Gene name
SLCO1B3 (LST2,OATP1B3,OATP8,SLC21A8)
Experiment(s)
For this entry:
SO1B3_HUMAN (SLCO1B3)
Species | Homo sapiens |
---|---|
Localization | Basolateral plasma membrane |
Reference |
König J,Cui Y,Nies AT,Keppler D (2000) Localization and genomic organization of a new hepatocellular organic anion transporting polypeptide., J Biol Chem, 275, 23161-8. [PubMed] [DOI] |
Evidence level | Antibody staining |
Organ | Kidney |
Cell | MDCK cells (distal tubule) |
Notes |
SO1B3_HUMAN (SLCO1B3)
Species | Homo sapiens |
---|---|
Localization | Basolateral plasma membrane |
Reference |
König J,Cui Y,Nies AT,Keppler D (2000) Localization and genomic organization of a new hepatocellular organic anion transporting polypeptide., J Biol Chem, 275, 23161-8. [PubMed] [DOI] |
Evidence level | Antibody staining |
Organ | Liver |
Cell | Hepatocytes |
Notes |
SO1B3_HUMAN (SLCO1B3)
Species | Homo sapiens |
---|---|
Localization | Basolateral plasma membrane |
Reference |
König J,Cui Y,Nies AT,Keppler D (2000) Localization and genomic organization of a new hepatocellular organic anion transporting polypeptide., J Biol Chem, 275, 23161-8. [PubMed] [DOI] |
Evidence level | Antibody staining |
Organ | Liver |
Cell | Hepatocytes |
Notes |
For ortholog entries:
Alignment and sequence features
Loading data
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 | 26 | Cytoplasmic |
27 | 48 | Membrane |
49 | 64 | Extracellular |
65 | 86 | Membrane |
87 | 95 | Cytoplasmic |
96 | 117 | Membrane |
118 | 171 | Extracellular |
172 | 193 | Membrane |
194 | 206 | Cytoplasmic |
207 | 230 | Membrane |
231 | 254 | Extracellular |
255 | 278 | Membrane |
279 | 336 | Cytoplasmic |
337 | 358 | Membrane |
359 | 375 | Extracellular |
376 | 397 | Membrane |
398 | 406 | Cytoplasmic |
407 | 428 | Membrane |
429 | 536 | Extracellular |
537 | 559 | Membrane |
560 | 572 | Cytoplasmic |
573 | 594 | Membrane |
595 | 624 | Extracellular |
625 | 647 | Membrane |
648 | 702 | Cytoplasmic |
Phosphorylation
Glycosylation
Position | Site resource | Glycan resource | PubMed link(s) |
---|---|---|---|
134 | N-GlycoSiteAtlas | 24495048 | |
145 | N-GlycoSiteAtlas | 24495048 | |
151 | N-GlycoSiteAtlas | 24495048 | |
445 | N-GlycoSiteAtlas | 24495048 | |
503 | N-GlycoSiteAtlas | 24495048 | |
516 | N-GlycoSiteAtlas | 24495048 |
Family and domain data
Database | Domain/Family name |
---|---|
InterPro | Kazal_dom |
InterPro | Kazal_dom_sf |
InterPro | MFS_dom |
InterPro | MFS_trans_sf |
InterPro | OATP |
Pfam | Kazal_2 |
Pfam | OATP |