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Q80TY0

- FNBP1_MOUSE

UniProt

Q80TY0 - FNBP1_MOUSE

Protein

Formin-binding protein 1

Gene

Fnbp1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 2 (28 Nov 2006)
      Previous versions | rss
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    Functioni

    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.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei166 – 1661Mediates end-to-end attachment of dimersBy similarity

    GO - Molecular functioni

    1. lipid binding Source: UniProtKB-KW

    GO - Biological processi

    1. endocytosis Source: UniProtKB-KW

    Keywords - Biological processi

    Endocytosis

    Keywords - Ligandi

    Lipid-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Formin-binding protein 1
    Alternative name(s):
    Formin-binding protein 17
    Gene namesi
    Name:Fnbp1
    Synonyms:Fbp17, Kiaa0554
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:109606. Fnbp1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cell cortex Source: UniProtKB-SubCell
    2. coated pit Source: UniProtKB-SubCell
    3. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
    4. cytoskeleton Source: UniProtKB-SubCell
    5. lysosome Source: UniProtKB-SubCell
    6. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Coated pit, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Lysosome, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 616616Formin-binding protein 1PRO_0000261431Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei66 – 661N6-acetyllysineBy similarity
    Modified residuei110 – 1101N6-acetyllysineBy similarity
    Modified residuei296 – 2961Phosphoserine1 Publication
    Modified residuei299 – 2991PhosphoserineBy similarity
    Modified residuei348 – 3481PhosphoserineBy similarity
    Modified residuei358 – 3581PhosphoserineBy similarity
    Modified residuei496 – 4961Phosphoserine1 Publication
    Modified residuei499 – 4991Phosphotyrosine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ80TY0.
    PaxDbiQ80TY0.
    PRIDEiQ80TY0.

    PTM databases

    PhosphoSiteiQ80TY0.

    Expressioni

    Tissue specificityi

    Expressed in brain and testis.1 Publication

    Gene expression databases

    ArrayExpressiQ80TY0.
    BgeeiQ80TY0.
    CleanExiMM_FNBP1.
    GenevestigatoriQ80TY0.

    Interactioni

    Subunit structurei

    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.By similarity

    Protein-protein interaction databases

    BioGridi199720. 1 interaction.
    IntActiQ80TY0. 2 interactions.
    MINTiMINT-4123990.
    STRINGi10090.ENSMUSP00000109183.

    Structurei

    3D structure databases

    ProteinModelPortaliQ80TY0.
    SMRiQ80TY0. Positions 1-288, 399-485, 554-607.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 6565FCHPROSITE-ProRule annotationAdd
    BLAST
    Repeati415 – 49076REMAdd
    BLAST
    Domaini549 – 61062SH3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 334334Interaction with microtubulesBy similarityAdd
    BLAST
    Regioni1 – 288288F-BAR domainBy similarityAdd
    BLAST
    Regioni1 – 7979Required for self-association and induction of membrane tubulationBy similarityAdd
    BLAST
    Regioni251 – 616366Required for self-association and induction of membrane tubulationBy similarityAdd
    BLAST
    Regioni399 – 551153Interaction with RND2By similarityAdd
    BLAST
    Regioni494 – 616123Interaction with PDE6GBy similarityAdd
    BLAST
    Regioni513 – 616104Required for interaction with TNKSBy similarityAdd
    BLAST
    Regioni534 – 61683Interaction with DNM1 and DNM3By similarityAdd
    BLAST
    Regioni549 – 61668Interaction with ARHGAP17, DAAM1, DIAPH1 and DIAPH2By similarityAdd
    BLAST
    Regioni552 – 60958Interaction with FASLGBy similarityAdd
    BLAST
    Regioni552 – 60857Interaction with DNM2 and WASLBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili67 – 259193By similarityAdd
    BLAST
    Coiled coili398 – 49093By similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi336 – 36530Pro-richAdd
    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.
    GeneTreeiENSGT00510000046403.
    HOVERGENiHBG002489.
    OMAiVYIKNPQ.
    PhylomeDBiQ80TY0.
    TreeFamiTF351162.

