| UniProt ID | SYUA_HUMAN | |
|---|---|---|
| UniProt AC | P37840 | |
| Protein Name | Alpha-synuclein | |
| Gene Name | SNCA | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 140 | |
| Subcellular Localization | Cytoplasm, cytosol . Membrane . Nucleus . Cell junction, synapse . Secreted . Membrane-bound in dopaminergic neurons. | |
| Protein Description | May be involved in the regulation of dopamine release and transport. Induces fibrillization of microtubule-associated protein tau. Reduces neuronal responsiveness to various apoptotic stimuli, leading to a decreased caspase-3 activation.. | |
| Protein Sequence | MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 1 | Acetylation | -------MDVFMKGL -------CCCCHHHH | 10.01 | 22407793 | |
| 1 | Sulfoxidation | -------MDVFMKGL -------CCCCHHHH | 10.01 | 23398174 | |
| 5 | Sulfoxidation | ---MDVFMKGLSKAK ---CCCCHHHHHHHH | 3.19 | 23398174 | |
| 6 | Sumoylation | --MDVFMKGLSKAKE --CCCCHHHHHHHHH | 45.28 | - | |
| 6 | Sumoylation | --MDVFMKGLSKAKE --CCCCHHHHHHHHH | 45.28 | - | |
| 9 | Phosphorylation | DVFMKGLSKAKEGVV CCCHHHHHHHHHHHH | 38.96 | 10852916 | |
| 10 | Sumoylation | VFMKGLSKAKEGVVA CCHHHHHHHHHHHHH | 69.40 | - | |
| 10 | Sumoylation | VFMKGLSKAKEGVVA CCHHHHHHHHHHHHH | 69.40 | - | |
| 12 | Ubiquitination | MKGLSKAKEGVVAAA HHHHHHHHHHHHHHH | 59.75 | 16847063 | |
| 12 | Sumoylation | MKGLSKAKEGVVAAA HHHHHHHHHHHHHHH | 59.75 | - | |
| 12 | Sumoylation | MKGLSKAKEGVVAAA HHHHHHHHHHHHHHH | 59.75 | - | |
| 21 | Acetylation | GVVAAAEKTKQGVAE HHHHHHHHHHHHHHH | 57.19 | 23954790 | |
| 21 | Sumoylation | GVVAAAEKTKQGVAE HHHHHHHHHHHHHHH | 57.19 | - | |
| 21 | Ubiquitination | GVVAAAEKTKQGVAE HHHHHHHHHHHHHHH | 57.19 | 16847063 | |
| 21 | Sumoylation | GVVAAAEKTKQGVAE HHHHHHHHHHHHHHH | 57.19 | - | |
| 23 | Sumoylation | VAAAEKTKQGVAEAA HHHHHHHHHHHHHHC | 57.00 | - | |
| 23 | Ubiquitination | VAAAEKTKQGVAEAA HHHHHHHHHHHHHHC | 57.00 | 1684706 | |
| 23 | Sumoylation | VAAAEKTKQGVAEAA HHHHHHHHHHHHHHC | 57.00 | - | |
| 34 | Sumoylation | AEAAGKTKEGVLYVG HHHCCCCCCEEEEEC | 56.83 | - | |
| 34 | Sumoylation | AEAAGKTKEGVLYVG HHHCCCCCCEEEEEC | 56.83 | - | |
| 39 | Nitration | KTKEGVLYVGSKTKE CCCCEEEEECCCCCC | 10.60 | - | |
| 39 | Phosphorylation | KTKEGVLYVGSKTKE CCCCEEEEECCCCCC | 10.60 | 21945579 | |
| 42 | Phosphorylation | EGVLYVGSKTKEGVV CEEEEECCCCCCCEE | 27.40 | 21945579 | |
| 45 | Sumoylation | LYVGSKTKEGVVHGV EEECCCCCCCEEEEE | 57.09 | - | |
| 45 | Sumoylation | LYVGSKTKEGVVHGV EEECCCCCCCEEEEE | 57.09 | - | |
| 54 | O-linked_Glycosylation | GVVHGVATVAEKTKE CEEEEEEEHHHHHHH | 20.17 | 31753312 | |
| 58 | Acetylation | GVATVAEKTKEQVTN EEEEHHHHHHHHHHC | 55.98 | 23954790 | |
| 60 | Sumoylation | ATVAEKTKEQVTNVG EEHHHHHHHHHHCCC | 58.16 | - | |
| 60 | Sumoylation | ATVAEKTKEQVTNVG EEHHHHHHHHHHCCC | 58.16 | - | |
| 64 | O-linked_Glycosylation | EKTKEQVTNVGGAVV HHHHHHHHCCCCEEE | 24.71 | 28673834 | |
