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FNBP1 - Wikipedia

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FNBP1

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
2EFL

Identifiers

Aliases

FNBP1, FBP17, formin binding protein 1

External IDs

OMIM: 606191; MGI: 109606; HomoloGene: 100983; GeneCards: FNBP1; OMA:FNBP1 - orthologs

Gene location (Human)

Chr.	Chromosome 9 (human)^[1]

Band	9q34.11	Start	129,887,187 bp^[1]
End	130,043,194 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 2 (mouse)^[2]

Band	2\|2 B	Start	30,916,218 bp^[2]
End	31,032,020 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

corpus callosum

gastric mucosa

cerebellar hemisphere

saphenous vein

right hemisphere of cerebellum

inferior ganglion of vagus nerve

paraflocculus of cerebellum

thymus

epithelium of colon

sural nerve

Top expressed in

cerebellar cortex

cerebellar vermis

lobe of cerebellum

pontine nuclei

deep cerebellar nuclei

ventral tegmental area

medial geniculate nucleus

lateral geniculate nucleus

medial dorsal nucleus

globus pallidus

More reference expression data

BioGPS

More reference expression data

Gene ontology
Molecular function	protein binding identical protein binding lipid binding
Cellular component	cytoplasm plasma membrane clathrin-coated pit lysosome cell cortex cytoskeleton membrane cytoplasmic vesicle cytosol
Biological process	endocytosis membrane organization
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


23048


14269

Ensembl


ENSG00000187239


ENSMUSG00000075415

UniProt


Q96RU3


Q80TY0

RefSeq (mRNA)


NM_015033 NM_001363755

NM_001038700 NM_001177648 NM_001177649 NM_001177650 NM_019406
NM_001355105 NM_001355106

RefSeq (protein)


NP_055848 NP_001350684

NP_001033789 NP_001171119 NP_001171120 NP_001171121 NP_062279
NP_001342034 NP_001342035

Location (UCSC)

Chr 9: 129.89 – 130.04 Mb

Chr 2: 30.92 – 31.03 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Formin-binding protein 1 is a protein that in humans is encoded by the FNBP1 gene.^[5]^[6]^[7]

The protein encoded by this gene is a member of the formin-binding-protein family. The protein contains an N-terminal Fer/Cdc42-interacting protein 4 (CIP4) homology (FCH) domain followed by a coiled-coil domain, a proline-rich motif, a second coiled-coil domain, a Rho family protein-binding domain (RBD), and a C-terminal SH3 domain. This protein binds sorting nexin 2 (SNX2), tankyrase (TNKS), and dynamin; an interaction between this protein and formin has not been demonstrated yet in human.^[7]

FNBP1 has been shown to interact with:

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000187239 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000075415 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (Aug 1998). "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". DNA Res. 5 (1): 31–9. doi:10.1093/dnares/5.1.31. PMID 9628581.
^ ^a ^b Fuchs U, Rehkamp G, Haas OA, Slany R, Kōnig M, Bojesen S, Bohle RM, Damm-Welk C, Ludwig WD, Harbott J, Borkhardt A (Jul 2001). "The human formin-binding protein 17 (FBP17) interacts with sorting nexin, SNX2, and is an MLL-fusion partner in acute myelogeneous leukemia". Proc Natl Acad Sci U S A. 98 (15): 8756–61. Bibcode:2001PNAS...98.8756F. doi:10.1073/pnas.121433898. PMC 37508. PMID 11438682.
^ ^a ^b "Entrez Gene: FNBP1 formin binding protein 1".
^ Larocca MC, Shanks RA, Tian L, Nelson DL, Stewart DM, Goldenring JR (Jun 2004). "AKAP350 interaction with cdc42 interacting protein 4 at the Golgi apparatus". Mol. Biol. Cell. 15 (6): 2771–81. doi:10.1091/mbc.E03-10-0757. PMC 420101. PMID 15047863.
^ Kamioka Y, Fukuhara S, Sawa H, Nagashima K, Masuda M, Matsuda M, Mochizuki N (Sep 2004). "A novel dynamin-associating molecule, formin-binding protein 17, induces tubular membrane invaginations and participates in endocytosis". J. Biol. Chem. 279 (38): 40091–9. doi:10.1074/jbc.M404899200. PMID 15252009.
^ Ghadimi MP, Sanzenbacher R, Thiede B, Wenzel J, Jing Q, Plomann M, Borkhardt A, Kabelitz D, Janssen O (May 2002). "Identification of interaction partners of the cytosolic polyproline region of CD95 ligand (CD178)". FEBS Lett. 519 (1–3): 50–8. doi:10.1016/s0014-5793(02)02709-6. PMID 12023017. S2CID 26765451.
^ ^a ^b Fuchs U, Rehkamp GF, Slany R, Follo M, Borkhardt A (Nov 2003). "The formin-binding protein 17, FBP17, binds via a TNKS binding motif to tankyrase, a protein involved in telomere maintenance". FEBS Lett. 554 (1–2): 10–6. doi:10.1016/s0014-5793(03)01063-9. PMID 14596906. S2CID 19552309.

