UniProt ID | HXT6_YEAST | |
---|---|---|
UniProt AC | P39003 | |
Protein Name | High-affinity hexose transporter HXT6 | |
Gene Name | HXT6 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 570 | |
Subcellular Localization |
Membrane Multi-pass membrane protein. |
|
Protein Description | High-affinity glucose transporter.. | |
Protein Sequence | MSQDAAIAEQTPVEHLSAVDSASHSVLSTPSNKAERDEIKAYGEGEEHEPVVEIPKRPASAYVTVSIMCIMIAFGGFVFGWDTGTISGFINQTDFIRRFGMKHKDGTNYLSKVRTGLIVSIFNIGCAIGGIILSKLGDMYGRKVGLIVVVVIYIIGIIIQIASINKWYQYFIGRIISGLGVGGIAVLSPMLISEVSPKHLRGTLVSCYQLMITAGIFLGYCTNFGTKNYSNSVQWRVPLGLCFAWALFMIGGMTFVPESPRYLAEVGKIEEAKRSIAVSNKVAVDDPSVLAEVEAVLAGVEAEKLAGNASWGELFSSKTKVLQRLIMGAMIQSLQQLTGDNYFFYYGTTIFKAVGLSDSFETSIVLGIVNFASTFVGIYVVERYGRRTCLLWGAASMTACMVVYASVGVTRLWPNGQDQPSSKGAGNCMIVFACFYIFCFATTWAPIPYVVVSETFPLRVKSKAMSIATAANWLWGFLIGFFTPFITGAINFYYGYVFMGCLVFMFFYVLLVVPETKGLTLEEVNTMWEEGVLPWKSASWVPPSRRGANYDAEEMAHDDKPLYKRMFSTK | |
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 | ------MSQDAAIAE ------CCHHHHHHH | 36.45 | 22369663 | |
11 | Phosphorylation | DAAIAEQTPVEHLSA HHHHHHCCCHHHHHH | 22.32 | 22369663 | |
17 | Phosphorylation | QTPVEHLSAVDSASH CCCHHHHHHHCCCCC | 28.31 | 22369663 | |
21 | Phosphorylation | EHLSAVDSASHSVLS HHHHHHCCCCCCCCC | 25.68 | 22369663 | |
23 | Phosphorylation | LSAVDSASHSVLSTP HHHHCCCCCCCCCCC | 21.90 | 22369663 | |
25 | Phosphorylation | AVDSASHSVLSTPSN HHCCCCCCCCCCCCC | 23.43 | 22369663 | |
28 | Phosphorylation | SASHSVLSTPSNKAE CCCCCCCCCCCCHHH | 35.80 | 22369663 | |
29 | Phosphorylation | ASHSVLSTPSNKAER CCCCCCCCCCCHHHH | 26.95 | 22369663 | |
31 | Phosphorylation | HSVLSTPSNKAERDE CCCCCCCCCHHHHHH | 51.56 | 22369663 | |
33 | Ubiquitination | VLSTPSNKAERDEIK CCCCCCCHHHHHHHH | 56.83 | 24961812 | |
40 | Ubiquitination | KAERDEIKAYGEGEE HHHHHHHHHCCCCCC | 33.24 | 23749301 | |
91 | N-linked_Glycosylation | GTISGFINQTDFIRR CCHHHHCCHHHHHHH | 36.12 | - | |
177 | Phosphorylation | YFIGRIISGLGVGGI HHHHHHHCCCCCCHH | 26.12 | 23749301 | |
193 | Phosphorylation | VLSPMLISEVSPKHL HHCCHHHCCCCHHHH | 28.16 | 23749301 | |
198 | Ubiquitination | LISEVSPKHLRGTLV HHCCCCHHHHHHHHH | 48.00 | 23749301 | |
228 | N-linked_Glycosylation | CTNFGTKNYSNSVQW HCCCCCCCCCCCCCC | 45.35 | - | |
229 | Phosphorylation | TNFGTKNYSNSVQWR CCCCCCCCCCCCCCC | 15.70 | 28889911 | |
268 | Ubiquitination | RYLAEVGKIEEAKRS HHHHHHCCHHHHHHH | 52.71 | 23749301 | |
268 | 2-Hydroxyisobutyrylation | RYLAEVGKIEEAKRS HHHHHHCCHHHHHHH | 52.71 | - | |
273 | 2-Hydroxyisobutyrylation | VGKIEEAKRSIAVSN HCCHHHHHHHHEECC | 50.38 | - | |
288 | Phosphorylation | KVAVDDPSVLAEVEA CEECCCHHHHHHHHH | 36.44 | 21440633 | |
318 | Ubiquitination | WGELFSSKTKVLQRL HHHHHCCHHHHHHHH | 51.68 | 12872131 | |
320 | 2-Hydroxyisobutyrylation | ELFSSKTKVLQRLIM HHHCCHHHHHHHHHH | 44.69 | - | |
544 | Phosphorylation | SASWVPPSRRGANYD CCCCCCCCCCCCCCC | 28.65 | 19779198 | |
560 | Ubiquitination | EEMAHDDKPLYKRMF HHHCCCCCCHHHHHH | 42.87 | 12872131 | |
564 | Acetylation | HDDKPLYKRMFSTK- CCCCCHHHHHHCCC- | 45.10 | 24489116 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HXT6_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 HXT6_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Ubiquitylation | |
Reference | PubMed |
"A proteomics approach to understanding protein ubiquitination."; Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.; Nat. Biotechnol. 21:921-926(2003). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-560, AND MASSSPECTROMETRY. |