SLC1A4 (ASCT1/SATT) is a plasma-membrane, sodium-coupled obligate antiporter (exchanger) of small neutral amino acids, a member of the SLC1/dicarboxylate-amino-acid:cation symporter (DAACS) family that also contains the glutamate transporters (EAATs) and ASCT2. It mediates electroneutral homo- and hetero-exchange of L- and D-serine, L-alanine, L-threonine, L-cysteine and L-asparagine (and, more weakly, proline/4-hydroxyproline), coupled to inward co-transport of Na+, with negligible net amino acid flux; unlike the related EAATs it does not transport the acidic amino acids L-glutamate or L-aspartate, nor glutamine, and it does not couple to protons or counter-transport K+. Like other SLC1 members it also displays a substrate-gated, thermodynamically uncoupled anion conductance (permeability SCN- > NO3- > I- > Cl-). It is a homotrimeric multi-pass membrane protein that moves substrate by a one-gate elevator mechanism (transport domain formed by transmembrane helices 3, 6, 7 and 8 and the HP1/HP2 hairpins). It is broadly expressed, with highest levels in brain, muscle and pancreas. In the brain it is enriched in astrocytes, where it is central to L-serine/D-serine homeostasis: by exchanging L-serine and D-serine it supports the astrocyte-to-neuron serine shuttle that supplies neurons with L-serine for de novo D-serine synthesis and helps regulate extracellular D-serine, the co-agonist of synaptic NMDA receptors. Biallelic loss-of-function variants cause spastic tetraplegia, thin corpus callosum and progressive microcephaly (SPATCCM).
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005254 chloride channel activity | IDA PMID:8910405 ASCT-1 is a neutral amino acid exchanger with chloride chann... | KEEP AS NON CORE | Summary: ASCT1 displays a substrate-gated, thermodynamically uncoupled anion conductance, a property shared across the SLC1 family. This is a genuine but secondary activity, distinct from the coupled amino acid exchange that is the transporter's core function. Reason: Direct electrophysiology shows an uncoupled anion channel activated by substrate/Na+, with anion preference SCN- > NO3- > I- > Cl- (chloride is actually the least permeant of the tested anions). The activity is real but peripheral to the Na+-coupled neutral amino acid exchange that defines the protein, so it is retained as non-core. Supporting Evidence: PMID:8910405 thermodynamically uncoupled chloride conductance file:human/SLC1A4/SLC1A4-uniprot.txt |
| GO:0005313 L-glutamate transmembrane transporter activity | IBA GO_REF:0000033 | REMOVE | Summary: ASCT1 is not a glutamate transporter. This IBA is propagated from the broad SLC1 node (PANTHER:PTN000238242) whose experimentally characterized donors are glutamate transporters (EAATs: P43003/SLC1A3/EAAT1, P43004/SLC1A2/EAAT2, P43005/SLC1A1/EAAT3, P48664/EAAT5). ASCT1 sits in the distinct neutral-amino-acid subfamily that does not carry glutamate. Reason: Direct human experiment shows no glutamate transport by ASCT1, and the IBA node is at a SLC1 ancestor that includes the EAATs; the glutamate function was not inherited into the neutral-amino-acid (ASCT) branch (PANTHER:PTN002632762), where ASCT1 lies. Over-propagation from the wrong subfamily, not a lineage-specific loss worth recording. Propagation Review Root cause: PROPAGATION BAD Failure modes: WRONG ORTHOLOG OR PARALOG FUNCTIONAL DIVERGENCE Sources checked: PANTHER:PTN000238242 SUPPORTS SOURCE BUT NOT TARGET Ancestral SLC1 node combining EAAT (glutamate) and ASCT (neutral AA) members; glutamate transporter activity is genuine for the EAAT donors but does not apply to ASCT1. Supporting Evidence: PMID:8340364 did not induce the transport of radiolabeled L-cysteine, L-glutamate, or related dicarboxylates |
| GO:0005313 L-glutamate transmembrane transporter activity | TAS PMID:21757002 The nuclear receptor FXR regulates hepatic transport and met... | REMOVE | Summary: This TAS rests on an FXR / hepatic glutamine-glutamate metabolism study that does not demonstrate glutamate transport by ASCT1. Glutamate is not an ASCT1 substrate. Reason: PMID:21757002 concerns FXR-regulated hepatic glutamine/glutamate metabolism and does not establish that ASCT1 transports glutamate; direct human transport assays show ASCT1 does not carry glutamate or related dicarboxylates. Kept consistent with the other GO:0005313 row (also REMOVE). Supporting Evidence: PMID:8340364 did not induce the transport of radiolabeled L-cysteine, L-glutamate, or related dicarboxylates |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Bare protein-binding annotation from a PDZ-domain quantitative fragmentomics interactome; the partner (GRID2IP) binds the ASCT1 C-terminal class-I PDZ ligand. Uninformative as a molecular function. Reason: GO:0005515 conveys no specific molecular function. The interaction is via the ASCT1 C-terminal PDZ-binding motif and, while real, does not establish an informative activity for ASCT1; removed per the protein-binding policy (removal does not imply the interaction is false). |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Bare protein binding (MPDZ), a PDZ-motif interactor; uninformative MF. Reason: Uninformative generic binding via the ASCT1 C-terminal PDZ ligand; removed per the protein-binding policy without implying the MPDZ interaction is false. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Bare protein binding (DLG4/PSD-95), a PDZ-motif interactor; uninformative MF. Reason: Uninformative generic binding via the ASCT1 C-terminal PDZ ligand; removed per the protein-binding policy without implying the DLG4 interaction is false. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Bare protein binding (APBA1), a PDZ-motif interactor; uninformative MF. Reason: Uninformative generic binding via the ASCT1 C-terminal PDZ ligand; removed per the protein-binding policy without implying the APBA1 interaction is false. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Bare protein binding (TJP1/ZO-1), a PDZ-motif interactor; uninformative MF. Reason: Uninformative generic binding via the ASCT1 C-terminal PDZ ligand; removed per the protein-binding policy without implying the TJP1 interaction is false. