TAT

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0004838 L-tyrosine:2-oxoglutarate transaminase activity	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetic (IBA) assertion of the core molecular function. This is the correct, specific enzymatic activity of TAT (EC 2.6.1.5), directly supported by experimental characterization of the human enzyme. Reason: This is the defining, experimentally validated molecular function of TAT. The IBA is consistent with the IDA on the same term and with the catalytic activity reported in UniProt (RHEA:15093). Core function. Supporting Evidence: PMID:7999802 The expressed protein catalyzed specifically the conversion of L-[14C]tyrosine into p-[14C]hydroxyphenylpyruvate.
GO:0006572 L-tyrosine catabolic process	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetic assertion that TAT participates in L-tyrosine catabolism. TAT catalyzes the first, committed step of tyrosine breakdown, so this is the correct biological process. Reason: Consistent with the IDA on the same term and with UniProt FUNCTION ("Transaminase involved in tyrosine breakdown"). Core process. Supporting Evidence: PMID:7999802 The expressed protein catalyzed specifically the conversion of L-[14C]tyrosine into p-[14C]hydroxyphenylpyruvate.
GO:0006559 L-phenylalanine catabolic process	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: Phylogenetic assertion of involvement in L-phenylalanine catabolism. Phenylalanine is degraded via conversion to tyrosine, and UniProt places TAT as step 2/6 of the L-phenylalanine degradation pathway (the tyrosine transamination step). TAT itself has only weak, low-affinity activity directly on phenylalanine. Reason: Biologically defensible as pathway membership (Phe -> Tyr -> catabolism), matching the UniProt PATHWAY statement, and it is corroborated by an independent UniPathway mapping annotation. However, TAT's direct catalytic role is on tyrosine; its phenylalanine transaminase activity is much lower. Retain as a non-core, pathway-context process rather than a core function. Supporting Evidence: PMID:16640556 The narrow substrate specificity of human tyrosine aminotransferase -- the enzyme deficient in tyrosinemia type II.
GO:0003824 catalytic activity	IEA GO_REF:0000002	MARK AS OVER ANNOTATED	Summary: InterPro2GO electronic annotation to the root molecular-function catalytic-activity term. TAT is an enzyme, so the term is not wrong, but it is far too general given that the specific activity (GO:0004838) is known experimentally. Reason: GO:0004838 is an entailed subclass of GO:0003824; the specific transaminase activity is experimentally established for the human enzyme, so this uninformative parent should not be treated as a core function. Proposed replacements: L-tyrosine:2-oxoglutarate transaminase activity
GO:0004838 L-tyrosine:2-oxoglutarate transaminase activity	IEA GO_REF:0000120	ACCEPT	Summary: Combined multi-method electronic annotation to the correct, specific molecular function of TAT. Reason: Matches the experimentally supported core molecular function (IDA/IBA on the same term). Correct level of specificity. Supporting Evidence: PMID:7999802 The expressed protein catalyzed specifically the conversion of L-[14C]tyrosine into p-[14C]hydroxyphenylpyruvate.
GO:0006520 amino acid metabolic process	IEA GO_REF:0000120	KEEP AS NON CORE	Summary: Electronic annotation to a high-level amino-acid metabolic process term. TAT participates in amino-acid metabolism (tyrosine catabolism), so the term is correct but general. Reason: True but subsumed by the more specific and experimentally supported L-tyrosine catabolic process (GO:0006572). Retain as a broad-parent, non-core annotation. Proposed replacements: L-tyrosine catabolic process
GO:0008483 transaminase activity	IEA GO_REF:0000002	MARK AS OVER ANNOTATED	Summary: InterPro2GO annotation to the general transaminase-activity term. TAT is a transaminase, so the term is correct but broader than the known specific activity. Reason: GO:0004838 is an entailed subclass of GO:0008483; the specific tyrosine transaminase activity is experimentally known, so the general parent is an over-annotation for core-function purposes. Proposed replacements: L-tyrosine:2-oxoglutarate transaminase activity
GO:0009072 aromatic amino acid metabolic process	IEA GO_REF:0000002	KEEP AS NON CORE	Summary: InterPro2GO annotation to aromatic amino acid metabolic process. Tyrosine and phenylalanine are aromatic amino acids, so the term is correct but broad. Reason: Subsumed by the more specific tyrosine catabolic process (GO:0006572). Correct but general; retain as non-core parent. Proposed replacements: L-tyrosine catabolic process
GO:0009074 aromatic amino acid catabolic process	IEA GO_REF:0000002	KEEP AS NON CORE	Summary: InterPro2GO annotation to aromatic amino acid (family) catabolic process (current ontology primary label: "aromatic amino acid family catabolic process"). TAT catalyzes the first step of catabolism of the aromatic amino acid tyrosine, so the term is correct but broad. Reason: True but subsumed by the more specific and experimentally supported L-tyrosine catabolic process (GO:0006572). Retain as a broad-parent, non-core annotation. Proposed replacements: L-tyrosine catabolic process
