SLC10A6 encodes SOAT (sodium-dependent organic anion transporter), a 377-residue, N-glycosylated, multi-pass plasma membrane carrier belonging to the bile acid:sodium symporter (BASS/SLC10, TC 2.A.28) family, in which its closest relatives are the bile salt carriers ASBT (SLC10A2, 48% identity) and NTCP (SLC10A1) [PMID:17491011, PMID:34079822]. SOAT imports sulfoconjugated steroid hormones from the extracellular space into the cytosol, co-transporting the intact steroid sulfate with sodium ions down the inward sodium gradient and without hydrolysing the sulfate ester [PMID:17491011, PMID:23667501]. Characterized substrates are mono-sulfated steroids bearing the sulfate at the 3' or 17' position - dehydroepiandrosterone sulfate, estrone-3-sulfate and pregnenolone sulfate with low-micromolar Km values, plus 17beta-estradiol-3-sulfate, androstenediol-3-sulfate, androsterone and epiandrosterone sulfate, testosterone, epitestosterone and dihydrotestosterone 17-sulfates, 17alpha-hydroxypregnenolone sulfate and the placental estriol precursor 16alpha-hydroxy-DHEA sulfate; a second sulfate group abolishes recognition [PMID:17491011, PMID:23667501, PMID:28951227, PMID:24717977]. Despite the family name, the canonical bile acids (cholate, chenodeoxycholate, taurocholate, taurochenodeoxycholate, taurodeoxycholate) are not transported; the exceptions are taurolithocholate and its 3-sulfate, which lack 7'/12' hydroxylation and are taken up sodium-dependently [PMID:17491011, PMID:34079822]. Expression is highest in testis, where the protein is present in germ cells from zygotene spermatocytes to round spermatids, followed by placenta - where it occupies the apical membrane of syncytiotrophoblasts and the vessel endothelium - and pancreas, with lower levels in many hormone-responsive peripheral tissues [PMID:17491011, PMID:23667501, PMID:24717977]. Physiologically, SOAT is thought to deliver circulating, biologically inert steroid sulfates into specific target cells, where steroid sulfatase can reactivate them to free estrogens and androgens for intracrine signalling [PMID:23667501, PMID:37373074]. Loss of the mouse ortholog is nevertheless compatible with normal fertility and spermatogenesis and produces a peripheral lipid phenotype (raised serum cholesterol sulfate), indicating redundancy in the testis [PMID:28743544]. SOAT homo-oligomerizes and forms heterodimers with other SLC10 carriers including NTCP, without impairing NTCP transport [PMID:22029531, PMID:31256060]. Because SOAT-mediated estrone-3-sulfate uptake drives proliferation of hormone-dependent breast cancer cells, the transporter is of interest as an endocrine drug target [PMID:30186172, PMID:37373074].
Definition: Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: steroid sulfate(out) + Na(+)(out) = steroid sulfate(in) + Na(+)(in).
Justification: GO has no molecular-function term for sodium-coupled transport of steroid sulfate esters, which is the defining activity of SLC10A6/SOAT and of its rodent orthologs. Checked against OLS: the only existing term that GOA assigns to this gene is GO:0008508 bile acid:sodium symporter activity, whose definition is the bile acid/Na+ symport reaction and which is classified under GO:0015125 bile acid transmembrane transporter activity and GO:0015355 secondary active monocarboxylate transmembrane transporter activity - steroid sulfates are neither bile acids nor monocarboxylates. The generic alternative GO:0008514 organic anion transmembrane transporter activity is obsolete and was replaced by the uninformative GO:0022857 transmembrane transporter activity, and text searches of GO for 'steroid sulfate', 'estrone sulfate' and organosulfate transport return only sulfotransferase and sulfatase activities. The existing children of GO:0015370 solute:sodium symporter activity cover amino acids, sugars, nucleosides, bile acids, monocarboxylates, taurine, ascorbate, inositol, choline and inorganic ions, with no term for sulfate esters of steroids. The activity is directly demonstrated, with sodium dependence and kinetics, for the human protein, so it is not a speculative request. Candidate specific children, if wanted, would be estrone 3-sulfate:sodium symporter activity and dehydroepiandrosterone 3-sulfate:sodium symporter activity; a matching biological-process term (steroid sulfate import across plasma membrane) would also be useful, although GO:0043251 sodium-dependent organic anion transport is an adequate process term today.
