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SNCB
Identifiers
Aliases	SNCB, entrez:6620, synuclein beta
External IDs	OMIM: 602569; MGI: 1889011; HomoloGene: 2320; GeneCards: SNCB; OMA:SNCB - orthologs
Gene location (Human) Chr. Chromosome 5 (human) Band 5q35.2 Start 176,620,082 bp End 176,630,556 bp
Gene location (Mouse) Chr. Chromosome 13 (mouse) Band 13 B1|13 29.28 cM Start 54,906,673 bp End 54,914,408 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right hemisphere of cerebellum right frontal lobe Brodmann area 10 anterior cingulate cortex dorsolateral prefrontal cortex paraflocculus of cerebellum Brodmann area 9 frontal pole Amygdala Hypothalamus Top expressed in dentate gyrus of hippocampal formation granule cell neural layer of retina primary visual cortex superior frontal gyrus perirhinal cortex entorhinal cortex CA3 field cerebellar cortex central gray substance of midbrain superior colliculus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function phospholipase inhibitor activity calcium ion binding transition metal ion binding cuprous ion binding Cellular component inclusion body synapse cytoplasm cytosol presynapse Biological process negative regulation of neuron apoptotic process synapse organization dopamine metabolic process chemical synaptic transmission negative regulation of catalytic activity response to metal ion synaptic vesicle endocytosis Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6620 104069 Ensembl ENSG00000074317 ENSMUSG00000034891 UniProt Q16143 Q91ZZ3 RefSeq (mRNA) NM_001001502 NM_003085 NM_001318034 NM_001318035 NM_001318036 NM_001318037 NM_001363140 NM_033610 NM_001362407 RefSeq (protein) NP_001001502 NP_001304963 NP_001304964 NP_001304965 NP_001304966 NP_003076 NP_001350069 NP_291088 NP_001349336 Location (UCSC) Chr 5: 176.62 – 176.63 Mb Chr 13: 54.91 – 54.91 Mb PubMed search
Wikidata
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Beta-synuclein is a protein that in humans is encoded by the SNCB gene.

The protein encoded by this gene is highly homologous to alpha-synuclein. These proteins are abundantly expressed in the brain and putatively inhibit phospholipase D2 selectively. The encoded protein, which may play a role in neuronal plasticity, is abundant in neurofibrillary lesions of patients with Alzheimer's disease. This protein has been shown to be highly expressed in the substantia nigra of the brain, a region of neuronal degeneration in patients with Parkinson's disease; however, no direct relation to Parkinson's disease has been established. Two transcript variants encoding the same protein have been found for this gene.

Beta-synuclein is a synuclein protein found primarily in brain tissue and is seen mainly in presynaptic terminals. Beta-synuclein is predominantly expressed in the neocortex, hippocampus, striatum, thalamus, and cerebellum. It is not found in Lewy bodies, but it is associated with hippocampal pathology in PD and DLB.

Beta-synuclein is suggested to be an inhibitor of alpha-synuclein aggregation, which occurs in neurodegenerative diseases such as Parkinson's disease. Thus, beta-synuclein may protect the central nervous system from the neurotoxic effects of alpha-synuclein and provide a novel treatment of neurodegenerative disorders.

See also

• Synuclein

References

1. ^ GRCh38: Ensembl release 89: ENSG00000074317 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000034891 – 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. Spillantini MG, Divane A, Goedert M (Nov 1995). "Assignment of human alpha-synuclein (SNCA) and beta-synuclein (SNCB) genes to chromosomes 4q21 and 5q35". Genomics. 27 (2): 379–81. doi:10.1006/geno.1995.1063. PMID 7558013.
6. Lavedan C, Leroy E, Torres R, Dehejia A, Dutra A, Buchholtz S, Nussbaum RL, Polymeropoulos MH (Jan 1999). "Genomic organization and expression of the human beta-synuclein gene (SNCB)". Genomics. 54 (1): 173–5. doi:10.1006/geno.1998.5556. PMID 9806846.
7. ^ "Entrez Gene: SNCB synuclein, beta".
8. George, JM (2002). "The synucleins". Genome Biology. 3 (1): REVIEWS3002. doi:10.1186/gb-2001-3-1-reviews3002. PMC 150459. PMID 11806835.
9. Hashimoto, M; Bar-On, P; Ho, G; Takenouchi, T; Rockenstein, E; Crews, L; Masliah, E (2004). "Beta-synuclein regulates Akt activity in neuronal cells. A possible mechanism for neuroprotection in Parkinson's disease". The Journal of Biological Chemistry. 279 (22): 23622–9. doi:10.1074/jbc.M313784200. PMID 15026413.
10. Hashimoto, M; Rockenstein, E; Mante, M; Mallory, M; Masliah, E (2001). "beta-Synuclein inhibits alpha-synuclein aggregation: a possible role as an anti-parkinsonian factor". Neuron. 32 (2): 213–23. doi:10.1016/S0896-6273(01)00462-7. PMID 11683992. S2CID 14766899.

