SULT1B1

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0004062 aryl sulfotransferase activity	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetic assertion of aryl (phenol) sulfotransferase activity across the SULT1 clade, matching the directly measured activity of human SULT1B1. Reason: Core molecular function, independently established by direct enzyme assay on the human protein, so the IBA node placement is corroborated on the target itself. Supporting Evidence: PMID:9463486 Expressed hST1B2 sulfates small phenols such as 1-naphthol and p-nitrophenol and thyroid hormones, including 3,3'-diiodothyronine, triiodothyronine, reverse triiodothyronine, and thyroxine.
GO:0005737 cytoplasm	IBA GO_REF:0000033	ACCEPT	Summary: The SULT1/SULT2 families are soluble cytosolic enzymes; the phylogenetic assertion is correct for SULT1B1. Reason: Correct, although the cytosol (GO:0005829) annotations this gene also carries are more informative.
GO:0051923 sulfation	IBA GO_REF:0000033	ACCEPT	Summary: The biological process matching the enzyme's catalytic activity. Reason: Correct and directly entailed by the aryl sulfotransferase activity.
GO:0004062 aryl sulfotransferase activity	IEA GO_REF:0000120	ACCEPT	Summary: Automated assignment of EC 2.8.2.1 / RHEA:12164 to SULT1B1. Reason: Agrees with the experimental data; same term and action as the EXP and IDA rows.
GO:0005737 cytoplasm	IEA GO_REF:0000044	ACCEPT	Summary: Transfer of the UniProt SUBCELLULAR LOCATION 'Cytoplasm' keyword, itself backed by experimental evidence from both founding papers. Reason: Correct location.
GO:0006790 sulfur compound metabolic process	IEA GO_REF:0000117	MODIFY	Summary: An ARBA machine-learning assignment of a very high-level sulfur metabolism parent. Reason: Not wrong, but uninformatively general - it is a distant ancestor of the specific process this enzyme carries out. The sulfation term already annotated to this gene should be used instead. Proposed replacements: sulfation
GO:0008146 sulfotransferase activity	IEA GO_REF:0000120	MODIFY	Summary: Family-level sulfotransferase assignment from the InterPro sulfotransferase domain signature. Reason: Correct but under-specific. SULT1B1's acceptor preference (phenols and iodothyronines) is established, so the aryl sulfotransferase child term should be used. Proposed replacements: aryl sulfotransferase activity
GO:0005515 protein binding	IPI PMID:21044950 Genome-wide YFP fluorescence complementation screen identifi...	REMOVE	Summary: Bare protein binding from a genome-wide YFP fluorescence complementation screen. Reason: "GO:0005515 carries no functional information, and this partner (UniProtKB:Q9NUX5) comes\ \ from a high-throughput two-hybrid-like screen with no follow-up implicating SULT1B1 in a complex\ \ or adapter role.". No more informative molecular function is supportable from this evidence, so the row is removed rather than rewritten. Removal does not imply the reported interaction is false.
GO:0005515 protein binding	IPI PMID:25416956 A proteome-scale map of the human interactome network.	REMOVE	Summary: Bare protein binding from a systematic yeast two-hybrid interactome map. Reason: Uninformative term from a high-throughput interactome screen; no specific molecular function follows from it. No more informative molecular function is supportable from this evidence, so the row is removed rather than rewritten. Removal does not imply the reported interaction is false.
GO:0005515 protein binding	IPI PMID:25910212 Widespread macromolecular interaction perturbations in human...	REMOVE	Summary: Bare protein binding from an interactome-perturbation survey of disease alleles. Reason: Uninformative term; high-throughput binary interaction data without functional follow-up. No more informative molecular function is supportable from this evidence, so the row is removed rather than rewritten. Removal does not imply the reported interaction is false.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	REMOVE	Summary: Bare protein binding from the HuRI binary interactome reference map. Reason: Uninformative term; high-throughput binary interaction data without functional follow-up. No more informative molecular function is supportable from this evidence, so the row is removed rather than rewritten. Removal does not imply the reported interaction is false.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	REMOVE	Summary: Bare protein binding from a neurodegenerative-disease interactome mapping study. Reason: Uninformative term; high-throughput interaction data with no evidence that SULT1B1 acts through protein binding. No more informative molecular function is supportable from this evidence, so the row is removed rather than rewritten. Removal does not imply the reported interaction is false.
