SNCAIP

From Wikipedia, the free encyclopedia

Synuclein, alpha interacting protein (synphilin)

Identifiers

SNCAIP; MGC39814; SYPH1

External IDs

OMIM: 603779 MGI: 1915097 HomoloGene: 3987

Gene ontology
Molecular Function:	• protein binding
Cellular Component:	• cytoplasm • presynaptic membrane • cell soma
Biological Process:	• dopamine metabolic process • regulation of neurotransmitter secretion

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

Refseq

NM_005460 (mRNA)
NP_005451 (protein)

NM_026408 (mRNA)
NP_080684 (protein)

Location

Chr 5: 121.68 - 121.83 Mb

Chr 18: 52.89 - 53.04 Mb

Pubmed search

[1]

[2]

Synuclein, alpha interacting protein (synphilin), also known as SNCAIP, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: SNCAIP synuclein, alpha interacting protein (synphilin).

[edit] Further reading

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, Kaminsky Z, Guo X, et al. (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.
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. 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. 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. 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. 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. 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. 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.