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| Open reading frame (ORF) annotation in the exon skipping event |
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| 3'-UTR located exon skipping events lost miRNA binding sites |
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| Splicing Quantitative Trait Loci (sQTLs) in the skipped exons |
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Gene summary for SNCA |
 Gene summary |
| Gene information | Gene symbol | SNCA | Gene ID | 6622 |
| Gene name | synuclein alpha | |
| Synonyms | NACP|PARK1|PARK4|PD1 | |
| Cytomap | 4q22.1 | |
| Type of gene | protein-coding | |
| Description | alpha-synucleinI+/--synucleinnon A-beta component of AD amyloidsynuclein alpha-140synuclein, alpha (non A4 component of amyloid precursor)truncated alpha synuclein | |
| Modification date | 20200329 | |
| UniProtAcc | ||
| Context | - 27184464(SNCA Gene Polymorphism May Contribute to an Increased Risk of Alzheimer's Disease) |
| Gene ontology of each this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Gene | GO ID | GO term | PubMed ID |
| SNCA | GO:0001921 | positive regulation of receptor recycling | 18980610 |
| SNCA | GO:0006919 | activation of cysteine-type endopeptidase activity involved in apoptotic process | 21050448 |
| SNCA | GO:0010040 | response to iron(II) ion | 11850416 |
| SNCA | GO:0010517 | regulation of phospholipase activity | 15641770 |
| SNCA | GO:0010642 | negative regulation of platelet-derived growth factor receptor signaling pathway | 12239163 |
| SNCA | GO:0016079 | synaptic vesicle exocytosis | 28288128 |
| SNCA | GO:0031115 | negative regulation of microtubule polymerization | 21127069 |
| SNCA | GO:0031623 | receptor internalization | 18980610 |
| SNCA | GO:0031648 | protein destabilization | 21320589 |
| SNCA | GO:0032026 | response to magnesium ion | 11850416 |
| SNCA | GO:0032410 | negative regulation of transporter activity | 16882008 |
| SNCA | GO:0032496 | response to lipopolysaccharide | 12406186 |
| SNCA | GO:0032769 | negative regulation of monooxygenase activity | 11943812 |
| SNCA | GO:0034341 | response to interferon-gamma | 19157893 |
| SNCA | GO:0035067 | negative regulation of histone acetylation | 16959795 |
| SNCA | GO:0035493 | SNARE complex assembly | 20798282 |
| SNCA | GO:0035543 | positive regulation of SNARE complex assembly | 20798282 |
| SNCA | GO:0045807 | positive regulation of endocytosis | 18980610 |
| SNCA | GO:0050729 | positive regulation of inflammatory response | 25533483 |
| SNCA | GO:0051262 | protein tetramerization | 21841800 |
| SNCA | GO:0051281 | positive regulation of release of sequestered calcium ion into cytosol | 15641770 |
| SNCA | GO:0051585 | negative regulation of dopamine uptake involved in synaptic transmission | 12958153 |
| SNCA | GO:0051612 | negative regulation of serotonin uptake | 16882008 |
| SNCA | GO:0051622 | negative regulation of norepinephrine uptake | 17156375 |
| SNCA | GO:0055074 | calcium ion homeostasis | 12239163 |
| SNCA | GO:0055114 | oxidation-reduction process | 21320589 |
| SNCA | GO:0060732 | positive regulation of inositol phosphate biosynthetic process | 15641770 |
| SNCA | GO:0070495 | negative regulation of thrombin-activated receptor signaling pathway | 12239163 |
| SNCA | GO:0070555 | response to interleukin-1 | 12406186 |
| SNCA | GO:0071280 | cellular response to copper ion | 21320589 |
| SNCA | GO:0071902 | positive regulation of protein serine/threonine kinase activity | 21127069 |
| SNCA | GO:1901215 | negative regulation of neuron death | 15863497 |
| SNCA | GO:1901216 | positive regulation of neuron death | 25533483 |
| SNCA | GO:1903284 | positive regulation of glutathione peroxidase activity | 23507046 |
| SNCA | GO:1903285 | positive regulation of hydrogen peroxide catabolic process | 23507046 |
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Gene structures and expression levels for SNCA |
| Skipped exons in the ROSMAP, MSBB, and Mayo based on Ensembl gene isoform structure. * Click on the image to open the UCSC genome browser with custom track showing this image in a new window. |
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ENSG00000145335
| Differentially expressed gene analysis across multiple brain tissues between AD and control. |
| Tissue type | DEG direction | Base mean exp. | log2FC(AD/control) | P-value | Adj. p-value |
| Differentially expressed isoform analysis across multiple brain tissues between AD and control. |
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| Tissue type | DEG direction | ENST | Transcript info. | Base mean exp. | log2FC(AD/control) | P-value | Adjc. p-value |
| STG | UP | ENST00000394991.7 | SNCA-205:protein_coding:SNCA | 8.863219e+01 | 2.272956e+00 | 5.569282e-04 | 2.836766e-02 |
| Landscape of isoform expressions across multiple brain tissues between AD and control. |
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Exon skipping events with PSIs in ROSMAP, MSBB, and Mayo for SNCA |
| Landscape of individual exon skipping event across AD tissues and controls (PSI heatmap). |
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| All exon skipping events in AD cohorts. |
| Exon skip ID | chr | Exons involved in exon skipping | Skipped exon |
| exon_skip_124546 | chr4 | 89726628:89726660:89729194:89729277:89822246:89822388 | 89729194:89729277 |
| exon_skip_131710 | chr4 | 89828143:89828184:89835547:89835692:89836743:89836789 | 89835547:89835692 |
| exon_skip_137915 | chr4 | 89822246:89822388:89828143:89828184:89835547:89835667 | 89828143:89828184 |
| exon_skip_20106 | chr4 | 89822373:89822388:89828143:89828184:89835547:89835667 | 89828143:89828184 |
| exon_skip_261848 | chr4 | 89726628:89726660:89729194:89729277:89822246:89822343 | 89729194:89729277 |
| exon_skip_291793 | chr4 | 89726628:89726660:89729194:89729277:89822246:89822289 | 89729194:89729277 |
| exon_skip_292947 | chr4 | 89822352:89822388:89828143:89828184:89835547:89835667 | 89828143:89828184 |
| exon_skip_35743 | chr4 | 89835547:89835692:89836743:89836789:89836962:89837076 | 89836743:89836789 |
| exon_skip_38053 | chr4 | 89729194:89729277:89822246:89822388:89835547:89835667 | 89822246:89822388 |
| exon_skip_47209 | chr4 | 89835655:89835692:89836743:89836789:89836962:89837076 | 89836743:89836789 |
| exon_skip_90238 | chr4 | 89835671:89835692:89836743:89836789:89836962:89837076 | 89836743:89836789 |