Parent term: solute:sodium symporter activity
Supporting Evidence:
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput binary interaction screen (HuRI) reports an interaction between SLC10A6 and this partner [PMID:32296183]. The annotation records only the generic term protein binding and says nothing about what SLC10A6 does. Reason: GO:0005515 protein binding is uninformative: it records that a binding event was detected without identifying any molecular function of SLC10A6. The source is a systematic proteome-scale yeast two-hybrid map [PMID:32296183] that assigns no function to either partner, and nothing in it supports a more specific molecular-function term for SLC10A6, so MODIFY is not available. Removing the annotation does not assert that the reported interaction is false; it removes a row that adds no functional knowledge beyond SLC10A6's established activity as a sodium-coupled importer of sulfated steroid hormones [PMID:17491011, PMID:34079822]. Note that informative, hypothesis-driven interaction data do exist for this protein - SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, and co-immunoprecipitates with NTCP without impairing its transport [PMID:22029531, PMID:31256060] - but those studies are not the source of these rows and still do not establish a binding-based molecular function for SOAT. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT places plasma-membrane localization at PANTHER:PTN000040759, the ancestral SLC10 node, from experimentally grounded rodent and human descendants; SLC10A6 inherits it. Human SOAT is directly shown to sort to the plasma membrane in transfected cells, and every functional assay for the protein is an uptake measurement on intact cells, which requires the carrier to be at the cell surface [PMID:37373074, PMID:28743544]. Reason: The node placement is sound and the target is squarely inside the clade: all functionally characterized SLC10 carriers are plasma-membrane transporters. For SLC10A6 specifically, sorting studies in HEK293 cells localize the protein to the plasma membrane [PMID:37373074], the mouse ortholog is described as a plasma membrane transporter in germ cells [PMID:28743544], and immunohistochemistry places it in the apical membrane of placental syncytiotrophoblasts [PMID:24717977]. This is the location where the gene's core activity is executed, so it is retained as core. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000040759 SUPPORTS TRANSFER Ancestral SLC10 node; plasma-membrane residence is experimentally established in both the rodent and human descendants used to place the IBD, and independently for SLC10A6 itself. Supporting Evidence: PMID:37373074 Sorting studies in transfected HEK293 cells clearly localized the SOAT protein to the plasma membrane PMID:28743544 SOAT (gene name SLC10A6 in man and Slc10a6 in mice) is a plasma membrane transporter for sulfated steroids, which is highly expressed in germ cells of the testis. PMID:24717977 Immunohistochemical studies and in situ hybridization of formalin fixed and paraffin embedded sections of human late term placenta showed expression of SOAT in syncytiotrophoblasts, predominantly at the apical membrane as well as in the vessel endothelium. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-433089 | ACCEPT | Summary: Reactome asserts plasma-membrane localization for SOAT as part of its taurolithocholate-3-sulphate uptake reaction [Reactome:R-HSA-433089]. Independent experimental data agree: transfected human SOAT sorts to the plasma membrane and placental SOAT is apical-membrane localized [PMID:37373074, PMID:24717977]. Reason: The location is correct and independently supported outside Reactome. A sodium-coupled importer of circulating steroid sulfates must sit in the plasma membrane to encounter its substrates and the inward sodium gradient, and sorting studies confirm it [PMID:37373074]. Duplication with the IBA row for the same term is not a problem. Supporting Evidence: Reactome:R-HSA-433089 Unlike the other SLC10A gene products, SOAT shows no affinity for binding bile acids. However, SOAT is able to transport sulpho-conjugated bile acids such as taurolithocholate 3-sulphate (Geyer J et al, 2007). PMID:37373074 Sorting studies in transfected HEK293 cells clearly localized the SOAT protein to the plasma membrane PMID:24717977 Immunohistochemical studies and in situ hybridization of formalin fixed and paraffin embedded sections of human late term placenta showed expression of SOAT in syncytiotrophoblasts, predominantly at the apical membrane as well as in the vessel endothelium. |
