DBN1

Drebrin is a protein that in humans is encoded by the DBN1 gene.[5][6]

DBN1
Identifiers
Aliases	DBN1, D0S117E, drebrin 1
External IDs	OMIM: 126660 MGI: 1931838 HomoloGene: 3236 GeneCards: DBN1
Gene location (Human) Chr. Chromosome 5 (human)[1] Band 5q35.3 Start 177,456,608 bp[1] End 177,474,401 bp[1]
Gene location (Mouse) Chr. Chromosome 13 (mouse)[2] Band 13 B1|13 30.06 cM Start 55,473,429 bp[2] End 55,488,111 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • profilin binding • GO:0001948 protein binding • actin binding • cadherin binding Cellular component • cell projection • membrane • intercellular junction • intracellular • cell junction • dendrite • cell cortex • gap junction • actomyosin • cytoplasm • growth cone • cell membrane • actin cytoskeleton • cytoskeleton • GO:0097483, GO:0097481 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_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: 55.47 – 55.49 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[6]

Model organisms

Model organisms have been used in the study of DBN1 function. A conditional knockout mouse line called Dbn1^{tm1b(KOMP)Wtsi} was generated at the Wellcome Trust Sanger Institute.[7] Male and female animals underwent a standardized phenotypic screen[8] to determine the effects of deletion.[9][10][11][12] Additional screens performed: - In-depth immunological phenotyping[13]

Dbn1 knockout mouse phenotype

Characteristic	Phenotype
All data available at.[8][13]
Peripheral blood leukocytes 6 Weeks	Normal
Haematology 6 Weeks	Normal
Homozygous viability at P14	Abnormal
Recessive lethal study	Normal
Body weight	Normal
Neurological assessment	Normal
Grip strength	Normal
Dysmorphology	Normal
Indirect calorimetry	Normal
Glucose tolerance test	Normal
Auditory brainstem response	Normal
DEXA	Normal
Radiography	Normal
Eye morphology	Normal
Clinical chemistry	Normal
Haematology 16 Weeks	Normal
Peripheral blood leukocytes 16 Weeks	Normal
Heart weight	Normal
Salmonella infection	Normal
Cytotoxic T Cell Function	Normal
Spleen Immunophenotyping	Normal
Mesenteric Lymph Node Immunophenotyping	Normal
Bone Marrow Immunophenotyping	Normal
Epidermal Immune Composition	Normal
Trichuris Challenge	Normal

References

1. GRCh38: Ensembl release 89: ENSG00000113758 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000034675 - 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.
5. Toda M, Shirao T, Minoshima S, Shimizu N, Toya S, Uyemura K (Nov 1993). "Molecular cloning of cDNA encoding human drebrin E and chromosomal mapping of its gene". Biochem Biophys Res Commun. 196 (1): 468–72. doi:10.1006/bbrc.1993.2273. PMID 8216329.
6. "Entrez Gene: DBN1 drebrin 1".
7. Gerdin AK (2010). "The Sanger Mouse Genetics Programme: high throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
8. "International Mouse Phenotyping Consortium".
9. Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (Jun 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
10. Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
11. Collins FS, Rossant J, Wurst W (Jan 2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
12. White JK, Gerdin AK, Karp NA, Ryder E, Buljan M, Bussell JN, Salisbury J, Clare S, Ingham NJ, Podrini C, Houghton R, Estabel J, Bottomley JR, Melvin DG, Sunter D, Adams NC, Sanger Institute Mouse Genetics Project, Tannahill D, Logan DW, Macarthur DG, Flint J, Mahajan VB, Tsang SH, Smyth I, Watt FM, Skarnes WC, Dougan G, Adams DJ, Ramirez-Solis R, Bradley A, Steel KP (2013). "Genome-wide generation and systematic phenotyping of knockout mice reveals new roles for many genes". Cell. 154 (2): 452–64. doi:10.1016/j.cell.2013.06.022. PMC 3717207. PMID 23870131.
13. "Infection and Immunity Immunophenotyping (3i) Consortium".

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.
• 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.
• 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.
• 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. 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.
• 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.
• 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.