    Family and domain databases

    InterProiIPR001060. FCH_dom.
    IPR028532. FNBP1.
    IPR001452. SH3_domain.
    [Graphical view]
    PANTHERiPTHR12602:SF21. PTHR12602:SF21. 1 hit.
    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: Q80TY0-1) [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 FDNLEKHTQW GIDILEKYIK FVKERTEIEL SYAKQLRNLS    50
    KKYQPKKNSK EEEEYKYTAC KAFLSTLNEM NDYAGQHEVI SENMTSQITV 100
    DLMRYVQELK QERKSNFHDG RKAQQHIETC WKQLESSKRR FERDCKEADR 150
    AQQYFEKMDA DINVTKADVE KARQQAQIRQ QMAEDSKADY SLILQRFNQE 200
    QWEYYHTHIP NIFQKIQEME ERRIVRIGES MKTYAEVDRQ VIPIIGKCLD 250
    GIVKAAESID QKNDSQLVVE AYKSGFEPPG DIEFEDYTQP MKRTVSDNSL 300
    SSSKEGKPEL RFGGKSRGKL WPFIKKNKLM SLLTSPHQPP PPPPASASPS 350
    AVPNGPQSPK QPKEPLSHRF NEFMTSKPKI HCFRSLKRGL SLKLGVTPED 400
    FSNFPPEQRR KKLQQKVDDL NREIQKETDQ RDAITKMKDV YLKNPQMGDP 450
    ASLDQKLTEV TQNIEKLRLE AQKFEAWLAE VEGRLPARSE QARRQSGLYD 500
    GQTHQTVTNC AQDRESPDGS YTEEQSQESE HKVLAPDFDD EFDDEEPLPA 550
    IGTCKALYTF EGQNEGTISV VEGETLSVIE EDKGDGWTRI RRNEDEEGYV 600
    PTSYVEVYLD KNAKGS 616
    Length:616
    Mass (Da):71,344
    Last modified:November 28, 2006 - v2
    Checksum:i947BFCFCCA4BD1E2
    GO
    Isoform 2 (identifier: Q80TY0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         329-394: Missing.

    Show »
    Length:550
    Mass (Da):64,139
    Checksum:iAA80F83DEBE4AC5B
    GO
    Isoform 3 (identifier: Q80TY0-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         329-394: Missing.
         515-515: E → ES

    Show »
    Length:551
    Mass (Da):64,226
    Checksum:iE73927365F88D8C2
    GO
    Isoform 4 (identifier: Q80TY0-4) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:522
    Mass (Da):60,086
    Checksum:i482B1709BE440057
    GO
    Isoform 5 (identifier: Q80TY0-5) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:338
    Mass (Da):39,972
    Checksum:iF83CA4FE103657D2
    GO

    Sequence cautioni

    The sequence BAC65590.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAE33974.1 differs from that shown. Reason: Erroneous initiation.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7979Missing in isoform 4. 1 PublicationVSP_021697Add
    BLAST
    Alternative sequencei329 – 39466Missing in isoform 2 and isoform 3. 1 PublicationVSP_021698Add
    BLAST
    Alternative sequencei329 – 33810Missing in isoform 4. 1 PublicationVSP_021699
    Alternative sequencei329 – 33810LMSLLTSPHQ → VLAIWTLRGL in isoform 5. 2 PublicationsVSP_021700
    Alternative sequencei339 – 616278Missing in isoform 5. 2 PublicationsVSP_021701Add
    BLAST
    Alternative sequencei390 – 3945Missing in isoform 4. 1 PublicationVSP_021702
    Alternative sequencei515 – 5151E → ES in isoform 3. 1 PublicationVSP_021703

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS15894.1. [Q80TY0-5]
    CCDS38097.1. [Q80TY0-2]
    CCDS50560.1. [Q80TY0-4]
    CCDS50561.1. [Q80TY0-1]
    CCDS57165.1. [Q80TY0-3]
    RefSeqiNP_001033789.1. NM_001038700.2. [Q80TY0-2]
    NP_001171119.1. NM_001177648.1. [Q80TY0-1]
    NP_001171120.1. NM_001177649.1. [Q80TY0-3]
    NP_001171121.1. NM_001177650.1. [Q80TY0-4]
    NP_062279.1. NM_019406.3. [Q80TY0-5]
    UniGeneiMm.440993.
    Mm.52297.

