SNCAIP

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Synuclein, alpha interacting protein
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols SNCAIP ; SYPH1; Sph1
External IDs OMIM603779 MGI1915097 HomoloGene3987 GeneCards: SNCAIP Gene
RNA expression pattern
PBB GE SNCAIP 219511 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 9627 67847
Ensembl ENSG00000064692 ENSMUSG00000024534
UniProt Q9Y6H5 Q99ME3
RefSeq (mRNA) NM_001242935 NM_001199151
RefSeq (protein) NP_001229864 NP_001186080
Location (UCSC) Chr 5:
121.65 – 121.8 Mb
Chr 18:
52.77 – 52.92 Mb
PubMed search [1] [2]

Synphilin-1 is a protein that in humans is encoded by the SNCAIP gene.[1][2] SNCAIP stands for "synuclein, alpha interacting protein" and can be signified by SNCAP_HUMAN, synphilin 1, synuclein, alpha interacting protein (synphilin), and SYPH1.

This gene encodes a protein containing several protein-protein interaction domains, including ankyrin-like repeats, a coiled-coil domain, and an ATP/GTP-binding motif. The encoded protein interacts with alpha-synuclein in neuronal tissue and may play a role in the formation of cytoplasmic inclusions and neurodegeneration. A mutation in this gene has been associated with Parkinson's disease. Alternatively spliced transcript variants encoding different isoforms of this gene have been described, but their full-length nature has yet to be determined.[2]

Interactions[edit]

SNCAIP has been shown to interact with Alpha-synuclein[1][3][4][5] and Parkin (ligase).[6]

The SNCAIP gene provides instructions for making a protein called synphilin-1 and a slightly different version of this protein called synphilin-1A. These proteins are produced in the brain. They are usually located in specialized structures called presynaptic terminals, found at the tips of nerve cells. In nerve cells, synphilin-1 and synphilin-1A interact with another protein called alpha-synuclein. The functions of synphilin-1 and synphilin-1A, however, are unknown.

References[edit]

  1. ^ a b Engelender S, Kaminsky Z, Guo X, Sharp AH, Amaravi RK, Kleiderlein JJ, Margolis RL, Troncoso JC, Lanahan AA, Worley PF, Dawson VL, Dawson TM, Ross CA (May 1999). "Synphilin-1 associates with alpha-synuclein and promotes the formation of cytosolic inclusions". Nat Genet 22 (1): 110–4. doi:10.1038/8820. PMID 10319874. 
  2. ^ a b "Entrez Gene: SNCAIP synuclein, alpha interacting protein (synphilin)". 
  3. ^ Neystat, Michael; Rzhetskaya Margarita; Kholodilov Nikolai; Burke Robert E (June 2002). "Analysis of synphilin-1 and synuclein interactions by yeast two-hybrid beta-galactosidase liquid assay". Neurosci. Lett. (Ireland) 325 (2): 119–23. doi:10.1016/S0304-3940(02)00253-7. ISSN 0304-3940. PMID 12044636. 
  4. ^ Nagano, Y; Yamashita H; Nakamura T; Takahashi T; Kondo E; Nakamura S (Dec 2001). "Lack of binding observed between human alpha-synuclein and Bcl-2 protein family". Neurosci. Lett. (Ireland) 316 (2): 103–7. doi:10.1016/S0304-3940(01)02330-8. ISSN 0304-3940. PMID 11742726. 
  5. ^ Kawamata, H; McLean P J; Sharma N; Hyman B T (May 2001). "Interaction of alpha-synuclein and synphilin-1: effect of Parkinson's disease-associated mutations". J. Neurochem. (United States) 77 (3): 929–34. doi:10.1046/j.1471-4159.2001.00301.x. ISSN 0022-3042. PMID 11331421. 
  6. ^ Chung, K K; Zhang Y; Lim K L; Tanaka Y; Huang H; Gao J; Ross C A; Dawson V L; Dawson T M (October 2001). "Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease". Nat. Med. (United States) 7 (10): 1144–50. doi:10.1038/nm1001-1144. ISSN 1078-8956. PMID 11590439. 