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Bare protein binding (DLG1), a PDZ-motif interactor; uninformative MF. Reason: Uninformative generic binding via the ASCT1 C-terminal PDZ ligand; removed per the protein-binding policy without implying the DLG1 interaction is false. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Bare protein binding (IL16), a PDZ-motif interactor; uninformative MF. Reason: Uninformative generic binding via the ASCT1 C-terminal PDZ ligand; removed per the protein-binding policy without implying the IL16 interaction is false. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Bare protein binding (SCRIB), a PDZ-motif interactor; uninformative MF. Reason: Uninformative generic binding via the ASCT1 C-terminal PDZ ligand; removed per the protein-binding policy without implying the SCRIB interaction is false. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Bare protein binding (PDZK1), a PDZ-motif interactor; uninformative MF. Reason: Uninformative generic binding via the ASCT1 C-terminal PDZ ligand; removed per the protein-binding policy without implying the PDZK1 interaction is false. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Bare protein binding (FRMPD2), a PDZ-motif interactor; uninformative MF. Reason: Uninformative generic binding via the ASCT1 C-terminal PDZ ligand; removed per the protein-binding policy without implying the FRMPD2 interaction is false. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Bare protein binding (MAGI2), a PDZ-motif interactor; uninformative MF. Reason: Uninformative generic binding via the ASCT1 C-terminal PDZ ligand; removed per the protein-binding policy without implying the MAGI2 interaction is false. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Bare protein binding (NHERF4/PDZD3), a PDZ-motif interactor; uninformative MF. Reason: Uninformative generic binding via the ASCT1 C-terminal PDZ ligand; removed per the protein-binding policy without implying the NHERF4 interaction is false. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Bare protein binding (LNX2), a PDZ-motif interactor; uninformative MF. Reason: Uninformative generic binding via the ASCT1 C-terminal PDZ ligand; removed per the protein-binding policy without implying the LNX2 interaction is false. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Bare protein binding (PATJ/INADL), a PDZ-motif interactor; uninformative MF. Reason: Uninformative generic binding via the ASCT1 C-terminal PDZ ligand; removed per the protein-binding policy without implying the PATJ interaction is false. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Bare protein binding (LNX1), a PDZ-motif interactor; uninformative MF. Reason: Uninformative generic binding via the ASCT1 C-terminal PDZ ligand; removed per the protein-binding policy without implying the LNX1 interaction is false. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Bare protein binding (DLG3), a PDZ-motif interactor; uninformative MF. Reason: Uninformative generic binding via the ASCT1 C-terminal PDZ ligand; removed per the protein-binding policy without implying the DLG3 interaction is false. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Bare protein binding (MAGI1), a PDZ-motif interactor; uninformative MF. Reason: Uninformative generic binding via the ASCT1 C-terminal PDZ ligand; removed per the protein-binding policy without implying the MAGI1 interaction is false. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Bare protein binding (APBA2), a PDZ-motif interactor; uninformative MF. Reason: Uninformative generic binding via the ASCT1 C-terminal PDZ ligand; removed per the protein-binding policy without implying the APBA2 interaction is false. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Bare protein binding (GRIP2), a PDZ-motif interactor; uninformative MF. Reason: Uninformative generic binding via the ASCT1 C-terminal PDZ ligand; removed per the protein-binding policy without implying the GRIP2 interaction is false. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Bare protein binding (GRIP1), a PDZ-motif interactor; uninformative MF. Reason: Uninformative generic binding via the ASCT1 C-terminal PDZ ligand; removed per the protein-binding policy without implying the GRIP1 interaction is false. |
| GO:0005813 centrosome | IDA GO_REF:0000052 | MARK AS OVER ANNOTATED | Summary: Single-antibody HPA immunofluorescence localization to the centrosome. Biologically implausible for a polytopic plasma-membrane transporter and not corroborated by any other method. Reason: ASCT1 is a multi-pass plasma-membrane protein; centrosomal localization from a single immunofluorescence screen is most likely antibody cross-reactivity or a staining artifact and conflicts with the established cell-surface topology. |
| GO:0005882 intermediate filament | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Intermediate-filament localization electronically transferred from the mouse ortholog (O35874). Implausible for an integral plasma-membrane transporter. Reason: A polytopic plasma-membrane transporter is not an intermediate-filament component; this is a propagated annotation that most likely reflects co-fractionation or a questionable source annotation on the mouse ortholog. |
| GO:0005882 intermediate filament | ISS GO_REF:0000024 | MARK AS OVER ANNOTATED | Summary: ISS transfer of the same implausible intermediate-filament localization from mouse O35874. Reason: Same rationale as the IEA row: intermediate-filament localization is inconsistent with an integral membrane transporter and is not supported by direct evidence on the human protein. |
