| UniProt ID | EAA1_MOUSE | |
|---|---|---|
| UniProt AC | P56564 | |
| Protein Name | Excitatory amino acid transporter 1 | |
| Gene Name | Slc1a3 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 543 | |
| Subcellular Localization |
Cell membrane Multi-pass membrane protein . |
|
| Protein Description | Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate. [PubMed: 7903437] | |
| Protein Sequence | MTKSNGEEPRMGGRMERLQQGVRKRTLLAKKKVQSLTKEDVKSYLFRNAFVLLTVTAVIVGTILGFALRPYKMSYREVKYFSFPGELLMRMLQMLVLPLIISSLVTGMAALDSKASGKMGMRAVVYYMTTTIIAVVIGIIIVIIIHPGKGTKENMYREGKIVQVTAADAFLDLIRNMFPPNLVEACFKQFKTSYEKRSFKVPIQSNETLLGAVINNVSEAMETLTRIREEMVPVPGSVNGVNALGLVVFSMCFGFVIGNMKEQGQALREFFDSLNEAIMRLVAVIMWYAPLGILFLIAGKIVEMEDMGVIGGQLAMYTVTVIVGLLIHAVIVLPLLYFLVTRKNPWVFIGGLLQALITALGTSSSSATLPITFKCLEENNGVDKRITRFVLPVGATINMDGTALYEALAAIFIAQVNNFDLNFGQIITISITATAASIGAAGIPQAGLVTMVIVLTSVGLPTDDITLIIAVDWFLDRLRTTTNVLGDSLGAGIVEHLSRHELKNRDVEMGNSVIEENEMKKPYQLIAQDNEPEKPVADSETKM | |
| 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 |
|---|---|---|---|---|---|
| 3 | Acetylation | -----MTKSNGEEPR -----CCCCCCCCCC | 40.40 | 19857865 | |
| 4 | Phosphorylation | ----MTKSNGEEPRM ----CCCCCCCCCCC | 40.68 | 25521595 | |
| 26 | Phosphorylation | QQGVRKRTLLAKKKV HHHHHHHHHHHHHHH | 29.20 | 29899451 | |
| 35 | Phosphorylation | LAKKKVQSLTKEDVK HHHHHHHHCCHHHHH | 40.78 | 22817900 | |
| 42 | Ubiquitination | SLTKEDVKSYLFRNA HCCHHHHHHHHHHHH | 45.78 | 22790023 | |
| 206 | N-linked_Glycosylation | FKVPIQSNETLLGAV EECCCCCCCHHHHHH | 29.87 | 19656770 | |
| 215 | N-linked_Glycosylation | TLLGAVINNVSEAME HHHHHHHHCHHHHHH | 35.93 | 19656770 | |
| 216 | N-linked_Glycosylation | LLGAVINNVSEAMET HHHHHHHCHHHHHHH | 27.80 | 19656770 | |
| 384 | Ubiquitination | EENNGVDKRITRFVL HHCCCCCCCEEEEEE | 43.20 | 22790023 | |
| 503 | Ubiquitination | HLSRHELKNRDVEMG HHHHHHHHCCCCCCC | 47.13 | 22790023 | |
| 512 | Phosphorylation | RDVEMGNSVIEENEM CCCCCCCCHHCCCCC | 20.81 | 25521595 | |
| 520 | Ubiquitination | VIEENEMKKPYQLIA HHCCCCCCCCEEEEC | 44.40 | 22790023 | |
| 521 | Ubiquitination | IEENEMKKPYQLIAQ HCCCCCCCCEEEECC | 47.88 | 22790023 | |
| 523 | Phosphorylation | ENEMKKPYQLIAQDN CCCCCCCEEEECCCC | 25.49 | 29550500 | |
| 534 | Ubiquitination | AQDNEPEKPVADSET CCCCCCCCCCCCCCC | 56.35 | 22790023 | |
| 539 | Phosphorylation | PEKPVADSETKM--- CCCCCCCCCCCC--- | 37.11 | 25521595 | |
| 541 | Phosphorylation | KPVADSETKM----- CCCCCCCCCC----- | 36.04 | 29899451 | |
| 542 | Ubiquitination | PVADSETKM------ CCCCCCCCC------ | 38.26 | 22790023 |
| 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 EAA1_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of EAA1_MOUSE !! | ||||||
* 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 EAA1_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| SEPT4_MOUSE | Sept4 | physical | 14723703 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| N-linked Glycosylation | |
| Reference | PubMed |
| "The mouse C2C12 myoblast cell surface N-linked glycoproteome:identification, glycosite occupancy, and membrane orientation."; Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,Wollscheid B.; Mol. Cell. Proteomics 8:2555-2569(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-206; ASN-215 AND ASN-216,AND MASS SPECTROMETRY. | |
| Phosphorylation | |
| Reference | PubMed |
| "Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, AND MASSSPECTROMETRY. | |