{ "bcoid": "GLY_000318", "title": "Rat Protein PTM Annotation (UniProtKB)", "description": "The Rat Protein PTM Annotation (UniProtKB) dataset contains rat [taxid:10116] PTM annotations for UniProtKB ...", "filename": "rat_protein_ptm_annotation_uniprotkb.csv", "filetype": "csv", "categories": { "species": [ "Rattus norvegicus" ], "molecule": [ "Protein" ], "tag": [ "PTM annotation" ], "file_type": [ "csv" ], "status": [ "Reviewed" ], "scope": [ "internal" ] }, "minitable": { "content": [ [ "P30936-1...", "protein_xref..." ], [ "P30936-1...", "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" } ], [ "P30936-1", "protein_xref_uniprotkb", "P30936", "ECO_0000269", "Phosphorylated. Phosphorylation increases upon somatostatin binding." ], [ "P30936-1", "protein_xref_pubmed", "9295322", "ECO_0000269", "Phosphorylated. Phosphorylation increases upon somatostatin binding." ], [ "O35158-1", "protein_xref_uniprotkb", "O35158", "ECO_0000269", "N-glycosylated." ], [ "O35158-1", "protein_xref_pubmed", "9214393", "ECO_0000269", "N-glycosylated." ], [ "P09006-1", "protein_xref_uniprotkb", "P09006", "ECO_0000269", "N-glycosylated." ], [ "P09006-1", "protein_xref_pubmed", "1694763", "ECO_0000269", "N-glycosylated." ], [ "Q9WU49-1", "protein_xref_uniprotkb", "Q9WU49", "ECO_0000269", "Can be phosphorylated by DYRK2 (in vitro) (By similarity). Dephosphorylated by calcineurin in a Ca(2+) dependent manner, and probably by PP2A or PP4 serine phosphatases in cAMP- and PKC-mediated pathways." ], [ "Q9WU49-1", "protein_xref_pubmed", "9712905", "ECO_0000269", "Can be phosphorylated by DYRK2 (in vitro) (By similarity). Dephosphorylated by calcineurin in a Ca(2+) dependent manner, and probably by PP2A or PP4 serine phosphatases in cAMP- and PKC-mediated pathways." ], [ "Q9WU49-1", "protein_xref_pubmed", "19477163", "ECO_0000269", "Can be phosphorylated by DYRK2 (in vitro) (By similarity). Dephosphorylated by calcineurin in a Ca(2+) dependent manner, and probably by PP2A or PP4 serine phosphatases in cAMP- and PKC-mediated pathways." ], [ "Q9R1N3-1", "protein_xref_uniprotkb", "Q9R1N3", "ECO_0000269", "N-glycosylated." ], [ "Q9R1N3-1", "protein_xref_pubmed", "11053051", "ECO_0000269", "N-glycosylated." ], [ "Q9R1N3-1", "protein_xref_uniprotkb", "Q9R1N3", "ECO_0000269", "Undergoes lysosome-mediated degradation." ], [ "Q9R1N3-1", "protein_xref_pubmed", "29743600", "ECO_0000269", "Undergoes lysosome-mediated degradation." ], [ "Q9QYH7-1", "protein_xref_uniprotkb", "Q9QYH7", "ECO_0000269", "Amidation of Leu-98 is essential for obestatin activity." ], [ "Q9QYH7-1", "protein_xref_pubmed", "16284174", "ECO_0000269", "Amidation of Leu-98 is essential for obestatin activity." ], [ "Q9QYH7-1", "protein_xref_uniprotkb", "Q9QYH7", "ECO_0000269", "O-octanoylated by GOAT/MBOAT4 (By similarity). O-octanoylation is essential for ghrelin activity. The replacement of Ser-26 by aromatic tryptophan preserves ghrelin activity (PubMed:10604470, PubMed:10801861)." ], [ "Q9QYH7-1", "protein_xref_pubmed", "10801861", "ECO_0000269", "O-octanoylated by GOAT/MBOAT4 (By similarity). O-octanoylation is essential for ghrelin activity. The replacement of Ser-26 by aromatic tryptophan preserves ghrelin activity (PubMed:10604470, PubMed:10801861)." ], [ "Q9QYH7-1", "protein_xref_pubmed", "10604470", "ECO_0000269", "O-octanoylated by GOAT/MBOAT4 (By similarity). O-octanoylation is essential for ghrelin activity. The replacement of Ser-26 by aromatic tryptophan preserves ghrelin activity (PubMed:10604470, PubMed:10801861)." ], [ "Q9ESR9-1", "protein_xref_uniprotkb", "Q9ESR9", "ECO_0000269", "N-glycosylated." ], [ "Q9ESR9-1", "protein_xref_pubmed", "10970803", "ECO_0000269", "N-glycosylated." ], [ "P37089-1", "protein_xref_uniprotkb", "P37089", "ECO_0000269", "N-glycosylated." ], [ "P37089-1", "protein_xref_pubmed", "11773057", "ECO_0000269", "N-glycosylated." ], [ "P37089-1", "protein_xref_uniprotkb", "P37089", "ECO_0000269", "Ubiquitinated; this targets individual subunits for endocytosis and proteasome-mediated degradation." ], [ "P37089-1", "protein_xref_pubmed", "9351815", "ECO_0000269", "Ubiquitinated; this targets individual subunits for endocytosis and proteasome-mediated degradation." ], [ "Q00972-1", "protein_xref_uniprotkb", "Q00972", "ECO_0000269", "Autophosphorylated." ], [ "Q00972-1", "protein_xref_pubmed", "7649998", "ECO_0000269", "Autophosphorylated." ], [ "P31016-1", "protein_xref_uniprotkb", "P31016", "ECO_0000269", "Palmitoylated (PubMed:10629226, PubMed:27307232). Palmitoylation is required for targeting to postsynaptic density, plasma membrane and synapses (PubMed:10629226, PubMed:27307232). Palmitoylation by ZDHHC2 occurs when the synaptic activity decreases and induces DLG4 synaptic clustering (PubMed:19596852). Palmitoylation by ZDHHC15 regulates trafficking to the postsynaptic density and function in synaptogenesis (PubMed:15603741, PubMed:31189538). Palmitoylation may play a role in glutamate receptor GRIA1 synapse clustering (PubMed:27307232). Depalmitoylated by ABHD17A and ABHD17B and to a lesser extent by ABHD17C, ABHD12, ABHD13, LYPLA1 and LYPLA2 (PubMed:27307232). Undergoes rapid synaptic palmitoylation/depalmitoylation cycle during neuronal development which slows down in mature neurons (PubMed:27307232)." ], [ "P31016-1", "protein_xref_pubmed", "10629226", "ECO_0000269", "Palmitoylated (PubMed:10629226, PubMed:27307232). Palmitoylation is required for targeting to postsynaptic density, plasma membrane and synapses (PubMed:10629226, PubMed:27307232). Palmitoylation by ZDHHC2 occurs when the synaptic activity decreases and induces DLG4 synaptic clustering (PubMed:19596852). Palmitoylation by ZDHHC15 regulates trafficking to the postsynaptic density and function in synaptogenesis (PubMed:15603741, PubMed:31189538). Palmitoylation may play a role in glutamate receptor GRIA1 synapse clustering (PubMed:27307232). Depalmitoylated by ABHD17A and ABHD17B and to a lesser extent by ABHD17C, ABHD12, ABHD13, LYPLA1 and LYPLA2 (PubMed:27307232). Undergoes rapid synaptic palmitoylation/depalmitoylation cycle during neuronal development which slows down in mature neurons (PubMed:27307232)." ], [ "P31016-1", "protein_xref_pubmed", "27307232", "ECO_0000269", "Palmitoylated (PubMed:10629226, PubMed:27307232). Palmitoylation is required for targeting to postsynaptic density, plasma membrane and synapses (PubMed:10629226, PubMed:27307232). Palmitoylation by ZDHHC2 occurs when the synaptic activity decreases and induces DLG4 synaptic clustering (PubMed:19596852). Palmitoylation by ZDHHC15 regulates trafficking to the postsynaptic density and function in synaptogenesis (PubMed:15603741, PubMed:31189538). Palmitoylation may play a role in glutamate receptor GRIA1 synapse clustering (PubMed:27307232). Depalmitoylated by ABHD17A and ABHD17B and to a lesser extent by ABHD17C, ABHD12, ABHD13, LYPLA1 and LYPLA2 (PubMed:27307232). Undergoes rapid synaptic palmitoylation/depalmitoylation cycle during neuronal development which slows down in mature neurons (PubMed:27307232)." ], [ "P31016-1", "protein_xref_pubmed", "15603741", "ECO_0000269", "Palmitoylated (PubMed:10629226, PubMed:27307232). Palmitoylation is required for targeting to postsynaptic density, plasma membrane and synapses (PubMed:10629226, PubMed:27307232). Palmitoylation by ZDHHC2 occurs when the synaptic activity decreases and induces DLG4 synaptic clustering (PubMed:19596852). Palmitoylation by ZDHHC15 regulates trafficking to the postsynaptic density and function in synaptogenesis (PubMed:15603741, PubMed:31189538). Palmitoylation may play a role in glutamate