| Differentially expressed PSI values of individual exon skipping events in multiple brain tissues between AD and control. |
| Exon skipping information | Tissue type | Avg(PSIs) in AD | Avg(PSIs) in control | Difference (PSI) | Adj. p-value |
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Open reading frame (ORF) annotation in the exon skipping event for SNCA |
| Open reading frame (ORF) of individual exon skipping events in ROSMAP based on the Ensembl gene structure combined from isoforms. |
| ENST | Start of skipped exon | End of skipped exon | ORF |
| ENST00000336904 | 89729194 | 89729277 | In-frame |
| ENST00000394986 | 89729194 | 89729277 | In-frame |
| ENST00000394991 | 89729194 | 89729277 | In-frame |
| ENST00000506244 | 89729194 | 89729277 | In-frame |
| ENST00000508895 | 89729194 | 89729277 | In-frame |
| ENST00000336904 | 89828143 | 89828184 | In-frame |
| ENST00000394986 | 89828143 | 89828184 | In-frame |
| ENST00000394991 | 89828143 | 89828184 | In-frame |
| ENST00000506244 | 89828143 | 89828184 | In-frame |
| ENST00000508895 | 89828143 | 89828184 | In-frame |
| Open reading frame (ORF) of individual exon skipping events in MSBB based on the Ensembl gene structure combined from isoforms. |
| ENST | Start of skipped exon | End of skipped exon | ORF |
| ENST00000336904 | 89729194 | 89729277 | In-frame |
| ENST00000394986 | 89729194 | 89729277 | In-frame |
| ENST00000394991 | 89729194 | 89729277 | In-frame |
| ENST00000506244 | 89729194 | 89729277 | In-frame |
| ENST00000508895 | 89729194 | 89729277 | In-frame |
| Open reading frame (ORF) of individual exon skipping events in Mayo based on the Ensembl gene structure combined from isoforms. |
| ENST | Start of skipped exon | End of skipped exon | ORF |
| ENST00000394986 | 89835547 | 89835692 | 3UTR-3CDS |
| ENST00000336904 | 89729194 | 89729277 | In-frame |
| ENST00000394986 | 89729194 | 89729277 | In-frame |
| ENST00000394991 | 89729194 | 89729277 | In-frame |
| ENST00000506244 | 89729194 | 89729277 | In-frame |
| ENST00000508895 | 89729194 | 89729277 | In-frame |
| ENST00000336904 | 89828143 | 89828184 | In-frame |
| ENST00000394986 | 89828143 | 89828184 | In-frame |
| ENST00000394991 | 89828143 | 89828184 | In-frame |
| ENST00000506244 | 89828143 | 89828184 | In-frame |
| ENST00000508895 | 89828143 | 89828184 | In-frame |
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Infer the effects of exon skipping event on protein functional features for SNCA |
p-ENSG00000145335_img4.png |
| Loci of skipped exons in ROSMAP across genomic, transcript, and protein sequence levels of In-frame cases. |
| ENST | Length of mRNA | Length of AA seq. | Genomic start | Genomic end | mRNA start | mRNA end | AA start | AA end |
| ENST00000336904 | 3058 | 140 | 89828143 | 89828184 | 211 | 251 | 40 | 54 |
| ENST00000394986 | 1437 | 140 | 89828143 | 89828184 | 544 | 584 | 40 | 54 |
| ENST00000394991 | 1307 | 140 | 89828143 | 89828184 | 414 | 454 | 40 | 54 |
| ENST00000506244 | 587 | 140 | 89828143 | 89828184 | 218 | 258 | 40 | 54 |
| ENST00000508895 | 922 | 140 | 89828143 | 89828184 | 234 | 274 | 40 | 54 |
| ENST00000336904 | 3058 | 140 | 89729194 | 89729277 | 396 | 478 | 102 | 129 |
| ENST00000394986 | 1437 | 140 | 89729194 | 89729277 | 729 | 811 | 102 | 129 |
| ENST00000394991 | 1307 | 140 | 89729194 | 89729277 | 599 | 681 | 102 | 129 |
| ENST00000506244 | 587 | 140 | 89729194 | 89729277 | 403 | 485 | 102 | 129 |
| ENST00000508895 | 922 | 140 | 89729194 | 89729277 | 419 | 501 | 102 | 129 |
| Loci of skipped exons in MSBB across genomic, transcript, and protein sequence levels of In-frame cases. |
| ENST | Length of mRNA | Length of AA seq. | Genomic start | Genomic end | mRNA start | mRNA end | AA start | AA end |
| ENST00000336904 | 3058 | 140 | 89729194 | 89729277 | 396 | 478 | 102 | 129 |
| ENST00000394986 | 1437 | 140 | 89729194 | 89729277 | 729 | 811 | 102 | 129 |
| ENST00000394991 | 1307 | 140 | 89729194 | 89729277 | 599 | 681 | 102 | 129 |
| ENST00000506244 | 587 | 140 | 89729194 | 89729277 | 403 | 485 | 102 | 129 |
| ENST00000508895 | 922 | 140 | 89729194 | 89729277 | 419 | 501 | 102 | 129 |
| Loci of skipped exons in Mayo across genomic, transcript, and protein sequence levels of In-frame cases. |
| ENST | Length of mRNA | Length of AA seq. | Genomic start | Genomic end | mRNA start | mRNA end | AA start | AA end |
| ENST00000336904 | 3058 | 140 | 89828143 | 89828184 | 211 | 251 | 40 | 54 |
| ENST00000394986 | 1437 | 140 | 89828143 | 89828184 | 544 | 584 | 40 | 54 |
| ENST00000394991 | 1307 | 140 | 89828143 | 89828184 | 414 | 454 | 40 | 54 |
| ENST00000506244 | 587 | 140 | 89828143 | 89828184 | 218 | 258 | 40 | 54 |
| ENST00000508895 | 922 | 140 | 89828143 | 89828184 | 234 | 274 | 40 | 54 |
| ENST00000336904 | 3058 | 140 | 89729194 | 89729277 | 396 | 478 | 102 | 129 |
| ENST00000394986 | 1437 | 140 | 89729194 | 89729277 | 729 | 811 | 102 | 129 |
| ENST00000394991 | 1307 | 140 | 89729194 | 89729277 | 599 | 681 | 102 | 129 |
| ENST00000506244 | 587 | 140 | 89729194 | 89729277 | 403 | 485 | 102 | 129 |
| ENST00000508895 | 922 | 140 | 89729194 | 89729277 | 419 | 501 | 102 | 129 |
| Lost protein functional features of individual exon skipping events in ROSMAP. |
| UniProt acc. | Start of exon skipping (AA) | End of exon skipping (AA) | Protein feature start (AA) | Protein feature end (AA) | Category of protein feature | Description of feature |
| P37840 | 40 | 54 | 41 | 54 | Alternative sequence | ID=VSP_006363;Note=In isoform 2-5. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:7601450;Dbxref=PMID:7601450 |
| P37840 | 40 | 54 | 41 | 54 | Alternative sequence | ID=VSP_006363;Note=In isoform 2-5. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:7601450;Dbxref=PMID:7601450 |
| P37840 | 40 | 54 | 41 | 54 | Alternative sequence | ID=VSP_006363;Note=In isoform 2-5. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:7601450;Dbxref=PMID:7601450 |
| P37840 | 40 | 54 | 41 | 54 | Alternative sequence | ID=VSP_006363;Note=In isoform 2-5. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:7601450;Dbxref=PMID:7601450 |
| P37840 | 40 | 54 | 41 | 54 | Alternative sequence | ID=VSP_006363;Note=In isoform 2-5. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:7601450;Dbxref=PMID:7601450 |
| P37840 | 40 | 54 | 45 | 47 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BXL |
