{ "bcoid": "GLY_000317", "title": "Mouse Protein PTM Annotation (UniProtKB)", "description": "The Mouse Protein PTM Annotation (UniProtKB) dataset contains mouse [taxid:10090] PTM annotations for ...", "filename": "mouse_protein_ptm_annotation_uniprotkb.csv", "filetype": "csv", "categories": { "species": [ "Mus musculus" ], "molecule": [ "Protein" ], "tag": [ "PTM annotation" ], "file_type": [ "csv" ], "status": [ "Reviewed" ], "scope": [ "internal" ] }, "minitable": { "content": [ [ "Q3URK3-1...", "protein_xref..." ], [ "Q3URK3-1...", "protein_xref..." ] ], "headers": [ "uniprotkb_ca...", "xref_key..." ], "colwidth": [ "40%", "20%" ] }, "sampledata": { "type": "table", "data": [ [ { "type": "string", "label": "uniprotkb_canonical_ac" }, { "type": "string", "label": "xref_key" }, { "type": "string", "label": "xref_id" }, { "type": "string", "label": "eco_id" }, { "type": "string", "label": "ptm_annotation" } ], [ "Q3URK3-1", "protein_xref_uniprotkb", "Q3URK3", "ECO_0000269", "Glycosylated. Interaction with OGT leads to GlcNAcylation." ], [ "Q3URK3-1", "protein_xref_pubmed", "23352454", "ECO_0000269", "Glycosylated. Interaction with OGT leads to GlcNAcylation." ], [ "Q3URK3-1", "protein_xref_uniprotkb", "Q3URK3", "ECO_0000269", "Monoubiquitinated by the DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex called CRL4(VprBP) or CUL4A-RBX1-DDB1-DCAF1/VPRBP complex; this modification promotes binding to DNA." ], [ "Q3URK3-1", "protein_xref_pubmed", "25557551", "ECO_0000269", "Monoubiquitinated by the DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex called CRL4(VprBP) or CUL4A-RBX1-DDB1-DCAF1/VPRBP complex; this modification promotes binding to DNA." ], [ "Q3URK3-1", "protein_xref_uniprotkb", "Q3URK3", "ECO_0000269", "Monoubiquitinated by the DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex called CRL4(VprBP) or CUL4A-RBX1-DDB1-DCAF1/VPRBP complex." ], [ "Q3URK3-1", "protein_xref_pubmed", "36056023", "ECO_0000269", "Monoubiquitinated by the DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex called CRL4(VprBP) or CUL4A-RBX1-DDB1-DCAF1/VPRBP complex." ], [ "Q9EP73-1", "protein_xref_uniprotkb", "Q9EP73", "ECO_0000250", "Ubiquitinated; STUB1 likely mediates polyubiquitination of PD-L1/CD274 triggering its degradation. Ubiquitinated by MARCHF8; leading to degradation." ], [ "Q9EP73-1", "protein_xref_pubmed", "Q9NZQ7", "ECO_0000250", "Ubiquitinated; STUB1 likely mediates polyubiquitination of PD-L1/CD274 triggering its degradation. Ubiquitinated by MARCHF8; leading to degradation." ], [ "O08911-1", "protein_xref_uniprotkb", "O08911", "ECO_0000269", "Dually phosphorylated on Thr-183 and Tyr-185 by MAP2K3/MKK3 and MAP2K6/MKK6, which activates the enzyme." ], [ "O08911-1", "protein_xref_pubmed", "20004242", "ECO_0000269", "Dually phosphorylated on Thr-183 and Tyr-185 by MAP2K3/MKK3 and MAP2K6/MKK6, which activates the enzyme." ], [ "G5E8Q8-1", "protein_xref_uniprotkb", "G5E8Q8", "ECO_0000250", "Highly glycosylated." ], [ "G5E8Q8-1", "protein_xref_pubmed", "Q9WVT0", "ECO_0000250", "Highly glycosylated." ], [ "G5E8Q8-1", "protein_xref_uniprotkb", "G5E8Q8", "ECO_0000250", "Proteolytically cleaved at multiple sites: one in the GPS domain (S1 site) and the other in the SEA domain (S2 site). The proteolytic cleavage at S1 site generates an extracellular subunit and a seven-transmembrane subunit. The proteolytic cleavage at S2 site generates a fragment