Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

Q5T0N5

- FBP1L_HUMAN

UniProt

Q5T0N5 - FBP1L_HUMAN

Protein

Formin-binding protein 1-like

Gene

FNBP1L

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 3 (09 Jul 2014)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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/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.3 Publications

    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
    2. protein binding Source: IntAct

    GO - Biological processi

    1. autophagy Source: UniProtKB-KW
    2. clathrin-mediated endocytosis Source: BHF-UCL
    3. membrane budding Source: BHF-UCL
    4. membrane invagination Source: BHF-UCL
    5. membrane tubulation Source: BHF-UCL
    6. positive regulation of filopodium assembly Source: BHF-UCL
    7. vesicle organization Source: BHF-UCL
    8. vesicle transport along actin filament Source: BHF-UCL

    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:C1orf39, TOCA1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:20851. FNBP1L.

    Subcellular locationi

    Cytoplasm 1 Publication. 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. cell cortex Source: UniProtKB-SubCell
    2. cytoplasmic membrane-bounded vesicle Source: BHF-UCL
    3. cytoskeleton Source: UniProtKB-SubCell
    4. extracellular vesicular exosome Source: UniProt
    5. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi441 – 4433MGD → IST: Impairs interaction with CDC42 and reduces CDC42-induced actin assembly.
    Mutagenesisi576 – 5761W → K: Impairs interaction with WASL and reduces CDC42-induced actin assembly. 1 Publication

    Organism-specific databases

    PharmGKBiPA128394675.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 605605Formin-binding protein 1-likePRO_0000261434Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei295 – 2951Phosphoserine3 Publications
    Modified residuei488 – 4881Phosphoserine3 Publications
    Modified residuei501 – 5011Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ5T0N5.
    PaxDbiQ5T0N5.
    PRIDEiQ5T0N5.

    PTM databases

    PhosphoSiteiQ5T0N5.

    Expressioni

    Gene expression databases

    ArrayExpressiQ5T0N5.
    BgeeiQ5T0N5.
    CleanExiHS_FNBP1L.
    GenevestigatoriQ5T0N5.

    Interactioni

    Subunit structurei

    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.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DAAM1Q9Y4D12EBI-714058,EBI-2817289

    Protein-protein interaction databases

    BioGridi120222. 9 interactions.
    IntActiQ5T0N5. 6 interactions.
    MINTiMINT-1424364.
    STRINGi9606.ENSP00000271234.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5T0N5.
    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 CDC42Add
    BLAST
    Regioni522 – 60584Interaction with DNM1Add
    BLAST
    Regioni541 – 60565Interaction with DAAM1, DIAPH1 and DIAPH2Add
    BLAST
    Regioni541 – 59757Interaction with DNM2 and WASLAdd
    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.
    OrthoDBiEOG780RQK.
    PhylomeDBiQ5T0N5.

    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 (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q5T0N5-1) [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 DEEPRFTSCV 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
    ASKQESGKMD AKTTVGKAKG KLWLFGKKPK PQSPPLTPTS LFTSSTPNGS 350
    QFLTFSIEPV HYCMNEIKTG KPRIPSFRSL KRGWSVKMGP ALEDFSHLPP 400
    EQRRKKLQQR IDELNRELQK ESDQKDALNK MKDVYEKNPQ MGDPGSLQPK 450
    LAETMNNIDR LRMEIHKNEA WLSEVEGKTG GRGDRRHSSD INHLVTQGRE 500
    SPEGSYTDDA NQEVRGPPQQ HGHHNEFDDE FEDDDPLPAI GHCKAIYPFD 550
    GHNEGTLAMK EGEVLYIIEE DKGDGWTRAR RQNGEEGYVP TSYIDVTLEK 600
    NSKGS 605

    Note: Gene prediction based on EST data.

    Length:605
    Mass (Da):70,065
    Last modified:July 9, 2014 - v3
    Checksum:i1D9237185C3006ED
    GO
    Isoform 2 (identifier: Q5T0N5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         384-388: Missing.

    Note: Gene prediction based on EST data.

    Show »
    Length:600
    Mass (Da):69,434
    Checksum:i1C2DDFB3A3A5F0B3
    GO
    Isoform 3 (identifier: Q5T0N5-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         331-388: Missing.

