| UniProt ID | ERV29_YEAST | |
|---|---|---|
| UniProt AC | P53337 | |
| Protein Name | ER-derived vesicles protein ERV29 | |
| Gene Name | ERV29 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 310 | |
| Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein . |
|
| Protein Description | Constituent of COPII-coated endoplasmic reticulum-derived transport vesicles. Required for efficient transport of a subset of secretory proteins to the Golgi. The C-terminal di-lysine motif is required for exit from the endoplasmic reticulum. Required directly for packaging glycosylated pro-alpha-factor into COPII vesicles. Facilitates retrograde transport from the Golgi to the endoplasmic reticulum.. | |
| Protein Sequence | MSYRGPIGNFGGMPMSSSQGPYSGGAQFRSNQNQSTSGILKQWKHSFEKFASRIEGLTDNAVVYKLKPYIPSLSRFFIVATFYEDSFRILSQWSDQIFYLNKWKHYPYFFVVVFLVVVTVSMLIGASLLVLRKQTNYATGVLCACVISQALVYGLFTGSSFVLRNFSVIGGLLIAFSDSIVQNKTTFGMLPELNSKNDKAKGYLLFAGRILIVLMFIAFTFSKSWFTVVLTIIGTICFAIGYKTKFASIMLGLILTFYNITLNNYWFYNNTKRDFLKYEFYQNLSIIGGLLLVTNTGAGELSVDEKKKIY | |
| 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 | Phosphorylation | ------MSYRGPIGN ------CCCCCCCCC | 24.44 | 22369663 | |
| 3 | Phosphorylation | -----MSYRGPIGNF -----CCCCCCCCCC | 20.49 | 22369663 | |
| 16 | Phosphorylation | NFGGMPMSSSQGPYS CCCCCCCCCCCCCCC | 22.44 | 22369663 | |
| 17 | Phosphorylation | FGGMPMSSSQGPYSG CCCCCCCCCCCCCCC | 22.04 | 22369663 | |
| 18 | Phosphorylation | GGMPMSSSQGPYSGG CCCCCCCCCCCCCCC | 31.67 | 22369663 | |
| 22 | Phosphorylation | MSSSQGPYSGGAQFR CCCCCCCCCCCCCCC | 27.11 | 23749301 | |
| 23 | Phosphorylation | SSSQGPYSGGAQFRS CCCCCCCCCCCCCCC | 33.61 | 22369663 | |
| 49 | Acetylation | QWKHSFEKFASRIEG HHHHHHHHHHHHHCC | 44.19 | 24489116 | |
| 67 | Acetylation | NAVVYKLKPYIPSLS CCEEEECCCCCCCCH | 31.46 | 24489116 |
| 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 ERV29_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ERV29_YEAST !! | ||||||
* 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 ERV29_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND MASSSPECTROMETRY. | |