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: Plasma membrane is the correct and core site of ASCT1 action; the phylogenetic node for SLC1 membrane localization is sound, and ASCT1 itself appears among the WITH/FROM sources, consistent with direct experimental grounding on the target. Reason: ASCT1 is an integral plasma-membrane transporter active at the cell surface; the IBA is at the right level and is corroborated by direct human evidence (disease-variant functional assays confirm plasma-membrane expression). Supporting Evidence: PMID:26041762 the mutations did not affect the protein level at the plasma membrane but abolished or markedly |
| GO:0005886 plasma membrane | IC PMID:8910405 ASCT-1 is a neutral amino acid exchanger with chloride chann... | ACCEPT | Summary: Curator inference of plasma-membrane localization from demonstrated serine transport activity. Correct. Reason: Plasma-membrane localization logically follows from the demonstrated cell-surface amino acid exchange activity and is the core site of function. |
| GO:0005886 plasma membrane | IEA GO_REF:0000044 | ACCEPT | Summary: UniProt SubCell keyword mapping to plasma membrane. Correct and core. Reason: Consistent with the curated UniProt subcellular location (Cell membrane) and all direct evidence. Supporting Evidence: file:human/SLC1A4/SLC1A4-uniprot.txt Cell membrane |
| GO:0005886 plasma membrane | IMP PMID:26041762 Mutations in SLC1A4, encoding the brain serine transporter, ... | ACCEPT | Summary: Disease-variant functional study confirms ASCT1 is active at the plasma membrane (mutants traffic normally but lose transport). Reason: Direct evidence that the protein localizes to and functions at the plasma membrane. Supporting Evidence: PMID:26041762 the mutations did not affect the protein level at the plasma membrane but abolished or markedly |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-352347 | ACCEPT | Summary: Reactome plasma-membrane localization for SLC1A4-mediated amino acid exchange. Correct. Reason: Core site of function; consistent with all other evidence. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-352354 | ACCEPT | Summary: Reactome plasma-membrane localization for SLC1A4-mediated amino acid exchange. Correct. Reason: Core site of function; consistent with all other evidence. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-352364 | ACCEPT | Summary: Reactome plasma-membrane localization for SLC1A4-mediated amino acid exchange. Correct. Reason: Core site of function; consistent with all other evidence. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-352371 | ACCEPT | Summary: Reactome plasma-membrane localization for SLC1A4-mediated amino acid exchange. Correct. Reason: Core site of function; consistent with all other evidence. |
| GO:0006865 amino acid transport | TAS Reactome:R-HSA-352230 | TOO GENERAL | Summary: True but general parent process; specific neutral amino acid transport processes (serine, alanine, threonine) are asserted and accepted elsewhere in this review. Reason: The accepted specific processes (e.g. L-serine transport GO:0015825, L-alanine transport GO:0015808) entail this broad amino acid transport term, which adds no information. |
| GO:0009986 cell surface | HDA PMID:19581412 Quantitative proteomics identifies a Dab2/integrin module re... | KEEP AS NON CORE | Summary: High-throughput cell-surface proteomics; consistent with plasma-membrane localization. Reason: Cell-surface detection corroborates plasma-membrane residence but is less specific than the plasma-membrane annotations; retained as non-core. |
| GO:0015171 amino acid transmembrane transporter activity | TAS Reactome:R-HSA-352347 | TOO GENERAL | Summary: True but general transporter activity; the specific neutral amino acid transporter activities (serine, alanine, threonine, etc.) accepted here entail it. Reason: A broad parent of the specific accepted activities such as GO:0015194 L-serine and GO:0015180 L-alanine transmembrane transporter activity; uninformative at this level. |
| GO:0015171 amino acid transmembrane transporter activity | TAS Reactome:R-HSA-352354 | TOO GENERAL | Summary: True but general transporter activity, entailed by the specific accepted neutral amino acid activities. Reason: Broad parent of the specific accepted neutral amino acid transporter activities; uninformative. |
| GO:0015171 amino acid transmembrane transporter activity | TAS Reactome:R-HSA-352364 | TOO GENERAL | Summary: True but general transporter activity, entailed by the specific accepted neutral amino acid activities. Reason: Broad parent of the specific accepted neutral amino acid transporter activities; uninformative. |
| GO:0015171 amino acid transmembrane transporter activity | TAS Reactome:R-HSA-352371 | TOO GENERAL | Summary: True but general transporter activity, entailed by the specific accepted neutral amino acid activities. Reason: Broad parent of the specific accepted neutral amino acid transporter activities; uninformative. |
| GO:0015175 neutral L-amino acid transmembrane transporter activity | IEA GO_REF:0000107 | ACCEPT | Summary: Family/ortholog-level activity that accurately captures ASCT1 as a neutral amino acid transporter; well supported by direct substrate data. Reason: ASCT1 transports small neutral amino acids (serine, alanine, threonine, cysteine, asparagine); this term is correct and informative at the overall substrate-class level. Supporting Evidence: PMID:8101838 Superfusion of alanine, serine, and cysteine evoked sodium-dependent inward |
| GO:0015180 L-alanine transmembrane transporter activity | IBA GO_REF:0000033 | ACCEPT | Summary: Alanine transport is a core, experimentally established ASCT1 activity; the IBA is placed at the neutral-amino-acid subfamily node (PTN002632762) and ASCT1's own experimental annotation legitimately appears among the sources. Reason: Alanine is a canonical ASCT1 substrate (original clones and later studies); the IBA node placement in the ASCT subfamily is sound. Supporting Evidence: PMID:8101838 Superfusion of alanine, serine, and cysteine evoked sodium-dependent inward |
