# SNCAIP

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SNCAIP Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2KES Identifiers Aliases SNCAIP, SYPH1, Sph1, synuclein alpha interacting protein External IDs OMIM: 603779; MGI: 1915097; HomoloGene: 3987; GeneCards: SNCAIP; OMA:SNCAIP - orthologs Gene location (Human) Chr. Chromosome 5 (human)[1] Band 5q23.2 Start 122,311,354 bp[1] End 122,464,219 bp[1] Gene location (Mouse) Chr. Chromosome 18 (mouse)[2] Band 18|18 D1 Start 52,900,781 bp[2] End 53,049,007 bp[2] RNA expression pattern Bgee Human Mouse (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 soma 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 Species Human Mouse 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 Mb Chr 18: 52.9 – 53.05 Mb PubMed search [3] [4] Wikidata View/Edit Human View/Edit Mouse

**Synphilin-1** is a [protein](/source/Protein) that in humans is encoded by the *SNCAIP* [gene](/source/Gene).[5][6] *SNCAIP* stands for "synuclein, alpha interacting protein".

Synphilin-1 is a cytosolic [protein](/source/Protein) first identified in 1999 as a novel binding partner of α-synuclein, localized within Lewy bodies in Parkinson's disease brain tissue.[7] Experimental studies in mammalian cells and yeast demonstrated that co-expression of synphilin-1 with α-synuclein promotes the formation of cytoplasmic inclusions resembling Lewy bodies.[7]

## Structure

The SNCAIP gene encodes synphilin-1, a multi-domain protein with a complex structure integral to neuronal function and implicated in [neurodegenerative diseases](/source/Neurodegenerative_disease). Structurally, synphilin-1 is composed of approximately 919 amino acids and is characterized by several functional domains, notably including six [ankyrin repeats](/source/Ankyrin_repeat) and a central [coiled-coil domain](/source/Coiled-coil_domain) spanning residues 510–557. These domains are typical protein-protein interaction motifs, facilitating synphilin-1's ability to interact with partner proteins such as [alpha-synuclein](/source/Alpha-synuclein) (SNCA). SNCAIP binds to the [N-terminal](/source/N-terminal) region of SNCA, allowing synphilin-1 to play a role in the formation of cytosolic inclusions mimicking [Lewy bodies](/source/Lewy_bodies), which are hallmark features of [synucleinopathies](/source/Synucleinopathies). The ankyrin repeats provide scaffolding for additional protein interactions, while the coiled-coil domain is crucial for the association with alpha-synuclein and possibly other synaptic or vesicular components.[8][9]

## Function

SNCAIP encodes synphilin-1, a cytoplasmic protein that interacts with alpha-synuclein in neuronal tissue and is involved in a variety of physiological processes related to synaptic function and protein homeostasis. Synphilin-1 is developmentally localized to [synaptic terminals](/source/Synaptic_terminal) and participates in the regulation of [synaptic vesicle trafficking](/source/Synaptic_vesicle_trafficking). It may act as a [scaffold protein](/source/Scaffold_protein), contributing to cellular processes like [protein degradation](/source/Protein_degradation) through the [ubiquitin](/source/Ubiquitin)-[proteasome](/source/Proteasome) system and autophagy. Experimental evidence suggests that binding of synphilin-1 to alpha-synuclein can modulate synaptic vesicle dynamics, potentially impacting [neurotransmitter release](/source/Neurotransmitter_release) and [synaptic plasticity](/source/Synaptic_plasticity). Synphilin-1's [cytoprotective](/source/Cytoprotective) effects include inhibiting [mitochondrial](/source/Mitochondrial) dysfunction, reducing [reactive oxygen species](/source/Reactive_oxygen_species) production, and promoting neuronal survival under certain conditions.[10][11][12][13]