GO:0030170 pyridoxal phosphate binding	IEA GO_REF:0000002	ACCEPT	Summary: InterPro2GO annotation for PLP cofactor binding. TAT is a PLP-dependent aminotransferase that binds pyridoxal 5'-phosphate as a Schiff base to Lys-280, confirmed by the crystal structure (PDB 3DYD). Reason: Directly supported by the UniProt COFACTOR annotation and the N6-(pyridoxal phosphate)lysine modified residue at Lys-280 seen in the crystal structure. A correct, mechanistically important molecular function.
GO:0005515 protein binding	IPI PMID:24722188 Protein interaction network of alternatively spliced isoform...	MARK AS OVER ANNOTATED	Summary: Interaction reported in a genome-scale interactome map. Bare "protein binding" is uninformative about molecular function and this specific interaction is not discussed for TAT in the body of the paper. Reason: Per curation guidelines, the bare protein-binding term does not convey TAT's function and is derived from a high-throughput screen without a TAT-specific functional interpretation. Not a core function.
GO:0005515 protein binding	IPI PMID:25910212 Widespread macromolecular interaction perturbations in human...	MARK AS OVER ANNOTATED	Summary: High-throughput interactome IPI annotation. Bare "protein binding" is uninformative and the interaction is not functionally characterized for TAT in the paper. Reason: Uninformative molecular-function term from a systematic screen; provides no insight into TAT's function. Not a core function.
GO:0005515 protein binding	IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari...	MARK AS OVER ANNOTATED	Summary: High-throughput interactome IPI annotation. Bare "protein binding" is uninformative for molecular function. Reason: Uninformative term derived from a genome-scale binary interaction assay; not functionally characterized for TAT. Not a core function.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	MARK AS OVER ANNOTATED	Summary: Annotation from the HuRI reference human binary protein interactome. Bare "protein binding" does not describe TAT's molecular function. Reason: Uninformative molecular-function term from a systematic Y2H interactome map; no TAT-specific functional interpretation. Not a core function.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	MARK AS OVER ANNOTATED	Summary: Interaction from a neurodegenerative-disease interactome map. Bare "protein binding" is uninformative for molecular function. Reason: Uninformative term from a high-throughput screen; provides no functional insight for TAT. Not a core function.
GO:0042802 identical protein binding	IPI PMID:25502805 A massively parallel pipeline to clone DNA variants and exam...	KEEP AS NON CORE	Summary: Self-interaction (homodimerization) annotation. TAT is documented as a homodimer, so self-association is real biology, though it is not the core catalytic function. Reason: Corroborated by the UniProt SUBUNIT statement ("Homodimer.") and the IntAct self-interaction record (P17735-P17735). More informative than bare protein binding, but a structural/quaternary property rather than a core molecular function.
GO:0042802 identical protein binding	IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari...	KEEP AS NON CORE	Summary: Self-interaction annotation consistent with TAT being a homodimer. Reason: Corroborated by the UniProt SUBUNIT "Homodimer." statement. A quaternary structural property, not a core molecular function.
GO:0042802 identical protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	KEEP AS NON CORE	Summary: Self-interaction annotation from the HuRI interactome, consistent with the documented homodimer. Reason: Corroborated by the UniProt SUBUNIT "Homodimer." statement. Structural quaternary property, not a core function.
GO:0005829 cytosol	IEA GO_REF:0000107	ACCEPT	Summary: Ensembl-Compara orthology-based location. TAT is a cytosolic enzyme, and this is independently supported by the Reactome TAS annotations to the same term. Reason: Correct subcellular location; TAT is a soluble cytosolic aminotransferase. Core location, corroborated by Reactome. This is a location transfer, not a phenotype-response transfer, so it is reliable regardless of GO_REF source.
GO:0006103 2-oxoglutarate metabolic process	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: Orthology-transferred annotation reflecting that 2-oxoglutarate is a cosubstrate of the transamination reaction. Duplicated by the IDA on the same term. Reason: 2-oxoglutarate is consumed as the amino-group acceptor cosubstrate, so the process is a real consequence of the reaction, but it is a cosubstrate/co-metabolite consequence rather than TAT's core biological role (tyrosine catabolism).
GO:0006536 glutamate metabolic process	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: Orthology-transferred annotation reflecting that L-glutamate is produced as the co-product of the transamination reaction. Duplicated by the IDA on the same term. Reason: L-glutamate is the amino-group-carrying co-product, so the process is a real consequence of the reaction, but it is a co-product consequence rather than TAT's core biological role.