GO:0042403 thyroid hormone metabolic process	IEA GO_REF:0000107	ACCEPT	Summary: Orthology transfer from mouse Sult1b1, agreeing with the human experimental data. Reason: Consistent with the direct demonstration of iodothyronine sulfation by the human enzyme.
GO:0008146 sulfotransferase activity	IDA PMID:20056724 Phase II metabolism of hesperetin by individual UDP-glucuron...	MODIFY	Summary: SULT1B1 was one of twelve purified human SULTs assayed for hesperetin sulfo-conjugation. Reason: The observation is real, but the acceptor here is a phenolic flavonoid, so the aryl sulfotransferase child term is the accurate assignment. Same action as the other GO:0008146 rows. Proposed replacements: aryl sulfotransferase activity Supporting Evidence: PMID:20056724 Based on expression levels SULT1A3 and SULT1B1 also will probably play a role in the sulfo-conjugation of hesperetin in vivo.
GO:0004062 aryl sulfotransferase activity	EXP PMID:28084139 A high frequency missense SULT1B1 allelic variant (L145V) se...	ACCEPT	Summary: Kinetic characterization of wild-type and L145V SULT1B1 on small phenolic substrates. Reason: Direct experimental support for the core molecular function on the human protein. Supporting Evidence: PMID:28084139 Human cytosolic sulfotransferase 1B1 (SULT1B1) sulfates small phenolic compounds and bioactivates polycyclic aromatic hydrocarbons.
GO:0004062 aryl sulfotransferase activity	EXP PMID:9463486 Expression and characterization of a novel thyroid hormone-s...	ACCEPT	Summary: Recombinant human SULT1B1 (hST1B2) sulfates 1-naphthol and p-nitrophenol. Reason: Founding experimental evidence for the core molecular function. Supporting Evidence: PMID:9463486 Expressed hST1B2 sulfates small phenols such as 1-naphthol and p-nitrophenol and thyroid hormones, including 3,3'-diiodothyronine, triiodothyronine, reverse triiodothyronine, and thyroxine.
GO:0005737 cytoplasm	EXP PMID:9443824 Molecular cloning and characterization of rat ST1B1 and huma...	ACCEPT	Summary: The cloned enzyme behaves as a soluble cytosolic protein and is detected in liver cytosol. Reason: Correct; the cytosol term carried by this gene is the more precise form.
GO:0005737 cytoplasm	EXP PMID:9463486 Expression and characterization of a novel thyroid hormone-s...	ACCEPT	Summary: SULT1B1 was isolated and characterized as a cytosolic sulfotransferase. Reason: Correct location, supported by the founding characterization. Supporting Evidence: PMID:9463486 These results indicate that a novel cytosolic ST is present in human tissues, which may have an important role in thyroid hormone and xenobiotic metabolism.
GO:0042403 thyroid hormone metabolic process	IDA PMID:9463486 Expression and characterization of a novel thyroid hormone-s...	ACCEPT	Summary: Recombinant SULT1B1 sulfates T2, T3, rT3 and T4. Reason: Well-supported endogenous role; iodothyronine sulfation is the reason the enzyme was originally named iodothyronine sulfotransferase. Supporting Evidence: PMID:9463486 Expressed hST1B2 sulfates small phenols such as 1-naphthol and p-nitrophenol and thyroid hormones, including 3,3'-diiodothyronine, triiodothyronine, reverse triiodothyronine, and thyroxine.
GO:0004062 aryl sulfotransferase activity	IDA PMID:9443824 Molecular cloning and characterization of rat ST1B1 and huma...	ACCEPT	Summary: Recombinant human ST1B2 (SULT1B1) expressed in COS-1 cells sulfates p-nitrophenol. Reason: Direct experimental support for the core molecular function. Supporting Evidence: PMID:9443824 The recombinant forms catalyzed sulfation of p-nitrophenol, 3,3',5-triiodothyronine (T3) and dopamine, but not of beta-estradiol and dehydroepiandrosterone.
GO:0051923 sulfation	IDA PMID:9443824 Molecular cloning and characterization of rat ST1B1 and huma...	ACCEPT	Summary: The process term corresponding to the measured sulfotransferase reaction. Reason: Correct and directly observed.
