UniProt ID | AGP1_YEAST | |
---|---|---|
UniProt AC | P25376 | |
Protein Name | General amino acid permease AGP1 | |
Gene Name | AGP1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 633 | |
Subcellular Localization |
Cell membrane Multi-pass membrane protein. |
|
Protein Description | Broad substrate range permease which transports asparagine and glutamine with intermediate specificity. Also transports Ala, Cys, Gly, Ile, Leu, Met, Phe, Ser, Thr, Tyr and Val. Important for the utilization of amino acids as a nitrogen source.. | |
Protein Sequence | MSSSKSLYELKDLKNSSTEIHATGQDNEIEYFETGSNDRPSSQPHLGYEQHNTSAVRRFFDSFKRADQGPQDEVEATQMNDLTSAISPSSRQAQELEKNESSDNIGANTGHKSDSLKKTIQPRHVLMIALGTGIGTGLLVGNGTALVHAGPAGLLIGYAIMGSILYCIIQACGEMALVYSNLTGGYNAYPSFLVDDGFGFAVAWVYCLQWLCVCPLELVTASMTIKYWTTSVNPDVFVIIFYVLVITINIFGARGYAEAEFFFNCCKILMMTGFFILGIIIDVGGAGNDGFIGGKYWHDPGAFNGKHAIDRFKGVAATLVTAAFAFGGSEFIAITTAEQSNPRKAIPGAAKQMIYRILFLFLATIILLGFLVPYNSDQLLGSTGGGTKASPYVIAVASHGVRVVPHFINAVILLSVLSMANSSFYSSARLFLTLSEQGYAPKVFSYIDRAGRPLIAMGVSALFAVIAFCAASPKEEQVFTWLLAISGLSQLFTWTAICLSHLRFRRAMKVQGRSLGELGFKSQTGVWGSAYACIMMILILIAQFWVAIAPIGEGKLDAQAFFENYLAMPILIALYVGYKVWHKDWKLFIRADKIDLDSHRQIFDEELIKQEDEEYRERLRNGPYWKRVVAFWC | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSSSKSLYE ------CCCCCCHHH | 43.23 | 22369663 | |
3 | Phosphorylation | -----MSSSKSLYEL -----CCCCCCHHHH | 40.25 | 22369663 | |
4 | Phosphorylation | ----MSSSKSLYELK ----CCCCCCHHHHH | 20.96 | 22369663 | |
6 | Phosphorylation | --MSSSKSLYELKDL --CCCCCCHHHHHHH | 37.82 | 22369663 | |
8 | Phosphorylation | MSSSKSLYELKDLKN CCCCCCHHHHHHHHC | 26.72 | 22369663 | |
11 | Acetylation | SKSLYELKDLKNSST CCCHHHHHHHHCCCC | 49.42 | 24489116 | |
11 | Ubiquitination | SKSLYELKDLKNSST CCCHHHHHHHHCCCC | 49.42 | 23749301 | |
14 | Ubiquitination | LYELKDLKNSSTEIH HHHHHHHHCCCCEEE | 65.99 | 22817900 | |
16 | Phosphorylation | ELKDLKNSSTEIHAT HHHHHHCCCCEEEEC | 36.73 | 27017623 | |
17 | Phosphorylation | LKDLKNSSTEIHATG HHHHHCCCCEEEECC | 39.18 | 27017623 | |
77 | Phosphorylation | PQDEVEATQMNDLTS CHHHHHHHHHHHHHH | 18.16 | 22369663 | |
83 | Phosphorylation | ATQMNDLTSAISPSS HHHHHHHHHHCCCCH | 20.98 | 22369663 | |
84 | Phosphorylation | TQMNDLTSAISPSSR HHHHHHHHHCCCCHH | 30.79 | 22369663 | |
87 | Phosphorylation | NDLTSAISPSSRQAQ HHHHHHCCCCHHHHH | 20.60 | 22369663 | |
89 | Phosphorylation | LTSAISPSSRQAQEL HHHHCCCCHHHHHHH | 31.21 | 20377248 | |
90 | Phosphorylation | TSAISPSSRQAQELE HHHCCCCHHHHHHHH | 31.62 | 22369663 | |
98 | Ubiquitination | RQAQELEKNESSDNI HHHHHHHHCCCCCCC | 77.85 | 23749301 | |
101 | Phosphorylation | QELEKNESSDNIGAN HHHHHCCCCCCCCCC | 53.00 | 22369663 | |
102 | Phosphorylation | ELEKNESSDNIGANT HHHHCCCCCCCCCCC | 28.62 | 22369663 | |
109 | Phosphorylation | SDNIGANTGHKSDSL CCCCCCCCCCCCHHH | 39.88 | 22890988 | |
112 | Ubiquitination | IGANTGHKSDSLKKT CCCCCCCCCHHHHHH | 58.25 | 24961812 | |
113 | Phosphorylation | GANTGHKSDSLKKTI CCCCCCCCHHHHHHC | 27.10 | 22369663 | |
115 | Phosphorylation | NTGHKSDSLKKTIQP CCCCCCHHHHHHCCH | 49.53 | 22369663 | |
633 | S-palmitoylation | KRVVAFWC------- HHEEEEEC------- | 3.02 | - |
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 AGP1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of AGP1_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 AGP1_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-87, AND MASSSPECTROMETRY. |