FNBP1

FNBP1
Available structures
PDB	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
Gene location (Human)
Chr.	Chromosome 9 (human)
End	130,043,194 bp
Gene location (Mouse)
Chr.	Chromosome 2 (mouse)
End	31,032,020 bp
RNA expression pattern
	Top expressed in
	corpus callosum; ; gastric mucosa; ; cerebellar hemisphere; ; saphenous vein; ; inferior ganglion of vagus nerve; ; thymus; ; sural nerve; ; seminal vesicula; ; middle frontal gyrus; ; inferior olivary nucleus;
	Top expressed in
	cerebellar cortex; ; cerebellar vermis; ; pontine nuclei; ; ventral tegmental area; ; medial geniculate nucleus; ; lateral geniculate nucleus; ; medial dorsal nucleus; ; globus pallidus; ; dorsal tegmental nucleus; ; anterior horn of spinal cord;
	More reference expression data
	; ;
	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
	23048
	14269
	ENSG00000187239
	ENSMUSG00000075415
	Q96RU3
	Q80TY0
	NM_015033 ; NM_001363755
NM_001038700 ; NM_001177648 ; NM_001177649 ; NM_001177650 ; NM_019406 ;
	NM_001355105 ; NM_001355106
	NP_055848 ; NP_001350684
NP_001033789 ; NP_001171119 ; NP_001171120 ; NP_001171121 ; NP_062279 ;
	NP_001342034 ; NP_001342035
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated August 19, 2023

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

Function

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]

Interactions

FNBP1 has been shown to interact with:

Related Research Articles

Fas ligand is a type-II transmembrane protein expressed on cytotoxic T lymphocytes and natural killer (NK) cells. Its binding with Fas receptor (FasR) induces programmed cell death in the FasR-carrying target cell. Fas ligand/receptor interactions play an important role in the regulation of the immune system and the progression of cancer.

In molecular biology, BAR domains are highly conserved protein dimerisation domains that occur in many proteins involved in membrane dynamics in a cell. The BAR domain is banana-shaped and binds to membrane via its concave face. It is capable of sensing membrane curvature by binding preferentially to curved membranes. BAR domains are named after three proteins that they are found in: Bin, Amphiphysin and Rvs.

Dynamin-2 is a protein that in humans is encoded by the DNM2 gene.

Alpha-actinin-1 is a protein that in humans is encoded by the ACTN1 gene.

Dynamin-1 is a protein that in humans is encoded by the DNM1 gene.

Telomeric repeat-binding factor 1 is a protein that in humans is encoded by the TERF1 gene.

Laminin subunit alpha-1 is a protein that in humans is encoded by the LAMA1 gene.

Dedicator of cytokinesis protein 1 (Dock1), also (DOCK180), is a large protein encoded in the human by the DOCK1 gene, involved in intracellular signalling networks. It is the mammalian ortholog of the C. elegans protein CED-5 and belongs to the DOCK family of guanine nucleotide exchange factors (GEFs).

Pre-mRNA-processing factor 40 homolog A is a protein that in humans is encoded by the PRPF40A gene.

Tankyrase, also known as tankyrase 1, is an enzyme that in humans is encoded by the TNKS gene. It inhibits the binding of TERF1 to telomeric DNA. Tankyrase attracts substantial interest in cancer research through its interaction with AXIN1 and AXIN2, which are negative regulators of pro-oncogenic β-catenin signaling. Importantly, activity in the β-catenin destruction complex can be increased by tankyrase inhibitors and thus such inhibitors are a potential therapeutic option to reduce the growth of β-catenin-dependent cancers.

Sorting nexin-9 is a protein that in humans is encoded by the SNX9 gene.

Sorting nexin-2 is a protein that in humans is encoded by the SNX2 gene.

Multiple PDZ domain protein is a protein that in humans is encoded by the MPDZ gene.

Dynamin-3 is a protein that in humans is encoded by the DNM3 gene. The protein encoded by this gene is a member of the dynamin family which possess mechanochemical properties involved in actin-membrane processes, predominantly in membrane budding. DNM3 is upregulated in Sézary's syndrome.

Formin-binding protein 1-like is a protein that in humans is encoded by the FNBP1L gene.

Tankyrase-2 is an enzyme that in humans is encoded by the TNKS2 gene.

182 kDa tankyrase-1-binding protein is an enzyme that in humans is encoded by the TNKS1BP1 gene.

Caveolin-2 is a protein that in humans is encoded by the CAV2 gene.

Di-N-acetylchitobiase is an enzyme that in humans is encoded by the CTBS gene.

Sorting Nexin 6 also known as SNX6 is a well-conserved membrane-associated protein belonging to the sorting nexin family that is a component of the retromer complex. The protein contains a coiled-coil domain at its C terminus and a PX domain at its N terminus. Binding to PIM1 causes translocation to the nucleus. SNX6 has been shown to associate with TRAF4.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000187239 - Ensembl, May 2017
1 2 3 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.
1 2 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.
1 2 "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.
1 2 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. 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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000187239 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000075415 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid9628581-5] 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.

[pmid11438682-6] 1 2 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.

[entrez-7] 1 2 "Entrez Gene: FNBP1 formin binding protein 1".

[pmid15047863-8] 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.

[pmid15252009-9] 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.

[pmid12023017-10] 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.

[pmid14596906-11] 1 2 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.

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FNBP1

Contents

Function

Interactions

Related Research Articles

References

Further reading