GO:0006068 ethanol catabolic process	IDA PMID:23207770 Ethanol sulfation by the human cytosolic sulfotransferases: ...	MARK AS OVER ANNOTATED	Summary: SULT1B1 was one of eleven purified human SULTs screened for ethanol sulfation, and it was not among the enzymes found to be active. Reason: The cited paper's own summary names the ethanol-sulfating SULTs explicitly and SULT1B1 is not among them, so this looks like a panel-wide transfer of the screen's positive result to every enzyme tested. Additionally, sulfation of ethanol to ethyl sulfate is a minor conjugation route rather than ethanol catabolism. Flagged rather than removed because this is an experimental annotation whose full text I could not read (the cached record is abstract-only), per project policy; a curator with the full text should confirm or retire it. Supporting Evidence: PMID:23207770 A systematic analysis revealed four ethanol-sulfating SULTs, SULT1A1, SULT1A2, SULT1A3, and SULT1C4, among the eleven human SULT enzymes previously prepared and purified.
GO:0004062 aryl sulfotransferase activity	IDA PMID:23207770 Ethanol sulfation by the human cytosolic sulfotransferases: ...	ACCEPT	Summary: SULT1B1 was among the eleven purified, PAPS-dependent human SULT enzymes used in this systematic assay. Reason: Consistent with the established core function, even though this particular paper's positive substrate hits were other SULTs.
GO:0050427 3'-phosphoadenosine 5'-phosphosulfate metabolic process	IDA PMID:23207770 Ethanol sulfation by the human cytosolic sulfotransferases: ...	KEEP AS NON CORE	Summary: SULT1B1 consumes PAPS as the sulfonate donor in every reaction it catalyses. Reason: True but generic to the whole cytosolic sulfotransferase family; it describes cofactor turnover rather than a distinguishing biological role of SULT1B1.
GO:0051923 sulfation	IDA PMID:23207770 Ethanol sulfation by the human cytosolic sulfotransferases: ...	ACCEPT	Summary: The process term matching the assayed sulfotransferase reaction. Reason: Correct; same term and action as the other sulfation rows.
GO:0008146 sulfotransferase activity	IDA PMID:19548878 Inhibitory effects of kynurenic acid, a tryptophan metabolit...	MODIFY	Summary: Recombinant hSULT1B1 activity was measured in order to characterize kynurenic acid as an inhibitor. Reason: The activity is real but the general parent term is used; the aryl sulfotransferase child term is accurate for this enzyme. Same action as the other GO:0008146 rows. Proposed replacements: aryl sulfotransferase activity Supporting Evidence: PMID:19548878 KYNA also exerted an inhibitory activity towards hSULT1A1 and hSULT1B1.
GO:0051923 sulfation	IDA PMID:19548878 Inhibitory effects of kynurenic acid, a tryptophan metabolit...	ACCEPT	Summary: The process term matching the assayed reaction; the qualifier is weaker than the involved_in used on the other sulfation rows. Reason: Correct process. The enzyme directly performs sulfation, so involved_in would be the better qualifier, but the term assignment itself is sound.
GO:0030855 epithelial cell differentiation	IEP PMID:21492153 Analysis of proteomic changes induced upon cellular differen...	MARK AS OVER ANNOTATED	Summary: SULT1B1 was one of 53 spots differentially abundant between proliferating and differentiated Caco-2 cells on 2-D gels. Reason: An expression correlation during enterocyte differentiation, with no perturbation showing that SULT1B1 participates in the differentiation programme. SULT1B1 being induced in differentiated enterocytes is expected from its role in intestinal first-pass phenol conjugation and does not make it a differentiation factor. Supporting Evidence: PMID:21492153 Two-dimensional gel analysis yielded 53 proteins that were differently regulated during the differentiation process.
GO:0005829 cytosol	TAS Reactome:R-HSA-176474	ACCEPT	Summary: Reactome places SULT1B1 in the cytosol as the catalyst of 3,3'-diiodothyronine sulfation. Reason: Correct and more specific than the cytoplasm annotations; consistent with the experimental localization.
GO:0005829 cytosol	TAS Reactome:R-HSA-176585	ACCEPT	Summary: Reactome places SULT1B1 in the cytosol as the catalyst of T3 sulfation. Reason: Correct and specific; same term and action as the other cytosol rows.
