SNCAIP

Protein-coding gene in the species Homo sapiens
SNCAIP
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2KES

Identifiers
AliasesSNCAIP, SYPH1, Sph1, synuclein alpha interacting protein
External IDsOMIM: 603779; MGI: 1915097; HomoloGene: 3987; GeneCards: SNCAIP; OMA:SNCAIP - orthologs
Gene location (Human)
Chromosome 5 (human)
Chr.Chromosome 5 (human)[1]
Chromosome 5 (human)
Genomic location for SNCAIP
Genomic location for SNCAIP
Band5q23.2Start122,311,354 bp[1]
End122,464,219 bp[1]
Gene location (Mouse)
Chromosome 18 (mouse)
Chr.Chromosome 18 (mouse)[2]
Chromosome 18 (mouse)
Genomic location for SNCAIP
Genomic location for SNCAIP
Band18|18 D1Start52,900,781 bp[2]
End53,049,007 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • ventricular zone

  • ganglionic eminence

  • germinal epithelium

  • periodontal fiber

  • endometrium

  • parietal pleura

  • stromal cell of endometrium

  • epithelium of bronchus

  • bronchial epithelial cell

  • myometrium
Top expressed in
  • genital tubercle

  • ventricular zone

  • ganglionic eminence

  • lumbar subsegment of spinal cord

  • external carotid artery

  • saccule

  • internal carotid artery

  • neural tube

  • Rostral migratory stream

  • renal corpuscle
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • protein binding
  • ubiquitin protein ligase binding
  • identical protein binding
Cellular component
  • cytoplasm
  • cytosol
  • neuronal cell body
  • presynaptic membrane
  • synaptic vesicle
  • nucleoplasm
  • cytoplasmic ribonucleoprotein granule
Biological process
  • regulation of inclusion body assembly
  • dopamine metabolic process
  • cell death
  • regulation of neurotransmitter secretion
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

9627

67847

Ensembl

ENSG00000064692

ENSMUSG00000024534

UniProt

Q9Y6H5

Q99ME3

RefSeq (mRNA)
NM_001242935
NM_001308100
NM_001308105
NM_001308106
NM_001308107

NM_001308108
NM_001308109
NM_005460

NM_001199151
NM_001199153
NM_001199154
NM_026408

RefSeq (protein)
NP_001229864
NP_001295029
NP_001295034
NP_001295035
NP_001295036

NP_001295037
NP_001295038
NP_005451

NP_001186080
NP_001186082
NP_001186083
NP_080684
NP_001390575

NP_001390576
NP_001390577

Location (UCSC)Chr 5: 122.31 – 122.46 MbChr 18: 52.9 – 53.05 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Synphilin-1 is a protein that in humans is encoded by the SNCAIP gene.[5][6] SNCAIP stands for "synuclein, alpha interacting protein" and can be signified by SNCAP_HUMAN, synphilin 1, synuclein, alpha interacting protein (synphilin), and SYPH1.

Function

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.[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.

Interactions

SNCAIP has been shown to interact with:

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000064692 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000024534 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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. S2CID 2611127.
  6. ^ a b "Entrez Gene: SNCAIP synuclein, alpha interacting protein (synphilin)".
  7. ^ Neystat M, Rzhetskaya M, Kholodilov N, Burke RE (June 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. S2CID 11517781.
  8. ^ 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. 316 (2): 103–7. doi:10.1016/s0304-3940(01)02330-8. PMID 11742726. S2CID 54363210.
  9. ^ Kawamata H, McLean PJ, Sharma N, Hyman BT (May 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. S2CID 83885937.
  10. ^ Chung KK, Zhang Y, Lim KL, Tanaka Y, Huang H, Gao J, Ross CA, Dawson VL, Dawson TM (October 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. S2CID 12487644.

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. S2CID 12186058.
  • Engelender S, Wanner T, Kleiderlein JJ, Wakabayashi K, Tsuji S, Takahashi H, Ashworth R, Margolis RL, Ross CA (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. S2CID 22420090.
  • 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. S2CID 83885937.
  • Chung KK, Zhang Y, Lim KL, Tanaka Y, Huang H, Gao J, Ross CA, Dawson VL, Dawson TM (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. S2CID 12487644.
  • Ribeiro CS, Carneiro K, Ross CA, Menezes JR, Engelender S (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, McGowan E, Cookson MR (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. S2CID 9654263.
  • 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. S2CID 11517781.
  • 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.
  • Ihara M, Tomimoto H, Kitayama H, Morioka Y, Akiguchi I, Shibasaki H, Noda M, Kinoshita M (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, Ishigaki S, Doyu M, Sobue G (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, Li L, Eberhardt O, Gerhardt E, Cookson MR, Hernandez D, Farrer MJ, Kachergus J, Engelender S, Ross CA, Berger K, Schöls L, Schulz JB, Riess O, Krüger R (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, Kishida S, Nakamura T, Iseki E, Hattori N, Mizuno Y, Kikuchi A, Matsumoto M (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, Junn E, Iwatsubo T, Mouradian MM (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, Lee SS, Kim YM, Junn E, Lee SH, Mouradian MM (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.
  • Chung KK, Thomas B, Li X, Pletnikova O, Troncoso JC, Marsh L, Dawson VL, Dawson TM (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. S2CID 86854030.


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