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Q96RU3

- FNBP1_HUMAN

UniProt

Q96RU3 - FNBP1_HUMAN

Protein

Formin-binding protein 1

Gene

FNBP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 2 (28 Nov 2006)
      Previous versions | rss
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    Functioni

    May act as a link between RND2 signaling and regulation of the actin cytoskeleton By similarity. 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 be required for the lysosomal retention of FASLG/FASL.By similarity5 Publications

    Sites

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

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. lipid binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB

    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
    Short name:
    hFBP17
    Gene namesi
    Name:FNBP1
    Synonyms:FBP17, KIAA0554
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:17069. FNBP1.

    Subcellular locationi

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

    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

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving FNBP1 is found in acute leukemias. Translocation t(9;11)(q34;q23) with KMT2A/MLL1. The relatively low incidence of the KMT2A/MLL1-FNBP1 fusion protein in acute leukemia may reflect the marginal capacity of this fusion protein to induce cellular transformation.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi7 – 71L → E: Impairs membrane tubulation but does not affect lipid-binding. 1 Publication
    Mutagenesisi33 – 331K → E: Abolishes membrane invagination. 2 Publications
    Mutagenesisi33 – 331K → Q: Impairs lipid-binding and induction of membrane tubulation; when associated with Q-35. 2 Publications
    Mutagenesisi35 – 351R → Q: Impairs lipid-binding and induction of membrane tubulation; when associated with Q-33. 1 Publication
    Mutagenesisi51 – 522KK → QQ: Impairs lipid-binding and induction of membrane tubulation.
    Mutagenesisi113 – 1142RK → QQ: Impairs lipid-binding and induction of membrane tubulation.
    Mutagenesisi165 – 1651T → A: Abolishes membrane invagination. 1 Publication
    Mutagenesisi166 – 1661K → A: Abolishes membrane invagination. 1 Publication
    Mutagenesisi168 – 1681D → A, N or R: No significant effect. 1 Publication
    Mutagenesisi210 – 2101P → A: Disrupts helix kink and moderately increases diameter of the induced tubular membrane. 1 Publication
    Mutagenesisi515 – 5206Missing: Abrogates interaction with TNKS. 1 Publication
    Mutagenesisi515 – 5151R → A: Impairs interaction with TNKS. 1 Publication
    Mutagenesisi519 – 5191D → A: Impairs interaction with TNKS; when associated with A-515. 1 Publication
    Mutagenesisi602 – 6021P → L: Abrogates interaction with DNM1, DNM2 and DNM3. 1 Publication

    Organism-specific databases

    PharmGKBiPA128394597.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 617617Formin-binding protein 1PRO_0000261430Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei66 – 661N6-acetyllysine1 Publication
    Modified residuei110 – 1101N6-acetyllysine1 Publication
    Modified residuei296 – 2961Phosphoserine4 Publications
    Modified residuei299 – 2991Phosphoserine2 Publications
    Modified residuei349 – 3491Phosphoserine1 Publication
    Modified residuei359 – 3591Phosphoserine3 Publications
    Modified residuei497 – 4971PhosphoserineBy similarity
    Modified residuei500 – 5001PhosphotyrosineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ96RU3.
    PaxDbiQ96RU3.
    PRIDEiQ96RU3.

    PTM databases

    PhosphoSiteiQ96RU3.

    Miscellaneous databases

    PMAP-CutDBQ96RU3.

    Expressioni

    Tissue specificityi

    Very highly expressed in the epithelial cells of the gastrointestinal tract, respiratory, reproductive and urinary systems. Also highly expressed in brown adipose tissue, cardiomyocytes, enteric ganglia and glucagon producing cells of the pancreas. Expressed in germ cells of the testis and all regions of the brain.2 Publications

    Gene expression databases

    ArrayExpressiQ96RU3.
    BgeeiQ96RU3.
    GenevestigatoriQ96RU3.

    Organism-specific databases

    HPAiHPA019691.
    HPA022119.

    Interactioni

    Subunit structurei

    Interacts specifically with GTP-bound RND2 and CDC42. Interacts with PDE6G and microtubules By similarity. Homodimerizes, the dimers can polymerize end-to-end to form filamentous structures. Interacts with AKAP9, ARHGAP17, DAAM1, DIAPH1, DIAPH2, DNM1, DNM2, DNM3, FASLG/FASL, SNX2 and WASL/N-WASP. May interact with TNKS.By similarity11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-1111248,EBI-1111248
    DNM1Q051935EBI-1111248,EBI-713135
    FASLGP480234EBI-1111248,EBI-495538
    GABARAPO951662EBI-1111248,EBI-712001
    SNX2O607494EBI-1111248,EBI-1046690
    TNKSO952714EBI-1111248,EBI-1105254

    Protein-protein interaction databases

    BioGridi116686. 19 interactions.
    IntActiQ96RU3. 17 interactions.
    MINTiMINT-238223.