| GO:0015180 L-alanine transmembrane transporter activity | IDA PMID:8101838 Cloning and expression of a human neutral amino acid transpo... | ACCEPT | Summary: Direct demonstration of Na+-dependent alanine transport in oocytes. Core activity. Reason: Alanine evoked Na+-dependent currents in ASCT1-expressing oocytes. Supporting Evidence: PMID:8101838 Superfusion of alanine, serine, and cysteine evoked sodium-dependent inward |
| GO:0015180 L-alanine transmembrane transporter activity | IDA PMID:8340364 Cloning and expression of a novel Na(+)-dependent neutral am... | ACCEPT | Summary: Direct HeLa uptake of L-alanine by SATT/ASCT1. Core activity. Reason: Stereospecific Na+-dependent L-alanine uptake upon ASCT1 expression. Supporting Evidence: PMID:8340364 Expression of SATT cDNA in HeLa cells induced stereospecific uptake of L-serine, |
| GO:0015180 L-alanine transmembrane transporter activity | IDA PMID:8910405 ASCT-1 is a neutral amino acid exchanger with chloride chann... | ACCEPT | Summary: Alanine participates in ASCT1-mediated Na+-dependent neutral amino acid exchange. Core activity. Reason: ASCT1 mediates homo-/hetero-exchange of neutral amino acids including alanine. Supporting Evidence: PMID:8910405 ASCT-1 mediates only homo- and heteroexchange of amino acids and is insensitive |
| GO:0015180 L-alanine transmembrane transporter activity | IMP PMID:26041762 Mutations in SLC1A4, encoding the brain serine transporter, ... | ACCEPT | Summary: Disease-variant functional assays measure ASCT1-dependent L-alanine transport. Core activity. Reason: Pathogenic variants reduce/abolish L-alanine (and L-serine) transport, confirming the activity. Supporting Evidence: PMID:26041762 reduced L-serine transport for p.R457W and p.E256K mutations, respectively. |
| GO:0015183 L-aspartate transmembrane transporter activity | IBA GO_REF:0000033 | MARK AS OVER ANNOTATED | Summary: Aspartate (an acidic/dicarboxylate amino acid) is not an ASCT1 substrate; direct human data show no transport of glutamate or related dicarboxylates. Reason: ASCT1 is a neutral amino acid exchanger; dicarboxylate (aspartate) transport is a property of the EAAT branch, not of ASCT1. The node-level aspartate assignment overstates the substrate scope for this subfamily. Propagation Review Root cause: SOURCE WEAK OR INFERRED Failure modes: FUNCTIONAL DIVERGENCE Sources checked: PANTHER:PTN002632762 SOURCE WEAK OR INFERRED ASCT neutral-amino-acid subfamily node; the aspartate (dicarboxylate) assignment at this node is weakly grounded and contradicted by direct human data showing no dicarboxylate transport. Supporting Evidence: PMID:8340364 did not induce the transport of radiolabeled L-cysteine, L-glutamate, or related dicarboxylates |
| GO:0015183 L-aspartate transmembrane transporter activity | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Aspartate transporter activity transferred from mouse ortholog; not supported for ASCT1. Reason: Dicarboxylate transport is not an ASCT1 function; contradicted by direct human data showing no dicarboxylate transport. Supporting Evidence: PMID:8340364 did not induce the transport of radiolabeled L-cysteine, L-glutamate, or related dicarboxylates |
| GO:0015183 L-aspartate transmembrane transporter activity | ISS GO_REF:0000024 | MARK AS OVER ANNOTATED | Summary: ISS transfer of aspartate activity from mouse O35874; not an ASCT1 substrate. Reason: Same rationale; aspartate (dicarboxylate) is not transported by ASCT1. Supporting Evidence: PMID:8340364 did not induce the transport of radiolabeled L-cysteine, L-glutamate, or related dicarboxylates |
| GO:0015184 L-cystine transmembrane transporter activity | IDA PMID:8101838 Cloning and expression of a human neutral amino acid transpo... | MODIFY | Summary: The assayed substrate was L-cysteine (the monomer), not L-cystine (the oxidized disulfide dimer, which is a system xc-/SLC7A11 substrate). The term should name L-cysteine. Reason: ASCT1 transports L-cysteine (UniProt curates L-cysteine exchange, Rhea:RHEA:84347; original clone showed cysteine-evoked currents). L-cystine (dimer) is not an ASCT1 substrate, so the activity should be re-pointed to the cysteine term. Proposed replacements: L-cysteine transmembrane transporter activity Supporting Evidence: PMID:8101838 Superfusion of alanine, serine, and cysteine evoked sodium-dependent inward |
| GO:0015184 L-cystine transmembrane transporter activity | IDA NOT PMID:8340364 Cloning and expression of a novel Na(+)-dependent neutral am... | ACCEPT | Summary: Negated annotation to the L-cystine (disulfide dimer) term. The curated NOT derives from PMID:8340364, which assayed the monomer L-cysteine (not the dimer L-cystine) and reported no uptake in HeLa; UniProt mapped this to the L-cystine term. L-cystine itself is genuinely not an ASCT1 substrate (it is carried by system xc-/SLC7A11), so the negation is literally correct for the term as written. Reason: L-cystine (the oxidized dimer) is not an ASCT1 substrate, so a NOT annotation to the L-cystine term stands as a true statement. The positive cystine rows are re-pointed (MODIFY) to the L-cysteine term because the underlying experiments and UniProt's curated catalytic activity concern L-cysteine (monomer). The source record's NOT, however, rests on a cysteine-negative result mapped to a cystine term: this cystine-vs-cysteine term mis-mapping is recorded in source_defects, and the genuine literature conflict over whether L-cysteine is transported is captured in the finding_review on PMID:8340364. Supporting Evidence: PMID:8340364 did not induce the transport of radiolabeled L-cysteine, L-glutamate, or related dicarboxylates |
| GO:0015184 L-cystine transmembrane transporter activity | IDA PMID:8910405 ASCT-1 is a neutral amino acid exchanger with chloride chann... | MODIFY | Summary: Exchange assays and UniProt catalytic activity establish L-cysteine (monomer) as an ASCT1 substrate; the term should name L-cysteine, not L-cystine. Reason: UniProt curates a L-cysteine exchange reaction (Rhea:RHEA:84347) from this study; L-cystine (dimer) is not an ASCT1 substrate. Re-point to the cysteine term. Proposed replacements: L-cysteine transmembrane transporter activity Supporting Evidence: file:human/SLC1A4/SLC1A4-uniprot.txt L-cysteine(out) + L-alanine(in) + Na(+)(out) |