| P37840 | 40 | 54 | 45 | 47 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BXL |
| P37840 | 40 | 54 | 45 | 47 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BXL |
| P37840 | 40 | 54 | 45 | 47 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BXL |
| P37840 | 40 | 54 | 45 | 47 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BXL |
| P37840 | 40 | 54 | 1 | 140 | Chain | ID=PRO_0000184022;Note=Alpha-synuclein |
| P37840 | 40 | 54 | 1 | 140 | Chain | ID=PRO_0000184022;Note=Alpha-synuclein |
| P37840 | 40 | 54 | 1 | 140 | Chain | ID=PRO_0000184022;Note=Alpha-synuclein |
| P37840 | 40 | 54 | 1 | 140 | Chain | ID=PRO_0000184022;Note=Alpha-synuclein |
| P37840 | 40 | 54 | 1 | 140 | Chain | ID=PRO_0000184022;Note=Alpha-synuclein |
| P37840 | 40 | 54 | 41 | 44 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q27 |
| P37840 | 40 | 54 | 41 | 44 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q27 |
| P37840 | 40 | 54 | 41 | 44 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q27 |
| P37840 | 40 | 54 | 41 | 44 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q27 |
| P37840 | 40 | 54 | 41 | 44 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q27 |
| P37840 | 40 | 54 | 52 | 55 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q27 |
| P37840 | 40 | 54 | 52 | 55 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q27 |
| P37840 | 40 | 54 | 52 | 55 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q27 |
| P37840 | 40 | 54 | 52 | 55 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q27 |
| P37840 | 40 | 54 | 52 | 55 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q27 |
| P37840 | 40 | 54 | 50 | 50 | Metal binding | Note=Copper;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P37840 | 40 | 54 | 50 | 50 | Metal binding | Note=Copper;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P37840 | 40 | 54 | 50 | 50 | Metal binding | Note=Copper;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P37840 | 40 | 54 | 50 | 50 | Metal binding | Note=Copper;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P37840 | 40 | 54 | 50 | 50 | Metal binding | Note=Copper;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P37840 | 40 | 54 | 50 | 50 | Mutagenesis | Note=Impairs copper-binding. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21319811;Dbxref=PMID:21319811 |
| P37840 | 40 | 54 | 50 | 50 | Mutagenesis | Note=Impairs copper-binding. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21319811;Dbxref=PMID:21319811 |
| P37840 | 40 | 54 | 50 | 50 | Mutagenesis | Note=Impairs copper-binding. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21319811;Dbxref=PMID:21319811 |
| P37840 | 40 | 54 | 50 | 50 | Mutagenesis | Note=Impairs copper-binding. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21319811;Dbxref=PMID:21319811 |
| P37840 | 40 | 54 | 50 | 50 | Mutagenesis | Note=Impairs copper-binding. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21319811;Dbxref=PMID:21319811 |
| P37840 | 40 | 54 | 46 | 46 | Natural variant | ID=VAR_022703;Note=In PARK1 and DLB%3B significant increase in binding to negatively charged phospholipid liposomes%3B increases oligomerization. E->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14755719,ECO:0000269|PubMe |
| P37840 | 40 | 54 | 46 | 46 | Natural variant | ID=VAR_022703;Note=In PARK1 and DLB%3B significant increase in binding to negatively charged phospholipid liposomes%3B increases oligomerization. E->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14755719,ECO:0000269|PubMe |
| P37840 | 40 | 54 | 46 | 46 | Natural variant | ID=VAR_022703;Note=In PARK1 and DLB%3B significant increase in binding to negatively charged phospholipid liposomes%3B increases oligomerization. E->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14755719,ECO:0000269|PubMe |
| P37840 | 40 | 54 | 46 | 46 | Natural variant | ID=VAR_022703;Note=In PARK1 and DLB%3B significant increase in binding to negatively charged phospholipid liposomes%3B increases oligomerization. E->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14755719,ECO:0000269|PubMe |
| P37840 | 40 | 54 | 46 | 46 | Natural variant | ID=VAR_022703;Note=In PARK1 and DLB%3B significant increase in binding to negatively charged phospholipid liposomes%3B increases oligomerization. E->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14755719,ECO:0000269|PubMe |
| P37840 | 40 | 54 | 50 | 50 | Natural variant | ID=VAR_070171;Note=In PARK1%3B no effect on protein structure%3B no effect on phosphorylation of the protein%3B no effect on membrane- and lipid-binding%3B increases oligomerization%3B increases fibril formation%3B increases secretion of the protein%3B im |
| P37840 | 40 | 54 | 50 | 50 | Natural variant | ID=VAR_070171;Note=In PARK1%3B no effect on protein structure%3B no effect on phosphorylation of the protein%3B no effect on membrane- and lipid-binding%3B increases oligomerization%3B increases fibril formation%3B increases secretion of the protein%3B im |
| P37840 | 40 | 54 | 50 | 50 | Natural variant | ID=VAR_070171;Note=In PARK1%3B no effect on protein structure%3B no effect on phosphorylation of the protein%3B no effect on membrane- and lipid-binding%3B increases oligomerization%3B increases fibril formation%3B increases secretion of the protein%3B im |
| P37840 | 40 | 54 | 50 | 50 | Natural variant | ID=VAR_070171;Note=In PARK1%3B no effect on protein structure%3B no effect on phosphorylation of the protein%3B no effect on membrane- and lipid-binding%3B increases oligomerization%3B increases fibril formation%3B increases secretion of the protein%3B im |
| P37840 | 40 | 54 | 50 | 50 | Natural variant | ID=VAR_070171;Note=In PARK1%3B no effect on protein structure%3B no effect on phosphorylation of the protein%3B no effect on membrane- and lipid-binding%3B increases oligomerization%3B increases fibril formation%3B increases secretion of the protein%3B im |
| P37840 | 40 | 54 | 53 | 53 | Natural variant | ID=VAR_007454;Note=In PARK1%3B no effect on osmotic stress-induced phosphorylation%3B increases oligomerization. A->T;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12893833,ECO:0000269|PubMed:25561023,ECO:0000269|PubMed:919 |
| P37840 | 40 | 54 | 53 | 53 | Natural variant | ID=VAR_007454;Note=In PARK1%3B no effect on osmotic stress-induced phosphorylation%3B increases oligomerization. A->T;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12893833,ECO:0000269|PubMed:25561023,ECO:0000269|PubMed:919 |