    Structurei

    Secondary structure

    1
    617
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 64
    Turni7 – 93
    Helixi11 – 5242
    Helixi68 – 16093
    Helixi166 – 20641
    Helixi208 – 23831
    Helixi241 – 25717
    Helixi261 – 27212

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EFLX-ray2.61A1-300[»]
    ProteinModelPortaliQ96RU3.
    SMRiQ96RU3. Positions 1-288, 400-486, 555-608.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96RU3.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 6565FCHPROSITE-ProRule annotationAdd
    BLAST
    Repeati416 – 49176REMAdd
    BLAST
    Domaini550 – 61162SH3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 335335Interaction with microtubulesBy similarityAdd
    BLAST
    Regioni1 – 288288F-BAR domainAdd
    BLAST
    Regioni1 – 7979Required for self-association and induction of membrane tubulationAdd
    BLAST
    Regioni251 – 617367Required for self-association and induction of membrane tubulationAdd
    BLAST
    Regioni400 – 552153Interaction with RND2By similarityAdd
    BLAST
    Regioni495 – 617123Interaction with PDE6GBy similarityAdd
    BLAST
    Regioni514 – 617104Required for interaction with TNKSAdd
    BLAST
    Regioni535 – 61783Interaction with DNM1 and DNM3Add
    BLAST
    Regioni550 – 61768Interaction with ARHGAP17, DAAM1, DIAPH1 and DIAPH2Add
    BLAST
    Regioni553 – 61058Interaction with FASLGAdd
    BLAST
    Regioni553 – 60957Interaction with DNM2 and WASLAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili67 – 2591931 PublicationAdd
    BLAST
    Coiled coili398 – 49093By similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi340 – 3456Poly-Pro

    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.1 Publication

    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.
    HOVERGENiHBG002489.
    OMAiVYIKNPQ.
    OrthoDBiEOG780RQK.
    PhylomeDBiQ96RU3.
    TreeFamiTF351162.

    Family and domain databases

    Gene3Di3.40.50.620. 1 hit.
    InterProiIPR001060. FCH_dom.
    IPR028532. FNBP1.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR001452. SH3_domain.
    [Graphical view]
    PANTHERiPTHR12602:SF21. PTHR12602:SF21. 1 hit.
    PfamiPF00611. FCH. 1 hit.
    PF14604. SH3_9. 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 (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96RU3-1) [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 EEEEYKYTSC KAFISNLNEM NDYAGQHEVI SENMASQIIV 100
    DLARYVQELK QERKSNFHDG RKAQQHIETC WKQLESSKRR FERDCKEADR 150
    AQQYFEKMDA DINVTKADVE KARQQAQIRH QMAEDSKADY SSILQKFNHE 200
    QHEYYHTHIP NIFQKIQEME ERRIVRMGES MKTYAEVDRQ VIPIIGKCLD 250
    GIVKAAESID QKNDSQLVIE AYKSGFEPPG DIEFEDYTQP MKRTVSDNSL 300
    SNSRGEGKPD LKFGGKSKGK LWPFIKKNKL MSLLTSPHQP PPPPPASASP 350
    SAVPNGPQSP KQQKEPLSHR FNEFMTSKPK IHCFRSLKRG LSLKLGATPE 400
    DFSNLPPEQR RKKLQQKVDE LNKEIQKEMD QRDAITKMKD VYLKNPQMGD 450
    PASLDHKLAE VSQNIEKLRV ETQKFEAWLA EVEGRLPARS EQARRQSGLY 500
    DSQNPPTVNN CAQDRESPDG SYTEEQSQES EMKVLATDFD DEFDDEEPLP 550
    AIGTCKALYT FEGQNEGTIS VVEGETLYVI EEDKGDGWTR IRRNEDEEGY 600
    VPTSYVEVCL DKNAKDS 617
    Length:617
    Mass (Da):71,307
    Last modified:November 28, 2006 - v2
    Checksum:iF06E847C6E631EC3
    GO
    Isoform 2 (identifier: Q96RU3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         391-395: Missing.
         616-617: DS → GAKTYI

    Show »
    Length:616
    Mass (Da):71,184
    Checksum:iE82282A5164793B3
    GO
    Isoform 3 (identifier: Q96RU3-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         330-358: Missing.
         616-617: DS → GAKTYI

    Show »
    Length:592
    Mass (Da):68,883
    Checksum:i0CB6B44D9E174667
    GO
    Isoform 4 (identifier: Q96RU3-4) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:551
    Mass (Da):64,056
    Checksum:iBA7F73CA1A28A467
    GO