Richnau N, Aspenström P (2001). "Rich, a rho GTPase-activating protein domain-containing protein involved in signaling by Cdc42 and Rac1". J. Biol. Chem. 276 (37): 35060–70. doi:10.1074/jbc.M103540200. PMID 11431473.
Ghadimi MP, Sanzenbacher R, Thiede B, Wenzel J, Jing Q, Plomann M, Borkhardt A, Kabelitz D, Janssen O (2002). "Identification of interaction partners of the cytosolic polyproline region of CD95 ligand (CD178)". FEBS Lett. 519 (1–3): 50–8. doi:10.1016/S0014-5793(02)02709-6. PMID 12023017. S2CID 26765451.
Fujita H, Katoh H, Ishikawa Y, Mori K, Negishi M (2003). "Rapostlin is a novel effector of Rnd2 GTPase inducing neurite branching". J. Biol. Chem. 277 (47): 45428–34. doi:10.1074/jbc.M208090200. PMID 12244061.
Katoh M, Katoh M (2004). "FNBP2 gene on human chromosome 1q32.1 encodes ARHGAP family protein with FCH, FBH, RhoGAP and SH3 domains". Int. J. Mol. Med. 11 (6): 791–7. doi:10.3892/ijmm.11.6.791. PMID 12736724.
Fuchs U, Rehkamp GF, Slany R, Follo M, Borkhardt A (2003). "The formin-binding protein 17, FBP17, binds via a TNKS binding motif to tankyrase, a protein involved in telomere maintenance". FEBS Lett. 554 (1–2): 10–6. doi:10.1016/S0014-5793(03)01063-9. PMID 14596906. S2CID 19552309.
Larocca MC, Shanks RA, Tian L, Nelson DL, Stewart DM, Goldenring JR (2004). "AKAP350 Interaction with cdc42 Interacting Protein 4 at the Golgi Apparatus". Mol. Biol. Cell. 15 (6): 2771–81. doi:10.1091/mbc.E03-10-0757. PMC 420101. PMID 15047863.
Brill LM, Salomon AR, Ficarro SB, Mukherji M, Stettler-Gill M, Peters EC (2004). "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry". Anal. Chem. 76 (10): 2763–72. doi:10.1021/ac035352d. PMID 15144186.
Kamioka Y, Fukuhara S, Sawa H, Nagashima K, Masuda M, Matsuda M, Mochizuki N (2004). "A novel dynamin-associating molecule, formin-binding protein 17, induces tubular membrane invaginations and participates in endocytosis". J. Biol. Chem. 279 (38): 40091–9. doi:10.1074/jbc.M404899200. PMID 15252009.
Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455. S2CID 7200157.
Zhou FL, Zhang WG, Chen G, Zhao WH, Cao XM, Chen YX, Tian W, Liu J, Liu SH (2006). "Serological identification and bioinformatics analysis of immunogenic antigens in multiple myeloma". Cancer Immunol. Immunother. 55 (8): 910–7. doi:10.1007/s00262-005-0074-x. PMC 11030602. PMID 16193335. S2CID 24083118.
Qian J, Chen W, Lettau M, Podda G, Zörnig M, Kabelitz D, Janssen O (2006). "Regulation of FasL expression: a SH3 domain containing protein family involved in the lysosomal association of FasL". Cell. Signal. 18 (8): 1327–37. doi:10.1016/j.cellsig.2005.10.015. PMID 16318909.
Itoh T, Erdmann KS, Roux A, Habermann B, Werner H, De Camilli P (2006). "Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins". Dev. Cell. 9 (6): 791–804. doi:10.1016/j.devcel.2005.11.005. PMID 16326391.
Tsujita K, Suetsugu S, Sasaki N, Furutani M, Oikawa T, Takenawa T (2006). "Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis". J. Cell Biol. 172 (2): 269–79. doi:10.1083/jcb.200508091. PMC 2063556. PMID 16418535.