| P37840 | 40 | 54 | 53 | 53 | Natural variant | ID=VAR_007454;Note=In PARK1%3B no effect on osmotic stress-induced phosphorylation%3B increases oligomerization. A->T;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12893833,ECO:0000269|PubMed:25561023,ECO:0000269|PubMed:919 |
| P37840 | 40 | 54 | 53 | 53 | Natural variant | ID=VAR_007454;Note=In PARK1%3B no effect on osmotic stress-induced phosphorylation%3B increases oligomerization. A->T;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12893833,ECO:0000269|PubMed:25561023,ECO:0000269|PubMed:919 |
| P37840 | 40 | 54 | 53 | 53 | Natural variant | ID=VAR_007454;Note=In PARK1%3B no effect on osmotic stress-induced phosphorylation%3B increases oligomerization. A->T;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12893833,ECO:0000269|PubMed:25561023,ECO:0000269|PubMed:919 |
| P37840 | 40 | 54 | 20 | 67 | Region | Note=4 X 11 AA tandem repeats of [EGS]-K-T-K-[EQ]-[GQ]-V-X(4) |
| P37840 | 40 | 54 | 20 | 67 | Region | Note=4 X 11 AA tandem repeats of [EGS]-K-T-K-[EQ]-[GQ]-V-X(4) |
| P37840 | 40 | 54 | 20 | 67 | Region | Note=4 X 11 AA tandem repeats of [EGS]-K-T-K-[EQ]-[GQ]-V-X(4) |
| P37840 | 40 | 54 | 20 | 67 | Region | Note=4 X 11 AA tandem repeats of [EGS]-K-T-K-[EQ]-[GQ]-V-X(4) |
| P37840 | 40 | 54 | 20 | 67 | Region | Note=4 X 11 AA tandem repeats of [EGS]-K-T-K-[EQ]-[GQ]-V-X(4) |
| P37840 | 40 | 54 | 31 | 41 | Repeat | Note=2 |
| P37840 | 40 | 54 | 31 | 41 | Repeat | Note=2 |
| P37840 | 40 | 54 | 31 | 41 | Repeat | Note=2 |
| P37840 | 40 | 54 | 31 | 41 | Repeat | Note=2 |
| P37840 | 40 | 54 | 31 | 41 | Repeat | Note=2 |
| P37840 | 40 | 54 | 42 | 56 | Repeat | Note=3%3B approximate |
| P37840 | 40 | 54 | 42 | 56 | Repeat | Note=3%3B approximate |
| P37840 | 40 | 54 | 42 | 56 | Repeat | Note=3%3B approximate |
| P37840 | 40 | 54 | 42 | 56 | Repeat | Note=3%3B approximate |
| P37840 | 40 | 54 | 42 | 56 | Repeat | Note=3%3B approximate |
| P37840 | 102 | 129 | 103 | 130 | Alternative sequence | ID=VSP_006364;Note=In isoform 2-4. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:7601450,ECO:0000303|PubMed:7802671;Dbxref=PMID:7601450,PMID:7802671 |
| P37840 | 102 | 129 | 103 | 130 | Alternative sequence | ID=VSP_006364;Note=In isoform 2-4. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:7601450,ECO:0000303|PubMed:7802671;Dbxref=PMID:7601450,PMID:7802671 |
| P37840 | 102 | 129 | 103 | 130 | Alternative sequence | ID=VSP_006364;Note=In isoform 2-4. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:7601450,ECO:0000303|PubMed:7802671;Dbxref=PMID:7601450,PMID:7802671 |
| P37840 | 102 | 129 | 103 | 130 | Alternative sequence | ID=VSP_006364;Note=In isoform 2-4. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:7601450,ECO:0000303|PubMed:7802671;Dbxref=PMID:7601450,PMID:7802671 |
| P37840 | 102 | 129 | 103 | 130 | Alternative sequence | ID=VSP_006364;Note=In isoform 2-4. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:7601450,ECO:0000303|PubMed:7802671;Dbxref=PMID:7601450,PMID:7802671 |
| P37840 | 102 | 129 | 110 | 113 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 110 | 113 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 110 | 113 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 110 | 113 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 110 | 113 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 1 | 140 | Chain | ID=PRO_0000184022;Note=Alpha-synuclein |
| P37840 | 102 | 129 | 1 | 140 | Chain | ID=PRO_0000184022;Note=Alpha-synuclein |
| P37840 | 102 | 129 | 1 | 140 | Chain | ID=PRO_0000184022;Note=Alpha-synuclein |
| P37840 | 102 | 129 | 1 | 140 | Chain | ID=PRO_0000184022;Note=Alpha-synuclein |
| P37840 | 102 | 129 | 1 | 140 | Chain | ID=PRO_0000184022;Note=Alpha-synuclein |
| P37840 | 102 | 129 | 125 | 125 | Modified residue | Note=Phosphotyrosine%3B by FYN;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11162638,ECO:0000269|PubMed:12893833;Dbxref=PMID:11162638,PMID:12893833 |
| P37840 | 102 | 129 | 125 | 125 | Modified residue | Note=Phosphotyrosine%3B by FYN;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11162638,ECO:0000269|PubMed:12893833;Dbxref=PMID:11162638,PMID:12893833 |
| P37840 | 102 | 129 | 125 | 125 | Modified residue | Note=Phosphotyrosine%3B by FYN;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11162638,ECO:0000269|PubMed:12893833;Dbxref=PMID:11162638,PMID:12893833 |
| P37840 | 102 | 129 | 125 | 125 | Modified residue | Note=Phosphotyrosine%3B by FYN;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11162638,ECO:0000269|PubMed:12893833;Dbxref=PMID:11162638,PMID:12893833 |
| P37840 | 102 | 129 | 125 | 125 | Modified residue | Note=Phosphotyrosine%3B by FYN;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11162638,ECO:0000269|PubMed:12893833;Dbxref=PMID:11162638,PMID:12893833 |
| P37840 | 102 | 129 | 129 | 129 | Modified residue | Note=Phosphoserine%3B by BARK1%2C PLK2%2C CK2%2C CK1 and GRK5;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10617630,ECO:0000269|PubMed:11813001,ECO:0000269|PubMed:24936070;Dbxref=PMID:10617630,PMID:11813001,PMID:24936070 |
| P37840 | 102 | 129 | 129 | 129 | Modified residue | Note=Phosphoserine%3B by BARK1%2C PLK2%2C CK2%2C CK1 and GRK5;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10617630,ECO:0000269|PubMed:11813001,ECO:0000269|PubMed:24936070;Dbxref=PMID:10617630,PMID:11813001,PMID:24936070 |
| P37840 | 102 | 129 | 129 | 129 | Modified residue | Note=Phosphoserine%3B by BARK1%2C PLK2%2C CK2%2C CK1 and GRK5;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10617630,ECO:0000269|PubMed:11813001,ECO:0000269|PubMed:24936070;Dbxref=PMID:10617630,PMID:11813001,PMID:24936070 |
| P37840 | 102 | 129 | 129 | 129 | Modified residue | Note=Phosphoserine%3B by BARK1%2C PLK2%2C CK2%2C CK1 and GRK5;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10617630,ECO:0000269|PubMed:11813001,ECO:0000269|PubMed:24936070;Dbxref=PMID:10617630,PMID:11813001,PMID:24936070 |
| P37840 | 102 | 129 | 129 | 129 | Modified residue | Note=Phosphoserine%3B by BARK1%2C PLK2%2C CK2%2C CK1 and GRK5;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10617630,ECO:0000269|PubMed:11813001,ECO:0000269|PubMed:24936070;Dbxref=PMID:10617630,PMID:11813001,PMID:24936070 |
