ASNSD1 (also called NS3TP1) is a protein with an N-terminal glutamine amidotransferase type-2 domain and a C-terminal asparagine synthetase domain, related to asparagine synthetase; whether it has amidotransferase or synthetase activity is unknown. It is most highly expressed in skeletal muscle, and mice lacking it develop a progressive degenerative myopathy with severe sarcopenia and replacement of muscle by fat. Its C-terminal class I PDZ-binding motif binds many PDZ domains in phage-display and quantitative fragmentomics screens. The ASNSD1 mRNA also encodes, from an upstream open reading frame, a separate microprotein (ASDURF) that is a subunit of the PAQosome chaperone; that activity belongs to ASDURF, not to the ASNSD1 protein.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003674 molecular_function | ND GO_REF:0000015 | REMOVE | Summary: Molecular function (ND). Superseded: PDZ-motif screens give ASNSD1 a specific, if peptide-level, molecular function (PDZ domain binding, via the MODIFY rows). Its catalytic potential (glutamine amidotransferase and asparagine synthetase domains) remains untested. The no-data root statement no longer holds, so the row is removed. Reason: [PMID:36115835 "Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer."] [file:human/ASNSD1/ASNSD1-uniprot.txt "FT /note="Glutamine amidotransferase type-2""] NO_DATA re-check: The review refines the human high-throughput IPIs (PMID:36115835) to PDZ domain binding, an informative activity from literature on this gene product. Supporting Evidence: PMID:36115835 Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer. file:human/ASNSD1/ASNSD1-uniprot.txt FT /note="Glutamine amidotransferase type-2" |
| GO:0005515 protein binding | IPI PMID:30126976 Proteome-wide analysis of phospho-regulated PDZ domain inter... | MODIFY | Summary: Protein binding (IPI) with SNTB1, from a phospho-regulated PDZ interaction screen. SNTB1 is a PDZ-domain protein, and the assay measured binding of the ASNSD1 C-terminal peptide, which ends in a class I PDZ-binding motif (T-x-L). The evidence supports the more informative term PDZ domain binding, as for the equivalent NRXN3 rows from the same screen. This rewrite does not imply that each screen-detected partner is physiologically relevant. Reason: Bare protein binding is uninformative; the partner is a PDZ protein and the assay measures PDZ-PBM binding. [PMID:30126976 "We computationally designed an oligonucleotide library encoding human C-terminal peptides containing known or predicted Ser/Thr phosphosites and phosphomimetic variants thereof."] Proposed replacements: PDZ domain binding Supporting Evidence: PMID:30126976 We computationally designed an oligonucleotide library encoding human C-terminal peptides containing known or predicted Ser/Thr phosphosites and phosphomimetic variants thereof. |
| GO:0005515 protein binding | IPI PMID:30126976 Proteome-wide analysis of phospho-regulated PDZ domain inter... | MODIFY | Summary: Protein binding (IPI) with SCRIB, from a phospho-regulated PDZ interaction screen. SCRIB is a PDZ-domain protein, and the assay measured binding of the ASNSD1 C-terminal peptide, which ends in a class I PDZ-binding motif (T-x-L). The evidence supports the more informative term PDZ domain binding, as for the equivalent NRXN3 rows from the same screen. This rewrite does not imply that each screen-detected partner is physiologically relevant. Reason: Bare protein binding is uninformative; the partner is a PDZ protein and the assay measures PDZ-PBM binding. [PMID:30126976 "We computationally designed an oligonucleotide library encoding human C-terminal peptides containing known or predicted Ser/Thr phosphosites and phosphomimetic variants thereof."] Proposed replacements: PDZ domain binding Supporting Evidence: PMID:30126976 We computationally designed an oligonucleotide library encoding human C-terminal peptides containing known or predicted Ser/Thr phosphosites and phosphomimetic variants thereof. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Protein binding (IPI) with PDZK1, from the BioPlex dual proteome-scale network (affinity purification, not a PDZ-motif assay). Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Protein binding (IPI) with GRID2IP, from a quantitative PDZ-binding-motif fragmentomics screen. GRID2IP is a PDZ-domain protein, and the assay measured binding of the ASNSD1 C-terminal peptide, which ends in a class I PDZ-binding motif (T-x-L). The evidence supports the more informative term PDZ domain binding, as for the equivalent NRXN3 rows from the same screen. This rewrite does not imply that each screen-detected partner is physiologically relevant. Reason: Bare protein binding is uninformative; the partner is a PDZ protein and the assay measures PDZ-PBM binding. [PMID:36115835 "Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer."] Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Protein binding (IPI) with MPDZ, from a quantitative PDZ-binding-motif fragmentomics screen. MPDZ is a PDZ-domain protein, and the assay measured binding of the ASNSD1 C-terminal peptide, which ends in a class I PDZ-binding motif (T-x-L). The evidence supports the more informative term PDZ domain binding, as for the equivalent NRXN3 rows from the same screen. This rewrite does not imply that each screen-detected partner is physiologically relevant. Reason: Bare protein binding is uninformative; the partner is a PDZ protein and the assay measures PDZ-PBM binding. [PMID:36115835 "Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer."] Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Protein binding (IPI) with DLG4, from a quantitative PDZ-binding-motif fragmentomics screen. DLG4 is a PDZ-domain protein, and the assay measured binding of the ASNSD1 C-terminal peptide, which ends in a class I PDZ-binding motif (T-x-L). The evidence supports the more informative term PDZ domain binding, as for the equivalent NRXN3 rows from the same screen. This rewrite does not imply that each screen-detected partner is physiologically relevant. Reason: Bare protein binding is uninformative; the partner is a PDZ protein and the assay measures PDZ-PBM binding. [PMID:36115835 "Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer."] Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Protein binding (IPI) with APBA1, from a quantitative PDZ-binding-motif fragmentomics screen. APBA1 is a PDZ-domain protein, and the assay measured binding of the ASNSD1 C-terminal peptide, which ends in a class I PDZ-binding motif (T-x-L). The evidence supports the more informative term PDZ domain binding, as for the equivalent NRXN3 rows from the same screen. This rewrite does not imply that each screen-detected partner is physiologically relevant. Reason: Bare protein binding is uninformative; the partner is a PDZ protein and the assay measures PDZ-PBM binding. [PMID:36115835 "Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer."] Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Protein binding (IPI) with TJP1, from a quantitative PDZ-binding-motif fragmentomics screen. TJP1 is a PDZ-domain protein, and the assay measured binding of the ASNSD1 C-terminal peptide, which ends in a class I PDZ-binding motif (T-x-L). The evidence supports the more informative term PDZ domain binding, as for the equivalent NRXN3 rows from the same screen. This rewrite does not imply that each screen-detected partner is physiologically relevant. Reason: Bare protein binding is uninformative; the partner is a PDZ protein and the assay measures PDZ-PBM binding. [PMID:36115835 "Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer."] Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Protein binding (IPI) with DLG1, from a quantitative PDZ-binding-motif fragmentomics screen. DLG1 is a PDZ-domain protein, and the assay measured binding of the ASNSD1 C-terminal peptide, which ends in a class I PDZ-binding motif (T-x-L). The evidence supports the more informative term PDZ domain binding, as for the equivalent NRXN3 rows from the same screen. This rewrite does not imply that each screen-detected partner is physiologically relevant. Reason: Bare protein binding is uninformative; the partner is a PDZ protein and the assay measures PDZ-PBM binding. [PMID:36115835 "Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer."] Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Protein binding (IPI) with SNTB1, from a quantitative PDZ-binding-motif fragmentomics screen. SNTB1 is a PDZ-domain protein, and the assay measured binding of the ASNSD1 C-terminal peptide, which ends in a class I PDZ-binding motif (T-x-L). The evidence supports the more informative term PDZ domain binding, as for the equivalent NRXN3 rows from the same screen. This rewrite does not imply that each screen-detected partner is physiologically relevant. Reason: Bare protein binding is uninformative; the partner is a PDZ protein and the assay measures PDZ-PBM binding. [PMID:36115835 "Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer."] Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Protein binding (IPI) with IL16, from a quantitative PDZ-binding-motif fragmentomics screen. IL16 is a PDZ-domain protein, and the assay measured binding of the ASNSD1 C-terminal peptide, which ends in a class I PDZ-binding motif (T-x-L). The evidence supports the more informative term PDZ domain binding, as for the equivalent NRXN3 rows from the same screen. This rewrite does not imply that each screen-detected partner is physiologically relevant. Reason: Bare protein binding is uninformative; the partner is a PDZ protein and the assay measures PDZ-PBM binding. [PMID:36115835 "Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer."] Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Protein binding (IPI) with SCRIB, from a quantitative PDZ-binding-motif fragmentomics screen. SCRIB is a PDZ-domain protein, and the assay measured binding of the ASNSD1 C-terminal peptide, which ends in a class I PDZ-binding motif (T-x-L). The evidence supports the more informative term PDZ domain binding, as for the equivalent NRXN3 rows from the same screen. This rewrite does not imply that each screen-detected partner is physiologically relevant. Reason: Bare protein binding is uninformative; the partner is a PDZ protein and the assay measures PDZ-PBM binding. [PMID:36115835 "Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer."] Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Protein binding (IPI) with PDZK1, from a quantitative PDZ-binding-motif fragmentomics screen. PDZK1 is a PDZ-domain protein, and the assay measured binding of the ASNSD1 C-terminal peptide, which ends in a class I PDZ-binding motif (T-x-L). The evidence supports the more informative term PDZ domain binding, as for the equivalent NRXN3 rows from the same screen. This rewrite does not imply that each screen-detected partner is physiologically relevant. Reason: Bare protein binding is uninformative; the partner is a PDZ protein and the assay measures PDZ-PBM binding. [PMID:36115835 "Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer."] Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Protein binding (IPI) with FRMPD2, from a quantitative PDZ-binding-motif fragmentomics screen. FRMPD2 is a PDZ-domain protein, and the assay measured binding of the ASNSD1 C-terminal peptide, which ends in a class I PDZ-binding motif (T-x-L). The evidence supports the more informative term PDZ domain binding, as for the equivalent NRXN3 rows from the same screen. This rewrite does not imply that each screen-detected partner is physiologically relevant. Reason: Bare protein binding is uninformative; the partner is a PDZ protein and the assay measures PDZ-PBM binding. [PMID:36115835 "Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer."] Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Protein binding (IPI) with MAGI2, from a quantitative PDZ-binding-motif fragmentomics screen. MAGI2 is a PDZ-domain protein, and the assay measured binding of the ASNSD1 C-terminal peptide, which ends in a class I PDZ-binding motif (T-x-L). The evidence supports the more informative term PDZ domain binding, as for the equivalent NRXN3 rows from the same screen. This rewrite does not imply that each screen-detected partner is physiologically relevant. Reason: Bare protein binding is uninformative; the partner is a PDZ protein and the assay measures PDZ-PBM binding. [PMID:36115835 "Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer."] Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Protein binding (IPI) with NHERF4 (current HGNC symbol; formerly PDZD3), from a quantitative PDZ-binding-motif fragmentomics screen. NHERF4 is a PDZ-domain protein, and the assay measured binding of the ASNSD1 C-terminal peptide, which ends in a class I PDZ-binding motif (T-x-L). The evidence supports the more informative term PDZ domain binding, as for the equivalent NRXN3 rows from the same screen. This rewrite does not imply that each screen-detected partner is physiologically relevant. Reason: Bare protein binding is uninformative; the partner is a PDZ protein and the assay measures PDZ-PBM binding. [PMID:36115835 "Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer."] Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Protein binding (IPI) with LNX2, from a quantitative PDZ-binding-motif fragmentomics screen. LNX2 is a PDZ-domain protein, and the assay measured binding of the ASNSD1 C-terminal peptide, which ends in a class I PDZ-binding motif (T-x-L). The evidence supports the more informative term PDZ domain binding, as for the equivalent NRXN3 rows from the same screen. This rewrite does not imply that each screen-detected partner is physiologically relevant. Reason: Bare protein binding is uninformative; the partner is a PDZ protein and the assay measures PDZ-PBM binding. [PMID:36115835 "Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer."] Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Protein binding (IPI) with PATJ, from a quantitative PDZ-binding-motif fragmentomics screen. PATJ is a PDZ-domain protein, and the assay measured binding of the ASNSD1 C-terminal peptide, which ends in a class I PDZ-binding motif (T-x-L). The evidence supports the more informative term PDZ domain binding, as for the equivalent NRXN3 rows from the same screen. This rewrite does not imply that each screen-detected partner is physiologically relevant. Reason: Bare protein binding is uninformative; the partner is a PDZ protein and the assay measures PDZ-PBM binding. [PMID:36115835 "Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer."] Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Protein binding (IPI) with LNX1, from a quantitative PDZ-binding-motif fragmentomics screen. LNX1 is a PDZ-domain protein, and the assay measured binding of the ASNSD1 C-terminal peptide, which ends in a class I PDZ-binding motif (T-x-L). The evidence supports the more informative term PDZ domain binding, as for the equivalent NRXN3 rows from the same screen. This rewrite does not imply that each screen-detected partner is physiologically relevant. Reason: Bare protein binding is uninformative; the partner is a PDZ protein and the assay measures PDZ-PBM binding. [PMID:36115835 "Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer."] Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Protein binding (IPI) with DLG3, from a quantitative PDZ-binding-motif fragmentomics screen. DLG3 is a PDZ-domain protein, and the assay measured binding of the ASNSD1 C-terminal peptide, which ends in a class I PDZ-binding motif (T-x-L). The evidence supports the more informative term PDZ domain binding, as for the equivalent NRXN3 rows from the same screen. This rewrite does not imply that each screen-detected partner is physiologically relevant. Reason: Bare protein binding is uninformative; the partner is a PDZ protein and the assay measures PDZ-PBM binding. [PMID:36115835 "Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer."] Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Protein binding (IPI) with MAGI1, from a quantitative PDZ-binding-motif fragmentomics screen. MAGI1 is a PDZ-domain protein, and the assay measured binding of the ASNSD1 C-terminal peptide, which ends in a class I PDZ-binding motif (T-x-L). The evidence supports the more informative term PDZ domain binding, as for the equivalent NRXN3 rows from the same screen. This rewrite does not imply that each screen-detected partner is physiologically relevant. Reason: Bare protein binding is uninformative; the partner is a PDZ protein and the assay measures PDZ-PBM binding. [PMID:36115835 "Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer."] Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Protein binding (IPI) with APBA2, from a quantitative PDZ-binding-motif fragmentomics screen. APBA2 is a PDZ-domain protein, and the assay measured binding of the ASNSD1 C-terminal peptide, which ends in a class I PDZ-binding motif (T-x-L). The evidence supports the more informative term PDZ domain binding, as for the equivalent NRXN3 rows from the same screen. This rewrite does not imply that each screen-detected partner is physiologically relevant. Reason: Bare protein binding is uninformative; the partner is a PDZ protein and the assay measures PDZ-PBM binding. [PMID:36115835 "Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer."] Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Protein binding (IPI) with GRIP2, from a quantitative PDZ-binding-motif fragmentomics screen. GRIP2 is a PDZ-domain protein, and the assay measured binding of the ASNSD1 C-terminal peptide, which ends in a class I PDZ-binding motif (T-x-L). The evidence supports the more informative term PDZ domain binding, as for the equivalent NRXN3 rows from the same screen. This rewrite does not imply that each screen-detected partner is physiologically relevant. Reason: Bare protein binding is uninformative; the partner is a PDZ protein and the assay measures PDZ-PBM binding. [PMID:36115835 "Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer."] Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Protein binding (IPI) with WHRN, from a quantitative PDZ-binding-motif fragmentomics screen. WHRN is a PDZ-domain protein, and the assay measured binding of the ASNSD1 C-terminal peptide, which ends in a class I PDZ-binding motif (T-x-L). The evidence supports the more informative term PDZ domain binding, as for the equivalent NRXN3 rows from the same screen. This rewrite does not imply that each screen-detected partner is physiologically relevant. Reason: Bare protein binding is uninformative; the partner is a PDZ protein and the assay measures PDZ-PBM binding. [PMID:36115835 "Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer."] Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Protein binding (IPI) with GRIP1, from a quantitative PDZ-binding-motif fragmentomics screen. GRIP1 is a PDZ-domain protein, and the assay measured binding of the ASNSD1 C-terminal peptide, which ends in a class I PDZ-binding motif (T-x-L). The evidence supports the more informative term PDZ domain binding, as for the equivalent NRXN3 rows from the same screen. This rewrite does not imply that each screen-detected partner is physiologically relevant. Reason: Bare protein binding is uninformative; the partner is a PDZ protein and the assay measures PDZ-PBM binding. [PMID:36115835 "Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer."] Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM) within a human interactome region particularly relevant for viral infection and cancer. |
| GO:0005575 cellular_component | ND GO_REF:0000015 | ACCEPT | Summary: Cellular_component (ND). No subcellular location of the ASNSD1 protein has been determined experimentally. Its only asserted molecular function is peptide-level PDZ domain binding, and its catalytic potential is untested. The no-data statement for this aspect is accurate; accepted. Reason: [file:human/ASNSD1/ASNSD1-uniprot.txt "FT /note="Glutamine amidotransferase type-2""] [file:human/ASNSD1/ASNSD1-uniprot.txt "FT /note="Asparagine synthetase""] [PMID:32638637 "Mice with an inactivating mutation in the gene encoding asparagine synthetase domain containing 1 (ASNSD1) develop a progressive degenerative myopathy that results in severe sarcopenia and myosteatosis."] Supporting Evidence: file:human/ASNSD1/ASNSD1-uniprot.txt FT /note="Glutamine amidotransferase type-2" file:human/ASNSD1/ASNSD1-uniprot.txt FT /note="Asparagine synthetase" PMID:32638637 Mice with an inactivating mutation in the gene encoding asparagine synthetase domain containing 1 (ASNSD1) develop a progressive degenerative myopathy that results in severe sarcopenia and myosteatosis. |
| GO:0008150 biological_process | ND GO_REF:0000015 | ACCEPT | Summary: Biological_process (ND). No biological process of the ASNSD1 protein has been established; the only phenotype is a mouse knockout myopathy, with no mechanism. Its only asserted molecular function is peptide-level PDZ domain binding, and its catalytic potential is untested. The no-data statement for this aspect is accurate; accepted. Reason: [file:human/ASNSD1/ASNSD1-uniprot.txt "FT /note="Glutamine amidotransferase type-2""] [file:human/ASNSD1/ASNSD1-uniprot.txt "FT /note="Asparagine synthetase""] [PMID:32638637 "Mice with an inactivating mutation in the gene encoding asparagine synthetase domain containing 1 (ASNSD1) develop a progressive degenerative myopathy that results in severe sarcopenia and myosteatosis."] Supporting Evidence: file:human/ASNSD1/ASNSD1-uniprot.txt FT /note="Glutamine amidotransferase type-2" file:human/ASNSD1/ASNSD1-uniprot.txt FT /note="Asparagine synthetase" PMID:32638637 Mice with an inactivating mutation in the gene encoding asparagine synthetase domain containing 1 (ASNSD1) develop a progressive degenerative myopathy that results in severe sarcopenia and myosteatosis. |
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Download this section (compressed HTML)Q: Is any of the screen-detected PDZ interactions physiological? Syntrophin beta-1 (SNTB1), a sarcolemmal PDZ scaffold, is a natural first test given the knockout myopathy.
Q: Is ASNSD1 an active amidotransferase or asparagine synthetase in muscle, and does loss of that activity explain the knockout myopathy?
Experiment: Assay purified ASNSD1 for glutaminase and asparagine synthetase activity, and test mutants of the predicted glutamine amidotransferase nucleophile (Cys2) for rescue of the Asnsd1-null muscle phenotype.
What is not known — curated, literature-grounded statements of the open unknowns (the inverse of core functions).
Gap: The molecular function of the ASNSD1 protein is unknown beyond peptide-level PDZ-motif binding, including whether its glutamine amidotransferase and asparagine synthetase domains are catalytically active.
OPEN BIOLOGY WHOLLY_DARK
What is known: Established: domain architecture, maximal skeletal-muscle expression, and a degenerative myopathy in knockout mice. Reported: binding of its C-terminal PDZ-binding-motif peptide to many PDZ domains in screens. Not established: any enzymatic activity, substrate, location or mechanism for the muscle phenotype; the PAQosome role belongs to the uORF microprotein ASDURF.
Provenance (the field's own admissions):
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