| UniProt ID | GTR3_HUMAN | |
|---|---|---|
| UniProt AC | P11169 | |
| Protein Name | Solute carrier family 2, facilitated glucose transporter member 3 | |
| Gene Name | SLC2A3 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 496 | |
| Subcellular Localization |
Cell membrane Multi-pass membrane protein . |
|
| Protein Description | Facilitative glucose transporter that can also mediate the uptake of various other monosaccharides across the cell membrane. [PubMed: 9477959] | |
| Protein Sequence | MGTQKVTPALIFAITVATIGSFQFGYNTGVINAPEKIIKEFINKTLTDKGNAPPSEVLLTSLWSLSVAIFSVGGMIGSFSVGLFVNRFGRRNSMLIVNLLAVTGGCFMGLCKVAKSVEMLILGRLVIGLFCGLCTGFVPMYIGEISPTALRGAFGTLNQLGIVVGILVAQIFGLEFILGSEELWPLLLGFTILPAILQSAALPFCPESPRFLLINRKEEENAKQILQRLWGTQDVSQDIQEMKDESARMSQEKQVTVLELFRVSSYRQPIIISIVLQLSQQLSGINAVFYYSTGIFKDAGVQEPIYATIGAGVVNTIFTVVSLFLVERAGRRTLHMIGLGGMAFCSTLMTVSLLLKDNYNGMSFVCIGAILVFVAFFEIGPGPIPWFIVAELFSQGPRPAAMAVAGCSNWTSNFLVGLLFPSAAHYLGAYVFIIFTGFLITFLAFTFFKVPETRGRTFEDITRAFEGQAHGADRSGKDGVMEMNSIEPAKETTTNV | |
| 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 |
|---|---|---|---|---|---|
| 43 | N-linked_Glycosylation | KIIKEFINKTLTDKG HHHHHHHHHHHCCCC | 36.26 | UniProtKB CARBOHYD | |
| 217 | Ubiquitination | RFLLINRKEEENAKQ CEEEEECCCHHHHHH | 66.06 | 21963094 | |
| 223 | Ubiquitination | RKEEENAKQILQRLW CCCHHHHHHHHHHHH | 49.83 | 21963094 | |
| 232 | Phosphorylation | ILQRLWGTQDVSQDI HHHHHHCCCCHHHHH | 15.26 | 19664994 | |
| 236 | Phosphorylation | LWGTQDVSQDIQEMK HHCCCCHHHHHHHHH | 30.35 | 20068231 | |
| 243 | Ubiquitination | SQDIQEMKDESARMS HHHHHHHHHHHHHHC | 58.55 | 21963094 | |
| 246 | Phosphorylation | IQEMKDESARMSQEK HHHHHHHHHHHCHHH | 31.17 | 21406692 | |
| 250 | Phosphorylation | KDESARMSQEKQVTV HHHHHHHCHHHCCHH | 29.63 | 21406692 | |
| 253 | Ubiquitination | SARMSQEKQVTVLEL HHHHCHHHCCHHHHH | 42.29 | 21963094 | |
| 333 | Phosphorylation | VERAGRRTLHMIGLG HHHHCCCEEEEECCC | 21.47 | - | |
| 352 | Phosphorylation | CSTLMTVSLLLKDNY HHHHHHHHHHHCCCC | 12.25 | - | |
| 475 | Phosphorylation | QAHGADRSGKDGVME CCCCCCCCCCCCCEE | 51.22 | 24114839 | |
| 477 | Ubiquitination | HGADRSGKDGVMEMN CCCCCCCCCCCEECC | 53.18 | 21963094 | |
| 485 | Phosphorylation | DGVMEMNSIEPAKET CCCEECCCCCCCCCC | 27.33 | 19664994 | |
| 490 | Ubiquitination | MNSIEPAKETTTNV- CCCCCCCCCCCCCC- | 67.33 | 21963094 | |
| 492 | Phosphorylation | SIEPAKETTTNV--- CCCCCCCCCCCC--- | 37.91 | 22210691 | |
| 493 | Phosphorylation | IEPAKETTTNV---- CCCCCCCCCCC---- | 19.91 | 28060719 | |
| 494 | Phosphorylation | EPAKETTTNV----- CCCCCCCCCC----- | 41.21 | 28060719 |
| 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 GTR3_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GTR3_HUMAN !! | ||||||
* 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 GTR3_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of GTR3_HUMAN !! | ||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-485, AND MASSSPECTROMETRY. | |