| P37840 | 102 | 129 | 125 | 125 | Mutagenesis | Note=Abolishes osmotic stress-induced phosphorylation. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12893833;Dbxref=PMID:12893833 |
| P37840 | 102 | 129 | 125 | 125 | Mutagenesis | Note=Abolishes osmotic stress-induced phosphorylation. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12893833;Dbxref=PMID:12893833 |
| P37840 | 102 | 129 | 125 | 125 | Mutagenesis | Note=Abolishes osmotic stress-induced phosphorylation. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12893833;Dbxref=PMID:12893833 |
| P37840 | 102 | 129 | 125 | 125 | Mutagenesis | Note=Abolishes osmotic stress-induced phosphorylation. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12893833;Dbxref=PMID:12893833 |
| P37840 | 102 | 129 | 125 | 125 | Mutagenesis | Note=Abolishes osmotic stress-induced phosphorylation. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12893833;Dbxref=PMID:12893833 |
| P37840 | 102 | 129 | 120 | 122 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 120 | 122 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 120 | 122 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 120 | 122 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 120 | 122 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 124 | 126 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 124 | 126 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 124 | 126 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 124 | 126 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 124 | 126 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| Lost protein functional features of individual exon skipping events in MSBB. |
| UniProt acc. | Start of exon skipping (AA) | End of exon skipping (AA) | Protein feature start (AA) | Protein feature end (AA) | Category of protein feature | Description of feature |
| P37840 | 102 | 129 | 103 | 130 | Alternative sequence | ID=VSP_006364;Note=In isoform 2-4. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:7601450,ECO:0000303|PubMed:7802671;Dbxref=PMID:7601450,PMID:7802671 |
| P37840 | 102 | 129 | 103 | 130 | Alternative sequence | ID=VSP_006364;Note=In isoform 2-4. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:7601450,ECO:0000303|PubMed:7802671;Dbxref=PMID:7601450,PMID:7802671 |
| P37840 | 102 | 129 | 103 | 130 | Alternative sequence | ID=VSP_006364;Note=In isoform 2-4. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:7601450,ECO:0000303|PubMed:7802671;Dbxref=PMID:7601450,PMID:7802671 |
| P37840 | 102 | 129 | 103 | 130 | Alternative sequence | ID=VSP_006364;Note=In isoform 2-4. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:7601450,ECO:0000303|PubMed:7802671;Dbxref=PMID:7601450,PMID:7802671 |
| P37840 | 102 | 129 | 103 | 130 | Alternative sequence | ID=VSP_006364;Note=In isoform 2-4. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:7601450,ECO:0000303|PubMed:7802671;Dbxref=PMID:7601450,PMID:7802671 |
| P37840 | 102 | 129 | 110 | 113 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 110 | 113 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 110 | 113 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 110 | 113 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 110 | 113 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 1 | 140 | Chain | ID=PRO_0000184022;Note=Alpha-synuclein |
| P37840 | 102 | 129 | 1 | 140 | Chain | ID=PRO_0000184022;Note=Alpha-synuclein |
| P37840 | 102 | 129 | 1 | 140 | Chain | ID=PRO_0000184022;Note=Alpha-synuclein |
| P37840 | 102 | 129 | 1 | 140 | Chain | ID=PRO_0000184022;Note=Alpha-synuclein |
| P37840 | 102 | 129 | 1 | 140 | Chain | ID=PRO_0000184022;Note=Alpha-synuclein |
| P37840 | 102 | 129 | 125 | 125 | Modified residue | Note=Phosphotyrosine%3B by FYN;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11162638,ECO:0000269|PubMed:12893833;Dbxref=PMID:11162638,PMID:12893833 |
| P37840 | 102 | 129 | 125 | 125 | Modified residue | Note=Phosphotyrosine%3B by FYN;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11162638,ECO:0000269|PubMed:12893833;Dbxref=PMID:11162638,PMID:12893833 |
| P37840 | 102 | 129 | 125 | 125 | Modified residue | Note=Phosphotyrosine%3B by FYN;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11162638,ECO:0000269|PubMed:12893833;Dbxref=PMID:11162638,PMID:12893833 |
| P37840 | 102 | 129 | 125 | 125 | Modified residue | Note=Phosphotyrosine%3B by FYN;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11162638,ECO:0000269|PubMed:12893833;Dbxref=PMID:11162638,PMID:12893833 |
| P37840 | 102 | 129 | 125 | 125 | Modified residue | Note=Phosphotyrosine%3B by FYN;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11162638,ECO:0000269|PubMed:12893833;Dbxref=PMID:11162638,PMID:12893833 |
| P37840 | 102 | 129 | 129 | 129 | Modified residue | Note=Phosphoserine%3B by BARK1%2C PLK2%2C CK2%2C CK1 and GRK5;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10617630,ECO:0000269|PubMed:11813001,ECO:0000269|PubMed:24936070;Dbxref=PMID:10617630,PMID:11813001,PMID:24936070 |
| P37840 | 102 | 129 | 129 | 129 | Modified residue | Note=Phosphoserine%3B by BARK1%2C PLK2%2C CK2%2C CK1 and GRK5;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10617630,ECO:0000269|PubMed:11813001,ECO:0000269|PubMed:24936070;Dbxref=PMID:10617630,PMID:11813001,PMID:24936070 |
| P37840 | 102 | 129 | 129 | 129 | Modified residue | Note=Phosphoserine%3B by BARK1%2C PLK2%2C CK2%2C CK1 and GRK5;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10617630,ECO:0000269|PubMed:11813001,ECO:0000269|PubMed:24936070;Dbxref=PMID:10617630,PMID:11813001,PMID:24936070 |
| P37840 | 102 | 129 | 129 | 129 | Modified residue | Note=Phosphoserine%3B by BARK1%2C PLK2%2C CK2%2C CK1 and GRK5;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10617630,ECO:0000269|PubMed:11813001,ECO:0000269|PubMed:24936070;Dbxref=PMID:10617630,PMID:11813001,PMID:24936070 |
| P37840 | 102 | 129 | 129 | 129 | Modified residue | Note=Phosphoserine%3B by BARK1%2C PLK2%2C CK2%2C CK1 and GRK5;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10617630,ECO:0000269|PubMed:11813001,ECO:0000269|PubMed:24936070;Dbxref=PMID:10617630,PMID:11813001,PMID:24936070 |
| P37840 | 102 | 129 | 125 | 125 | Mutagenesis | Note=Abolishes osmotic stress-induced phosphorylation. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12893833;Dbxref=PMID:12893833 |