| GO:0015193 L-proline transmembrane transporter activity | IDA PMID:14502423 Transport of proline and hydroxyproline by the neutral amino... | KEEP AS NON CORE | Summary: ASCT1 transports L-proline (Na+-dependent, saturable), but at lower affinity than the canonical neutral amino acid substrates; a genuine but peripheral activity. Reason: Direct oocyte uptake demonstrates proline transport (K0.5 ~704 uM, about 3x higher than alanine), a lower-affinity secondary substrate rather than a core physiological function. Supporting Evidence: PMID:14502423 demonstrates for the first time the ability of ASCT1 |
| GO:0015194 L-serine transmembrane transporter activity | IBA GO_REF:0000033 | ACCEPT | Summary: Serine transport is the central, defining ASCT1 activity; the IBA sits at the ASCT subfamily node (PTN002632762) with ASCT1's own experimental annotation among the sources. Reason: Serine (L- and D-) exchange is the best-characterized ASCT1 function and underlies its brain serine-shuttle role; node placement is correct. Supporting Evidence: PMID:8101838 Superfusion of alanine, serine, and cysteine evoked sodium-dependent inward |
| GO:0015194 L-serine transmembrane transporter activity | IDA PMID:8101838 Cloning and expression of a human neutral amino acid transpo... | ACCEPT | Summary: Direct Na+-dependent L-serine transport in oocytes. Core activity. Reason: Serine evoked Na+-dependent currents in ASCT1-expressing oocytes. Supporting Evidence: PMID:8101838 Superfusion of alanine, serine, and cysteine evoked sodium-dependent inward |
| GO:0015194 L-serine transmembrane transporter activity | IDA PMID:8340364 Cloning and expression of a novel Na(+)-dependent neutral am... | ACCEPT | Summary: Direct HeLa uptake of L-serine by SATT/ASCT1. Core activity. Reason: Stereospecific Na+-dependent L-serine uptake upon ASCT1 expression. Supporting Evidence: PMID:8340364 Expression of SATT cDNA in HeLa cells induced stereospecific uptake of L-serine, |
| GO:0015194 L-serine transmembrane transporter activity | IDA PMID:8910405 ASCT-1 is a neutral amino acid exchanger with chloride chann... | ACCEPT | Summary: Serine is a core substrate of ASCT1-mediated neutral amino acid exchange. Core activity. Reason: ASCT1 mediates Na+-dependent homo-/hetero-exchange of neutral amino acids including serine. Supporting Evidence: PMID:8910405 ASCT-1 mediates only homo- and heteroexchange of amino acids and is insensitive |
| GO:0015194 L-serine transmembrane transporter activity | IEA GO_REF:0000120 | ACCEPT | Summary: Electronic/ortholog support for the core L-serine transporter activity. Correct. Reason: Consistent with abundant direct human evidence for serine transport. |
| GO:0015194 L-serine transmembrane transporter activity | IMP PMID:26041762 Mutations in SLC1A4, encoding the brain serine transporter, ... | ACCEPT | Summary: Disease-variant functional assays directly measure ASCT1-dependent L-serine transport. Core activity. Reason: Pathogenic variants abolish or markedly reduce L-serine transport, confirming the activity. Supporting Evidence: PMID:26041762 reduced L-serine transport for p.R457W and p.E256K mutations, respectively. |
| GO:0015195 L-threonine transmembrane transporter activity | IBA GO_REF:0000033 | ACCEPT | Summary: Threonine is an established ASCT1 substrate; IBA at the ASCT subfamily node with target self-support. Reason: Threonine uptake demonstrated directly; node placement in the ASCT subfamily is sound. Supporting Evidence: PMID:8340364 Expression of SATT cDNA in HeLa cells induced stereospecific uptake of L-serine, |
| GO:0015195 L-threonine transmembrane transporter activity | IDA PMID:8340364 Cloning and expression of a novel Na(+)-dependent neutral am... | ACCEPT | Summary: Direct HeLa uptake of L-threonine by SATT/ASCT1. Reason: Stereospecific Na+-dependent L-threonine uptake upon ASCT1 expression. Supporting Evidence: PMID:8340364 Expression of SATT cDNA in HeLa cells induced stereospecific uptake of L-serine, |
| GO:0015293 symporter activity | IEA GO_REF:0000002 | MODIFY | Summary: Wrong transport mode. The InterPro DAACS family name contains "symporter" (true of the EAATs), but ASCT1 is an obligate antiporter/exchanger that mediates negligible net flux. Reason: ASCT1 is a Na+-coupled neutral amino acid exchanger (UniProt keyword Antiport; electroneutral exchange with negligible net flux), not a symporter that produces net cotransport. This is a lateral transport-mode correction: the family-level InterPro mapping assigns the wrong mechanism to this member, so the term is re-pointed to antiporter activity rather than removed. Proposed replacements: antiporter activity Supporting Evidence: PMID:8910405 an electroneutral exchanger that mediates negligible net amino acid flux PMID:34630942 perform the obligatory exchange of the amino acid pools |
| GO:0015808 L-alanine transport | IDA PMID:8101838 Cloning and expression of a human neutral amino acid transpo... | ACCEPT | Summary: Alanine transport process directly demonstrated. Core. Reason: Na+-dependent alanine transport shown in ASCT1-expressing oocytes. Supporting Evidence: PMID:8101838 Superfusion of alanine, serine, and cysteine evoked sodium-dependent inward |
| GO:0015808 L-alanine transport | IDA PMID:8340364 Cloning and expression of a novel Na(+)-dependent neutral am... | ACCEPT | Summary: Alanine transport process directly demonstrated (HeLa uptake). Core. Reason: Stereospecific Na+-dependent L-alanine uptake upon ASCT1 expression. Supporting Evidence: PMID:8340364 Expression of SATT cDNA in HeLa cells induced stereospecific uptake of L-serine, |
| GO:0015808 L-alanine transport | IDA PMID:8910405 ASCT-1 is a neutral amino acid exchanger with chloride chann... | ACCEPT | Summary: Alanine participates in ASCT1-mediated neutral amino acid exchange. Core. Reason: ASCT1 mediates homo-/hetero-exchange of neutral amino acids including alanine. Supporting Evidence: PMID:8910405 ASCT-1 mediates only homo- and heteroexchange of amino acids and is insensitive |