## Ubiquitination

Synphilin-1 undergoes [ubiquitination](/source/Ubiquitination). [Parkin](/source/Parkin_(protein)) (an [E3 ligase](/source/E3_ligase)) modifies synphilin-1 and, together with [α-synuclein](/source/%CE%91-synuclein), promotes the formation of ubiquitin-positive [inclusion bodies](/source/Inclusion_bodies).[14] Mutations in parkin gene disrupt this activity. Additional E3 ligases, including [SIAH1](/source/SIAH1) and [SIAH2](/source/SIAH2), also ubiquitinate synphilin-1, influencing whether the protein is directed to [proteasomal degradation](/source/Proteasomal_degradation) or accumulates in inclusions.[15] Inclusions containing α-synuclein and synphilin-1 share features with [aggresomes](/source/Aggresome), which may act to sequester [misfolded proteins](/source/Misfolded_protein) and limit [cellular toxicity](/source/Cytotoxicity).[16]

## Clinical significance

Clinically, synphilin-1 is heavily implicated in [neurodegenerative diseases](/source/Neurodegenerative_disease), particularly [Parkinson's disease](/source/Parkinson's_disease) (PD). It serves as a major component of [Lewy bodies](/source/Lewy_bodies)—the pathological protein aggregates characteristic of PD—and contributes to the formation of these cytoplasmic inclusions. While wild-type synphilin-1 may help sequester potentially toxic protein aggregates, certain isoforms and mutants, such as synphilin-1A, are highly aggregation-prone and associated with neuronal toxicity and degeneration. Genetic variation and altered methylation of the SNCAIP gene are linked with increased vulnerability to PD and related synucleinopathies. Thus, synphilin-1 exerts complex effects on neuronal health, acting as both a potential protector and a contributor to disease pathology depending on its expression, isoform, and interaction context.[17][18][13][19]

Beyond Parkinson's disease, synphilin-1 has recently been implicated in glioblastoma. Transcriptomic and single-cell RNA sequencing analyses identified *SNCAIP* among histone lactylation related genes upregulated in glioblastoma, with elevated expression correlating with poorer patient survival.[20] This has raised interest in synphilin-1 as a potential biomarker in cancer biology.

## Interactions

SNCAIP has been shown to [interact](/source/Protein-protein_interaction) with:

- [Alpha-synuclein](/source/Alpha-synuclein)[5][21][22][23] and

- [Parkin (ligase)](/source/Parkin_(ligase)).[24]

## References

1. ^ [***a***](#cite_ref-refGRCh38Ensembl_1-0) [***b***](#cite_ref-refGRCh38Ensembl_1-1) [***c***](#cite_ref-refGRCh38Ensembl_1-2) [GRCh38: Ensembl release 89: ENSG00000064692](http://May2017.archive.ensembl.org/Homo_sapiens/Gene/Summary?db=core;g=ENSG00000064692) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. ^ [***a***](#cite_ref-refGRCm38Ensembl_2-0) [***b***](#cite_ref-refGRCm38Ensembl_2-1) [***c***](#cite_ref-refGRCm38Ensembl_2-2) [GRCm38: Ensembl release 89: ENSMUSG00000024534](http://May2017.archive.ensembl.org/Mus_musculus/Gene/Summary?db=core;g=ENSMUSG00000024534) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. **[^](#cite_ref-3)** ["Human PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=9627). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-4)** ["Mouse PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=67847). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. ^ [***a***](#cite_ref-Engelender_1999_5-0) [***b***](#cite_ref-Engelender_1999_5-1) Engelender S, Kaminsky Z, Guo X, Sharp AH, Amaravi RK, Kleiderlein JJ, et al. (May 1999). "Synphilin-1 associates with alpha-synuclein and promotes the formation of cytosolic inclusions". *Nat Genet*. **22** (1): 110–114. [doi](/source/Doi_(identifier)):[10.1038/8820](https://doi.org/10.1038%2F8820). [PMID](/source/PMID_(identifier)) [10319874](https://pubmed.ncbi.nlm.nih.gov/10319874). [S2CID](/source/S2CID_(identifier)) [2611127](https://api.semanticscholar.org/CorpusID:2611127).

1. **[^](#cite_ref-entrez_6-0)** ["Entrez Gene: SNCAIP synuclein, alpha interacting protein (synphilin)"](https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=9627).

