Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8K012

- FBP1L_MOUSE

UniProt

Q8K012 - FBP1L_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Formin-binding protein 1-like

Gene

Fnbp1l

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).By similarity

Sites

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

GO - Molecular functioni

  1. lipid binding Source: UniProtKB-KW

GO - Biological processi

  1. autophagy Source: UniProtKB-KW
  2. cilium assembly Source: MGI
  3. 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 By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytoplasmic vesicle Source: UniProtKB-KW
  3. cytoskeleton Source: UniProtKB-KW
  4. plasma membrane Source: UniProtKB-KW
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-likePRO_0000261435Add
BLAST

Amino acid modifications

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

Protein-protein interaction databases

IntActiQ8K012. 1 interaction.
MINTiMINT-4116706.

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 6565FCHPROSITE-ProRule annotationAdd
BLAST
Repeati409 – 48476REMAdd
BLAST
Domaini538 – 59962SH3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 287287F-BAR domainBy similarityAdd
BLAST
Regioni245 – 535291Interaction with CDC42By similarityAdd
BLAST
Regioni522 – 60584Interaction with DNM1By similarityAdd
BLAST
Regioni541 – 60565Interaction with DAAM1, DIAPH1 and DIAPH2By similarityAdd
BLAST
Regioni541 – 59757Interaction with DNM2 and WASLBy similarityAdd
BLAST

Coiled coil

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

Sequence similaritiesi

Belongs to the FNBP1 family.Curated
Contains 1 FCH 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

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

        10         20         30         40         50
MSWGTELWDQ FDSLDKHTQW GIDFLERYAK FVKERIEIEQ NYAKQLRNLV
60 70 80 90 100
KKYCPKRSSK DEEPRFTSCI AFFNILNELN DYAGQREVVA EEMAHRVYGE
110 120 130 140 150
LMRYAHDLKT ERKMHLQEGR KAQQYLDMCW KQMDNSKKKF ERECREAEKA
160 170 180 190 200
QQSYERLDND TNATKADVEK AKQQLNLRTH MADENKNEYA AQLQNFNGEQ
210 220 230 240 250
HKHFYVVIPQ IYKQLQEMDE RRTIKLSECY RGFADSERKV IPIISKCLEG
260 270 280 290 300
MILAAKSVDE RRDSQMVVDS FKSGFEPPGD FPFEDYSQHI YRTISDGTIS
310 320 330 340 350
AAKQESGKMD SKSTVGKAKG KLWLFGKKPK PQSPPLTPTS LFTSSTPNGS
360 370 380 390 400
QFLTLSIEPV HYCMNEIKTG KPRIPSFRSL KRGVSLIMGP ALEDFSHLPP
410 420 430 440 450
EQRRKKLQQR IDELNRGLQK EADQKEALNK MKDVYEKNPQ MGDPGSLQPK
460 470 480 490 500
LAETMNNIDR LRMEIHKNEA WLSEVEGKTG IRGDRRHSSD INHLVTQGRE
510 520 530 540 550
SPEGSYTDDA NQEVRGPPQQ HGHHSEFDDE FEDDDPLPAI GHCKAIYPFD
560 570 580 590 600
GHNEGTLAMK EGEVLYIIEE DKGDGWTRAR RQNGEEGYVP TTYIDVTLEK

SSKGS

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. 1 PublicationVSP_021712Add
BLAST
Alternative sequencei605 – 6051S → AVTYI in isoform 2. 1 PublicationVSP_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: October 29, 2014
This is version 107 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