GO:0006572 L-tyrosine catabolic process	IEA GO_REF:0000107	ACCEPT	Summary: Orthology-transferred annotation to the core biological process, tyrosine catabolism. Duplicated by the IDA and IBA on the same term. Reason: Correct core biological process; TAT catalyzes the first step of tyrosine breakdown. Consistent with experimental (IDA) and phylogenetic (IBA) annotations.
GO:0006979 response to oxidative stress	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: Ensembl-Compara orthology-transferred response term, largely derived from rodent orthologs. Represents a physiological/regulatory response context, not TAT's molecular activity or its direct catabolic role. Reason: Plausible regulatory context transferred by orthology, but not verified for the human protein and not a core function. Retain as non-core.
GO:0016597 amino acid binding	IEA GO_REF:0000107	MARK AS OVER ANNOTATED	Summary: Orthology-transferred molecular function reflecting that TAT binds its amino-acid substrate (tyrosine). The term is a general parent; substrate binding is inherent to the specific transaminase activity. Reason: Binding of the amino-acid substrate is subsumed by the specific catalytic activity (GO:0004838); the standalone "amino acid binding" term adds no functional information beyond the enzyme activity. Not a core function. Proposed replacements: L-tyrosine:2-oxoglutarate transaminase activity
GO:0032869 cellular response to insulin stimulus	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: Ensembl-Compara orthology-transferred response term (largely from rodent orthologs). Reflects hormonal regulation of TAT expression rather than the protein's molecular activity. Reason: TAT is a classical hormonally regulated hepatic gene; insulin-response context is plausible but transferred by orthology and unverified for the human protein. Regulatory context, not a core function.
GO:0045471 response to ethanol	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: Orthology-transferred response term. Represents a physiological response context of the gene rather than TAT's core molecular or catabolic role. Reason: Regulatory/response context transferred by orthology and unverified for the human protein. Not a core function.
GO:0046689 response to mercury ion	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: Orthology-transferred response term. Represents a physiological response context of the gene rather than TAT's core function. Reason: Regulatory/response context transferred by orthology and unverified for the human protein. Not a core function.
GO:0051384 response to glucocorticoid	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: Orthology-transferred response term. TAT is the textbook glucocorticoid-inducible hepatic gene, but induction is regulation of expression rather than TAT's molecular activity, and the human promoter GREs are notably degenerate relative to rat. Reason: Well-established regulatory context (glucocorticoid induction) but a response/regulation term, not TAT's core molecular or catabolic function. The human upstream GREs are mutated/replaced by Alu elements, so even the regulatory transfer from rat is imperfect. Retain as non-core. Supporting Evidence: PMID:1973834 Two functional glucocorticoid response elements (GREs) reside 2.5 kb upstream of the rat TAT gene. The DNA sequence of the corresponding region of the human TAT gene shows the distal GRE mutated and the proximal GRE replaced by Alu elements.
GO:0051414 response to cortisol	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: Orthology-transferred response term, a specific instance of the glucocorticoid-response context of the gene. Reason: Regulatory/response context transferred by orthology; not a core molecular or catabolic function. Retain as non-core.
GO:0051591 response to cAMP	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: Orthology-transferred response term. TAT is a classical cAMP/glucagon- inducible gene, but induction is regulation of expression, not the protein's molecular activity. Reason: Well-known regulatory context but a response/regulation term, not a core function. Retain as non-core.
GO:0071300 cellular response to retinoic acid	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: Orthology-transferred response term. Physiological response context rather than TAT's core molecular or catabolic role. Reason: Regulatory/response context transferred by orthology and unverified for the human protein. Not a core function.
GO:0071548 response to dexamethasone	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: Orthology-transferred response term; a synthetic-glucocorticoid instance of the well-known hormonal induction of TAT expression. Reason: Regulatory/response context transferred by orthology; not a core molecular or catabolic function. Retain as non-core.
GO:0097421 liver regeneration	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: Orthology-transferred process term reflecting hepatic expression dynamics. TAT is a liver-enriched enzyme, but there is no evidence it functions in the regeneration process itself as opposed to being expressed in liver. Reason: Association with liver-expression context, transferred by orthology and unverified mechanistically for the human protein. Not a core function.