    Genome annotation databases

    EnsembliENSMUST00000113552; ENSMUSP00000109181; ENSMUSG00000075415. [Q80TY0-5]
    ENSMUST00000113559; ENSMUSP00000109189; ENSMUSG00000075415. [Q80TY0-4]
    ENSMUST00000113560; ENSMUSP00000109190; ENSMUSG00000075415. [Q80TY0-1]
    ENSMUST00000113562; ENSMUSP00000109192; ENSMUSG00000075415. [Q80TY0-2]
    ENSMUST00000113564; ENSMUSP00000109194; ENSMUSG00000075415. [Q80TY0-3]
    GeneIDi14269.
    KEGGimmu:14269.
    UCSCiuc008jdh.1. mouse. [Q80TY0-4]
    uc008jdi.2. mouse. [Q80TY0-2]
    uc008jdj.2. mouse. [Q80TY0-1]
    uc008jdk.2. mouse. [Q80TY0-3]
    uc008jdm.2. mouse. [Q80TY0-5]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS15894.1. [Q80TY0-5 ]
    CCDS38097.1. [Q80TY0-2 ]
    CCDS50560.1. [Q80TY0-4 ]
    CCDS50561.1. [Q80TY0-1 ]
    CCDS57165.1. [Q80TY0-3 ]
    RefSeqi NP_001033789.1. NM_001038700.2. [Q80TY0-2 ]
    NP_001171119.1. NM_001177648.1. [Q80TY0-1 ]
    NP_001171120.1. NM_001177649.1. [Q80TY0-3 ]
    NP_001171121.1. NM_001177650.1. [Q80TY0-4 ]
    NP_062279.1. NM_019406.3. [Q80TY0-5 ]
    UniGenei Mm.440993.
    Mm.52297.

    3D structure databases

    ProteinModelPortali Q80TY0.
    SMRi Q80TY0. Positions 1-288, 399-485, 554-607.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199720. 1 interaction.
    IntActi Q80TY0. 2 interactions.
    MINTi MINT-4123990.
    STRINGi 10090.ENSMUSP00000109183.

    PTM databases

    PhosphoSitei Q80TY0.

    Proteomic databases

    MaxQBi Q80TY0.
    PaxDbi Q80TY0.
    PRIDEi Q80TY0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000113552 ; ENSMUSP00000109181 ; ENSMUSG00000075415 . [Q80TY0-5 ]
    ENSMUST00000113559 ; ENSMUSP00000109189 ; ENSMUSG00000075415 . [Q80TY0-4 ]
    ENSMUST00000113560 ; ENSMUSP00000109190 ; ENSMUSG00000075415 . [Q80TY0-1 ]
    ENSMUST00000113562 ; ENSMUSP00000109192 ; ENSMUSG00000075415 . [Q80TY0-2 ]
    ENSMUST00000113564 ; ENSMUSP00000109194 ; ENSMUSG00000075415 . [Q80TY0-3 ]
    GeneIDi 14269.
    KEGGi mmu:14269.
    UCSCi uc008jdh.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

    CTDi 23048.
    MGIi MGI:109606. Fnbp1.
    Rougei Search...

    Phylogenomic databases

    eggNOGi NOG323796.
    GeneTreei ENSGT00510000046403.
    HOVERGENi HBG002489.
    OMAi VYIKNPQ.
    PhylomeDBi Q80TY0.
    TreeFami TF351162.

    Miscellaneous databases

    ChiTaRSi FNBP1. mouse.
    NextBioi 285633.
    PROi Q80TY0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q80TY0.
    Bgeei Q80TY0.
    CleanExi MM_FNBP1.
    Genevestigatori Q80TY0.

    Family and domain databases

    InterProi IPR001060. FCH_dom.
    IPR028532. FNBP1.
    IPR001452. SH3_domain.
    [Graphical view ]
    PANTHERi PTHR12602:SF21. PTHR12602:SF21. 1 hit.
    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. "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.
      , 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. 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].

    Entry informationi

    Entry nameiFNBP1_MOUSE
    AccessioniPrimary (citable) accession number: Q80TY0
    Secondary accession number(s): A2AQ40
    , A2AQ46, Q3TA45, Q3TCW9, Q3U081, Q3UPI7, Q8C727, Q99L37
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2006
    Last sequence update: November 28, 2006
    Last modified: October 1, 2014
    This is version 82 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

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