| GO:0008508 bile acid:sodium symporter activity | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: PAINT places bile acid:sodium symporter activity at PANTHER:PTN000040761, the ancestor of the sodium-dependent SLC10 clade (human SLC10A1, SLC10A2, SLC10A4 and SLC10A6 all receive rows from this node), seeded by the rat descendants Ntcp (RGD:3681) and Asbt (RGD:3682). SLC10A6/SOAT inherits it by descent. The canonical bile acids are not SOAT substrates [PMID:17491011, PMID:34079822], but one bile salt, taurolithocholate, is transported sodium-dependently with Km 19.3 uM, comparable to NTCP and ASBT [PMID:34079822]. Reason: Challenging an IBA means arguing with the node placement, and that argument does not succeed here. SLC10A6 is inside the clade descending from PTN000040761, and the inherited activity has been narrowed rather than lost: cholate, chenodeoxycholate, taurocholate, taurochenodeoxycholate and taurodeoxycholate are not transported [PMID:17491011, PMID:34079822], but taurolithocholate - a genuine taurine-conjugated bile salt - is a sodium-coupled SOAT substrate, and the restriction is positional rather than categorical, since adding a 7' and/or 12' hydroxyl abolishes transport [PMID:34079822]. The authors of that systematic three-carrier comparison explicitly leave open whether taurolithocholate transport is ancestral to NTCP/ASBT/SOAT or acquired independently, so there is no basis for asserting functional loss at this node. REMOVE would therefore overstate what the evidence shows. What is wrong is only the implication that this is what SOAT is for: the carrier is a specific transporter of 3'- and 17'-monosulfated steroids [PMID:28951227, PMID:37373074], a chemistry this term cannot express (its definition is the bile acid/Na+ symport reaction and it sits under GO:0015355 secondary active monocarboxylate transmembrane transporter activity, verified via OLS; steroid sulfate esters are neither bile acids nor monocarboxylates). The row is therefore retained as a real but peripheral activity, and the core activity is raised as a proposed new term, steroid sulfate:sodium symporter activity, since GO has no term for it. Propagation Review Root cause: NO FAILURE NON CORE Failure modes: FUNCTIONAL DIVERGENCE Sources checked: PANTHER:PTN000040761 SUPPORTS TRANSFER Ancestral node of the Na+-dependent SLC10 clade. Node placement is not falsified for SLC10A6: the paralog retains sodium-coupled symport of taurolithocholate, and whether that is ancestral or convergent is explicitly unresolved in the literature. Substrate scope has narrowed, so the inherited term is kept as non-core rather than removed. Supporting Evidence: PMID:34079822 Surprisingly, SOAT showed significant sodium-dependent uptake of TLC and, therefore, TLC is the only common substrate of all three carriers NTCP, ASBT and SOAT, identified so far. PMID:34079822 However, the question if TLC was also a substrate of the common NTCP/ASBT/SOAT ancestor or if all three carriers later acquired the TLC transport function cannot be finally answered. PMID:34079822 This is, however, not possible when TLC is additionally hydroxylated at the 7β² and/or 12β positions, as it is the case for the BAs TCA, TCDCA, or TDCA, which all are not transported by SOAT. PMID:17491011 Although bile acids, such as taurocholic acid, cholic acid, and chenodeoxycholic acid, were not substrates of SOAT, the sulfoconjugated bile acid taurolithocholic acid-3-sulfate was transported by SOAT-HEK293 cells in a sodium-dependent manner PMID:37373074 The sodium-dependent organic anion transporter (SOAT, gene symbol SLC10A6) specifically transports 3'- and 17'-monosulfated steroid hormones, such as estrone sulfate and dehydroepiandrosterone sulfate, into specific target cells. |
| GO:0008508 bile acid:sodium symporter activity | TAS Reactome:R-HSA-433089 | KEEP AS NON CORE | Summary: Reactome asserts bile acid:sodium symporter activity for SOAT on the basis of its own reaction 'SOAT can transport taurolithocholate-3-sulphate' [Reactome:R-HSA-433089], which is grounded in the primary characterization showing sodium-dependent uptake of taurolithocholic acid-3-sulfate [PMID:17491011]. Reason: The underlying reaction is real and experimentally supported: taurolithocholic acid-3-sulfate, a sulfoconjugated bile salt, is taken up by SOAT-HEK293 cells in a sodium-dependent manner and is a potent competitive inhibitor [PMID:17491011]; the unsulfated parent taurolithocholate is likewise a substrate [PMID:34079822]. So the annotation is not false and should not be removed. But the Reactome entry itself states that SOAT, unlike the other SLC10A gene products, shows no affinity for bile acids and that it transports structurally similar sulfated steroids, which is the physiologically relevant activity [Reactome:R-HSA-433089]. A curator reading only this term would conclude SOAT is a bile acid carrier, which the primary literature denies [PMID:34079822]. The row is kept, marked non-core, with the steroid-sulfate symport activity proposed as a new term because GO has none. Supporting Evidence: Reactome:R-HSA-433089 Unlike the other SLC10A gene products, SOAT shows no affinity for binding bile acids. However, SOAT is able to transport sulpho-conjugated bile acids such as taurolithocholate 3-sulphate (Geyer J et al, 2007). Reactome:R-HSA-433089 It can also transport the structurally similar sulphated steroids (not shown here), thus SOAT may play a role in delivery of these prohormones to testis, pancreas and placenta. PMID:17491011 Although bile acids, such as taurocholic acid, cholic acid, and chenodeoxycholic acid, were not substrates of SOAT, the sulfoconjugated bile acid taurolithocholic acid-3-sulfate was transported by SOAT-HEK293 cells in a sodium-dependent manner PMID:34079822 In addition, sodium-dependent organic anion transporter SOAT specifically transports sulfated steroid hormones, but not bile acids. |
| GO:0015721 bile acid and bile salt transport | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Process-level counterpart of the GO:0008508 IBA, propagated from PANTHER:PTN000040761 with the same rat Ntcp/Asbt seeds. SOAT does participate in bile salt transport to a limited extent - it imports taurolithocholate and taurolithocholate-3-sulfate sodium-dependently [PMID:34079822, PMID:17491011] - but its physiological role is the import of circulating sulfated steroid hormones [PMID:37373074]. Reason: As for the molecular-function row, the node placement survives scrutiny and SOAT does execute transport of at least one bile salt, so the process term is not false. It is, however, a minor part of the carrier's activity and not the process it exists to perform: SOAT is testis-, placenta- and pancreas-dominant, not enterohepatic, and it does not transport the bile acids that drive enterohepatic cycling [PMID:17491011, PMID:34079822]. Marking it non-core keeps the true but peripheral claim while leaving GO:0043251 sodium-dependent organic anion transport as the core process. The possible physiological relevance of SOAT-mediated taurolithocholate handling in peripheral organs is raised in the primary comparison and is an open question rather than an established role [PMID:34079822]. Propagation Review Root cause: NO FAILURE NON CORE Failure modes: FUNCTIONAL DIVERGENCE Sources checked: PANTHER:PTN000040761 SUPPORTS TRANSFER Same ancestral Na+-dependent SLC10 node as the GO:0008508 row. Retained for SLC10A6 because taurolithocholate and its 3-sulfate are demonstrated sodium-coupled substrates, but the paralog's substrate preference has shifted to steroid sulfates, so the process is non-core. Supporting Evidence: PMID:34079822 Surprisingly, SOAT showed significant sodium-dependent uptake of TLC and, therefore, TLC is the only common substrate of all three carriers NTCP, ASBT and SOAT, identified so far. PMID:17491011 Although bile acids, such as taurocholic acid, cholic acid, and chenodeoxycholic acid, were not substrates of SOAT, the sulfoconjugated bile acid taurolithocholic acid-3-sulfate was transported by SOAT-HEK293 cells in a sodium-dependent manner PMID:17491011 SOAT mRNA is most highly expressed in testis. Relatively high SOAT expression was also detected in placenta and pancreas. PMID:37373074 The sodium-dependent organic anion transporter (SOAT, gene symbol SLC10A6) specifically transports 3'- and 17'-monosulfated steroid hormones, such as estrone sulfate and dehydroepiandrosterone sulfate, into specific target cells. |
| GO:0015721 bile acid and bile salt transport | TAS Reactome:R-HSA-9958517 | KEEP AS NON CORE | Summary: Reactome places SLC10A6 in its container pathway 'SLC-mediated bile acid transport' [Reactome:R-HSA-9958517]. SOAT's only member reaction in that pathway is the uptake of the sulfoconjugated bile salt taurolithocholate-3-sulphate [Reactome:R-HSA-433089, PMID:17491011]. Reason: The pathway membership is justified by a real reaction, so the term is retained rather than removed. But it is inherited from a grouping node, and the one SOAT reaction it collects is a sulfoconjugated bile salt - Reactome itself notes that SOAT has no affinity for bile acids [Reactome:R-HSA-433089]. SLC10A6 therefore does not belong to bile salt physiology in the way SLC10A1 and SLC10A2 do, and the annotation is marked non-core so that GO:0043251 sodium-dependent organic anion transport carries the gene's core process. Supporting Evidence: Reactome:R-HSA-9958517 This pathway serves as collection of reactions categorized as SLC-mediated bile acid transport Reactome:R-HSA-433089 Unlike the other SLC10A gene products, SOAT shows no affinity for binding bile acids. However, SOAT is able to transport sulpho-conjugated bile acids such as taurolithocholate 3-sulphate (Geyer J et al, 2007). PMID:17491011 Although bile acids, such as taurocholic acid, cholic acid, and chenodeoxycholic acid, were not substrates of SOAT, the sulfoconjugated bile acid taurolithocholic acid-3-sulfate was transported by SOAT-HEK293 cells in a sodium-dependent manner |