Further reading

• Jakes R, Spillantini MG, Goedert M (1994). "Identification of two distinct synucleins from human brain". FEBS Lett. 345 (1): 27–32. doi:10.1016/0014-5793(94)00395-5. PMID 8194594. S2CID 36840279.
• Jensen PH, Hojrup P, Hager H, et al. (1997). "Binding of Abeta to alpha- and beta-synucleins: identification of segments in alpha-synuclein/NAC precursor that bind Abeta and NAC". Biochem. J. 323 (Pt 2): 539–46. doi:10.1042/bj3230539. PMC 1218353. PMID 9163350.
• Pronin AN, Morris AJ, Surguchov A, Benovic JL (2000). "Synucleins are a novel class of substrates for G protein-coupled receptor kinases". J. Biol. Chem. 275 (34): 26515–22. doi:10.1074/jbc.M003542200. PMID 10852916.
• Rockenstein E, Hansen LA, Mallory M, et al. (2001). "Altered expression of the synuclein family mRNA in Lewy body and Alzheimer's disease". Brain Res. 914 (1–2): 48–56. doi:10.1016/S0006-8993(01)02772-X. PMID 11578596. S2CID 35448948.
• Tanji K, Mori F, Nakajo S, et al. (2001). "Expression of beta-synuclein in normal human astrocytes". NeuroReport. 12 (13): 2845–8. doi:10.1097/00001756-200109170-00018. PMID 11588588. S2CID 84671534.
• Hashimoto M, Rockenstein E, Mante M, et al. (2001). "beta-Synuclein inhibits alpha-synuclein aggregation: a possible role as an anti-parkinsonian factor". Neuron. 32 (2): 213–23. doi:10.1016/S0896-6273(01)00462-7. PMID 11683992. S2CID 14766899.
• Uversky VN, Li J, Souillac P, et al. (2002). "Biophysical properties of the synucleins and their propensities to fibrillate: inhibition of alpha-synuclein assembly by beta- and gamma-synucleins". J. Biol. Chem. 277 (14): 11970–8. doi:10.1074/jbc.M109541200. PMID 11812782.
• 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.
• Ihara M, Tomimoto H, Kitayama H, et al. (2003). "Association of the cytoskeletal GTP-binding protein Sept4/H5 with cytoplasmic inclusions found in Parkinson's disease and other synucleinopathies". J. Biol. Chem. 278 (26): 24095–102. doi:10.1074/jbc.M301352200. PMID 12695511.
• Fung KM, Rorke LB, Giasson B, et al. (2003). "Expression of alpha-, beta-, and gamma-synuclein in glial tumors and medulloblastomas". Acta Neuropathol. 106 (2): 167–75. doi:10.1007/s00401-003-0718-x. PMID 12783249. S2CID 39712533.
• da Costa CA, Masliah E, Checler F (2003). "Beta-synuclein displays an antiapoptotic p53-dependent phenotype and protects neurons from 6-hydroxydopamine-induced caspase 3 activation: cross-talk with alpha-synuclein and implication for Parkinson's disease". J. Biol. Chem. 278 (39): 37330–5. doi:10.1074/jbc.M306083200. PMID 12867415.
• Ohtake H, Limprasert P, Fan Y, et al. (2005). "β-Synuclein gene alterations in dementia with Lewy bodies". Neurology. 63 (5): 805–11. doi:10.1212/01.wnl.0000139870.14385.3c. PMC 1808539. PMID 15365127.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Snyder H, Mensah K, Hsu C, et al. (2005). "beta-Synuclein reduces proteasomal inhibition by alpha-synuclein but not gamma-synuclein". J. Biol. Chem. 280 (9): 7562–9. doi:10.1074/jbc.M412887200. PMID 15591046.
• Sung YH, Eliezer D (2006). "Secondary structure and dynamics of micelle bound β- and γ-synuclein". Protein Sci. 15 (5): 1162–74. doi:10.1110/ps.051803606. PMC 2242515. PMID 16597821.
• Fan Y, Limprasert P, Murray IV, et al. (2006). "Beta-synuclein modulates alpha-synuclein neurotoxicity by reducing alpha-synuclein protein expression". Hum. Mol. Genet. 15 (20): 3002–11. doi:10.1093/hmg/ddl242. PMID 16959793.
• Myslinski E, Gérard MA, Krol A, Carbon P (2007). "A genome scale location analysis of human Staf/ZNF143-binding sites suggests a widespread role for human Staf/ZNF143 in mammalian promoters". J. Biol. Chem. 281 (52): 39953–62. doi:10.1074/jbc.M608507200. PMID 17092945.
• Sung YH, Eliezer D (2007). "Residual structure, backbone dynamics, and interactions within the synuclein family". J. Mol. Biol. 372 (3): 689–707. doi:10.1016/j.jmb.2007.07.008. PMC 2094134. PMID 17681534.

External links

• Human SNCB genome location and SNCB gene details page in the UCSC Genome Browser.

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