1. ^ [***a***](#cite_ref-Engelender_1999a_7-0) [***b***](#cite_ref-Engelender_1999a_7-1) Engelender S, Kaminsky Z, Guo X, Sharp AH, Amaravi RK, Kleiderlein JJ, et al. (May 1999). "Synphilin-1 associates with alpha-synuclein and promotes the formation of cytosolic inclusions". *Nature Genetics*. **22** (1): 110–114. [doi](/source/Doi_(identifier)):[10.1038/8820](https://doi.org/10.1038%2F8820). [PMID](/source/PMID_(identifier)) [10319874](https://pubmed.ncbi.nlm.nih.gov/10319874).

1. **[^](#cite_ref-Siddiqui_2016_8-0)** Siddiqui IJ, Pervaiz N, Abbasi AA (April 2016). ["The Parkinson Disease gene SNCA: Evolutionary and structural insights with pathological implication"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4832246). *Scientific Reports*. **6** 24475. [Bibcode](/source/Bibcode_(identifier)):[2016NatSR...624475S](https://ui.adsabs.harvard.edu/abs/2016NatSR...624475S). [doi](/source/Doi_(identifier)):[10.1038/srep24475](https://doi.org/10.1038%2Fsrep24475). [PMC](/source/PMC_(identifier)) [4832246](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4832246). [PMID](/source/PMID_(identifier)) [27080380](https://pubmed.ncbi.nlm.nih.gov/27080380).

1. **[^](#cite_ref-9)** ["SNCAP_HUMAN"](https://www.uniprot.org/uniprotkb/Q9Y6H5/entry). *UniProt*. Q9Y6H5.

1. **[^](#cite_ref-Ribeiro_2002_10-0)** Ribeiro CS, Carneiro K, Ross CA, Menezes JR, Engelender S (Jun 2002). ["Synphilin-1 is developmentally localized to synaptic terminals, and its association with synaptic vesicles is modulated by alpha-synuclein"](https://doi.org/10.1074%2Fjbc.M201115200). *Journal of Biological Chemistry*. **277** (26): 23927–23933. [doi](/source/Doi_(identifier)):[10.1074/jbc.M201115200](https://doi.org/10.1074%2Fjbc.M201115200). [PMID](/source/PMID_(identifier)) [11956199](https://pubmed.ncbi.nlm.nih.gov/11956199).

1. **[^](#cite_ref-Krüger_2004_11-0)** Krüger R (Oct 2004). "The role of synphilin-1 in synaptic function and protein degradation". *Cell Tissue Res*. **318** (1): 195–199. [doi](/source/Doi_(identifier)):[10.1007/s00441-004-0953-z](https://doi.org/10.1007%2Fs00441-004-0953-z). [PMID](/source/PMID_(identifier)) [15322916](https://pubmed.ncbi.nlm.nih.gov/15322916). [S2CID](/source/S2CID_(identifier)) [12186058](https://api.semanticscholar.org/CorpusID:12186058).

1. **[^](#cite_ref-12)** Mirghani M. [*Synphilin-1 and its Effects on Pathogenesis of Parkinson's Synphilin-1 and its Effects on Pathogenesis of Parkinson's Disease*](https://digitalcommons.lib.uconn.edu/cgi/viewcontent.cgi?article=1871&context=srhonors_theses) (B.S. thesis). University of Connecticut.

1. ^ [***a***](#cite_ref-Shishido_2019_13-0) [***b***](#cite_ref-Shishido_2019_13-1) Shishido T, Nagano Y, Araki M, Kurashige T, Obayashi H, Nakamura T, et al. (January 2019). "Synphilin-1 has neuroprotective effects on MPP+-induced Parkinson's disease model cells by inhibiting ROS production and apoptosis". *Neuroscience Letters*. **690**: 145–150. [doi](/source/Doi_(identifier)):[10.1016/j.neulet.2018.10.020](https://doi.org/10.1016%2Fj.neulet.2018.10.020). [PMID](/source/PMID_(identifier)) [30316984](https://pubmed.ncbi.nlm.nih.gov/30316984).

1. **[^](#cite_ref-Chung_2001_14-0)** Chung KK, Zhang Y, Lim KL, Tanaka Y, Huang H, Gao J, et al. (October 2001). "Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease". *Nature Medicine*. **7** (10): 1144–1150. [doi](/source/Doi_(identifier)):[10.1038/nm1001-1144](https://doi.org/10.1038%2Fnm1001-1144). [PMID](/source/PMID_(identifier)) [11590439](https://pubmed.ncbi.nlm.nih.gov/11590439).