| GO:0016020 membrane | IEA GO_REF:0000120 | ACCEPT | Summary: Automated IEA pipeline assigns the broad term membrane from the InterPro bile acid:sodium symporter signature (IPR002657) and the UniProt SubCell keyword SL-0162. UniProt itself records only Membrane, multi-pass, for this protein. Reason: SOAT is a nine-transmembrane-helix integral membrane protein, so the term is correct. It is less specific than the plasma-membrane annotations also present, but per review policy a broader IEA term that is not wrong can be accepted rather than modified; it is also the location UniProt is willing to assert from the evidence it has. Keeping it costs nothing and the more specific GO:0005886 rows carry the informative claim. Propagation Review Root cause: NO FAILURE NON CORE Failure modes: GRANULARITY MISMATCH Sources checked: InterPro:IPR002657 Β· Bile acid:Na+ symporter family SUPPORTS TRANSFER Family signature that SLC10A6 genuinely carries; it supports membrane integration but cannot resolve which membrane. UniProtKB-SubCell:SL-0162 SUPPORTS TRANSFER UniProt subcellular-location keyword Membrane, the only location UniProt asserts for Q3KNW5. Supporting Evidence: PMID:37373074 Sorting studies in transfected HEK293 cells clearly localized the SOAT protein to the plasma membrane |
| GO:0043251 sodium-dependent organic anion transport | IEA GO_REF:0000107 | ACCEPT | Summary: Ensembl Compara transfers the sodium-dependent organic anion transport annotation from the rat ortholog Soat (UniProtKB:Q70EX6, SOAT_RAT, gene Slc10a6) to human SLC10A6. The human protein independently and directly performs this process: it mediates strictly sodium-dependent uptake of steroid sulfate anions - DHEAS, estrone-3-sulfate, pregnenolone sulfate and many others - across the plasma membrane [PMID:17491011, PMID:28951227]. Reason: This is the best-fitting existing GO process term for SLC10A6 and the one that matches the gene's own name. Steroid 3'- and 17'-mono-sulfates are organic anions, their transport by SOAT is obligatorily sodium-dependent in every assay reported, and the activity is demonstrated directly for the human protein, not merely inferred [PMID:17491011, PMID:28951227, PMID:37373074]. The orthology is one-to-one (rat Slc10a6/Soat to human SLC10A6), so the propagation is also sound on its own terms. Verified against OLS that GO:0043251 is current (its only parent is GO:0055085 transmembrane transport, so it is neither ancestor nor descendant of the bile-acid process terms also annotated), while the candidate alternatives GO:0015711 organic anion transport and GO:0008514 organic anion transmembrane transporter activity are obsolete. Retained as the core process. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:Q70EX6 Β· Slc10a6 SUPPORTS TRANSFER Rat Soat, the true one-to-one ortholog of human SLC10A6; the same sodium-dependent steroid sulfate transport activity is demonstrated directly for the human protein. ensembl:ENSRNOP00000072386 SUPPORTS TRANSFER Ensembl protein identifier for the same rat Slc10a6 gene product used as the Compara donor. Supporting Evidence: PMID:17491011 We established a stable SOAT-HEK293 cell line that showed sodium-dependent transport of dehydroepiandrosterone sulfate, estrone-3-sulfate, and pregnenolone sulfate with apparent K(m) values of 28.7, 12.0, and 11.3 microm, respectively. PMID:28951227 The sodium-dependent organic anion transporter SOAT/Soat shows highly specific transport activity for sulfated steroids. PMID:37373074 The sodium-dependent organic anion transporter (SOAT, gene symbol SLC10A6) specifically transports 3'- and 17'-monosulfated steroid hormones, such as estrone sulfate and dehydroepiandrosterone sulfate, into specific target cells. |
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Download this section (compressed HTML)Q: Should GO create a molecular-function term for sodium-coupled steroid sulfate symport (and a matching import process term)? At present the only molecular function GOA gives SLC10A6 is GO:0008508 bile acid:sodium symporter activity, which cannot express transport of a steroid sulfate ester, while the generic GO:0008514 was obsoleted to GO:0022857.