| 72 | O-linked_Glycosylation | NVGGAVVTGVTAVAQ CCCCEEEECCCEEEE | 21.24 | 28673834 | |
| 75 | O-linked_Glycosylation | GAVVTGVTAVAQKTV CEEEECCCEEEECCC | 19.43 | - | |
| 80 | Sumoylation | GVTAVAQKTVEGAGS CCCEEEECCCCCCCH | 44.81 | - | |
| 80 | Sumoylation | GVTAVAQKTVEGAGS CCCEEEECCCCCCCH | 44.81 | - | |
| 81 | Phosphorylation | VTAVAQKTVEGAGSI CCEEEECCCCCCCHH | 16.23 | 28555341 | |
| 81 | O-linked_Glycosylation | VTAVAQKTVEGAGSI CCEEEECCCCCCCHH | 16.23 | 28673834 | |
| 87 | O-linked_Glycosylation | KTVEGAGSIAAATGF CCCCCCCHHHHHHCC | 14.44 | 10617630 | |
| 87 | Phosphorylation | KTVEGAGSIAAATGF CCCCCCCHHHHHHCC | 14.44 | 21082442 | |
| 92 | Phosphorylation | AGSIAAATGFVKKDQ CCHHHHHHCCEEHHH | 26.82 | 23532336 | |
| 96 | Sumoylation | AAATGFVKKDQLGKN HHHHCCEEHHHCCCC | 48.66 | - | |
| 96 | Acetylation | AAATGFVKKDQLGKN HHHHCCEEHHHCCCC | 48.66 | 66726745 | |
| 96 | Sumoylation | AAATGFVKKDQLGKN HHHHCCEEHHHCCCC | 48.66 | - | |
| 102 | Sumoylation | VKKDQLGKNEEGAPQ EEHHHCCCCCCCCCC | 70.54 | - | |
| 102 | Sumoylation | VKKDQLGKNEEGAPQ EEHHHCCCCCCCCCC | 70.54 | - | |
| 108 (in isoform 2) | Phosphorylation | - | 43.54 | 11744621 | |
| 125 | Nitration | VDPDNEAYEMPSEEG CCCCCCCCCCCCCCC | 13.44 | - | |
| 125 | Phosphorylation | VDPDNEAYEMPSEEG CCCCCCCCCCCCCCC | 13.44 | 11078745 | |
| 129 | Phosphorylation | NEAYEMPSEEGYQDY CCCCCCCCCCCCCCC | 47.14 | 24936070 | |
| 133 | Nitration | EMPSEEGYQDYEPEA CCCCCCCCCCCCCCC | 11.07 | - | |
| 133 | Phosphorylation | EMPSEEGYQDYEPEA CCCCCCCCCCCCCCC | 11.07 | 11078745 | |
| 136 | Nitration | SEEGYQDYEPEA--- CCCCCCCCCCCC--- | 20.18 | - | |
| 136 | Phosphorylation | SEEGYQDYEPEA--- CCCCCCCCCCCC--- | 20.18 | 11078745 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 39 | Y | Phosphorylation | Kinase | ABL1 | P00519 | GPS |
| 87 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
| 87 | S | Phosphorylation | Kinase | DYR1A | Q13627 | PhosphoELM |
| 87 | S | Phosphorylation | Kinase | CSNK1A1 | P48729 | GPS |
| 125 | Y | Phosphorylation | Kinase | SRC_GROUP | - | PhosphoELM |
| 125 | Y | Phosphorylation | Kinase | ABL | P00519 | PSP |
| 125 | Y | Phosphorylation | Kinase | SRC-FAMILY | - | GPS |
| 125 | Y | Phosphorylation | Kinase | SYK | Q15046 | PhosphoELM |
| 125 | Y | Phosphorylation | Kinase | SRC | P12931 | PSP |
| 125 | Y | Phosphorylation | Kinase | SYK | P43405 | PSP |
| 125 | Y | Phosphorylation | Kinase | PTK2B | Q14289 | GPS |
| 125 | Y | Phosphorylation | Kinase | FYN | P06241 | Uniprot |
| 129 | S | Phosphorylation | Kinase | ARBK1 | P25098 | PhosphoELM |
| 129 | S | Phosphorylation | Kinase | CSNK1A1 | P48729 | GPS |
| 129 | S | Phosphorylation | Kinase | CK1 | - | Uniprot |
| 129 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
| 129 | S | Phosphorylation | Kinase | CSK21 | P68400 | PhosphoELM |
| 129 | S | Phosphorylation | Kinase | CSNK2A1 | Q60737 | GPS |
