Gene name
SLC2A9 (Glut9)
Experiment(s)
For this entry:
GTR9_HUMAN (SLC2A9)
| Species | Homo sapiens |
|---|---|
| Localization | Basolateral plasma membrane |
| Reference |
Bibee KP,Augustin R,Gazit V,Moley KH (2013) The apical sorting signal for human GLUT9b resides in the N-terminus., Mol Cell Biochem, 376, 163-73. [PubMed] [DOI] |
| Evidence level | Antibody staining |
| Organ | Kidney |
| Cell | MDCK cells (distal tubule) |
| Notes | The shorter isoform carries a unique apical determinant (MKLSKKDRGEDEESDSAKKKL) on its N-terminus |
GTR9_HUMAN (SLC2A9)
| Species | Homo sapiens |
|---|---|
| Localization | Basolateral plasma membrane |
| Reference |
Uehara I,Kimura T,Tanigaki S,Fukutomi T,Sakai K,Shinohara Y,Ichida K,Iwashita M,Sakurai H (2014) Paracellular route is the major urate transport pathway across the blood-placental barrier., Physiol Rep, 2, . [PubMed] [DOI] |
| Evidence level | Antibody staining |
| Organ | Placenta |
| Cell | Trophoblast cells |
| Notes | The short isoform is apical in the same tissue |
For ortholog entries:
Alignment and sequence features
Wheel: zoom in/out; drag: scroll left/right. Sequences and features are drawn in three lines. Bottom line: topology (red bar: cytoplasmic region; yellow bar: transmembrane region; transmembrane re-entrant loop; blue bar: extracellular region; black bar: signal peptide). Middle line: amino acid sequence (grey bar or one letter code). Top line: post translational modifications (Y: N-glycosylation site; Y: O-glycosylation site;P: phosphorylation site), intrinsically disordered regions (light green bar: IDR) and short linear motifs (light steel blue bar: ELM region).
CCTOP topology prediction
| Start | End | Localisation |
|---|---|---|
| 1 | 58 | Cytoplasmic |
| 59 | 80 | Membrane |
| 81 | 110 | Extracellular |
| 111 | 132 | Membrane |
| 133 | 138 | Cytoplasmic |
| 139 | 158 | Membrane |
| 159 | 165 | Extracellular |
| 166 | 186 | Membrane |
| 187 | 200 | Cytoplasmic |
| 201 | 219 | Membrane |
| 220 | 232 | Extracellular |
| 233 | 252 | Membrane |
| 253 | 317 | Cytoplasmic |
| 318 | 337 | Membrane |
| 338 | 353 | Extracellular |
| 354 | 375 | Membrane |
| 376 | 382 | Cytoplasmic |
| 383 | 401 | Membrane |
| 402 | 414 | Extracellular |
| 415 | 436 | Membrane |
| 437 | 451 | Cytoplasmic |
| 452 | 473 | Membrane |
| 474 | 479 | Extracellular |
| 480 | 499 | Membrane |
| 500 | 540 | Cytoplasmic |
Phosphorylation
Glycosylation
| Position | Site resource | Glycan resource | PubMed link(s) |
|---|---|---|---|
| 90 | N-GlycoSiteAtlas | 24495048 , 26571101 | |
| 90 | PolarProtDb | 31844046 |
Family and domain data
| Database | Domain/Family name |
|---|---|
| InterPro | MFS_dom |
| InterPro | MFS_sugar_transport-like |
| InterPro | MFS_trans_sf |
| InterPro | Sugar/inositol_transpt |
| InterPro | Sugar_transporter_CS |
| Pfam | Sugar_tr |