Further reading[edit]

  • Krüger R (2005). "The role of synphilin-1 in synaptic function and protein degradation". Cell Tissue Res. 318 (1): 195–9. doi:10.1007/s00441-004-0953-z. PMID 15322916. 
  • Engelender S, Wanner T, Kleiderlein JJ, et al. (2000). "Organization of the human synphilin-1 gene, a candidate for Parkinson's disease". Mamm. Genome 11 (9): 763–6. doi:10.1007/s003350010123. PMID 10967135. 
  • Kawamata H, McLean PJ, Sharma N, Hyman BT (2001). "Interaction of alpha-synuclein and synphilin-1: effect of Parkinson's disease-associated mutations". J. Neurochem. 77 (3): 929–34. doi:10.1046/j.1471-4159.2001.00301.x. PMID 11331421. 
  • Chung KK, Zhang Y, Lim KL, et al. (2001). "Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease". Nat. Med. 7 (10): 1144–50. doi:10.1038/nm1001-1144. PMID 11590439. 
  • Ribeiro CS, Carneiro K, Ross CA, et al. (2002). "Synphilin-1 is developmentally localized to synaptic terminals, and its association with synaptic vesicles is modulated by alpha-synuclein". J. Biol. Chem. 277 (26): 23927–33. doi:10.1074/jbc.M201115200. PMID 11956199. 
  • O'Farrell C, Pickford F, Vink L, et al. (2002). "Sequence conservation between mouse and human synphilin-1". Neurosci. Lett. 322 (1): 9–12. doi:10.1016/S0304-3940(02)00068-X. PMID 11958831. 
  • Neystat M, Rzhetskaya M, Kholodilov N, Burke RE (2002). "Analysis of synphilin-1 and synuclein interactions by yeast two-hybrid beta-galactosidase liquid assay". Neurosci. Lett. 325 (2): 119–23. doi:10.1016/S0304-3940(02)00253-7. PMID 12044636. 
  • Junn E, Lee SS, Suhr UT, Mouradian MM (2003). "Parkin accumulation in aggresomes due to proteasome impairment". J. Biol. Chem. 277 (49): 47870–7. doi:10.1074/jbc.M203159200. PMID 12364339. 
  • 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. 
  • 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. 
  • Ito T, Niwa J, Hishikawa N, et al. (2003). "Dorfin localizes to Lewy bodies and ubiquitylates synphilin-1". J. Biol. Chem. 278 (31): 29106–14. doi:10.1074/jbc.M302763200. PMID 12750386. 
  • Marx FP, Holzmann C, Strauss KM, et al. (2004). "Identification and functional characterization of a novel R621C mutation in the synphilin-1 gene in Parkinson's disease". Hum. Mol. Genet. 12 (11): 1223–31. doi:10.1093/hmg/ddg134. PMID 12761037. 
  • Scherzer CR, Jensen RV, Gullans SR, Feany MB (2004). "Gene expression changes presage neurodegeneration in a Drosophila model of Parkinson's disease". Hum. Mol. Genet. 12 (19): 2457–66. doi:10.1093/hmg/ddg265. PMID 12915459. 
  • Nagano Y, Yamashita H, Takahashi T, et al. (2004). "Siah-1 facilitates ubiquitination and degradation of synphilin-1". J. Biol. Chem. 278 (51): 51504–14. doi:10.1074/jbc.M306347200. PMID 14506261. 
  • Tanaka M, Kim YM, Lee G, et al. (2004). "Aggresomes formed by alpha-synuclein and synphilin-1 are cytoprotective". J. Biol. Chem. 279 (6): 4625–31. doi:10.1074/jbc.M310994200. PMID 14627698. 
  • Lee G, Tanaka M, Park K, et al. (2004). "Casein kinase II-mediated phosphorylation regulates alpha-synuclein/synphilin-1 interaction and inclusion body formation". J. Biol. Chem. 279 (8): 6834–9. doi:10.1074/jbc.M312760200. PMID 14645218. 
  • 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. 
  • Chung KK, Thomas B, Li X, et al. (2004). "S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function". Science 304 (5675): 1328–31. doi:10.1126/science.1093891. PMID 15105460.