| P37840 | 102 | 129 | 125 | 125 | Mutagenesis | Note=Abolishes osmotic stress-induced phosphorylation. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12893833;Dbxref=PMID:12893833 |
| P37840 | 102 | 129 | 125 | 125 | Mutagenesis | Note=Abolishes osmotic stress-induced phosphorylation. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12893833;Dbxref=PMID:12893833 |
| P37840 | 102 | 129 | 125 | 125 | Mutagenesis | Note=Abolishes osmotic stress-induced phosphorylation. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12893833;Dbxref=PMID:12893833 |
| P37840 | 102 | 129 | 125 | 125 | Mutagenesis | Note=Abolishes osmotic stress-induced phosphorylation. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12893833;Dbxref=PMID:12893833 |
| P37840 | 102 | 129 | 120 | 122 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 120 | 122 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 120 | 122 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 120 | 122 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 120 | 122 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 124 | 126 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 124 | 126 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 124 | 126 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 124 | 126 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 124 | 126 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| Lost protein functional features of individual exon skipping events in Mayo. |
| UniProt acc. | Start of exon skipping (AA) | End of exon skipping (AA) | Protein feature start (AA) | Protein feature end (AA) | Category of protein feature | Description of feature |
| P37840 | 40 | 54 | 41 | 54 | Alternative sequence | ID=VSP_006363;Note=In isoform 2-5. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:7601450;Dbxref=PMID:7601450 |
| P37840 | 40 | 54 | 41 | 54 | Alternative sequence | ID=VSP_006363;Note=In isoform 2-5. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:7601450;Dbxref=PMID:7601450 |
| P37840 | 40 | 54 | 41 | 54 | Alternative sequence | ID=VSP_006363;Note=In isoform 2-5. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:7601450;Dbxref=PMID:7601450 |
| P37840 | 40 | 54 | 41 | 54 | Alternative sequence | ID=VSP_006363;Note=In isoform 2-5. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:7601450;Dbxref=PMID:7601450 |
| P37840 | 40 | 54 | 41 | 54 | Alternative sequence | ID=VSP_006363;Note=In isoform 2-5. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:7601450;Dbxref=PMID:7601450 |
| P37840 | 40 | 54 | 45 | 47 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BXL |
| P37840 | 40 | 54 | 45 | 47 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BXL |
| P37840 | 40 | 54 | 45 | 47 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BXL |
| P37840 | 40 | 54 | 45 | 47 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BXL |
| P37840 | 40 | 54 | 45 | 47 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BXL |
| P37840 | 40 | 54 | 1 | 140 | Chain | ID=PRO_0000184022;Note=Alpha-synuclein |
| P37840 | 40 | 54 | 1 | 140 | Chain | ID=PRO_0000184022;Note=Alpha-synuclein |
| P37840 | 40 | 54 | 1 | 140 | Chain | ID=PRO_0000184022;Note=Alpha-synuclein |
| P37840 | 40 | 54 | 1 | 140 | Chain | ID=PRO_0000184022;Note=Alpha-synuclein |
| P37840 | 40 | 54 | 1 | 140 | Chain | ID=PRO_0000184022;Note=Alpha-synuclein |
| P37840 | 40 | 54 | 41 | 44 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q27 |
| P37840 | 40 | 54 | 41 | 44 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q27 |
| P37840 | 40 | 54 | 41 | 44 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q27 |
| P37840 | 40 | 54 | 41 | 44 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q27 |
| P37840 | 40 | 54 | 41 | 44 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q27 |
| P37840 | 40 | 54 | 52 | 55 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q27 |
| P37840 | 40 | 54 | 52 | 55 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q27 |
| P37840 | 40 | 54 | 52 | 55 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q27 |
| P37840 | 40 | 54 | 52 | 55 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q27 |
| P37840 | 40 | 54 | 52 | 55 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q27 |
| P37840 | 40 | 54 | 50 | 50 | Metal binding | Note=Copper;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P37840 | 40 | 54 | 50 | 50 | Metal binding | Note=Copper;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P37840 | 40 | 54 | 50 | 50 | Metal binding | Note=Copper;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P37840 | 40 | 54 | 50 | 50 | Metal binding | Note=Copper;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P37840 | 40 | 54 | 50 | 50 | Metal binding | Note=Copper;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P37840 | 40 | 54 | 50 | 50 | Mutagenesis | Note=Impairs copper-binding. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21319811;Dbxref=PMID:21319811 |
| P37840 | 40 | 54 | 50 | 50 | Mutagenesis | Note=Impairs copper-binding. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21319811;Dbxref=PMID:21319811 |
| P37840 | 40 | 54 | 50 | 50 | Mutagenesis | Note=Impairs copper-binding. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21319811;Dbxref=PMID:21319811 |
| P37840 | 40 | 54 | 50 | 50 | Mutagenesis | Note=Impairs copper-binding. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21319811;Dbxref=PMID:21319811 |
| P37840 | 40 | 54 | 50 | 50 | Mutagenesis | Note=Impairs copper-binding. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21319811;Dbxref=PMID:21319811 |
| P37840 | 40 | 54 | 46 | 46 | Natural variant | ID=VAR_022703;Note=In PARK1 and DLB%3B significant increase in binding to negatively charged phospholipid liposomes%3B increases oligomerization. E->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14755719,ECO:0000269|PubMe |
| P37840 | 40 | 54 | 46 | 46 | Natural variant | ID=VAR_022703;Note=In PARK1 and DLB%3B significant increase in binding to negatively charged phospholipid liposomes%3B increases oligomerization. E->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14755719,ECO:0000269|PubMe |
| P37840 | 40 | 54 | 46 | 46 | Natural variant | ID=VAR_022703;Note=In PARK1 and DLB%3B significant increase in binding to negatively charged phospholipid liposomes%3B increases oligomerization. E->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14755719,ECO:0000269|PubMe |