Suggested experts: Joachim Geyer, Gary Grosser
Q: Is bile acid:sodium symporter activity (GO:0008508) ancestral at PANTHER:PTN000040761, or did taurolithocholate transport arise independently in NTCP, ASBT and SOAT? Grosser et al. state that this cannot currently be decided, which bears directly on whether the IBA row should be retained for SLC10A6 at all.
Suggested experts: Gary Grosser, Joachim Geyer
Q: Would GO prefer to record SOAT's substrate scope through has_input extensions on the transporter activity annotation (CHEBI:17474 estrone 3-sulfate, CHEBI:57905 dehydroepiandrosterone 3-sulfate, CHEBI:133000 pregnenolone sulfate) rather than relying on the broad process term GO:0043251?
Q: SOAT homo-oligomerizes and heterodimerizes with other SLC10 carriers, co-immunoprecipitating with NTCP without impairing its transport [PMID:22029531, PMID:31256060]. Is there enough evidence for a protein-containing complex annotation, or is the physiological relevance of SLC10 heterodimers still too uncertain?
Suggested experts: Joachim Geyer
Q: Where does the elevated serum cholesterol sulfate of Slc10a6-/- mice come from, and is cholesterol sulfate itself a SOAT substrate? If so, the substrate definition would need to extend beyond steroid hormone sulfates.
Suggested experts: Joachim Geyer
Experiment: Reconstitute purified human SOAT into proteoliposomes and measure transport of a defined panel (DHEAS, estrone-3-sulfate, pregnenolone sulfate, taurolithocholate, taurolithocholate-3-sulfate, taurocholate, cholesterol sulfate) with sodium-stoichiometry determination for each substrate class. This would establish in a cell-free system both the 2 Na+:1 steroid sulfate stoichiometry inferred from UniProt/Rhea and whether bile salt and steroid sulfate transport use the same translocation cycle.
Experiment: Determine cryo-EM structures of human SOAT with DHEAS and with taurolithocholate bound, and test the two competing explanations offered for the shared taurolithocholate substrate: a single site that accommodates the bile salt in antiparallel orientation to DHEAS, versus a separate taurolithocholate site conserved across NTCP, ASBT and SOAT. Structure-guided mutants that abolish steroid sulfate transport while retaining taurolithocholate transport (and the converse) would settle whether the two activities should be annotated separately.
Experiment: Reconstruct the SLC10 family phylogeny with ancestral sequence reconstruction and resurrect the PTN000040761 ancestral carrier, then assay it for taurocholate, taurolithocholate and DHEAS transport. This directly tests the PAINT node placement of bile acid:sodium symporter activity and would determine whether SOAT's steroid sulfate preference is a derived narrowing or an independent gain.
Experiment: Phenotype Slc10a6-/- mice in the tissues with highest Soat expression outside the testis (skin, lung, adipose, pancreas, placenta) with targeted steroid-sulfate and cholesterol-sulfate flux measurements, and cross them to Sts or Slco6a1 mutants to test the redundancy that must underlie their normal spermatogenesis.
Experiment: Quantify the contribution of SOAT to estrone-3-sulfate uptake in primary hormone-dependent breast tumour cells using the published SOAT-selective inhibitors alongside OATP and OAT inhibitors, to establish whether SOAT-mediated uptake is rate-limiting for intracrine estrogen formation in a native setting rather than in transfected cell lines.
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