UniProt ID | TRS31_YEAST | |
---|---|---|
UniProt AC | Q03337 | |
Protein Name | Trafficking protein particle complex subunit 31 | |
Gene Name | TRS31 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 283 | |
Subcellular Localization | Golgi apparatus, cis-Golgi network. Endoplasmic reticulum. Preautophagosomal structure. | |
Protein Description | Component of the TRAPP I, TRAPP II and TRAPP III complexes which act as guanine nucleotide exchange factors (GEF) for YPT1. TRAPP I plays a key role in the late stages of endoplasmic reticulum to Golgi traffic. TRAPP II plays a role in intra-Golgi transport. TRAPP III plays a role in autophagosome formation.. | |
Protein Sequence | MSQRIIQPSASDQQFPGKSDGYEYTVGPKQAITSEASTTYIPSRIYSESLLFKRQEASLSAMAFLFQEMISQLHRTCKTAGDFETKLSDYGHNIGIRLLELLNFRASVSPSSLPRASAFLSQNESSSKLSNASNSPGMLANSSTATSASANERLQEKQTESLSNYITKMRRRDLKILDILQFIHGTLWSYLFNHVSDDLVKSSERDNEYMIVDNFPTLTQFIPGENVSCEYFVCGIIKGFLFNAGFPCGVTAHRMPQGGHSQRTVYLIQFDRQVLDREGLRFG | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
9 | Phosphorylation | SQRIIQPSASDQQFP CCCCCCCCCCCCCCC | 24.83 | 24961812 | |
11 | Phosphorylation | RIIQPSASDQQFPGK CCCCCCCCCCCCCCC | 40.05 | 24961812 | |
86 | Acetylation | TAGDFETKLSDYGHN CCCCHHHHHHHHCCH | 38.50 | 24489116 | |
109 | Phosphorylation | LNFRASVSPSSLPRA HCCCCCCCHHHCHHH | 19.30 | 21082442 | |
111 | Phosphorylation | FRASVSPSSLPRASA CCCCCCHHHCHHHHH | 36.68 | 30377154 | |
117 | Phosphorylation | PSSLPRASAFLSQNE HHHCHHHHHHHCCCC | 22.34 | 23749301 | |
121 | Phosphorylation | PRASAFLSQNESSSK HHHHHHHCCCCCCHH | 25.22 | 30377154 | |
125 | Phosphorylation | AFLSQNESSSKLSNA HHHCCCCCCHHHCCC | 47.68 | 22369663 | |
126 | Phosphorylation | FLSQNESSSKLSNAS HHCCCCCCHHHCCCC | 25.88 | 22369663 | |
127 | Phosphorylation | LSQNESSSKLSNASN HCCCCCCHHHCCCCC | 47.06 | 22369663 | |
135 | Phosphorylation | KLSNASNSPGMLANS HHCCCCCCCCCCCCC | 21.97 | 25752575 | |
143 | Phosphorylation | PGMLANSSTATSASA CCCCCCCHHCCCCHH | 23.13 | 19779198 | |
144 | Phosphorylation | GMLANSSTATSASAN CCCCCCHHCCCCHHH | 33.50 | 27017623 | |
149 | Phosphorylation | SSTATSASANERLQE CHHCCCCHHHHHHHH | 31.24 | 19779198 | |
157 | Acetylation | ANERLQEKQTESLSN HHHHHHHHHHHHHHH | 49.94 | 24489116 | |
157 | Ubiquitination | ANERLQEKQTESLSN HHHHHHHHHHHHHHH | 49.94 | 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 TRS31_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TRS31_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 TRS31_YEAST !! |
Kegg Drug | ||||||
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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-109; SER-125 ANDSER-126, AND MASS SPECTROMETRY. |