| GO:0015811 L-cystine transport | IDA PMID:8101838 Cloning and expression of a human neutral amino acid transpo... | MODIFY | Summary: The transported species is L-cysteine (monomer), not L-cystine (dimer); the process term should name L-cysteine transport. Reason: ASCT1 transports L-cysteine; L-cystine (the disulfide dimer) is a system xc- substrate, not an ASCT1 substrate. Re-point to the cysteine transport process. Proposed replacements: L-cysteine transport Supporting Evidence: PMID:8101838 Superfusion of alanine, serine, and cysteine evoked sodium-dependent inward |
| GO:0015811 L-cystine transport | IDA NOT PMID:8340364 Cloning and expression of a novel Na(+)-dependent neutral am... | ACCEPT | Summary: Negated annotation to the L-cystine (disulfide dimer) transport term. The curated NOT derives from PMID:8340364, which assayed the monomer L-cysteine, not L-cystine, and was mapped to the cystine term. L-cystine itself is not an ASCT1 substrate (it is carried by system xc-/SLC7A11), so the negation is literally correct for the term as written. Reason: The NOT annotation to L-cystine transport stands as a true statement for the dimer. The positive rows are re-pointed (MODIFY) to L-cysteine transport because the experiments and UniProt's curated catalytic activity concern L-cysteine (monomer). The source record's NOT rests on a cysteine-negative result mapped to a cystine term: the term mis-mapping is recorded in source_defects, and the conflict over whether L-cysteine is transported is captured in the finding_review on PMID:8340364. Supporting Evidence: PMID:8340364 did not induce the transport of radiolabeled L-cysteine, L-glutamate, or related dicarboxylates |
| GO:0015811 L-cystine transport | IDA PMID:8910405 ASCT-1 is a neutral amino acid exchanger with chloride chann... | MODIFY | Summary: L-cysteine (monomer) is exchanged by ASCT1; term should name L-cysteine transport. Reason: UniProt curates a L-cysteine exchange reaction from this study (Rhea:RHEA:84347); cystine (dimer) is not an ASCT1 substrate. Re-point to the cysteine transport process. Proposed replacements: L-cysteine transport Supporting Evidence: file:human/SLC1A4/SLC1A4-uniprot.txt L-cysteine(out) + L-alanine(in) + Na(+)(out) |
| GO:0015813 L-glutamate transmembrane transport | IBA GO_REF:0000033 | REMOVE | Summary: Glutamate transport is a function of the EAAT branch of SLC1, not of ASCT1. This IBA is propagated from an ancestral node (PTN002278999) seeded by EAAT donors. Reason: ASCT1 does not transport glutamate (direct human data). The node combines EAAT and ASCT functions; glutamate transport was not inherited into the neutral-amino-acid branch where ASCT1 lies. Over-propagation from the wrong subfamily. Kept consistent with the GO:0005313 glutamate transporter activity rows (also REMOVE). Propagation Review Root cause: PROPAGATION BAD Failure modes: WRONG ORTHOLOG OR PARALOG FUNCTIONAL DIVERGENCE Sources checked: PANTHER:PTN002278999 SUPPORTS SOURCE BUT NOT TARGET Ancestral SLC1 node whose glutamate-transport function belongs to the EAAT descendants, not ASCT1. Supporting Evidence: PMID:8340364 did not induce the transport of radiolabeled L-cysteine, L-glutamate, or related dicarboxylates |
| GO:0015824 proline transport | IDA PMID:14502423 Transport of proline and hydroxyproline by the neutral amino... | KEEP AS NON CORE | Summary: ASCT1 transports proline (lower affinity); genuine but peripheral process. Reason: Direct oocyte uptake demonstrates Na+-dependent proline transport, a lower-affinity secondary substrate. Supporting Evidence: PMID:14502423 demonstrates for the first time the ability of ASCT1 |
| GO:0015825 L-serine transport | IBA GO_REF:0000033 | ACCEPT | Summary: Serine transport is the core ASCT1 process; IBA at the ASCT subfamily node with target self-support. Reason: Best-characterized ASCT1 process, underlying the brain serine shuttle; node placement correct. Supporting Evidence: PMID:26041762 The data underscore that ASCT1 is essential in |
| GO:0015825 L-serine transport | IDA PMID:8101838 Cloning and expression of a human neutral amino acid transpo... | ACCEPT | Summary: Direct Na+-dependent L-serine transport. Core. Reason: Serine transport demonstrated directly in ASCT1-expressing oocytes. Supporting Evidence: PMID:8101838 Superfusion of alanine, serine, and cysteine evoked sodium-dependent inward |
| GO:0015825 L-serine transport | IDA PMID:8340364 Cloning and expression of a novel Na(+)-dependent neutral am... | ACCEPT | Summary: Direct HeLa uptake of L-serine. Core. Reason: Stereospecific Na+-dependent L-serine uptake upon ASCT1 expression. Supporting Evidence: PMID:8340364 Expression of SATT cDNA in HeLa cells induced stereospecific uptake of L-serine, |
| GO:0015825 L-serine transport | IDA PMID:8910405 ASCT-1 is a neutral amino acid exchanger with chloride chann... | ACCEPT | Summary: Serine is a core substrate of ASCT1-mediated exchange. Core. Reason: ASCT1 mediates Na+-dependent neutral amino acid exchange including serine. Supporting Evidence: PMID:8910405 ASCT-1 mediates only homo- and heteroexchange of amino acids and is insensitive |
| GO:0015825 L-serine transport | IEA GO_REF:0000107 | ACCEPT | Summary: Ortholog-based electronic support for the core L-serine transport process. Correct. Reason: Consistent with abundant direct human evidence for serine transport. |
| GO:0015826 threonine transport | IDA PMID:8340364 Cloning and expression of a novel Na(+)-dependent neutral am... | ACCEPT | Summary: Direct HeLa uptake of L-threonine. Genuine ASCT1 process. Reason: Stereospecific Na+-dependent L-threonine uptake upon ASCT1 expression. Supporting Evidence: PMID:8340364 Expression of SATT cDNA in HeLa cells induced stereospecific uptake of L-serine, |
