| UniProt ID | TRS65_YEAST | |
|---|---|---|
| UniProt AC | P32893 | |
| Protein Name | Trafficking protein particle complex II-specific subunit 65 | |
| Gene Name | TRS65 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 560 | |
| Subcellular Localization | Cytoplasm. Golgi apparatus, cis-Golgi network. | |
| Protein Description | Specific subunit of the TRAPP II complex, a highly conserved vesicle tethering complex that functions in the late Golgi as a guanine nucleotide exchanger (GEF) for the Golgi YPT1 GTPase. TRS65 plays a role in the YPT GEF activity of TRAPP II in concert with the two other TRAPP II-specific subunits TRS120 and TRS130. Involved in cell wall (1-->6)-beta-glucan synthesis.. | |
| Protein Sequence | MECFVPLRCDLDGSNIEQLRQSHLSRKFIIFDEQLNLWLWFQGNSQENKRFVLQNMIILINEAQVTRTSTIDDYFTQVENNENLWRLKNDCCSKILFKSNVVMNNGYNNQIKFVFEYKSVDANFNNQDSLQDPQAKYTLDKYSSEEILPSFEPVYSWSSAATKSSKNTNNHLEKNNRATHRVSSKNSEVHEADVSRNPNTFTLKLQYPIFSLLNMRLRNISLKSEHCILSSLDFQTSKASEQLTKKFIYPQEHNSFLKLNFQEISYKLIDGTSQIELDPICPLKVPLTAFSYDSISATFKLVLLPKSTQPHRVKITLAYELELHPNLKLPVRTSWETEVTLKRSMPISSTSSQYSSNNNNTNHSASFNGAANNVNSGGLANLRLGGVSSSRFSLGAASTTSLVNSKLSNVKFKFINSNIKVIKGEKFTMRLQIINSSSSPLDLVVYYNNTINPIPSANNVRNSNGINNCGMNNGTIPNSPLTLENQYQLHNKYRKIAEGIILLSNDYKIPVVPPRETYFADLRFIGIMSGYYGTLSGLKVLDLNTNELIEVGNGASVLIQ | |
| 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 |
|---|---|---|---|---|---|
| 129 | Phosphorylation | ANFNNQDSLQDPQAK CCCCCCCCCCCHHHC | 20.40 | 25752575 | |
| 179 | Phosphorylation | LEKNNRATHRVSSKN HHHCHHHHHCCCCCC | 13.64 | 24961812 | |
| 183 | Phosphorylation | NRATHRVSSKNSEVH HHHHHCCCCCCCEEE | 35.24 | 28889911 | |
| 184 | Phosphorylation | RATHRVSSKNSEVHE HHHHCCCCCCCEEEE | 32.76 | 23749301 | |
| 187 | Phosphorylation | HRVSSKNSEVHEADV HCCCCCCCEEEECHH | 44.74 | 28889911 | |
| 221 | Phosphorylation | NMRLRNISLKSEHCI HHHHHCCCCCCCCEE | 33.04 | 15665377 | |
| 240 | Phosphorylation | DFQTSKASEQLTKKF CCCCCHHHHHHHHHH | 29.61 | 28889911 | |
| 348 | Phosphorylation | LKRSMPISSTSSQYS EEEECCCCCCCCCCC | 22.99 | 21440633 | |
| 355 | Phosphorylation | SSTSSQYSSNNNNTN CCCCCCCCCCCCCCC | 20.96 | 21440633 | |
| 388 | Phosphorylation | NLRLGGVSSSRFSLG CCEECCCCCCCEECC | 26.35 | 23749301 | |
| 390 | Phosphorylation | RLGGVSSSRFSLGAA EECCCCCCCEECCCC | 29.82 | 25752575 | |
| 393 | Phosphorylation | GVSSSRFSLGAASTT CCCCCCEECCCCCCH | 25.45 | 22890988 | |
| 398 | Phosphorylation | RFSLGAASTTSLVNS CEECCCCCCHHHHCC | 31.51 | 22369663 | |
| 399 | Phosphorylation | FSLGAASTTSLVNSK EECCCCCCHHHHCCC | 18.71 | 22369663 | |
| 400 | Phosphorylation | SLGAASTTSLVNSKL ECCCCCCHHHHCCCC | 19.98 | 22369663 | |
| 401 | Phosphorylation | LGAASTTSLVNSKLS CCCCCCHHHHCCCCC | 30.34 | 22369663 | |
| 405 | Phosphorylation | STTSLVNSKLSNVKF CCHHHHCCCCCCCEE | 27.74 | 22890988 | |
| 413 | Acetylation | KLSNVKFKFINSNIK CCCCCEEEEECCCEE | 39.35 | 24489116 | |
| 479 | Phosphorylation | NNGTIPNSPLTLENQ CCCCCCCCCCCCCHH | 18.87 | 23749301 |
| 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 TRS65_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TRS65_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 TRS65_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-393; SER-398 ANDSER-401, AND MASS SPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221 AND SER-398, ANDMASS SPECTROMETRY. | |
