| UniProt ID | SYPL1_HUMAN | |
|---|---|---|
| UniProt AC | Q16563 | |
| Protein Name | Synaptophysin-like protein 1 | |
| Gene Name | SYPL1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 259 | |
| Subcellular Localization |
Cytoplasmic vesicle membrane Multi-pass membrane protein. Melanosome . Cytoplasmic transport vesicles (By similarity). Identified by mass spectrometry in melanosome fractions from stage I to stage IV.. |
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| Protein Description | ||
| Protein Sequence | MAPNIYLVRQRISRLGQRMSGFQINLNPLKEPLGFIKVLEWIASIFAFATCGGFKGQTEIQVNCPPAVTENKTVTATFGYPFRLNEASFQPPPGVNICDVNWKDYVLIGDYSSSAQFYVTFAVFVFLYCIAALLLYVGYTSLYLDSRKLPMIDFVVTLVATFLWLVSTSAWAKALTDIKIATGHNIIDELPPCKKKAVLCYFGSVTSMGSLNVSVIFGFLNMILWGGNAWFVYKETSLHSPSNTSAPHSQGGIPPPTGI | |
| 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 |
|---|---|---|---|---|---|
| 2 (in isoform 2) | Phosphorylation | - | 13.07 | 29507054 | |
| 20 | Phosphorylation | SRLGQRMSGFQINLN HHHHHHHCCEECCCC | 38.35 | 20873877 | |
| 30 | Ubiquitination | QINLNPLKEPLGFIK ECCCCCCCCCHHHHH | 59.55 | - | |
| 71 | N-linked_Glycosylation | CPPAVTENKTVTATF CCCCCCCCCEEEEEE | 35.61 | 17660510 | |
| 77 | Phosphorylation | ENKTVTATFGYPFRL CCCEEEEEECCCEEE | 14.29 | 28152594 | |
| 80 | Phosphorylation | TVTATFGYPFRLNEA EEEEEECCCEEECCC | 8.59 | 28152594 | |
| 179 | 2-Hydroxyisobutyrylation | AKALTDIKIATGHNI HHHHCCCEECCCCCH | 29.15 | - | |
| 194 | 2-Hydroxyisobutyrylation | IDELPPCKKKAVLCY HHCCCCCCCCEEEEE | 64.18 | - | |
| 212 | N-linked_Glycosylation | VTSMGSLNVSVIFGF CCCCCCCCHHHHHHH | 26.22 | UniProtKB CARBOHYD | |
| 236 | Phosphorylation | AWFVYKETSLHSPSN EEEEEEECCCCCCCC | 32.22 | 25693802 | |
| 237 | Phosphorylation | WFVYKETSLHSPSNT EEEEEECCCCCCCCC | 25.77 | 25693802 | |
| 240 | Phosphorylation | YKETSLHSPSNTSAP EEECCCCCCCCCCCC | 35.00 | 25693802 | |
| 242 | Phosphorylation | ETSLHSPSNTSAPHS ECCCCCCCCCCCCCC | 56.61 | 25693802 | |
| 244 | Phosphorylation | SLHSPSNTSAPHSQG CCCCCCCCCCCCCCC | 30.51 | 25693802 | |
| 245 | Phosphorylation | LHSPSNTSAPHSQGG CCCCCCCCCCCCCCC | 44.01 | 25693802 | |
| 249 | Phosphorylation | SNTSAPHSQGGIPPP CCCCCCCCCCCCCCC | 29.48 | 25693802 | |
| 257 | Phosphorylation | QGGIPPPTGI----- CCCCCCCCCC----- | 53.97 | 28555341 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of SYPL1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SYPL1_HUMAN !! | ||||||
* 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 SYPL1_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| VAMP8_HUMAN | VAMP8 | physical | 28514442 | |
| VAMP3_HUMAN | VAMP3 | physical | 28514442 | |
| VAMP2_HUMAN | VAMP2 | physical | 28514442 | |
| LEG3_HUMAN | LGALS3 | physical | 28514442 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| N-linked Glycosylation | |
| Reference | PubMed |
| "Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-71, AND MASS SPECTROMETRY. | |