that undergoes proteolytic cleavage by the processing enzyme furin." ], [ "G5E8Q8-1", "protein_xref_pubmed", "Q9WVT0", "ECO_0000250", "Proteolytically cleaved at multiple sites: one in the GPS domain (S1 site) and the other in the SEA domain (S2 site). The proteolytic cleavage at S1 site generates an extracellular subunit and a seven-transmembrane subunit. The proteolytic cleavage at S2 site generates a fragment that undergoes proteolytic cleavage by the processing enzyme furin." ], [ "P50427-1", "protein_xref_uniprotkb", "P50427", "ECO_0000250", "The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity." ], [ "P50427-1", "protein_xref_pubmed", "P08842", "ECO_0000250", "The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity." ], [ "Q8VC03-1", "protein_xref_uniprotkb", "Q8VC03", "ECO_0000250", "Phosphorylation at Thr-882 during mitosis is required for interaction with TUBG1, HAUS1, HAUS2, HAUS3, HAUS4, HAUS5, HAUS6, HAUS7 and HAUS8 and their recruitment to spindle microtubules." ], [ "Q8VC03-1", "protein_xref_pubmed", "Q32P44", "ECO_0000250", "Phosphorylation at Thr-882 during mitosis is required for interaction with TUBG1, HAUS1, HAUS2, HAUS3, HAUS4, HAUS5, HAUS6, HAUS7 and HAUS8 and their recruitment to spindle microtubules." ], [ "P22727-1", "protein_xref_uniprotkb", "P22727", "ECO_0000250", "Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition." ], [ "P22727-1", "protein_xref_pubmed", "P56704", "ECO_0000250", "Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition." ], [ "P22727-1", "protein_xref_pubmed", "P27467", "ECO_0000250", "Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition." ], [ "Q8BGW0-1", "protein_xref_uniprotkb", "Q8BGW0", "ECO_0000269", "Phosphorylated on Tyr residues quickly after TCR stimulation." ], [ "Q8BGW0-1", "protein_xref_pubmed", "19597498", "ECO_0000269", "Phosphorylated on Tyr residues quickly after TCR stimulation." ], [ "Q8BGW0-1", "protein_xref_pubmed", "19597499", "ECO_0000269", "Phosphorylated on Tyr residues quickly after TCR stimulation." ], [ "Q9QZD4-1", "protein_xref_uniprotkb", "Q9QZD4", "ECO_0000250", "Acetylation at Lys-912 by KAT5 promotes interaction with ERCC1 by disrupting a salt bridge between Asp-908 and Lys-912, thereby exposing a second binding site for ERCC1 (By similarity). Deacetylated by SIRT1 (By similarity)." ], [ "Q9QZD4-1", "protein_xref_pubmed", "Q92889", "ECO_0000250", "Acetylation at Lys-912 by KAT5 promotes interaction with ERCC1 by disrupting a salt bridge between Asp-908 and Lys-912, thereby exposing a second binding site for ERCC1 (By similarity). Deacetylated by SIRT1 (By similarity)." ], [ "Q9QZD9-1", "protein_xref_uniprotkb", "Q9QZD9", "ECO_0000255", "Phosphorylated by TGF-beta type II receptor." ], [ "Q9QZD9-1", "protein_xref_pubmed", "MF_03008", "ECO_0000255", "Phosphorylated by TGF-beta type II receptor." ], [ "Q91YI1-1", "protein_xref_uniprotkb", "Q91YI1", "ECO_0000250", "Phosphorylated by ULK1, ULK2 and mTOR. Phosphorylation status depends on nutrient-rich conditions; dephosphorylated during starvation or following treatment with rapamycin. ULK1-mediated phosphorylation of ATG13 at Ser-354 is required for efficient clearance of depolarized mitochondria." ], [ "Q91YI1-1", "protein_xref_pubmed", "O75143", "ECO_0000250", "Phosphorylated by ULK1, ULK2 and mTOR. Phosphorylation status depends on nutrient-rich conditions; dephosphorylated during starvation or following