
LAETMNNIDR LRMEIHKNEA WLSEVEGKTG IRGDRRHSSD INHLVTQGRE 500
SPEGSYTDDA NQEVRGPPQQ HGHHSEFDDE FEDDDPLPAI GHCKAIYPFD 550
GHNEGTLAMK EGEVLYIIEE DKGDGWTRAR RQNGEEGYVP TTYIDVTLEK 600
SSKGS 605

Note: Gene prediction based on EST data.

Length:605
Mass (Da):69,885
Last modified:November 28, 2006 - v2
Checksum:iABFE6744EF4241E1
GO
Isoform 2 (identifier: Q8K012-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     331-389: Missing.
     605-605: S → AVTYI

Show »
Length:550
Mass (Da):63,918
Checksum:i1645834302E8AABE
GO

Sequence cautioni

The sequence AAH34510.1 differs from that shown. Reason: Erroneous initiation.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei331 – 38959Missing in isoform 2.
VSP_021712Add
BLAST
Alternative sequencei605 – 6051S → AVTYI in isoform 2.
VSP_021713

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC099584 Genomic DNA. No translation available.
AC138720 Genomic DNA. No translation available.
AK151930 mRNA. Translation: BAE30806.1.
AK152002 mRNA. Translation: BAE30866.1.
BC034510 mRNA. Translation: AAH34510.1. Different initiation.
UniGeneiMm.209491.
Mm.470230.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC099584 Genomic DNA. No translation available.
AC138720 Genomic DNA. No translation available.
AK151930 mRNA. Translation: BAE30806.1 .
AK152002 mRNA. Translation: BAE30866.1 .
BC034510 mRNA. Translation: AAH34510.1 . Different initiation.
UniGenei Mm.209491.
Mm.470230.

3D structure databases

ProteinModelPortali Q8K012.
SMRi Q8K012. Positions 10-287, 393-478, 542-602.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q8K012. 1 interaction.
MINTi MINT-4116706.

PTM databases

PhosphoSitei Q8K012.

Proteomic databases

MaxQBi Q8K012.
PaxDbi Q8K012.
PRIDEi Q8K012.

Protocols and materials databases

DNASUi 214459.
Structural Biology Knowledgebase Search...

Organism-specific databases

MGIi MGI:1925642. Fnbp1l.

Phylogenomic databases

eggNOGi NOG323796.
HOGENOMi HOG000231767.
HOVERGENi HBG002489.
InParanoidi Q8K012.
PhylomeDBi Q8K012.

Miscellaneous databases

ChiTaRSi FNBP1L. mouse.
NextBioi 374318.
PROi Q8K012.
SOURCEi Search...

Gene expression databases

CleanExi MM_FNBP1L.
Genevestigatori Q8K012.

Family and domain databases

InterProi IPR001060. FCH_dom.
IPR001452. SH3_domain.
[Graphical view ]
Pfami PF00611. FCH. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view ]
SMARTi SM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
PROSITEi PS50133. FCH. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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.
    , 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] OF 1-108 (ISOFORMS 1/2).
    Strain: C57BL/6J.
    Tissue: Bone marrow.
  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 132-605 (ISOFORM 2).
    Tissue: Eye.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "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-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFBP1L_MOUSE
AccessioniPrimary (citable) accession number: Q8K012
Secondary accession number(s): Q3U901
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 28, 2006
Last modified: May 14, 2014
This is version 105 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

External Data

Dasty 3

Similar proteinsi