    Show »
    Length:547
    Mass (Da):63,572
    Checksum:i416101498FF99567
    GO
    Isoform 4 (identifier: Q5T0N5-4) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:551
    Mass (Da):64,033
    Checksum:iB14EB59CE9010149
    GO
    Isoform 5 (identifier: Q5T0N5-5) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:604
    Mass (Da):69,894
    Checksum:i8C72A845744DDFB3
    GO

    Sequence cautioni

    The sequence BAA91051.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei331 – 38858Missing in isoform 3 and isoform 4. 3 PublicationsVSP_021709Add
    BLAST
    Alternative sequencei384 – 3885Missing in isoform 2 and isoform 5. CuratedVSP_021710
    Alternative sequencei605 – 6051S → AVTYI in isoform 4 and isoform 5. 1 PublicationVSP_021711

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY514449 mRNA. Translation: AAR98814.1.
    AC095034 Genomic DNA. No translation available.
    AL109613 Genomic DNA. No translation available.
    AL512651 Genomic DNA. No translation available.
    BC062477 mRNA. Translation: AAH62477.1.
    BC074891 mRNA. Translation: AAH74891.1.
    BC074892 mRNA. Translation: AAH74892.1.
    AK000282 mRNA. Translation: BAA91051.1. Different initiation.
    CCDSiCCDS53343.1. [Q5T0N5-1]
    CCDS53344.1. [Q5T0N5-4]
    CCDS60192.1. [Q5T0N5-3]
    RefSeqiNP_001020119.1. NM_001024948.2. [Q5T0N5-4]
    NP_001157945.1. NM_001164473.2.
    NP_060207.2. NM_017737.4. [Q5T0N5-3]
    UniGeneiHs.134060.

    Genome annotation databases

    EnsembliENST00000260506; ENSP00000260506; ENSG00000137942. [Q5T0N5-4]
    ENST00000271234; ENSP00000271234; ENSG00000137942. [Q5T0N5-1]
    ENST00000370253; ENSP00000359275; ENSG00000137942. [Q5T0N5-3]
    GeneIDi54874.
    KEGGihsa:54874.
    UCSCiuc001dpv.3. human. [Q5T0N5-3]
    uc001dpw.3. human. [Q5T0N5-4]

    Polymorphism databases

    DMDMi118572313.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY514449 mRNA. Translation: AAR98814.1 .
    AC095034 Genomic DNA. No translation available.
    AL109613 Genomic DNA. No translation available.
    AL512651 Genomic DNA. No translation available.
    BC062477 mRNA. Translation: AAH62477.1 .
    BC074891 mRNA. Translation: AAH74891.1 .
    BC074892 mRNA. Translation: AAH74892.1 .
    AK000282 mRNA. Translation: BAA91051.1 . Different initiation.
    CCDSi CCDS53343.1. [Q5T0N5-1 ]
    CCDS53344.1. [Q5T0N5-4 ]
    CCDS60192.1. [Q5T0N5-3 ]
    RefSeqi NP_001020119.1. NM_001024948.2. [Q5T0N5-4 ]
    NP_001157945.1. NM_001164473.2.
    NP_060207.2. NM_017737.4. [Q5T0N5-3 ]
    UniGenei Hs.134060.

    3D structure databases

    ProteinModelPortali Q5T0N5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120222. 9 interactions.
    IntActi Q5T0N5. 6 interactions.
    MINTi MINT-1424364.
    STRINGi 9606.ENSP00000271234.

    PTM databases

    PhosphoSitei Q5T0N5.

    Polymorphism databases

    DMDMi 118572313.

    Proteomic databases

    MaxQBi Q5T0N5.
    PaxDbi Q5T0N5.
    PRIDEi Q5T0N5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000260506 ; ENSP00000260506 ; ENSG00000137942 . [Q5T0N5-4 ]
    ENST00000271234 ; ENSP00000271234 ; ENSG00000137942 . [Q5T0N5-1 ]
    ENST00000370253 ; ENSP00000359275 ; ENSG00000137942 . [Q5T0N5-3 ]
    GeneIDi 54874.
    KEGGi hsa:54874.
    UCSCi uc001dpv.3. human. [Q5T0N5-3 ]
    uc001dpw.3. human. [Q5T0N5-4 ]

    Organism-specific databases

    CTDi 54874.
    GeneCardsi GC01P093913.
    HGNCi HGNC:20851. FNBP1L.
    MIMi 608848. gene.
    neXtProti NX_Q5T0N5.
    PharmGKBi PA128394675.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG323796.
    HOGENOMi HOG000231767.
    HOVERGENi HBG002489.
    OrthoDBi EOG780RQK.
    PhylomeDBi Q5T0N5.

    Miscellaneous databases

    GeneWikii FNBP1L.
    GenomeRNAii 54874.
    NextBioi 35537384.
    PROi Q5T0N5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q5T0N5.
    Bgeei Q5T0N5.
    CleanExi HS_FNBP1L.
    Genevestigatori Q5T0N5.

    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. "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.
      , 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.
      , 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. 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. 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].

    Entry informationi

    Entry nameiFBP1L_HUMAN
    AccessioniPrimary (citable) accession number: Q5T0N5
    Secondary accession number(s): J3QSS4
    , Q5T0N6, Q6B097, Q6P653, Q6R4Q4, Q9NXG1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2006
    Last sequence update: July 9, 2014
    Last modified: October 1, 2014
    This is version 100 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3