treatment with rapamycin. ULK1-mediated phosphorylation of ATG13 at Ser-354 is required for efficient clearance of depolarized mitochondria." ], [ "Q91YI0-1", "protein_xref_uniprotkb", "Q91YI0", "ECO_0000250", "Acetylation modifies enzyme activity in response to alterations of extracellular nutrient availability. Acetylation increased with trichostin A (TSA) or with nicotinamide (NAM). Glucose increases acetylation by about a factor of 3 with decreasing enzyme activity. Acetylation on Lys-288 is decreased on the addition of extra amino acids resulting in activation of enzyme activity." ], [ "Q91YI0-1", "protein_xref_pubmed", "P04424", "ECO_0000250", "Acetylation modifies enzyme activity in response to alterations of extracellular nutrient availability. Acetylation increased with trichostin A (TSA) or with nicotinamide (NAM). Glucose increases acetylation by about a factor of 3 with decreasing enzyme activity. Acetylation on Lys-288 is decreased on the addition of extra amino acids resulting in activation of enzyme activity." ], [ "Q91YI4-1", "protein_xref_uniprotkb", "Q91YI4", "ECO_0000250", "The ubiquitination status appears to regulate the formation and trafficking of beta-arrestin-GPCR complexes and signaling. Ubiquitination appears to occur GPCR-specific. Ubiquitinated by MDM2; the ubiquitination is required for rapid internalization of ADRB2. Deubiquitinated by USP33; the deubiquitination leads to a dissociation of the beta-arrestin-GPCR complex. Stimulation of a class A GPCR, such as ADRB2, induces transient ubiquitination and subsequently promotes association with USP33. Stimulation of a class B GPCR promotes a sustained ubiquitination. Deubiquitinated by USP20; allowing USP20 to deubiquitinate TRAF6 leading to inhibition of NF-kappa-B signaling (By similarity)." ], [ "Q91YI4-1", "protein_xref_pubmed", "P32121", "ECO_0000250", "The ubiquitination status appears to regulate the formation and trafficking of beta-arrestin-GPCR complexes and signaling. Ubiquitination appears to occur GPCR-specific. Ubiquitinated by MDM2; the ubiquitination is required for rapid internalization of ADRB2. Deubiquitinated by USP33; the deubiquitination leads to a dissociation of the beta-arrestin-GPCR complex. Stimulation of a class A GPCR, such as ADRB2, induces transient ubiquitination and subsequently promotes association with USP33. Stimulation of a class B GPCR promotes a sustained ubiquitination. Deubiquitinated by USP20; allowing USP20 to deubiquitinate TRAF6 leading to inhibition of NF-kappa-B signaling (By similarity)." ], [ "Q9WUZ9-1", "protein_xref_uniprotkb", "Q9WUZ9", "ECO_0000269", "N-glycosylated; high-mannose type." ], [ "Q9WUZ9-1", "protein_xref_pubmed", "10369669", "ECO_0000269", "N-glycosylated; high-mannose type." ], [ "Q9WUZ9-1", "protein_xref_pubmed", "21074248", "ECO_0000269", "N-glycosylated; high-mannose type." ], [ "Q69Z98-1", "protein_xref_uniprotkb", "Q69Z98", "ECO_0000269", "May be phosphorylated at Thr-261 by PKA (By similarity). Phosphorylated at Thr-175 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Not phosphorylated at Thr-175 by CaMKK2. In contrast, it is phosphorylated and activated by CaMKK1. May be inactivated via dephosphorylation of Thr-175 by PP2C." ], [ "Q69Z98-1", "protein_xref_pubmed", "17482548", "ECO_0000269", "May be phosphorylated at Thr-261 by PKA (By similarity). Phosphorylated at Thr-175 