GO:0006559 L-phenylalanine catabolic process	IEA GO_REF:0000041	KEEP AS NON CORE	Summary: UniPathway-mapping-based annotation to L-phenylalanine catabolism, matching the UniProt PATHWAY statement (step 2/6 of L-phenylalanine degradation). Phenylalanine is degraded via tyrosine, so TAT participates in the pathway through its tyrosine transamination step. Reason: Defensible as pathway membership (Phe -> Tyr -> catabolism) and consistent with the UniProt PATHWAY annotation, but TAT's direct catalytic role is on tyrosine, with only weak phenylalanine activity. Non-core pathway context. Supporting Evidence: PMID:16640556 The narrow substrate specificity of human tyrosine aminotransferase -- the enzyme deficient in tyrosinemia type II.
GO:0005829 cytosol	TAS Reactome:R-HSA-517444	ACCEPT	Summary: Reactome traceable-author-statement placing TAT in the cytosol, in the context of the reaction "TAT aminates HPP". Correct subcellular location. Reason: TAT is a soluble cytosolic aminotransferase; the location is well established and corroborated by the Ensembl location annotation. Core location.
GO:0005829 cytosol	TAS Reactome:R-HSA-71155	ACCEPT	Summary: Reactome TAS placing TAT in the cytosol in the context of the reaction "TAT deaminates tyrosine" (the forward tyrosine transamination step). Reason: Correct cytosolic location, consistent with the other cytosol annotations. Core location.
GO:0004838 L-tyrosine:2-oxoglutarate transaminase activity	IDA PMID:7999802 Cloning and expression of human tyrosine aminotransferase cD...	ACCEPT	Summary: Direct experimental demonstration that the cloned human TAT protein specifically converts L-tyrosine to 4-hydroxyphenylpyruvate. This is the primary experimental basis for the core molecular function. Reason: Human TAT cDNA expressed in HeLa cells produced a ~50 kDa protein that catalyzed specifically the conversion of L-[14C]tyrosine into p-[14C]hydroxyphenylpyruvate. Definitive core molecular function. Supporting Evidence: PMID:7999802 The expressed protein catalyzed specifically the conversion of L-[14C]tyrosine into p-[14C]hydroxyphenylpyruvate.
GO:0006103 2-oxoglutarate metabolic process	IDA PMID:7999802 Cloning and expression of human tyrosine aminotransferase cD...	KEEP AS NON CORE	Summary: Annotation reflecting consumption of 2-oxoglutarate as the amino-group acceptor cosubstrate in the demonstrated transamination reaction. Reason: 2-oxoglutarate is the cosubstrate consumed in the transamination; a real but co-metabolite consequence rather than TAT's core biological role of tyrosine catabolism. Supporting Evidence: PMID:7999802 The expressed protein catalyzed specifically the conversion of L-[14C]tyrosine into p-[14C]hydroxyphenylpyruvate.
GO:0006536 glutamate metabolic process	IDA PMID:7999802 Cloning and expression of human tyrosine aminotransferase cD...	KEEP AS NON CORE	Summary: Annotation reflecting production of L-glutamate as the co-product of the demonstrated transamination reaction. Reason: L-glutamate is the amino-group-carrying co-product; a real but co-product consequence rather than TAT's core biological role of tyrosine catabolism. Supporting Evidence: PMID:7999802 The expressed protein catalyzed specifically the conversion of L-[14C]tyrosine into p-[14C]hydroxyphenylpyruvate.
GO:0006572 L-tyrosine catabolic process	IDA PMID:7999802 Cloning and expression of human tyrosine aminotransferase cD...	ACCEPT	Summary: Direct experimental annotation to tyrosine catabolism, based on the demonstrated conversion of tyrosine to 4-hydroxyphenylpyruvate by the human enzyme (the first, committed step of tyrosine breakdown). Reason: Core biological process, directly supported by expression of functional human TAT that specifically transaminates tyrosine. Supporting Evidence: PMID:7999802 The expressed protein catalyzed specifically the conversion of L-[14C]tyrosine into p-[14C]hydroxyphenylpyruvate.
GO:0005575 cellular_component	ND GO_REF:0000015	REMOVE	Summary: Root cellular-component annotation with No Data evidence code, a placeholder indicating no specific component was curated by this source. Superseded by the specific cytosol annotations (TAS and IEA). Reason: This is an uninformative ND root-node placeholder that is superseded by the experimentally/authoritatively supported cytosol location annotations. It conveys no information and should not be retained.
GO:0004838 L-tyrosine:2-oxoglutarate transaminase activity	NAS PMID:1973834 Isolation and characterization of the human tyrosine aminotr...	ACCEPT	Summary: Non-traceable author statement of the core transaminase activity, from the paper characterizing the human TAT gene. Redundant with, and weaker than, the IDA/IBA/IEA support for the same term. Reason: Correct core molecular function; although the evidence code is NAS, the assignment is fully corroborated by the direct experimental (IDA) annotation and UniProt catalytic activity. Supporting Evidence: PMID:1973834 Isolation and characterization of the human tyrosine aminotransferase gene.

Gene Description

Existing Annotations Review

Core Functions

L-tyrosine:2-oxoglutarate transaminase (tyrosine aminotransferase), the PLP-dependent enzyme that catalyzes the first, committed step of L-tyrosine catabolism in the liver cytosol.

References

Deep Research

Falcon

📚 Additional Documentation

Notes

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