| P37840 | 40 | 54 | 46 | 46 | Natural variant | ID=VAR_022703;Note=In PARK1 and DLB%3B significant increase in binding to negatively charged phospholipid liposomes%3B increases oligomerization. E->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14755719,ECO:0000269|PubMe |
| P37840 | 40 | 54 | 46 | 46 | Natural variant | ID=VAR_022703;Note=In PARK1 and DLB%3B significant increase in binding to negatively charged phospholipid liposomes%3B increases oligomerization. E->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14755719,ECO:0000269|PubMe |
| P37840 | 40 | 54 | 50 | 50 | Natural variant | ID=VAR_070171;Note=In PARK1%3B no effect on protein structure%3B no effect on phosphorylation of the protein%3B no effect on membrane- and lipid-binding%3B increases oligomerization%3B increases fibril formation%3B increases secretion of the protein%3B im |
| P37840 | 40 | 54 | 50 | 50 | Natural variant | ID=VAR_070171;Note=In PARK1%3B no effect on protein structure%3B no effect on phosphorylation of the protein%3B no effect on membrane- and lipid-binding%3B increases oligomerization%3B increases fibril formation%3B increases secretion of the protein%3B im |
| P37840 | 40 | 54 | 50 | 50 | Natural variant | ID=VAR_070171;Note=In PARK1%3B no effect on protein structure%3B no effect on phosphorylation of the protein%3B no effect on membrane- and lipid-binding%3B increases oligomerization%3B increases fibril formation%3B increases secretion of the protein%3B im |
| P37840 | 40 | 54 | 50 | 50 | Natural variant | ID=VAR_070171;Note=In PARK1%3B no effect on protein structure%3B no effect on phosphorylation of the protein%3B no effect on membrane- and lipid-binding%3B increases oligomerization%3B increases fibril formation%3B increases secretion of the protein%3B im |
| P37840 | 40 | 54 | 50 | 50 | Natural variant | ID=VAR_070171;Note=In PARK1%3B no effect on protein structure%3B no effect on phosphorylation of the protein%3B no effect on membrane- and lipid-binding%3B increases oligomerization%3B increases fibril formation%3B increases secretion of the protein%3B im |
| P37840 | 40 | 54 | 53 | 53 | Natural variant | ID=VAR_007454;Note=In PARK1%3B no effect on osmotic stress-induced phosphorylation%3B increases oligomerization. A->T;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12893833,ECO:0000269|PubMed:25561023,ECO:0000269|PubMed:919 |
| P37840 | 40 | 54 | 53 | 53 | Natural variant | ID=VAR_007454;Note=In PARK1%3B no effect on osmotic stress-induced phosphorylation%3B increases oligomerization. A->T;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12893833,ECO:0000269|PubMed:25561023,ECO:0000269|PubMed:919 |
| P37840 | 40 | 54 | 53 | 53 | Natural variant | ID=VAR_007454;Note=In PARK1%3B no effect on osmotic stress-induced phosphorylation%3B increases oligomerization. A->T;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12893833,ECO:0000269|PubMed:25561023,ECO:0000269|PubMed:919 |
| P37840 | 40 | 54 | 53 | 53 | Natural variant | ID=VAR_007454;Note=In PARK1%3B no effect on osmotic stress-induced phosphorylation%3B increases oligomerization. A->T;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12893833,ECO:0000269|PubMed:25561023,ECO:0000269|PubMed:919 |
| P37840 | 40 | 54 | 53 | 53 | Natural variant | ID=VAR_007454;Note=In PARK1%3B no effect on osmotic stress-induced phosphorylation%3B increases oligomerization. A->T;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12893833,ECO:0000269|PubMed:25561023,ECO:0000269|PubMed:919 |
| P37840 | 40 | 54 | 20 | 67 | Region | Note=4 X 11 AA tandem repeats of [EGS]-K-T-K-[EQ]-[GQ]-V-X(4) |
| P37840 | 40 | 54 | 20 | 67 | Region | Note=4 X 11 AA tandem repeats of [EGS]-K-T-K-[EQ]-[GQ]-V-X(4) |
| P37840 | 40 | 54 | 20 | 67 | Region | Note=4 X 11 AA tandem repeats of [EGS]-K-T-K-[EQ]-[GQ]-V-X(4) |
| P37840 | 40 | 54 | 20 | 67 | Region | Note=4 X 11 AA tandem repeats of [EGS]-K-T-K-[EQ]-[GQ]-V-X(4) |
| P37840 | 40 | 54 | 20 | 67 | Region | Note=4 X 11 AA tandem repeats of [EGS]-K-T-K-[EQ]-[GQ]-V-X(4) |
| P37840 | 40 | 54 | 31 | 41 | Repeat | Note=2 |
| P37840 | 40 | 54 | 31 | 41 | Repeat | Note=2 |
| P37840 | 40 | 54 | 31 | 41 | Repeat | Note=2 |
| P37840 | 40 | 54 | 31 | 41 | Repeat | Note=2 |
| P37840 | 40 | 54 | 31 | 41 | Repeat | Note=2 |
| P37840 | 40 | 54 | 42 | 56 | Repeat | Note=3%3B approximate |
| P37840 | 40 | 54 | 42 | 56 | Repeat | Note=3%3B approximate |
| P37840 | 40 | 54 | 42 | 56 | Repeat | Note=3%3B approximate |
| P37840 | 40 | 54 | 42 | 56 | Repeat | Note=3%3B approximate |
| P37840 | 40 | 54 | 42 | 56 | Repeat | Note=3%3B approximate |
| P37840 | 102 | 129 | 103 | 130 | Alternative sequence | ID=VSP_006364;Note=In isoform 2-4. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:7601450,ECO:0000303|PubMed:7802671;Dbxref=PMID:7601450,PMID:7802671 |
| P37840 | 102 | 129 | 103 | 130 | Alternative sequence | ID=VSP_006364;Note=In isoform 2-4. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:7601450,ECO:0000303|PubMed:7802671;Dbxref=PMID:7601450,PMID:7802671 |
| P37840 | 102 | 129 | 103 | 130 | Alternative sequence | ID=VSP_006364;Note=In isoform 2-4. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:7601450,ECO:0000303|PubMed:7802671;Dbxref=PMID:7601450,PMID:7802671 |
| P37840 | 102 | 129 | 103 | 130 | Alternative sequence | ID=VSP_006364;Note=In isoform 2-4. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:7601450,ECO:0000303|PubMed:7802671;Dbxref=PMID:7601450,PMID:7802671 |
| P37840 | 102 | 129 | 103 | 130 | Alternative sequence | ID=VSP_006364;Note=In isoform 2-4. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:7601450,ECO:0000303|PubMed:7802671;Dbxref=PMID:7601450,PMID:7802671 |
| P37840 | 102 | 129 | 110 | 113 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 110 | 113 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 110 | 113 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 110 | 113 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 110 | 113 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 1 | 140 | Chain | ID=PRO_0000184022;Note=Alpha-synuclein |
| P37840 | 102 | 129 | 1 | 140 | Chain | ID=PRO_0000184022;Note=Alpha-synuclein |
| P37840 | 102 | 129 | 1 | 140 | Chain | ID=PRO_0000184022;Note=Alpha-synuclein |
| P37840 | 102 | 129 | 1 | 140 | Chain | ID=PRO_0000184022;Note=Alpha-synuclein |
| P37840 | 102 | 129 | 1 | 140 | Chain | ID=PRO_0000184022;Note=Alpha-synuclein |