1. **[^](#cite_ref-Liani_2004_15-0)** Liani E, Eyal A, Avraham E, Shemer R, Szargel R, Berg D, et al. (April 2004). ["Ubiquitylation of synphilin-1 and alpha-synuclein by SIAH and its presence in cellular inclusions and Lewy bodies imply a role in Parkinson's disease"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC397412). *Proceedings of the National Academy of Sciences of the United States of America*. **101** (15): 5500–5505. [Bibcode](/source/Bibcode_(identifier)):[2004PNAS..101.5500L](https://ui.adsabs.harvard.edu/abs/2004PNAS..101.5500L). [doi](/source/Doi_(identifier)):[10.1073/pnas.0401081101](https://doi.org/10.1073%2Fpnas.0401081101). [PMC](/source/PMC_(identifier)) [397412](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC397412). [PMID](/source/PMID_(identifier)) [15064394](https://pubmed.ncbi.nlm.nih.gov/15064394).

1. **[^](#cite_ref-Tanaka_2004_16-0)** Tanaka M, Kim YM, Lee G, Junn E, Iwatsubo T, Mouradian MM (February 2004). ["Aggresomes formed by alpha-synuclein and synphilin-1 are cytoprotective"](https://doi.org/10.1074%2Fjbc.M310994200). *The Journal of Biological Chemistry*. **279** (6): 4625–4631. [doi](/source/Doi_(identifier)):[10.1074/jbc.M310994200](https://doi.org/10.1074%2Fjbc.M310994200). [PMID](/source/PMID_(identifier)) [14627698](https://pubmed.ncbi.nlm.nih.gov/14627698).

1. **[^](#cite_ref-Eyal_2006_17-0)** Eyal A, Szargel R, Avraham E, Liani E, Haskin J, Rott R, et al. (April 2006). ["Synphilin-1A: an aggregation-prone isoform of synphilin-1 that causes neuronal death and is present in aggregates from alpha-synucleinopathy patients"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1458673). *Proceedings of the National Academy of Sciences of the United States of America*. **103** (15): 5917–22. [Bibcode](/source/Bibcode_(identifier)):[2006PNAS..103.5917E](https://ui.adsabs.harvard.edu/abs/2006PNAS..103.5917E). [doi](/source/Doi_(identifier)):[10.1073/pnas.0509707103](https://doi.org/10.1073%2Fpnas.0509707103). [PMC](/source/PMC_(identifier)) [1458673](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1458673). [PMID](/source/PMID_(identifier)) [16595633](https://pubmed.ncbi.nlm.nih.gov/16595633).

1. **[^](#cite_ref-pmid36857384_18-0)** Carvajal-Oliveros A, Dominguez-Baleón C, Sánchez-Díaz I, Zambrano-Tipan D, Hernández-Vargas R, Campusano JM, et al. (2023). ["Parkinsonian phenotypes induced by Synphilin-1 expression are differentially contributed by serotonergic and dopaminergic circuits and suppressed by nicotine treatment"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9977059). *PLOS ONE*. **18** (3) e0282348. [Bibcode](/source/Bibcode_(identifier)):[2023PLoSO..1882348C](https://ui.adsabs.harvard.edu/abs/2023PLoSO..1882348C). [doi](/source/Doi_(identifier)):[10.1371/journal.pone.0282348](https://doi.org/10.1371%2Fjournal.pone.0282348). [PMC](/source/PMC_(identifier)) [9977059](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9977059). [PMID](/source/PMID_(identifier)) [36857384](https://pubmed.ncbi.nlm.nih.gov/36857384).

1. **[^](#cite_ref-Dashtipour_2017_19-0)** Dashtipour K, Tafreshi A, Adler C, Beach T, Chen X, Serrano G, et al. (June 2017). ["Hypermethylation of Synphilin-1, Alpha-Synuclein-Interacting Protein (SNCAIP) Gene in the Cerebral Cortex of Patients with Sporadic Parkinson's Disease"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5532587). *Brain Sciences*. **7** (7): 74. [doi](/source/Doi_(identifier)):[10.3390/brainsci7070074](https://doi.org/10.3390%2Fbrainsci7070074). [PMC](/source/PMC_(identifier)) [5532587](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5532587). [PMID](/source/PMID_(identifier)) [28653979](https://pubmed.ncbi.nlm.nih.gov/28653979).

