| UniProt ID | TLG1_YEAST | |
|---|---|---|
| UniProt AC | Q03322 | |
| Protein Name | t-SNARE affecting a late Golgi compartment protein 1 | |
| Gene Name | TLG1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 224 | |
| Subcellular Localization |
Golgi apparatus, trans-Golgi network membrane Single-pass type IV membrane protein . Early endosome membrane Single-pass type IV membrane protein . Late endosome membrane Single-pass type IV membrane protein . Probably shuttling between TGN and |
|
| Protein Description | SNARE protein (of Qc type) involved in membrane fusion probably in retrograde traffic of cytosolic double-membrane vesicles derived from both, early and possibly late endosomes/PVC (prevacuolar compartment) back to the trans-Golgi network (TGN or late Golgi). It has been reported to function both as a (target membrane) t-SNARE and as a (vesicle) v-SNARE. Upon vesicle tethering to the target membrane, which requires additional proteins, a SNARE-pin is formed. This is a very stable 4 parallel alpha-helical coil bundle consisting of 4 SNARE domains (usually one of each type: Qa, Qb, Qc, and R), of which at least one is anchored in the opposite membrane. The formation of the SNARE-pin is believed to bring the two membranes in close proximity and to provide the energy to drive membrane fusion. Through its interaction with the VFT (or GARP) complex, it may also contribute to vesicle recognition specificity and tethering. Regulation of SNARE-pin formation also seems to depend on the phosphorylation state of the protein, phosphorylation by TPK1 causing inhibition and dephosphorylation by SIT4 activation.. | |
| Protein Sequence | MNNSEDPFQQVVKDTKEQLNRINNYITRHNTAGDDDQEEEIQDILKDVEETIVDLDRSIIVMKRDENEDVSGREAQVKNIKQQLDALKLRFDRRIQESTQTTIPLEETVENSTLNTSMAENNDGGMSNPFQEQMLREQDVHLDGIHKTMQNLHIQAQTMGDELENQGQLLDNMDEGMDGVVNKLARGRRQLEWVYEKNKEKYDDCCIGLLIVVLIVLLVLAFIA | |
| 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 |
|---|---|---|---|---|---|
| 31 | Phosphorylation | NYITRHNTAGDDDQE HHHHHCCCCCCCCCH | 26.37 | 15973437 | |
| 183 | Ubiquitination | GMDGVVNKLARGRRQ CCHHHHHHHHHHHHH | 31.73 | 23749301 | |
| 205 | S-palmitoylation | NKEKYDDCCIGLLIV CHHHHHHHHHHHHHH | 1.34 | 15973437 | |
| 206 | S-palmitoylation | KEKYDDCCIGLLIVV HHHHHHHHHHHHHHH | 3.39 | 15973437 |
| Modified Location | Modified Residue | Modification | Function | Reference |
|---|---|---|---|---|
| 31 | T | Phosphorylation |
| 12006655 |
* 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 TLG1_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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