    Sequence cautioni

    The sequence AAH62463.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAK49824.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAA25480.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAA91451.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAI12149.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI12150.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI13910.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI13911.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti388 – 3881K → E in BAA91451. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti490 – 4901S → N.1 Publication
    Corresponds to variant rs1023000 [ dbSNP | Ensembl ].
    VAR_029388

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei329 – 39466Missing in isoform 4. 1 PublicationVSP_021693Add
    BLAST
    Alternative sequencei330 – 35829Missing in isoform 3. 1 PublicationVSP_021694Add
    BLAST
    Alternative sequencei391 – 3955Missing in isoform 2. 1 PublicationVSP_021695
    Alternative sequencei616 – 6172DS → GAKTYI in isoform 2 and isoform 3. 1 PublicationVSP_021696

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF265550 mRNA. Translation: AAK49824.1. Different initiation.
    AB011126 mRNA. Translation: BAA25480.1. Different initiation.
    AK000975 mRNA. Translation: BAA91451.1. Different initiation.
    AK023681 mRNA. Translation: BAB14638.1.
    AL136141, AL158207 Genomic DNA. Translation: CAI12149.1. Sequence problems.
    AL136141, AL158207 Genomic DNA. Translation: CAI12150.1. Sequence problems.
    AL158207, AL136141 Genomic DNA. Translation: CAI13910.1. Sequence problems.
    AL158207, AL136141 Genomic DNA. Translation: CAI13911.1. Sequence problems.
    BC062463 mRNA. Translation: AAH62463.1. Sequence problems.
    BC101755 mRNA. Translation: AAI01756.1.
    CCDSiCCDS48040.1. [Q96RU3-1]
    RefSeqiNP_055848.1. NM_015033.2. [Q96RU3-1]
    XP_005251880.1. XM_005251823.1. [Q96RU3-2]
    XP_005251886.1. XM_005251829.1. [Q96RU3-3]
    UniGeneiHs.189409.

    Genome annotation databases

    EnsembliENST00000355681; ENSP00000347907; ENSG00000187239. [Q96RU3-3]
    ENST00000446176; ENSP00000413625; ENSG00000187239. [Q96RU3-1]
    GeneIDi23048.
    KEGGihsa:23048.
    UCSCiuc004byw.1. human. [Q96RU3-1]
    uc004byx.1. human. [Q96RU3-2]
    uc004byz.1. human. [Q96RU3-3]

    Polymorphism databases

    DMDMi118572321.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF265550 mRNA. Translation: AAK49824.1 . Different initiation.
    AB011126 mRNA. Translation: BAA25480.1 . Different initiation.
    AK000975 mRNA. Translation: BAA91451.1 . Different initiation.
    AK023681 mRNA. Translation: BAB14638.1 .
    AL136141 , AL158207 Genomic DNA. Translation: CAI12149.1 . Sequence problems.
    AL136141 , AL158207 Genomic DNA. Translation: CAI12150.1 . Sequence problems.
    AL158207 , AL136141 Genomic DNA. Translation: CAI13910.1 . Sequence problems.
    AL158207 , AL136141 Genomic DNA. Translation: CAI13911.1 . Sequence problems.
    BC062463 mRNA. Translation: AAH62463.1 . Sequence problems.
    BC101755 mRNA. Translation: AAI01756.1 .
    CCDSi CCDS48040.1. [Q96RU3-1 ]
    RefSeqi NP_055848.1. NM_015033.2. [Q96RU3-1 ]
    XP_005251880.1. XM_005251823.1. [Q96RU3-2 ]
    XP_005251886.1. XM_005251829.1. [Q96RU3-3 ]
    UniGenei Hs.189409.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2EFL X-ray 2.61 A 1-300 [» ]
    ProteinModelPortali Q96RU3.
    SMRi Q96RU3. Positions 1-288, 400-486, 555-608.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116686. 19 interactions.
    IntActi Q96RU3. 17 interactions.
    MINTi MINT-238223.

    PTM databases

    PhosphoSitei Q96RU3.

    Polymorphism databases

    DMDMi 118572321.

    Proteomic databases

    MaxQBi Q96RU3.
    PaxDbi Q96RU3.
    PRIDEi Q96RU3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000355681 ; ENSP00000347907 ; ENSG00000187239 . [Q96RU3-3 ]
    ENST00000446176 ; ENSP00000413625 ; ENSG00000187239 . [Q96RU3-1 ]
    GeneIDi 23048.
    KEGGi hsa:23048.
    UCSCi uc004byw.1. human. [Q96RU3-1 ]
    uc004byx.1. human. [Q96RU3-2 ]
    uc004byz.1. human. [Q96RU3-3 ]

    Organism-specific databases

    CTDi 23048.
    GeneCardsi GC09M132649.
    HGNCi HGNC:17069. FNBP1.
    HPAi HPA019691.
    HPA022119.
    MIMi 606191. gene.
    neXtProti NX_Q96RU3.
    PharmGKBi PA128394597.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG323796.
    HOVERGENi HBG002489.
    OMAi VYIKNPQ.
    OrthoDBi EOG780RQK.
    PhylomeDBi Q96RU3.
    TreeFami TF351162.