| GO:0016020 membrane | HDA PMID:19946888 Defining the membrane proteome of NK cells. | MODIFY | Summary: Generic membrane localization from membrane proteomics; the specific compartment is the plasma membrane. Reason: ASCT1 is an integral plasma-membrane transporter; the generic "membrane" term should be refined to plasma membrane (transporter convention), which is directly supported. Proposed replacements: plasma membrane |
| GO:0016020 membrane | IDA PMID:26041762 Mutations in SLC1A4, encoding the brain serine transporter, ... | MODIFY | Summary: Generic membrane localization; refine to plasma membrane, where ASCT1 is shown to reside and function. Reason: Disease study shows ASCT1 at the plasma membrane; refine the generic term to plasma membrane. Proposed replacements: plasma membrane Supporting Evidence: PMID:26041762 the mutations did not affect the protein level at the plasma membrane but abolished or markedly |
| GO:0016020 membrane | IEA GO_REF:0000002 | MODIFY | Summary: Generic membrane localization from InterPro family mapping; refine to plasma membrane. Reason: The specific compartment for ASCT1 is the plasma membrane. Proposed replacements: plasma membrane |
| GO:0016020 membrane | NAS PMID:8101838 Cloning and expression of a human neutral amino acid transpo... | MODIFY | Summary: Generic membrane localization asserted in the cloning paper; refine to plasma membrane. Reason: ASCT1 functions as an integral plasma-membrane transporter; refine the generic term. Proposed replacements: plasma membrane |
| GO:0030425 dendrite | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Neuronal dendrite localization transferred from rodent ortholog; plausible given neuronal expression but non-core. Reason: ASCT1 is expressed in neurons as well as astrocytes; a dendritic pool is plausible but the core functional location is the plasma membrane generally, so this is retained as non-core. |
| GO:0033162 melanosome membrane | EXP PMID:17081065 Proteomic and bioinformatic characterization of the biogenes... | KEEP AS NON CORE | Summary: Identified by mass spectrometry in melanosome fractions (stages I-IV); a non-core localization. Reason: Melanosome-fraction proteomics detected ASCT1; melanosomes are lysosome-related organelles and a minor pool is plausible, but this is peripheral to the transporter's core plasma-membrane function. |
| GO:0033162 melanosome membrane | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: UniProt SubCell mapping reflecting the same melanosome proteomics finding; non-core. Reason: Mirrors the melanosome-fraction MS evidence; retained as a non-core localization. |
| GO:0034589 hydroxyproline transport | IDA PMID:14502423 Transport of proline and hydroxyproline by the neutral amino... | KEEP AS NON CORE | Summary: ASCT1 transports trans-4-hydroxy-L-proline (high affinity, K0.5 ~33 uM); a genuine but peripheral process. Reason: Direct oocyte uptake demonstrates hydroxyproline transport; although high-affinity, this is a minor/peripheral physiological role rather than a core function. Supporting Evidence: PMID:14502423 K(0.5) was 33.2 +/- 4.3 microM |
| GO:0034590 L-hydroxyproline transmembrane transporter activity | IDA PMID:14502423 Transport of proline and hydroxyproline by the neutral amino... | KEEP AS NON CORE | Summary: Direct demonstration of hydroxyproline transport activity; genuine but peripheral. Reason: Hydroxyproline is transported by ASCT1 (high affinity), but as a secondary substrate rather than a core physiological activity. Supporting Evidence: PMID:14502423 demonstrates for the first time the ability of ASCT1 |
| GO:0035249 synaptic transmission, glutamatergic | NAS PMID:16897601 Changes in region- and cell type-specific expression pattern... | KEEP AS NON CORE | Summary: ASCT1 modulates glutamatergic (NMDA) transmission indirectly, via its role in L-serine/ D-serine homeostasis (D-serine is the NMDA co-agonist). The supporting paper is an expression-correlation study in psychiatric disorders. Reason: ASCT1 does not itself execute synaptic transmission; its connection to glutamatergic transmission is through supplying serine for D-serine synthesis. A real but indirect, non-core role. Supporting Evidence: PMID:16897601 The altered expression of ASCT-1 in neurons and astrocytes |
| GO:0035524 proline transmembrane transport | IEA GO_REF:0000108 | KEEP AS NON CORE | Summary: Logical-inference counterpart of the proline transporter activity; genuine but peripheral. Reason: Follows from the demonstrated (lower-affinity) proline transporter activity; consistent but peripheral to the core neutral amino acid exchange. Supporting Evidence: PMID:14502423 demonstrates for the first time the ability of ASCT1 |
| GO:0043025 neuronal cell body | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Neuronal cell-body localization transferred from rodent ortholog; plausible, non-core. Reason: ASCT1 is expressed in neurons; a somatic pool is plausible but peripheral to the core plasma-membrane function. |
| GO:0045202 synapse | IEA GO_REF:0000108 | KEEP AS NON CORE | Summary: Synapse localization inferred from the glutamatergic-transmission annotation; plausible but non-core/indirect. Reason: Derived by inter-ontology inference from the (indirect) glutamatergic-transmission term; ASCT1 acts at/near excitatory synapses in the serine shuttle, so a synaptic pool is plausible but peripheral. |
| GO:0050890 cognition | IMP PMID:16897601 Changes in region- and cell type-specific expression pattern... | KEEP AS NON CORE | Summary: ASCT1 loss affects cognition (intellectual disability is a hallmark of SPATCCM), via its role in brain serine/D-serine supply. A physiological, non-core role. Reason: Human loss-of-function causes severe intellectual disability, establishing necessity for normal cognition; but ASCT1's direct function is amino acid transport, so cognition is a downstream, non-core process. Supporting Evidence: PMID:26041762 The data underscore that ASCT1 is essential in |
| GO:0070062 extracellular exosome | HDA PMID:20458337 MHC class II-associated proteins in B-cell exosomes and pote... | KEEP AS NON CORE | Summary: Detected in exosome proteomics; common for plasma-membrane proteins, non-core. Reason: Membrane proteins are frequently recovered in exosome preparations; this reflects membrane trafficking rather than a core functional location. |