GO:0006805 xenobiotic metabolic process	IDA PMID:20056724 Phase II metabolism of hesperetin by individual UDP-glucuron...	ACCEPT	Summary: Phase II sulfo-conjugation of a dietary flavanone by purified SULT1B1. Reason: Phase II conjugation of ingested phenolic compounds is a genuine physiological role for this enzyme, which is most abundant in colon and small intestinal mucosa. Supporting Evidence: PMID:28084139 SULT1B1 is expressed at highest levels throughout the human colon and small intestine but can also be found at moderate levels in human liver, kidney, and white blood cells
GO:0009812 flavonoid metabolic process	IDA PMID:20056724 Phase II metabolism of hesperetin by individual UDP-glucuron...	KEEP AS NON CORE	Summary: SULT1B1 conjugates hesperetin in a purified-enzyme panel. Reason: Genuine but one instance of the enzyme's broad phenolic substrate range; flavonoids are not a distinguishing physiological substrate class for SULT1B1, and the paper itself infers an in vivo role from expression level rather than from potency. Supporting Evidence: PMID:20056724 Based on expression levels SULT1A3 and SULT1B1 also will probably play a role in the sulfo-conjugation of hesperetin in vivo.
GO:0051923 sulfation	IDA PMID:20056724 Phase II metabolism of hesperetin by individual UDP-glucuron...	ACCEPT	Summary: The process term matching the measured conjugation reaction. Reason: Correct; same term and action as the other sulfation rows.
GO:0005829 cytosol	NAS PMID:9463486 Expression and characterization of a novel thyroid hormone-s...	ACCEPT	Summary: Author statement that this is a cytosolic sulfotransferase. Reason: Correct, and corroborated by the EXP cytoplasm annotations from the same and the companion paper. Supporting Evidence: PMID:9463486 These results indicate that a novel cytosolic ST is present in human tissues, which may have an important role in thyroid hormone and xenobiotic metabolism.
GO:0008146 sulfotransferase activity	IDA PMID:9463486 Expression and characterization of a novel thyroid hormone-s...	MODIFY	Summary: Direct demonstration of sulfotransferase activity of recombinant human SULT1B1. Reason: The activity is directly demonstrated, but the acceptors identified in this very paper are phenols and iodothyronines, so the aryl sulfotransferase child term is the accurate assignment. Same action as the other GO:0008146 rows. Proposed replacements: aryl sulfotransferase activity
GO:0018958 phenol-containing compound metabolic process	IDA PMID:9463486 Expression and characterization of a novel thyroid hormone-s...	ACCEPT	Summary: Sulfation of 1-naphthol and p-nitrophenol by the recombinant enzyme. Reason: This is arguably the most accurate biological-process description of what SULT1B1 does - it is the process counterpart of aryl sulfotransferase activity. Supporting Evidence: PMID:9463486 Expressed hST1B2 sulfates small phenols such as 1-naphthol and p-nitrophenol and thyroid hormones, including 3,3'-diiodothyronine, triiodothyronine, reverse triiodothyronine, and thyroxine.
GO:0042403 thyroid hormone metabolic process	IDA PMID:9443824 Molecular cloning and characterization of rat ST1B1 and huma...	ACCEPT	Summary: T3 sulfation by recombinant human ST1B2, with higher affinity than the phenol sulfotransferases ST1A3 and ST1A5. Reason: Core endogenous role, directly measured and kinetically compared against other human SULTs. Supporting Evidence: PMID:9443824 These data indicate that the newly characterized sulfotransferases constitute a distinct ST1 subfamily of enzymes catalyzing the sulfation of T3 as a typical endogenous substrate in rats and humans.
GO:0006576 biogenic amine metabolic process	TAS PMID:9443824 Molecular cloning and characterization of rat ST1B1 and huma...	KEEP AS NON CORE	Summary: Dopamine sulfation was reported for recombinant ST1B2 in this paper. Reason: Kept but demoted because the two founding papers disagree: PMID:9443824 reports dopamine sulfation while PMID:9463486 reports no activity on dopamine. UniProt follows PMID:9443824. Catecholamine sulfation in humans is dominated by SULT1A3, so even if SULT1B1 has measurable activity it is unlikely to be a physiologically distinguishing role. Supporting Evidence: PMID:9443824 The recombinant forms catalyzed sulfation of p-nitrophenol, 3,3',5-triiodothyronine (T3) and dopamine, but not of beta-estradiol and dehydroepiandrosterone. PMID:9463486 No activity was detected when several steroids or dopamine were tested as substrates.
GO:0008146 sulfotransferase activity	TAS PMID:9443824 Molecular cloning and characterization of rat ST1B1 and huma...	MODIFY	Summary: Author-statement sulfotransferase assignment from the cloning paper. Reason: Correct but under-specific; the same paper identifies phenolic and iodothyronine acceptors. Same action as the other GO:0008146 rows. Proposed replacements: aryl sulfotransferase activity

Gene Description

Existing Annotations Review

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