1. **[^](#cite_ref-He_2025_20-0)** He W, Chen R, Chen G, Zhang L, Qian Y, Zhou J, et al. (2025). ["Identification and Validation of Prognostic Genes Related to Histone Lactylation Modification in Glioblastoma: An Integrated Analysis of Transcriptome and Single-cell RNA Sequencing"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12036088). *Journal of Cancer*. **16** (7): 2145–2166. [doi](/source/Doi_(identifier)):[10.7150/jca.110646](https://doi.org/10.7150%2Fjca.110646). [PMC](/source/PMC_(identifier)) [12036088](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12036088). [PMID](/source/PMID_(identifier)) [40302809](https://pubmed.ncbi.nlm.nih.gov/40302809).

1. **[^](#cite_ref-Neystat_2002_21-0)** 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): 119–123. [doi](/source/Doi_(identifier)):[10.1016/s0304-3940(02)00253-7](https://doi.org/10.1016%2Fs0304-3940%2802%2900253-7). [PMID](/source/PMID_(identifier)) [12044636](https://pubmed.ncbi.nlm.nih.gov/12044636). [S2CID](/source/S2CID_(identifier)) [11517781](https://api.semanticscholar.org/CorpusID:11517781).

1. **[^](#cite_ref-Nagano_2001_22-0)** 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): 103–107. [doi](/source/Doi_(identifier)):[10.1016/s0304-3940(01)02330-8](https://doi.org/10.1016%2Fs0304-3940%2801%2902330-8). [PMID](/source/PMID_(identifier)) [11742726](https://pubmed.ncbi.nlm.nih.gov/11742726). [S2CID](/source/S2CID_(identifier)) [54363210](https://api.semanticscholar.org/CorpusID:54363210).

1. **[^](#cite_ref-Kawamata_2001_23-0)** Kawamata H, McLean PJ, Sharma N, Hyman BT (May 2001). ["Interaction of alpha-synuclein and synphilin-1: effect of Parkinson's disease-associated mutations"](https://doi.org/10.1046%2Fj.1471-4159.2001.00301.x). *J. Neurochem*. **77** (3): 929–934. [doi](/source/Doi_(identifier)):[10.1046/j.1471-4159.2001.00301.x](https://doi.org/10.1046%2Fj.1471-4159.2001.00301.x). [PMID](/source/PMID_(identifier)) [11331421](https://pubmed.ncbi.nlm.nih.gov/11331421). [S2CID](/source/S2CID_(identifier)) [83885937](https://api.semanticscholar.org/CorpusID:83885937).

1. **[^](#cite_ref-Chung_2001a_24-0)** Chung KK, Zhang Y, Lim KL, Tanaka Y, Huang H, Gao J, et al. (October 2001). "Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease". *Nat. Med*. **7** (10): 1144–1150. [doi](/source/Doi_(identifier)):[10.1038/nm1001-1144](https://doi.org/10.1038%2Fnm1001-1144). [PMID](/source/PMID_(identifier)) [11590439](https://pubmed.ncbi.nlm.nih.gov/11590439). [S2CID](/source/S2CID_(identifier)) [12487644](https://api.semanticscholar.org/CorpusID:12487644).

## Further reading

- Engelender S, Wanner T, Kleiderlein JJ, Wakabayashi K, Tsuji S, Takahashi H, et al. (Sep 2000). "Organization of the human synphilin-1 gene, a candidate for Parkinson's disease". *Mamm. Genome*. **11** (9): 763–766. [doi](/source/Doi_(identifier)):[10.1007/s003350010123](https://doi.org/10.1007%2Fs003350010123). [PMID](/source/PMID_(identifier)) [10967135](https://pubmed.ncbi.nlm.nih.gov/10967135). [S2CID](/source/S2CID_(identifier)) [22420090](https://api.semanticscholar.org/CorpusID:22420090).