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Not phosphorylated at Thr-175 by CaMKK2. In contrast, it is phosphorylated and activated by CaMKK1. May be inactivated via dephosphorylation of Thr-175 by PP2C." ], [ "Q9ESN9-1", "protein_xref_uniprotkb", "Q9ESN9", "ECO_0000250", "Phosphorylation by ROCK1 is crucial for the recruitment of JNK." ], [ "Q9ESN9-1", "protein_xref_pubmed", "Q9UPT6", "ECO_0000250", "Phosphorylation by ROCK1 is crucial for the recruitment of JNK." ], [ "Q9ESN6-1", "protein_xref_uniprotkb", "Q9ESN6", "ECO_0000269", "RING-type zinc finger-dependent and UBE2D1-dependent autoubiquitination." ], [ "Q9ESN6-1", "protein_xref_pubmed", "18687884", "ECO_0000269", "RING-type zinc finger-dependent and UBE2D1-dependent autoubiquitination." ], [ "Q9ESN2-1", "protein_xref_uniprotkb", "Q9ESN2", "ECO_0000250", "Autoubiquitinated." ], [ "Q9ESN2-1", "protein_xref_pubmed", "Q9HCM9", "ECO_0000250", "Autoubiquitinated." ], [ "Q9ESN3-1", "protein_xref_uniprotkb", "Q9ESN3", "ECO_0000250", "Glycosylated." ], [ "Q9ESN3-1", "protein_xref_pubmed", "Q9HCN3", "ECO_0000250", "Glycosylated." ], [ "Q9D5T7-1", "protein_xref_uniprotkb", "Q9D5T7", "ECO_0000269", "Phosphorylated at Ser-375 in a SPO11-dependent manner." ], [ "Q9D5T7-1", "protein_xref_pubmed", "22346761", "ECO_0000269", "Phosphorylated at Ser-375 in a SPO11-dependent manner." ], [ "Q9D5T7-1", "protein_xref_pubmed", "19686734", "ECO_0000269", "Phosphorylated at Ser-375 in a SPO11-dependent manner." ], [ "O88307-1", "protein_xref_uniprotkb", "O88307", "ECO_0000250", "Within the Golgi apparatus, the propeptide may be cleaved off by FURIN or a furin-like protease. After cleavage, the propeptide interacts with the mature protein N-terminus, preventing the association with other ligands. At the cell surface, partially subjected to proteolytic shedding that releases the ectodomain in the extracellular milieu. The shedding may be catalyzed by ADAM17/TACE. Following shedding, PSEN1/presenilin-1 cleaves the remaining transmembrane fragment and catalyzes the release of a C-terminal fragment in the cytosol and of a soluble N-terminal beta fragment in the extracellular milieu. The C-terminal cytosolic fragment localizes to the nucleus." ], [ "O88307-1", "protein_xref_pubmed", "Q92673", "ECO_0000250", "Within the Golgi apparatus, the propeptide may be cleaved off by FURIN or a furin-like protease. After cleavage, the propeptide interacts with the mature protein N-terminus, preventing the association with other ligands. At the cell surface, partially subjected to proteolytic shedding that releases the ectodomain in the extracellular milieu. The shedding may be catalyzed by ADAM17/TACE. Following shedding, PSEN1/presenilin-1 cleaves the remaining transmembrane fragment and catalyzes the release of a C-terminal fragment in the cytosol and of a soluble N-terminal beta fragment in the extracellular milieu. The C-terminal cytosolic fragment localizes to the nucleus." ], [ "O88307-1", "protein_xref_uniprotkb", "O88307", "ECO_0000250", "Phosphorylation at Ser-2207 facilitates the interaction with GGA1." ], [ "O88307-1", "protein_xref_pubmed", "Q92673", "ECO_0000250", "Phosphorylation at Ser-2207 facilitates the interaction with GGA1." ], [ "P27467-1", "protein_xref_uniprotkb", "P27467", "ECO_0000269", "Proteolytic processing by TIKI1 and TIKI2 promotes oxidation and formation of large disulfide-bond oligomers, leading to inactivation of WNT3A." ], [ "P27467-1", "protein_xref_pubmed", "22726442", "ECO_0000269", "Proteolytic processing by TIKI1 and TIKI2 promotes oxidation and formation of large disulfide-bond oligomers, leading to inactivation of WNT3A." ], [ "P27467-1", "protein_xref_uniprotkb", "P27467", "ECO_0000269", "Disulfide bonds have critical and distinct roles in secretion and activity. Loss of each conserved cysteine in WNT3A results in high molecular weight oxidized Wnt oligomers, which are formed through inter-Wnt disulfide bonding." ], [ "P27467-1", "protein_xref_pubmed", "22726442", "ECO_0000269", "Disulfide bonds have critical and distinct roles in secretion and activity. Loss of each conserved cysteine in WNT3A results in high molecular weight oxidized Wnt oligomers, which are formed through inter-Wnt disulfide bonding." ], [ "P27467-1", "protein_xref_uniprotkb", "P27467", "ECO_0000269", "Palmitoleoylation by PORCN is required for efficient binding to frizzled receptors. Palmitoleoylation is required for proper trafficking to cell surface, vacuolar acidification is critical to release palmitoleoylated WNT3A from WLS in secretory vesicles (PubMed:17141155, PubMed:24798332). Depalmitoleoylated by NOTUM, leading to inhibit Wnt signaling pathway, possibly by promoting disulfide bond formation and oligomerization (PubMed:25771893)." ], [ "P27467-1", "protein_xref_pubmed", "17141155", "ECO_0000269", "Palmitoleoylation by PORCN is required for efficient binding to frizzled receptors. Palmitoleoylation is required for proper trafficking to cell surface, vacuolar acidification is critical to release palmitoleoylated WNT3A from WLS in secretory vesicles (PubMed:17141155, PubMed:24798332). Depalmitoleoylated by NOTUM, leading to inhibit Wnt signaling pathway, possibly by promoting disulfide bond formation and oligomerization (PubMed:25771893)." ], [ "P27467-1", "protein_xref_uniprotkb", "P27467", "ECO_0000250", "Palmitoleoylation by PORCN is required for efficient binding to frizzled receptors. Palmitoleoylation is required for proper trafficking to cell surface, vacuolar acidification is critical to release palmitoleoylated WNT3A from WLS in secretory vesicles (PubMed:17141155, PubMed:24798332). Depalmitoleoylated by NOTUM, leading to inhibit Wnt signaling pathway, possibly by promoting disulfide bond formation and oligomerization (PubMed:25771893)." ], [ "P27467-1", "protein_xref_pubmed", "P56704", "ECO_0000250", "Palmitoleoylation by PORCN is required for efficient binding to frizzled receptors. Palmitoleoylation is required for proper trafficking to cell surface, vacuolar acidification is critical to release palmitoleoylated WNT3A from WLS in secretory vesicles (PubMed:17141155, PubMed:24798332). Depalmitoleoylated by NOTUM, leading to inhibit Wnt signaling pathway, possibly by promoting disulfide bond formation and oligomerization (PubMed:25771893)." ], [ "P27467-1", "protein_xref_pubmed", "25771893", "ECO_0000269", "Palmitoleoylation by PORCN is required for efficient binding to frizzled receptors. Palmitoleoylation is required for proper trafficking to cell surface, vacuolar acidification is critical to release palmitoleoylated WNT3A from WLS in secretory vesicles (PubMed:17141155, PubMed:24798332). Depalmitoleoylated by NOTUM, leading to inhibit Wnt signaling pathway, possibly by promoting disulfide bond formation and oligomerization (PubMed:25771893)." ], [ "P27467-1", "protein_xref_pubmed", "24798332", "ECO_0000269", "Palmitoleoylation by PORCN is required for efficient binding to frizzled receptors. Palmitoleoylation is required for proper trafficking to cell surface, vacuolar acidification is critical to release palmitoleoylated WNT3A from WLS in secretory vesicles (PubMed:17141155, PubMed:24798332). Depalmitoleoylated by NOTUM, leading to inhibit Wnt signaling pathway, possibly by promoting disulfide bond formation and oligomerization (PubMed:25771893)." ], [ "Q8VEK3-1", "protein_xref_uniprotkb", "Q8VEK3", "ECO_0000250", "Cleaved at Asp-94 by CASP3 during T-cell apoptosis, resulting in a loss of DNA- and chromatin-binding activities." ], [ "Q8VEK3-1", "protein_xref_pubmed", "Q00839", "ECO_0000250", "Cleaved at Asp-94 by CASP3 during T-cell apoptosis, resulting in a loss of DNA- and chromatin-binding activities." ], [ "Q8VEK3-1", "protein_xref_uniprotkb", "Q8VEK3", "ECO_0000269", "Citrullinated by PADI4." ], [ "Q8VEK3-1", "protein_xref_pubmed", "24463520", "ECO_0000269", "Citrullinated by PADI4." ], [ "Q8VEK3-1", "protein_xref_uniprotkb", "Q8VEK3", "ECO_0000250", "Extensively phosphorylated. Phosphorylated on Ser-58 by PLK1 and dephosphorylated by protein phosphatase 2A (PP2A) in mitosis." ], [ "Q8VEK3-1", "protein_xref_pubmed", "Q00839", "ECO_0000250", "Extensively phosphorylated. Phosphorylated on Ser-58 by PLK1 and dephosphorylated by protein phosphatase 2A (PP2A) in mitosis." ], [ "Q8VEK0-1", "protein_xref_uniprotkb", "Q8VEK0", "ECO_0000269", "N-glycosylated. Contains high mannose-type oligosaccharides." ], [ "Q8VEK0-1", "protein_xref_pubmed", "22253360", "ECO_0000269", "N-glycosylated. Contains high mannose-type oligosaccharides." ], [ "Q8C0V1-1", "protein_xref_uniprotkb", "Q8C0V1", "ECO_0000269", "Phosphorylated by CDK (PubMed:24413433, PubMed:26548954). Phosphorylation by CDK takes place in late prophase when the cap exchange is prominent (PubMed:26548954). is important for the stabilization of telomere attachment but dispenable for the cap exchange (PubMed:26548954)." ], [ "Q8C0V1-1", "protein_xref_pubmed", "26548954", "ECO_0000269", "Phosphorylated by CDK (PubMed:24413433, PubMed:26548954). Phosphorylation by CDK takes place in late prophase when the cap exchange is prominent (PubMed:26548954). is important for the stabilization of telomere attachment but dispenable for the cap exchange (PubMed:26548954)." ], [ "Q8C0V1-1", "protein_xref_pubmed", "24413433", "ECO_0000269", "Phosphorylated by CDK (PubMed:24413433, PubMed:26548954). Phosphorylation by CDK takes place in late prophase when the cap exchange is prominent (PubMed:26548954). is important for the stabilization of telomere attachment but dispenable for the cap exchange (PubMed:26548954)." ], [ "Q9R002-1", "protein_xref_uniprotkb", "Q9R002", "ECO_0000269", "Phosphorylated." ], [ "Q9R002-1", "protein_xref_pubmed", "8454910", "ECO_0000269", "Phosphorylated." ], [ "Q9R001-1", "protein_xref_uniprotkb", "Q9R001", "ECO_0000250", "The precursor is cleaved by furin and PCSK7 outside of the cell." ], [ "Q9R001-1", "protein_xref_pubmed", "Q9UNA0", "ECO_0000250", "The precursor is cleaved by furin and PCSK7 outside of the cell." ], [ "Q9R007-3", "protein_xref_uniprotkb", "Q9R007", "ECO_0000269", "N-glycosylated (PubMed:19074552, PubMed:19251634). Contains sialic acid residues (PubMed:19074552)." ], [ "Q9R007-3", "protein_xref_pubmed", "19251634", "ECO_0000269", "N-glycosylated (PubMed:19074552, PubMed:19251634). Contains sialic acid residues (PubMed:19074552)." ], [ "Q9R007-3", "protein_xref_pubmed", "19074552", "ECO_0000269", "N-glycosylated (PubMed:19074552, PubMed:19251634). Contains sialic acid residues (PubMed:19074552)." ], [ "Q6QIY3-1", "protein_xref_uniprotkb", "Q6QIY3", "ECO_0000250", "Lacks the cysteine which covalently binds the conotoxin GVIIJ. This cysteine (position 815) is speculated in other sodium channel subunits alpha to be implied in covalent binding with the sodium channel subunit beta-2 or beta-4." ], [ "Q6QIY3-1", "protein_xref_pubmed", "P15389", "ECO_0000250", "Lacks the cysteine which covalently binds the conotoxin GVIIJ. This cysteine (position 815) is speculated in other sodium channel subunits alpha to be implied in covalent binding with the sodium channel subunit beta-2 or beta-4." ] ] }, "readme": "Name\n - Mouse Protein PTM Annotation (UniProtKB)\n\nVersion\n - v-2.2.1\n\nCreated on\n - 2019-11-30T14:05:28.986536\n\nModified on\n - 2022-09-26T09:05:27.622846\n\nCreated by\n - Jeet Vora [jeetvora@gwu.edu], Robel Kahsay [rykahsay@gwu.edu], Karina Martinez [karinamartinez@gwu.edu], Jingyue Wu [jingyue.wu@email.gwu.edu]\n\nAuthors\n - Maria Martin [martin@ebi.ac.uk], Preethi Vasudev [pvasudev@ebi.ac.uk]\n\nChecksum\n - \n\nUsability Domain\n - The Mouse Protein PTM Annotation (UniProtKB) dataset contains mouse [taxid:10090] PTM annotations for UniProtKB canonical accessions. The annotation is the curated statements of mainly about glycosylation and phosphorylation. The dataset is derived form 2019-09 UniprotKB release. If you use this dataset please give proper attribution to UniProtKB and GlyGen. \n\nDescription Domain\n Keywords\n - ptm annotation\n - glycosylation\n - phosphorylation\n\n Pipeline Steps\n - Step-1: The script extracts the ptm annotation strings from the triplestore for the UniProtKB canonical sequences and extracts as a dataset in a csv format. \n\nExecution Domain\n Scripts - https://github.com/glygener/glygen-backend-integration/blob/master/dataset-maker/make-protein-dataset.py\n\n\n Software Prerequisites\n Name: Python\n Version: 2.7.5\n URI: https://www.python.org/download/releases/2.7.5/\n\nI/O Domain\n Input Subdomain\n Name: uniprot-proteome-mus-musculus.nt\n URI: https:/data.glygen.org/ln2downloads/ebi/2023_10_30/uniprot-proteome-mus-musculus.nt\n Output Subdomain\n Name: mouse_protein_ptm_annotation_uniprotkb.csv\n URI: https:/data.glygen.org/ln2releases/data/v-2.2.1/reviewed/mouse_protein_ptm_annotation_uniprotkb.csv\n Name: mouse_protein_ptm_annotation_uniprotkb.stat.csv\n URI: https:/data.glygen.org/ln2releases/data/v-2.2.1/reviewed/mouse_protein_ptm_annotation_uniprotkb.stat.csv\n\nFields\n Name: \"uniprotkb_canonical_ac\"\n Description: \"\"\n Unique Values: \"3311\"\n Name: \"xref_key\"\n Description: \"Source key associated to the xref_id\"\n Unique Values: \"2\"\n Name: \"xref_id\"\n Description: \"ID of the X-ref\"\n Unique Values: \"7878\"\n Name: \"eco_id\"\n Description: \"Evidence & Conclusion Ontology (ECO) identifier\"\n Unique Values: \"7\"\n Name: \"ptm_annotation\"\n Description: \"The Post Translational Modifiaction (PTM) annotation in UniProtKB that provides more context and description about the PTMs occuring on a proein\"\n Unique Values: \"3807\"", "downloadurl": "/ln2data/releases/data/v-2.2.1/reviewed/mouse_protein_ptm_annotation_uniprotkb.csv" }