    Miscellaneous databases

    ChiTaRSi FNBP1. human.
    EvolutionaryTracei Q96RU3.
    GeneWikii FNBP1.
    GenomeRNAii 23048.
    NextBioi 44088.
    PMAP-CutDB Q96RU3.
    PROi Q96RU3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96RU3.
    Bgeei Q96RU3.
    Genevestigatori Q96RU3.

    Family and domain databases

    Gene3Di 3.40.50.620. 1 hit.
    InterProi IPR001060. FCH_dom.
    IPR028532. FNBP1.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR001452. SH3_domain.
    [Graphical view ]
    PANTHERi PTHR12602:SF21. PTHR12602:SF21. 1 hit.
    Pfami PF00611. FCH. 1 hit.
    PF14604. SH3_9. 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. "The human formin-binding protein 17 (FBP17) interacts with sorting nexin, SNX2, and is an MLL-fusion partner in acute myelogeneous leukemia."
      Fuchs U., Rehkamp G.F., Haas O.A., Slany R., Koenig M., Bojesen S., Bohle R.M., Damm-Welk C., Ludwig W.-D., Harbott J., Borkhardt A.
      Proc. Natl. Acad. Sci. U.S.A. 98:8756-8761(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH SNX2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, CHROMOSOMAL TRANSLOCATION WITH KMT2A/MLL1.
    2. "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    3. "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] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-617 (ISOFORM 2), VARIANT ASN-490.
      Tissue: Embryo and Placenta.
    4. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-409 (ISOFORM 4).
      Tissue: Liver and Uterus.
    6. "Rich, a rho GTPase-activating protein domain-containing protein involved in signaling by Cdc42 and Rac1."
      Richnau N., Aspenstroem P.
      J. Biol. Chem. 276:35060-35070(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARHGAP17.
    7. "Identification of interaction partners of the cytosolic polyproline region of CD95 ligand (CD178)."
      Ghadimi M.P., Sanzenbacher R., Thiede B., Wenzel J., Jing Q., Plomann M., Borkhardt A., Kabelitz D., Janssen O.
      FEBS Lett. 519:50-58(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH FASLG.
    8. "The formin-binding protein 17, FBP17, binds via a TNKS binding motif to tankyrase, a protein involved in telomere maintenance."
      Fuchs U., Rehkamp G.F., Slany R., Follo M., Borkhardt A.
      FEBS Lett. 554:10-16(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SNX2 AND TNKS, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-515; ASP-519 AND 515-ARG--GLY-520.
    9. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. "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: FUNCTION, SELF-ASSOCIATION, INTERACTION WITH DNM1; DNM2 AND DNM3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF PRO-602.
    11. "AKAP350 interaction with cdc42 interacting protein 4 at the Golgi apparatus."
      Larocca M.C., Shanks R.A., Tian L., Nelson D.L., Stewart D.M., Goldenring J.R.
      Mol. Biol. Cell 15:2771-2781(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AKAP9, SUBCELLULAR LOCATION.
    12. "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, SELF-ASSOCIATION, INTERACTION WITH DNM1 AND WASL, SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-7.
    13. "Regulation of FasL expression: a SH3 domain containing protein family involved in the lysosomal association of FasL."
      Qian J., Chen W., Lettau M., Podda G., Zoernig M., Kabelitz D., Janssen O.
      Cell. Signal. 18:1327-1337(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FASLG, SUBCELLULAR LOCATION.
    14. "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.
    15. "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: FUNCTION, INTERACTION WITH DNM2 AND WASL, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-33; ARG-35; 51-LYS-LYS-52 AND 113-ARG-LYS-114.
    16. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-299; SER-349 AND SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "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].
    20. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    21. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-66 AND LYS-110, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "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-296 AND SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "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-296 AND SER-299, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. Cited for: X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 1-300, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN F-BAR, COILED-COIL DOMAIN, MUTAGENESIS OF LYS-33; THR-165; LYS-166; ASP-168 AND PRO-210.

    Entry informationi

    Entry nameiFNBP1_HUMAN
    AccessioniPrimary (citable) accession number: Q96RU3
    Secondary accession number(s): O60301
    , Q3MIN8, Q5TC87, Q5TC88, Q6P658, Q7LGG2, Q9H8H8, Q9NWD1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2006
    Last sequence update: November 28, 2006
    Last modified: October 1, 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
    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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3