| P37840 | 102 | 129 | 125 | 125 | Modified residue | Note=Phosphotyrosine%3B by FYN;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11162638,ECO:0000269|PubMed:12893833;Dbxref=PMID:11162638,PMID:12893833 |
| P37840 | 102 | 129 | 125 | 125 | Modified residue | Note=Phosphotyrosine%3B by FYN;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11162638,ECO:0000269|PubMed:12893833;Dbxref=PMID:11162638,PMID:12893833 |
| P37840 | 102 | 129 | 125 | 125 | Modified residue | Note=Phosphotyrosine%3B by FYN;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11162638,ECO:0000269|PubMed:12893833;Dbxref=PMID:11162638,PMID:12893833 |
| P37840 | 102 | 129 | 125 | 125 | Modified residue | Note=Phosphotyrosine%3B by FYN;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11162638,ECO:0000269|PubMed:12893833;Dbxref=PMID:11162638,PMID:12893833 |
| P37840 | 102 | 129 | 125 | 125 | Modified residue | Note=Phosphotyrosine%3B by FYN;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11162638,ECO:0000269|PubMed:12893833;Dbxref=PMID:11162638,PMID:12893833 |
| P37840 | 102 | 129 | 129 | 129 | Modified residue | Note=Phosphoserine%3B by BARK1%2C PLK2%2C CK2%2C CK1 and GRK5;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10617630,ECO:0000269|PubMed:11813001,ECO:0000269|PubMed:24936070;Dbxref=PMID:10617630,PMID:11813001,PMID:24936070 |
| P37840 | 102 | 129 | 129 | 129 | Modified residue | Note=Phosphoserine%3B by BARK1%2C PLK2%2C CK2%2C CK1 and GRK5;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10617630,ECO:0000269|PubMed:11813001,ECO:0000269|PubMed:24936070;Dbxref=PMID:10617630,PMID:11813001,PMID:24936070 |
| P37840 | 102 | 129 | 129 | 129 | Modified residue | Note=Phosphoserine%3B by BARK1%2C PLK2%2C CK2%2C CK1 and GRK5;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10617630,ECO:0000269|PubMed:11813001,ECO:0000269|PubMed:24936070;Dbxref=PMID:10617630,PMID:11813001,PMID:24936070 |
| P37840 | 102 | 129 | 129 | 129 | Modified residue | Note=Phosphoserine%3B by BARK1%2C PLK2%2C CK2%2C CK1 and GRK5;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10617630,ECO:0000269|PubMed:11813001,ECO:0000269|PubMed:24936070;Dbxref=PMID:10617630,PMID:11813001,PMID:24936070 |
| P37840 | 102 | 129 | 129 | 129 | Modified residue | Note=Phosphoserine%3B by BARK1%2C PLK2%2C CK2%2C CK1 and GRK5;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10617630,ECO:0000269|PubMed:11813001,ECO:0000269|PubMed:24936070;Dbxref=PMID:10617630,PMID:11813001,PMID:24936070 |
| P37840 | 102 | 129 | 125 | 125 | Mutagenesis | Note=Abolishes osmotic stress-induced phosphorylation. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12893833;Dbxref=PMID:12893833 |
| P37840 | 102 | 129 | 125 | 125 | Mutagenesis | Note=Abolishes osmotic stress-induced phosphorylation. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12893833;Dbxref=PMID:12893833 |
| P37840 | 102 | 129 | 125 | 125 | Mutagenesis | Note=Abolishes osmotic stress-induced phosphorylation. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12893833;Dbxref=PMID:12893833 |
| P37840 | 102 | 129 | 125 | 125 | Mutagenesis | Note=Abolishes osmotic stress-induced phosphorylation. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12893833;Dbxref=PMID:12893833 |
| P37840 | 102 | 129 | 125 | 125 | Mutagenesis | Note=Abolishes osmotic stress-induced phosphorylation. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12893833;Dbxref=PMID:12893833 |
| P37840 | 102 | 129 | 120 | 122 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 120 | 122 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 120 | 122 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 120 | 122 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 120 | 122 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 124 | 126 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 124 | 126 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 124 | 126 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 124 | 126 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
| P37840 | 102 | 129 | 124 | 126 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XQ8 |
Top |
3'-UTR located exon skipping events that lost miRNA binding sites in SNCA |
| 3'-UTR exon skipping evnets lost miRNA binding. |
| Tissue type | ENST | Exon skip start | Exon skip end | microRNA | Binding site by TargetScan | Binding type by TargetScan | Bdinding site by miRanda | Score of miRanda | Energy by miRanda |
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SNVs in the skipped exons for SNCA |
| - Differential PSIs between mutated versus non-mutated samples. |
| - Depth of Coverage in the skipped exon of the mutated samples. |
| - Sashimi plot in the skipped exon of the mutated samples. |
| - Non-synonymous mutations located in the skipped exons. |
| Cancer type | Sample | ESID | Skipped exon start | Skipped exon end | Mutation start | Mutation end | Mutation type | Reference seq | Mutation seq | AAchange |
| - Non-synonymous mutations located in the skipped exons in CCLE. |
| Sample | Skipped exon start | Skipped exon end | Mutation start | Mutation end | Mutation type | Reference seq | Mutation seq | AAchange |
Top |
AD stage-associated exon skippint events for SNCA |
| Associated exon skipping events with Braak staging or Clinical Dementia Rating (CDR). |
| AD stage info | Cohort | Tissue | SE id | Coefficient | P-value | Chromosome | Strand | E1 start | E1 end | Skipped start | Skipped end | E2 start | E2 end |
Top |
Splicing Quantitative Trait Loci (sQTL) in the exon skipping event for SNCA |
| sQTL information located at the skipped exons. |
| Tissue type | Exon skip ID | SNP id | Location | P-value | FDR |
Top |
Correlation with RNA binding proteins (RBPs) for SNCA |
| Correlated RBP and related information. |
| Tissue type | RBP name | Exon skip ID | Correlation coeifficient | P-value |
Top |
RelatedDrugs for SNCA |
| Approved drugs targeting this gene. (DrugBank Version 5.1.0 2018-04-02) |
| UniProtAcc | DrugBank ID | Drug name | Drug activity | Drug type | Drug status |
Top |
RelatedDiseases for SNCA |
| Diseases associated with this gene. (DisGeNet 4.0) |
| Gene | Disease ID | Disease name | # pubmeds | Source |
Copyright 2018-Present -The University of Texas Health Science Center at Houston (UTHealth)
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