SYN1

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Synapsin I
File:PBB Protein SYN1 image.jpg
PDB rendering based on 1auv.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols SYN1 ; SYN1a; SYN1b; SYNI
External IDs Template:OMIM5 Template:MGI HomoloGene48483
RNA expression pattern
File:PBB GE SYN1 221914 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

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]

References

  1. 1.0 1.1 "Entrez Gene: SYN1 synapsin I".

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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