| GO:0090461 intracellular glutamate homeostasis | IEA GO_REF:0000117 | MARK AS OVER ANNOTATED | Summary: ASCT1 does not transport glutamate, so a direct role in glutamate homeostasis is not supported; this ARBA-derived term stems from the glutamate-transporter mis-classification. Reason: Unvetted ARBA association; glutamate is not an ASCT1 substrate, so an intracellular glutamate-homeostasis role is an over-annotation inherited from the EAAT branch. Supporting Evidence: PMID:8340364 did not induce the transport of radiolabeled L-cysteine, L-glutamate, or related dicarboxylates |
| GO:0090461 intracellular glutamate homeostasis | TAS PMID:21757002 The nuclear receptor FXR regulates hepatic transport and met... | MARK AS OVER ANNOTATED | Summary: TAS from an FXR/hepatic glutamate-metabolism paper; does not establish an ASCT1 role in glutamate homeostasis, and ASCT1 does not transport glutamate. Reason: The cited study concerns FXR regulation of hepatic glutamine/glutamate metabolism, not an ASCT1-mediated glutamate-homeostasis function; over-annotation. Kept consistent with the ARBA GO:0090461 row. |
| GO:0098657 import into cell | IEA GO_REF:0000117 | TOO GENERAL | Summary: True but general import process; the specific accepted imports (L-serine and L-alanine import across the plasma membrane) entail it. Reason: Generic "import into cell" is entailed by the accepted specific terms GO:1903812 (L-serine import) and GO:1904273 (L-alanine import); uninformative at this level. (ASCT1 imports are exchange-coupled rather than net import.) |
| GO:0098712 L-glutamate import across plasma membrane | TAS PMID:21757002 The nuclear receptor FXR regulates hepatic transport and met... | REMOVE | Summary: Glutamate is not an ASCT1 substrate; the FXR/hepatic metabolism paper does not show glutamate import by ASCT1. Reason: ASCT1 does not transport glutamate (direct human data); PMID:21757002 does not establish glutamate import by ASCT1. Consistent with the other glutamate rows (REMOVE). Supporting Evidence: PMID:8340364 did not induce the transport of radiolabeled L-cysteine, L-glutamate, or related dicarboxylates |
| GO:0140009 L-aspartate import across plasma membrane | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Aspartate (dicarboxylate) is not an ASCT1 substrate; transferred from mouse ortholog. Reason: Dicarboxylate import is an EAAT-branch function, not ASCT1; contradicted by direct human data showing no dicarboxylate transport. Supporting Evidence: PMID:8340364 did not induce the transport of radiolabeled L-cysteine, L-glutamate, or related dicarboxylates |
| GO:0140009 L-aspartate import across plasma membrane | ISS GO_REF:0000024 | MARK AS OVER ANNOTATED | Summary: ISS transfer of aspartate import from mouse O35874; not an ASCT1 function. Reason: Same rationale; aspartate is not transported by ASCT1. Supporting Evidence: PMID:8340364 did not induce the transport of radiolabeled L-cysteine, L-glutamate, or related dicarboxylates |
| GO:0150104 transport across blood-brain barrier | NAS PMID:26590417 Establishment and Dysfunction of the Blood-Brain Barrier. | MARK AS OVER ANNOTATED | Summary: NAS from a general blood-brain-barrier review that does not establish a specific ASCT1 BBB-transport role. ASCT1 is an obligate exchanger (no net flux), and brain L-serine is synthesized in situ because of poor BBB permeability. Reason: A net transport role across the BBB is mechanistically implausible for an electroneutral exchanger, and the literature indicates brain serine is made locally rather than imported across the BBB; the NAS rests on generic review text, not ASCT1-specific BBB evidence. Supporting Evidence: PMID:26041762 within the brain because of its poor permeability by the blood-brain barrier. |
| GO:0150104 transport across blood-brain barrier | NAS PMID:30280653 Blood-Brain Barrier: From Physiology to Disease and Back. | MARK AS OVER ANNOTATED | Summary: NAS from a second general BBB review; same concerns as the other GO:0150104 row. Reason: Generic BBB-review support; ASCT1's obligate-exchange mechanism and the in-brain synthesis of serine argue against a net BBB-transport function. Supporting Evidence: PMID:26041762 within the brain because of its poor permeability by the blood-brain barrier. |
| GO:1902476 chloride transmembrane transport | IEA GO_REF:0000108 | KEEP AS NON CORE | Summary: Follows from the substrate-gated uncoupled anion conductance; genuine but non-core (chloride is the least permeant of the tested anions). Reason: Consistent with the chloride-channel activity, which is a real but secondary property of ASCT1; retained as non-core like its parent activity. Supporting Evidence: PMID:8910405 thermodynamically uncoupled chloride conductance |
| GO:1903812 L-serine import across plasma membrane | IMP PMID:26041762 Mutations in SLC1A4, encoding the brain serine transporter, ... | ACCEPT | Summary: Disease-variant functional assays establish ASCT1-dependent L-serine import at the plasma membrane (exchange-coupled). Core to the brain serine shuttle. Reason: Pathogenic variants abolish/markedly reduce L-serine uptake; ASCT1 imports L-serine into cells (coupled to counter-substrate efflux) as part of its core serine-homeostasis role. Supporting Evidence: PMID:26041762 reduced L-serine transport for p.R457W and p.E256K mutations, respectively. |
| GO:1904273 L-alanine import across plasma membrane | IMP PMID:26041762 Mutations in SLC1A4, encoding the brain serine transporter, ... | ACCEPT | Summary: Disease-variant functional assays establish ASCT1-dependent L-alanine import at the plasma membrane. Reason: Pathogenic variants reduce L-alanine uptake; ASCT1 imports L-alanine (exchange-coupled) as part of neutral amino acid homeostasis. Supporting Evidence: PMID:26041762 reduced L-serine transport for p.R457W and p.E256K mutations, respectively. |
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