- Kawamata H, McLean PJ, Sharma N, Hyman BT (May 2001). ["Interaction of alpha-synuclein and synphilin-1: effect of Parkinson's disease-associated mutations"](https://doi.org/10.1046%2Fj.1471-4159.2001.00301.x). *J. Neurochem*. **77** (3): 929–934. [doi](/source/Doi_(identifier)):[10.1046/j.1471-4159.2001.00301.x](https://doi.org/10.1046%2Fj.1471-4159.2001.00301.x). [PMID](/source/PMID_(identifier)) [11331421](https://pubmed.ncbi.nlm.nih.gov/11331421). [S2CID](/source/S2CID_(identifier)) [83885937](https://api.semanticscholar.org/CorpusID:83885937).

- Chung KK, Zhang Y, Lim KL, Tanaka Y, Huang H, Gao J, et al. (Oct 2001). "Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease". *Nat. Med*. **7** (10): 1144–1150. [doi](/source/Doi_(identifier)):[10.1038/nm1001-1144](https://doi.org/10.1038%2Fnm1001-1144). [PMID](/source/PMID_(identifier)) [11590439](https://pubmed.ncbi.nlm.nih.gov/11590439). [S2CID](/source/S2CID_(identifier)) [12487644](https://api.semanticscholar.org/CorpusID:12487644).

- O'Farrell C, Pickford F, Vink L, McGowan E, Cookson MR (Mar 2002). "Sequence conservation between mouse and human synphilin-1". *Neurosci. Lett*. **322** (1): 9–12. [doi](/source/Doi_(identifier)):[10.1016/S0304-3940(02)00068-X](https://doi.org/10.1016%2FS0304-3940%2802%2900068-X). [PMID](/source/PMID_(identifier)) [11958831](https://pubmed.ncbi.nlm.nih.gov/11958831). [S2CID](/source/S2CID_(identifier)) [9654263](https://api.semanticscholar.org/CorpusID:9654263).

- Neystat M, Rzhetskaya M, Kholodilov N, Burke RE (Jun 2002). "Analysis of synphilin-1 and synuclein interactions by yeast two-hybrid beta-galactosidase liquid assay". *Neurosci. Lett*. **325** (2): 119–123. [doi](/source/Doi_(identifier)):[10.1016/S0304-3940(02)00253-7](https://doi.org/10.1016%2FS0304-3940%2802%2900253-7). [PMID](/source/PMID_(identifier)) [12044636](https://pubmed.ncbi.nlm.nih.gov/12044636). [S2CID](/source/S2CID_(identifier)) [11517781](https://api.semanticscholar.org/CorpusID:11517781).

- Junn E, Lee SS, Suhr UT, Mouradian MM (Dec 2002). ["Parkin accumulation in aggresomes due to proteasome impairment"](https://doi.org/10.1074%2Fjbc.M203159200). *Journal of Biological Chemistry*. **277** (49): 47870–47877. [doi](/source/Doi_(identifier)):[10.1074/jbc.M203159200](https://doi.org/10.1074%2Fjbc.M203159200). [PMID](/source/PMID_(identifier)) [12364339](https://pubmed.ncbi.nlm.nih.gov/12364339).

- Ihara M, Tomimoto H, Kitayama H, Morioka Y, Akiguchi I, Shibasaki H, et al. (Jun 2003). ["Association of the cytoskeletal GTP-binding protein Sept4/H5 with cytoplasmic inclusions found in Parkinson's disease and other synucleinopathies"](https://doi.org/10.1074%2Fjbc.M301352200). *Journal of Biological Chemistry*. **278** (26): 24095–24102. [doi](/source/Doi_(identifier)):[10.1074/jbc.M301352200](https://doi.org/10.1074%2Fjbc.M301352200). [PMID](/source/PMID_(identifier)) [12695511](https://pubmed.ncbi.nlm.nih.gov/12695511).

- Ito T, Niwa J, Hishikawa N, Ishigaki S, Doyu M, Sobue G (Aug 2003). ["Dorfin localizes to Lewy bodies and ubiquitylates synphilin-1"](https://doi.org/10.1074%2Fjbc.M302763200). *Journal of Biological Chemistry*. **278** (31): 29106–29114. [doi](/source/Doi_(identifier)):[10.1074/jbc.M302763200](https://doi.org/10.1074%2Fjbc.M302763200). [PMID](/source/PMID_(identifier)) [12750386](https://pubmed.ncbi.nlm.nih.gov/12750386).

