| UniProt ID | GTR1_MOUSE | |
|---|---|---|
| UniProt AC | P17809 | |
| Protein Name | Solute carrier family 2, facilitated glucose transporter member 1 | |
| Gene Name | Slc2a1 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 492 | |
| Subcellular Localization |
Cell membrane Multi-pass membrane protein . Melanosome. Localizes primarily at the cell surface.. |
|
| Protein Description | Facilitative glucose transporter. This isoform may be responsible for constitutive or basal glucose uptake. Has a very broad substrate specificity; can transport a wide range of aldoses including both pentoses and hexoses.. | |
| Protein Sequence | MDPSSKKVTGRLMLAVGGAVLGSLQFGYNTGVINAPQKVIEEFYNQTWNHRYGEPIPSTTLTTLWSLSVAIFSVGGMIGSFSVGLFVNRFGRRNSMLMMNLLAFVAAVLMGFSKLGKSFEMLILGRFIIGVYCGLTTGFVPMYVGEVSPTALRGALGTLHQLGIVVGILIAQVFGLDSIMGNADLWPLLLSVIFIPALLQCILLPFCPESPRFLLINRNEENRAKSVLKKLRGTADVTRDLQEMKEEGRQMMREKKVTILELFRSPAYRQPILIAVVLQLSQQLSGINAVFYYSTSIFEKAGVQQPVYATIGSGIVNTAFTVVSLFVVERAGRRTLHLIGLAGMAGCAVLMTIALALLERLPWMSYLSIVAIFGFVAFFEVGPGPIPWFIVAELFSQGPRPAAIAVAGFSNWTSNFIVGMCFQYVEQLCGPYVFIIFTVLLVLFFIFTYFKVPETKGRTFDEIASGFRQGGASQSDKTPEELFHPLGADSQV | |
| 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 |
|---|---|---|---|---|---|
| 1 | Acetylation | -------MDPSSKKV -------CCHHHHHC | 18.04 | - | |
| 45 | N-linked_Glycosylation | KVIEEFYNQTWNHRY HHHHHHHHHCCCCCC | 37.82 | 19656770 | |
| 49 | N-linked_Glycosylation | EFYNQTWNHRYGEPI HHHHHCCCCCCCCCC | 17.10 | 19656770 | |
| 113 | Phosphorylation | AAVLMGFSKLGKSFE HHHHHCHHHHCHHHH | 22.65 | 28059163 | |
| 226 | Phosphorylation | NEENRAKSVLKKLRG CHHHHHHHHHHHHHC | 31.53 | 24453211 | |
| 234 | Phosphorylation | VLKKLRGTADVTRDL HHHHHHCCCHHHHHH | 17.16 | 19144319 | |
| 241 | Ubiquitination | TADVTRDLQEMKEEG CCHHHHHHHHHHHHH | 4.13 | 27667366 | |
| 245 | Ubiquitination | TRDLQEMKEEGRQMM HHHHHHHHHHHHHHH | 52.43 | 22790023 | |
| 465 | Phosphorylation | RTFDEIASGFRQGGA CCHHHHHHHHHCCCC | 44.09 | 22006019 | |
| 473 | Phosphorylation | GFRQGGASQSDKTPE HHHCCCCCCCCCCHH | 33.23 | 26239621 | |
| 475 | Phosphorylation | RQGGASQSDKTPEEL HCCCCCCCCCCHHHH | 38.28 | 26239621 | |
| 477 | Ubiquitination | GGASQSDKTPEELFH CCCCCCCCCHHHHCC | 71.83 | 22790023 | |
| 478 | Phosphorylation | GASQSDKTPEELFHP CCCCCCCCHHHHCCC | 40.71 | 22942356 | |
| 490 | Phosphorylation | FHPLGADSQV----- CCCCCCCCCC----- | 32.10 | 28978645 |
| 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 GTR1_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference |
|---|---|---|---|---|
| 226 | S | Phosphorylation |
| - |
* 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 GTR1_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of GTR1_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| N-linked Glycosylation | |
| Reference | PubMed |
| "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."; Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.; Nat. Biotechnol. 27:378-386(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-45 AND ASN-49, AND MASSSPECTROMETRY. | |
| "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-45 AND ASN-49, AND MASSSPECTROMETRY. | |
| Phosphorylation | |
| Reference | PubMed |
| "The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-234, AND MASSSPECTROMETRY. | |