SYN1

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Synapsin I
PDB rendering based on 1auv.
Available structures: 1auv, 1aux, 1pk8, 1px2
Identifiers
Symbol(s) SYN1; SYN1a; SYN1b; SYNI
External IDs OMIM: 313440 MGI: 98460 HomoloGene: 48483
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 6853 20964
Ensembl ENSG00000008056 ENSMUSG00000037217
Uniprot P17600 O88935
Refseq NM_006950 (mRNA)
NP_008881 (protein)		 NM_013680 (mRNA)
NP_038708 (protein)
Location Chr X: 47.32 - 47.36 Mb Chr X: 20.02 - 20.08 Mb
Pubmed search [1] [2]

Synapsin I, also known as SYN1, is a human gene.[1]

This gene is a member of the synapsin gene family. Synapsins encode neuronal phosphoproteins which associate with the cytoplasmic surface of synaptic vesicles. Family members are characterized by common protein domains, and they are implicated in synaptogenesis and the modulation of neurotransmitter release, suggesting a potential role in several neuropsychiatric diseases. This member of the synapsin family plays a role in regulation of axonogenesis and synaptogenesis. The protein encoded serves as a substrate for several different protein kinases and phosphorylation may function in the regulation of this protein in the nerve terminal. Mutations in this gene may be associated with X-linked disorders with primary neuronal degeneration such as Rett syndrome. Alternatively spliced transcript variants encoding different isoforms have been identified.[1]

[edit] References

  1. ^ a b Entrez Gene: SYN1 synapsin I.

[edit] Further reading

  • Südhof TC, Czernik AJ, Kao HT, et al. (1989). "Synapsins: mosaics of shared and individual domains in a family of synaptic vesicle phosphoproteins.". Science 245 (4925): 1474–80. PMID 2506642. 
  • Greengard P, Valtorta F, Czernik AJ, Benfenati F (1993). "Synaptic vesicle phosphoproteins and regulation of synaptic function.". Science 259 (5096): 780–5. PMID 8430330. 
  • Kirchgessner CU, Trofatter JA, Mahtani MM, et al. (1991). "A highly polymorphic dinucleotide repeat on the proximal short arm of the human X chromosome: linkage mapping of the synapsin I/A-raf-1 genes.". Am. J. Hum. Genet. 49 (1): 184–91. PMID 1905878. 
  • Bennett AF, Hayes NV, Baines AJ (1991). "Site specificity in the interactions of synapsin 1 with tubulin.". Biochem. J. 276 ( Pt 3): 793–9. PMID 1905928. 
  • Südhof TC (1990). "The structure of the human synapsin I gene and protein.". J. Biol. Chem. 265 (14): 7849–52. PMID 2110562. 
  • Sauerwald A, Hoesche C, Oschwald R, Kilimann MW (1990). "The 5'-flanking region of the synapsin I gene. A G+C-rich, TATA- and CAAT-less, phylogenetically conserved sequence with cell type-specific promoter function.". J. Biol. Chem. 265 (25): 14932–7. PMID 2118519. 
  • Yang-Feng TL, DeGennaro LJ, Francke U (1986). "Genes for synapsin I, a neuronal phosphoprotein, map to conserved regions of human and murine X chromosomes.". Proc. Natl. Acad. Sci. U.S.A. 83 (22): 8679–83. PMID 3095840. 
  • Czernik AJ, Pang DT, Greengard P (1987). "Amino acid sequences surrounding the cAMP-dependent and calcium/calmodulin-dependent phosphorylation sites in rat and bovine synapsin I.". Proc. Natl. Acad. Sci. U.S.A. 84 (21): 7518–22. PMID 3118371. 
  • McPherson PS, Czernik AJ, Chilcote TJ, et al. (1994). "Interaction of Grb2 via its Src homology 3 domains with synaptic proteins including synapsin I.". Proc. Natl. Acad. Sci. U.S.A. 91 (14): 6486–90. PMID 8022809. 
  • Smith TW, Nikulasson S, De Girolami U, De Gennaro LJ (1994). "Immunohistochemistry of synapsin I and synaptophysin in human nervous system and neuroendocrine tumors. Applications in diagnostic neuro-oncology.". Clin. Neuropathol. 12 (6): 335–42. PMID 8287627. 
  • Matsubara M, Kusubata M, Ishiguro K, et al. (1996). "Site-specific phosphorylation of synapsin I by mitogen-activated protein kinase and Cdk5 and its effects on physiological functions.". J. Biol. Chem. 271 (35): 21108–13. PMID 8702879. 
  • Chin D, Winkler KE, Means AR (1998). "Characterization of substrate phosphorylation and use of calmodulin mutants to address implications from the enzyme crystal structure of calmodulin-dependent protein kinase I.". J. Biol. Chem. 272 (50): 31235–40. PMID 9395448. 
  • Witke W, Podtelejnikov AV, Di Nardo A, et al. (1998). "In mouse brain profilin I and profilin II associate with regulators of the endocytic pathway and actin assembly.". EMBO J. 17 (4): 967–76. doi:10.1093/emboj/17.4.967. PMID 9463375. 
  • Kimoto Y (1998). "A single human cell expresses all messenger ribonucleic acids: the arrow of time in a cell.". Mol. Gen. Genet. 258 (3): 233–9. PMID 9645429. 
  • Hosaka M, Südhof TC (1999). "Homo- and heterodimerization of synapsins.". J. Biol. Chem. 274 (24): 16747–53. PMID 10358015. 
  • Cole RN, Hart GW (1999). "Glycosylation sites flank phosphorylation sites on synapsin I: O-linked N-acetylglucosamine residues are localized within domains mediating synapsin I interactions.". J. Neurochem. 73 (1): 418–28. PMID 10386995. 
  • Hosaka M, Hammer RE, Südhof TC (1999). "A phospho-switch controls the dynamic association of synapsins with synaptic vesicles.". Neuron 24 (2): 377–87. PMID 10571231. 
  • Kao HT, Porton B, Hilfiker S, et al. (2000). "Molecular evolution of the synapsin gene family.". J. Exp. Zool. 285 (4): 360–77. PMID 10578110. 
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