| 129 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
| 129 | S | Phosphorylation | Kinase | PLK3 | Q9H4B4 | PSP |
| 129 | S | Phosphorylation | Kinase | PLK2 | P53351 | PSP |
| 129 | S | Phosphorylation | Kinase | PLK2 | Q9NYY3 | Uniprot |
| 129 | S | Phosphorylation | Kinase | PLK1 | P53350 | PSP |
| 129 | S | Phosphorylation | Kinase | GRK5 | P34947 | Uniprot |
| 129 | S | Phosphorylation | Kinase | CAMK2A | Q9UQM7 | PSP |
| 129 | S | Phosphorylation | Kinase | GSK3B | P49841 | PSP |
| 133 | Y | Phosphorylation | Kinase | SYK | Q15046 | PhosphoELM |
| 133 | Y | Phosphorylation | Kinase | SYK | P43405 | PSP |
| 136 | Y | Phosphorylation | Kinase | SYK | Q15046 | PhosphoELM |
| 136 | Y | Phosphorylation | Kinase | SYK | P43405 | PSP |
| - | K | Ubiquitination | E3 ubiquitin ligase | NEDD4 | P46934 | PMID:21953697 |
| - | K | Ubiquitination | E3 ubiquitin ligase | SIAH2 | O43255 | PMID:15064394 |
| - | K | Ubiquitination | E3 ubiquitin ligase | SIAH1 | Q8IUQ4 | PMID:14506261 |
| - | K | Ubiquitination | E3 ubiquitin ligase | STUB1 | Q9UNE7 | PMID:18436529 |
| - | K | Ubiquitination | E3 ubiquitin ligase | PRKN | O60260 | PMID:11431533 |
| - | K | Ubiquitination | E3 ubiquitin ligase | TRAF6 | Q9Y4K3 | PMID:20634198 |
| - | K | Ubiquitination | E3 ubiquitin ligase | UBE3A | Q05086 | PMID:19645749 |
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of SYUA_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| H00057 | Parkinson's disease (PD) | |||||
| H00066 | Lewy body dementia (LBD); Dementia with Lewy bodies (DLB) | |||||
| OMIM Disease | ||||||
| Note=Genetic alterations of SNCA resulting in aberrant polymerization into fibrils, are associated with several neurodegenerative diseases (synucleinopathies). SNCA fibrillar aggregates represent the major non A-beta component of Alzheimer disease amyloid plaque, and a major component of Lewy body inclusions. They are also found within Lewy body (LB)-like intraneuronal inclusions, glial inclusions and axonal spheroids in neurodegeneration with brain iron accumulation type 1. | ||||||
| 168601 | ||||||
| 605543 | Parkinson disease 4 (PARK4) | |||||
| 127750 | Dementia Lewy body (DLB) | |||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Identification and characterization of a novel Pyk2/related adhesionfocal tyrosine kinase-associated protein that inhibits alpha-synucleinphosphorylation."; Takahashi T., Yamashita H., Nagano Y., Nakamura T., Ohmori H.,Avraham H., Avraham S., Yasuda M., Matsumoto M.; J. Biol. Chem. 278:42225-42233(2003). Cited for: MUTAGENESIS OF TYR-39; TYR-125; TYR-133 AND TYR-136, CHARACTERIZATIONOF VARIANT THR-53, AND PHOSPHORYLATION AT TYR-125. | |
| "Activated Fyn phosphorylates alpha-synuclein at tyrosine residue125."; Nakamura T., Yamashita H., Takahashi T., Nakamura S.; Biochem. Biophys. Res. Commun. 280:1085-1092(2001). Cited for: PHOSPHORYLATION AT TYR-125 BY FYN. | |
