| UniProt ID | MEP2_YEAST | |
|---|---|---|
| UniProt AC | P41948 | |
| Protein Name | Ammonium transporter MEP2 | |
| Gene Name | MEP2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 499 | |
| Subcellular Localization |
Membrane Multi-pass membrane protein. |
|
| Protein Description | Transporter for ammonium (both charged and uncharged NH3 and NH4) to use as a nitrogen source. The affinity of MEP2 is about twenty times higher than that of MEP1. MEP3 has the lowest affinity. Under ammonium limitation acts as an ammonium sensor, generating a signal that leads to pseudohyphal growth.. | |
| Protein Sequence | MSYNFTGTPTGEGTGGNSLTTDLNTQFDLANMGWIGVASAGVWIMVPGIGLLYSGLSRKKHALSLLWASMMASAVCIFQWFFWGYSLAFSHNTRGNGFIGTLEFFGFRNVLGAPSSVSSLPDILFAVYQGMFAAVTGALMLGGACERARLFPMMVFLFLWMTIVYCPIACWVWNAEGWLVKLGSLDYAGGLCVHLTSGHGGLVYALILGKRNDPVTRKGMPKYKPHSVTSVVLGTVFLWFGWMFFNGGSAGNATIRAWYSIMSTNLAAACGGLTWMVIDYFRCGRKWTTVGLCSGIIAGLVGITPAAGFVPIWSAVVIGVVTGAGCNLAVDLKSLLRIDDGLDCYSIHGVGGCIGSVLTGIFAADYVNATAGSYISPIDGGWINHHYKQVGYQLAGICAALAWTVTVTSILLLTMNAIPFLKLRLSADEEELGTDAAQIGEFTYEESTAYIPEPIRSKTSAQMPPPHENIDDKIVGNTDAEKNSTPSDASSTKNTDHIV | |
| 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 |
|---|---|---|---|---|---|
| 4 | N-linked_Glycosylation | ----MSYNFTGTPTG ----CCCCCCCCCCC | 22.24 | 11069679 | |
| 422 | Ubiquitination | MNAIPFLKLRLSADE HCHHCHHHHHCCCCH | 31.75 | 17644757 | |
| 426 | Phosphorylation | PFLKLRLSADEEELG CHHHHHCCCCHHHHC | 27.52 | 28889911 | |
| 448 | Phosphorylation | EFTYEESTAYIPEPI CCEECCCCEECCCCC | 27.10 | 28889911 | |
| 457 | Phosphorylation | YIPEPIRSKTSAQMP ECCCCCCCCCCCCCC | 40.79 | 28747907 | |
| 458 | Ubiquitination | IPEPIRSKTSAQMPP CCCCCCCCCCCCCCC | 36.33 | 17644757 | |
| 459 | Phosphorylation | PEPIRSKTSAQMPPP CCCCCCCCCCCCCCC | 30.46 | 27821475 | |
| 460 | Phosphorylation | EPIRSKTSAQMPPPH CCCCCCCCCCCCCCC | 21.90 | 27821475 | |
| 473 | Ubiquitination | PHENIDDKIVGNTDA CCCCCCCCCCCCCCH | 35.23 | 17644757 | |
| 478 | Phosphorylation | DDKIVGNTDAEKNST CCCCCCCCCHHCCCC | 30.56 | 27214570 | |
| 482 | Ubiquitination | VGNTDAEKNSTPSDA CCCCCHHCCCCCCCC | 58.90 | 23749301 | |
| 484 | Phosphorylation | NTDAEKNSTPSDASS CCCHHCCCCCCCCCC | 53.41 | 27214570 | |
| 485 | Phosphorylation | TDAEKNSTPSDASST CCHHCCCCCCCCCCC | 35.88 | 28152593 | |
| 487 | Phosphorylation | AEKNSTPSDASSTKN HHCCCCCCCCCCCCC | 45.99 | 28152593 | |
| 490 | Phosphorylation | NSTPSDASSTKNTDH CCCCCCCCCCCCCCC | 43.46 | 28152593 | |
| 491 | Phosphorylation | STPSDASSTKNTDHI CCCCCCCCCCCCCCC | 45.16 | 25005228 | |
| 492 | Phosphorylation | TPSDASSTKNTDHIV CCCCCCCCCCCCCCC | 26.31 | 25005228 | |
| 493 | Ubiquitination | PSDASSTKNTDHIV- CCCCCCCCCCCCCC- | 60.85 | 17644757 | |
| 495 | Phosphorylation | DASSTKNTDHIV--- CCCCCCCCCCCC--- | 30.43 | 27214570 |
| 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 MEP2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MEP2_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 MEP2_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| N-linked Glycosylation | |
| Reference | PubMed |
| "In vivo N-glycosylation of the mep2 high-affinity ammoniumtransporter of Saccharomyces cerevisiae reveals an extracytosolic N-terminus."; Marini A.-M., Andre B.; Mol. Microbiol. 38:552-564(2000). Cited for: FUNCTION, TOPOLOGY, MUTAGENESIS OF ASN-4; ASN-252; ASN-368 ANDASN-483, AND GLYCOSYLATION AT ASN-4. | |