SNCAIP

Synuclein, alpha interacting protein (synphilin), also known as SNCAIP, is a human gene.cite web | title = Entrez Gene: SNCAIP synuclein, alpha interacting protein (synphilin)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9627| accessdate = ]

PBB_Summary
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summary_text = 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.cite web | title = Entrez Gene: SNCAIP synuclein, alpha interacting protein (synphilin)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9627| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Krüger R |title=The role of synphilin-1 in synaptic function and protein degradation. |journal=Cell Tissue Res. |volume=318 |issue= 1 |pages= 195–9 |year= 2005 |pmid= 15322916 |doi= 10.1007/s00441-004-0953-z
*cite journal | author=Engelender S, Kaminsky Z, Guo X, "et al." |title=Synphilin-1 associates with alpha-synuclein and promotes the formation of cytosolic inclusions. |journal=Nat. Genet. |volume=22 |issue= 1 |pages= 110–4 |year= 1999 |pmid= 10319874 |doi= 10.1038/8820
*cite journal | author=Engelender S, Wanner T, Kleiderlein JJ, "et al." |title=Organization of the human synphilin-1 gene, a candidate for Parkinson's disease. |journal=Mamm. Genome |volume=11 |issue= 9 |pages= 763–6 |year= 2000 |pmid= 10967135 |doi=
*cite journal | author=Kawamata H, McLean PJ, Sharma N, Hyman BT |title=Interaction of alpha-synuclein and synphilin-1: effect of Parkinson's disease-associated mutations. |journal=J. Neurochem. |volume=77 |issue= 3 |pages= 929–34 |year= 2001 |pmid= 11331421 |doi=
*cite journal | author=Chung KK, Zhang Y, Lim KL, "et al." |title=Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease. |journal=Nat. Med. |volume=7 |issue= 10 |pages= 1144–50 |year= 2001 |pmid= 11590439 |doi= 10.1038/nm1001-1144
*cite journal | author=Ribeiro CS, Carneiro K, Ross CA, "et al." |title=Synphilin-1 is developmentally localized to synaptic terminals, and its association with synaptic vesicles is modulated by alpha-synuclein. |journal=J. Biol. Chem. |volume=277 |issue= 26 |pages= 23927–33 |year= 2002 |pmid= 11956199 |doi= 10.1074/jbc.M201115200
*cite journal | author=O'Farrell C, Pickford F, Vink L, "et al." |title=Sequence conservation between mouse and human synphilin-1. |journal=Neurosci. Lett. |volume=322 |issue= 1 |pages= 9–12 |year= 2002 |pmid= 11958831 |doi=
*cite journal | author=Neystat M, Rzhetskaya M, Kholodilov N, Burke RE |title=Analysis of synphilin-1 and synuclein interactions by yeast two-hybrid beta-galactosidase liquid assay. |journal=Neurosci. Lett. |volume=325 |issue= 2 |pages= 119–23 |year= 2002 |pmid= 12044636 |doi=
*cite journal | author=Junn E, Lee SS, Suhr UT, Mouradian MM |title=Parkin accumulation in aggresomes due to proteasome impairment. |journal=J. Biol. Chem. |volume=277 |issue= 49 |pages= 47870–7 |year= 2003 |pmid= 12364339 |doi= 10.1074/jbc.M203159200
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Ihara M, Tomimoto H, Kitayama H, "et al." |title=Association of the cytoskeletal GTP-binding protein Sept4/H5 with cytoplasmic inclusions found in Parkinson's disease and other synucleinopathies. |journal=J. Biol. Chem. |volume=278 |issue= 26 |pages= 24095–102 |year= 2003 |pmid= 12695511 |doi= 10.1074/jbc.M301352200
*cite journal | author=Ito T, Niwa J, Hishikawa N, "et al." |title=Dorfin localizes to Lewy bodies and ubiquitylates synphilin-1. |journal=J. Biol. Chem. |volume=278 |issue= 31 |pages= 29106–14 |year= 2003 |pmid= 12750386 |doi= 10.1074/jbc.M302763200
*cite journal | author=Marx FP, Holzmann C, Strauss KM, "et al." |title=Identification and functional characterization of a novel R621C mutation in the synphilin-1 gene in Parkinson's disease. |journal=Hum. Mol. Genet. |volume=12 |issue= 11 |pages= 1223–31 |year= 2004 |pmid= 12761037 |doi=
*cite journal | author=Scherzer CR, Jensen RV, Gullans SR, Feany MB |title=Gene expression changes presage neurodegeneration in a Drosophila model of Parkinson's disease. |journal=Hum. Mol. Genet. |volume=12 |issue= 19 |pages= 2457–66 |year= 2004 |pmid= 12915459 |doi= 10.1093/hmg/ddg265
*cite journal | author=Nagano Y, Yamashita H, Takahashi T, "et al." |title=Siah-1 facilitates ubiquitination and degradation of synphilin-1. |journal=J. Biol. Chem. |volume=278 |issue= 51 |pages= 51504–14 |year= 2004 |pmid= 14506261 |doi= 10.1074/jbc.M306347200
*cite journal | author=Tanaka M, Kim YM, Lee G, "et al." |title=Aggresomes formed by alpha-synuclein and synphilin-1 are cytoprotective. |journal=J. Biol. Chem. |volume=279 |issue= 6 |pages= 4625–31 |year= 2004 |pmid= 14627698 |doi= 10.1074/jbc.M310994200
*cite journal | author=Lee G, Tanaka M, Park K, "et al." |title=Casein kinase II-mediated phosphorylation regulates alpha-synuclein/synphilin-1 interaction and inclusion body formation. |journal=J. Biol. Chem. |volume=279 |issue= 8 |pages= 6834–9 |year= 2004 |pmid= 14645218 |doi= 10.1074/jbc.M312760200
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Chung KK, Thomas B, Li X, "et al." |title=S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function. |journal=Science |volume=304 |issue= 5675 |pages= 1328–31 |year= 2004 |pmid= 15105460 |doi= 10.1126/science.1093891

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