- Marx FP, Holzmann C, Strauss KM, Li L, Eberhardt O, Gerhardt E, et al. (Jun 2003). ["Identification and functional characterization of a novel R621C mutation in the synphilin-1 gene in Parkinson's disease"](https://doi.org/10.1093%2Fhmg%2Fddg134). *Hum. Mol. Genet*. **12** (11): 1223–1231. [doi](/source/Doi_(identifier)):[10.1093/hmg/ddg134](https://doi.org/10.1093%2Fhmg%2Fddg134). [PMID](/source/PMID_(identifier)) [12761037](https://pubmed.ncbi.nlm.nih.gov/12761037).

- Scherzer CR, Jensen RV, Gullans SR, Feany MB (Oct 2003). ["Gene expression changes presage neurodegeneration in a Drosophila model of Parkinson's disease"](https://doi.org/10.1093%2Fhmg%2Fddg265). *Hum. Mol. Genet*. **12** (19): 2457–2466. [doi](/source/Doi_(identifier)):[10.1093/hmg/ddg265](https://doi.org/10.1093%2Fhmg%2Fddg265). [PMID](/source/PMID_(identifier)) [12915459](https://pubmed.ncbi.nlm.nih.gov/12915459).

- Nagano Y, Yamashita H, Takahashi T, Kishida S, Nakamura T, Iseki E, et al. (Dec 2003). ["Siah-1 facilitates ubiquitination and degradation of synphilin-1"](https://doi.org/10.1074%2Fjbc.M306347200). *Journal of Biological Chemistry*. **278** (51): 51504–51514. [doi](/source/Doi_(identifier)):[10.1074/jbc.M306347200](https://doi.org/10.1074%2Fjbc.M306347200). [PMID](/source/PMID_(identifier)) [14506261](https://pubmed.ncbi.nlm.nih.gov/14506261).

- Tanaka M, Kim YM, Lee G, Junn E, Iwatsubo T, Mouradian MM (Feb 2004). ["Aggresomes formed by alpha-synuclein and synphilin-1 are cytoprotective"](https://doi.org/10.1074%2Fjbc.M310994200). *Journal of Biological Chemistry*. **279** (6): 4625–4631. [doi](/source/Doi_(identifier)):[10.1074/jbc.M310994200](https://doi.org/10.1074%2Fjbc.M310994200). [PMID](/source/PMID_(identifier)) [14627698](https://pubmed.ncbi.nlm.nih.gov/14627698).

- Lee G, Tanaka M, Park K, Lee SS, Kim YM, Junn E, et al. (Feb 2004). ["Casein kinase II-mediated phosphorylation regulates alpha-synuclein/synphilin-1 interaction and inclusion body formation"](https://doi.org/10.1074%2Fjbc.M312760200). *Journal of Biological Chemistry*. **279** (8): 6834–6839. [doi](/source/Doi_(identifier)):[10.1074/jbc.M312760200](https://doi.org/10.1074%2Fjbc.M312760200). [PMID](/source/PMID_(identifier)) [14645218](https://pubmed.ncbi.nlm.nih.gov/14645218).

- Chung KK, Thomas B, Li X, Pletnikova O, Troncoso JC, Marsh L, et al. (May 2004). "S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function". *Science*. **304** (5675): 1328–1331. [Bibcode](/source/Bibcode_(identifier)):[2004Sci...304.1328C](https://ui.adsabs.harvard.edu/abs/2004Sci...304.1328C). [doi](/source/Doi_(identifier)):[10.1126/science.1093891](https://doi.org/10.1126%2Fscience.1093891). [PMID](/source/PMID_(identifier)) [15105460](https://pubmed.ncbi.nlm.nih.gov/15105460). [S2CID](/source/S2CID_(identifier)) [86854030](https://api.semanticscholar.org/CorpusID:86854030).

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Adapted from the Wikipedia article [SNCAIP](https://en.wikipedia.org/wiki/SNCAIP) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/SNCAIP?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.