DBN1

DBN1
Identifiers
Aliases	DBN1, D0S117E, drebrin 1
External IDs	OMIM: 126660 MGI: 1931838 HomoloGene: 3236 GeneCards: DBN1
Gene location (Human) Chr. Chromosome 5 (human) Band 5q35.3 Start 177,456,608 bp End 177,474,401 bp
Gene location (Mouse) Chr. Chromosome 13 (mouse) Band 13 B1|13 30.06 cM Start 55,621,242 bp End 55,635,924 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in ganglionic eminence sural nerve stromal cell of endometrium gastric mucosa ascending aorta left uterine tube nucleus accumbens caudate nucleus canal of the cervix anterior pituitary Top expressed in maxillary prominence ganglionic eminence superior frontal gyrus olfactory tubercle subiculum neural tube internal carotid artery medial ganglionic eminence somite external carotid artery More reference expression data BioGPS More reference expression data
Gene ontology Molecular function profilin binding protein binding actin binding cadherin binding Cellular component cell projection membrane cell-cell junction intracellular anatomical structure cell junction dendrite cell cortex gap junction actomyosin cytoplasm growth cone plasma membrane actin cytoskeleton cytoskeleton postsynaptic density cortical cytoskeleton postsynaptic membrane glutamatergic synapse postsynaptic cytosol Biological process cell differentiation cell communication by electrical coupling regulation of dendrite development nervous system development generation of neurons multicellular organism development neural precursor cell proliferation regulation of neuronal synaptic plasticity maintenance of protein location in cell cell communication by chemical coupling actin filament organization positive regulation of synaptic plasticity cytoplasmic sequestering of protein positive regulation of dendritic spine morphogenesis positive regulation of receptor localization to synapse Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 1627 56320 Ensembl ENSG00000113758 ENSMUSG00000034675 UniProt Q16643 Q9QXS6 RefSeq (mRNA) NM_004395 NM_080881 NM_001363541 NM_001364151 NM_001364152 NM_001393630 NM_001393631 NM_001177371 NM_001177372 NM_019813 RefSeq (protein) NP_004386 NP_543157 NP_001350470 NP_001351080 NP_001351081 NP_001170842 NP_001170843 NP_062787 Location (UCSC) Chr 5: 177.46 – 177.47 Mb Chr 13: 55.62 – 55.64 Mb PubMed search
Wikidata
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Drebrin is a protein that in humans is encoded by the DBN1 gene.

The protein encoded by this gene is a cytoplasmic actin-binding protein thought to play a role in the process of neuronal growth. It is a member of the drebrin family of proteins that are developmentally regulated in the brain. A decrease in the amount of this protein in the brain has been implicated as a possible contributing factor in the pathogenesis of memory disturbance in Alzheimer's disease. At least two alternative splice variants encoding different protein isoforms have been described for this gene.

Further reading

• Shirao T (1995). "The roles of microfilament-associated proteins, drebrins, in brain morphogenesis: a review". J. Biochem. 117 (2): 231–6. doi:10.1093/jb/117.2.231. PMID 7608104.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Harigaya Y, Shoji M, Shirao T, Hirai S (1996). "Disappearance of actin-binding protein, drebrin, from hippocampal synapses in Alzheimer's disease". J. Neurosci. Res. 43 (1): 87–92. doi:10.1002/jnr.490430111. PMID 8838578. S2CID 40336358.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Mammoto A, Sasaki T, Asakura T, et al. (1998). "Interactions of drebrin and gephyrin with profilin". Biochem. Biophys. Res. Commun. 243 (1): 86–9. doi:10.1006/bbrc.1997.8068. PMID 9473484.
• Hayashi K, Ishikawa R, Kawai-Hirai R, et al. (2000). "Domain analysis of the actin-binding and actin-remodeling activities of drebrin". Exp. Cell Res. 253 (2): 673–80. doi:10.1006/excr.1999.4663. PMID 10585290.
• Peitsch WK, Grund C, Kuhn C, et al. (2000). "Drebrin is a widespread actin-associating protein enriched at junctional plaques, defining a specific microfilament anchorage system in polar epithelial cells". Eur. J. Cell Biol. 78 (11): 767–78. doi:10.1016/s0171-9335(99)80027-2. PMID 10604653.
• Hartley JL, Temple GF, Brasch MA (2001). "DNA Cloning Using In Vitro Site-Specific Recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
• Wiemann S, Weil B, Wellenreuther R, et al. (2001). "Toward a Catalog of Human Genes and Proteins: Sequencing and Analysis of 500 Novel Complete Protein Coding Human cDNAs". Genome Res. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
• Simpson JC, Wellenreuther R, Poustka A, et al. (2001). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Rep. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMC 1083732. PMID 11256614.
• Kobayashi S, Shirao T, Sasaki T (2001). "Drebrin expression is increased in spinal motoneurons of rats after axotomy". Neurosci. Lett. 311 (3): 165–8. doi:10.1016/S0304-3940(01)02155-3. PMID 11578820. S2CID 15935730.
• Shim KS, Lubec G (2002). "Drebrin, a dendritic spine protein, is manifold decreased in brains of patients with Alzheimer's disease and Down syndrome". Neurosci. Lett. 324 (3): 209–12. doi:10.1016/S0304-3940(02)00210-0. PMID 12009525. S2CID 20834151.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801. S2CID 23783563.
• Shiraishi Y, Mizutani A, Mikoshiba K, Furuichi T (2003). "Coincidence in dendritic clustering and synaptic targeting of homer proteins and NMDA receptor complex proteins NR2B and PSD95 during development of cultured hippocampal neurons". Mol. Cell. Neurosci. 22 (2): 188–201. doi:10.1016/S1044-7431(03)00037-X. PMID 12676529. S2CID 38323844.
• Peitsch WK, Hofmann I, Endlich N, et al. (2003). "Cell biological and biochemical characterization of drebrin complexes in mesangial cells and podocytes of renal glomeruli". J. Am. Soc. Nephrol. 14 (6): 1452–63. doi:10.1097/01.ASN.0000069222.63700.DE. PMID 12761245.
• Salazar MA, Kwiatkowski AV, Pellegrini L, et al. (2004). "Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl homology domains, links dynamin to regulation of the actin cytoskeleton". J. Biol. Chem. 278 (49): 49031–43. doi:10.1074/jbc.M308104200. PMID 14506234.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.