receptor GRIA1 synapse clustering (PubMed:27307232). Depalmitoylated by ABHD17A and ABHD17B and to a lesser extent by ABHD17C, ABHD12, ABHD13, LYPLA1 and LYPLA2 (PubMed:27307232). Undergoes rapid synaptic palmitoylation/depalmitoylation cycle during neuronal development which slows down in mature neurons (PubMed:27307232)." ], [ "P31016-1", "protein_xref_pubmed", "31189538", "ECO_0000269", "Palmitoylated (PubMed:10629226, PubMed:27307232). Palmitoylation is required for targeting to postsynaptic density, plasma membrane and synapses (PubMed:10629226, PubMed:27307232). Palmitoylation by ZDHHC2 occurs when the synaptic activity decreases and induces DLG4 synaptic clustering (PubMed:19596852). Palmitoylation by ZDHHC15 regulates trafficking to the postsynaptic density and function in synaptogenesis (PubMed:15603741, PubMed:31189538). Palmitoylation may play a role in glutamate receptor GRIA1 synapse clustering (PubMed:27307232). Depalmitoylated by ABHD17A and ABHD17B and to a lesser extent by ABHD17C, ABHD12, ABHD13, LYPLA1 and LYPLA2 (PubMed:27307232). Undergoes rapid synaptic palmitoylation/depalmitoylation cycle during neuronal development which slows down in mature neurons (PubMed:27307232)." ], [ "P31016-1", "protein_xref_pubmed", "19596852", "ECO_0000269", "Palmitoylated (PubMed:10629226, PubMed:27307232). Palmitoylation is required for targeting to postsynaptic density, plasma membrane and synapses (PubMed:10629226, PubMed:27307232). Palmitoylation by ZDHHC2 occurs when the synaptic activity decreases and induces DLG4 synaptic clustering (PubMed:19596852). Palmitoylation by ZDHHC15 regulates trafficking to the postsynaptic density and function in synaptogenesis (PubMed:15603741, PubMed:31189538). Palmitoylation may play a role in glutamate receptor GRIA1 synapse clustering (PubMed:27307232). Depalmitoylated by ABHD17A and ABHD17B and to a lesser extent by ABHD17C, ABHD12, ABHD13, LYPLA1 and LYPLA2 (PubMed:27307232). Undergoes rapid synaptic palmitoylation/depalmitoylation cycle during neuronal development which slows down in mature neurons (PubMed:27307232)." ], [ "P31016-1", "protein_xref_uniprotkb", "P31016", "ECO_0000269", "Ubiquitinated by MDM2 in response to NMDA receptor activation, leading to proteasome-mediated degradation of DLG4 which is required for AMPA receptor endocytosis." ], [ "P31016-1", "protein_xref_pubmed", "14642282", "ECO_0000269", "Ubiquitinated by MDM2 in response to NMDA receptor activation, leading to proteasome-mediated degradation of DLG4 which is required for AMPA receptor endocytosis." ], [ "Q62736-1", "protein_xref_uniprotkb", "Q62736", "ECO_0000269", "In non-muscle cells, phosphorylation by CDK1 during mitosis causes caldesmon to dissociate from microfilaments. Phosphorylation reduces caldesmon binding to actin, myosin, and calmodulin as well as its inhibition of actomyosin ATPase activity. Phosphorylation also occurs in both quiescent and dividing smooth muscle cells with similar effects on the interaction with actin and calmodulin and on microfilaments reorganization. CDK1-mediated phosphorylation promotes Schwann cell migration during peripheral nerve regeneration." ], [ "Q62736-1", "protein_xref_pubmed", "17200138", "ECO_0000269", "In non-muscle cells, phosphorylation by CDK1 during mitosis causes caldesmon to dissociate from microfilaments. Phosphorylation reduces caldesmon binding to actin, myosin, and calmodulin as well as its inhibition of actomyosin ATPase activity. Phosphorylation also occurs in both quiescent and dividing smooth muscle cells with similar effects on the interaction with actin and calmodulin and on microfilaments reorganization. CDK1-mediated phosphorylation promotes Schwann cell migration during peripheral nerve regeneration." ], [ "Q62736-1", "protein_xref_pubmed", "7876150", "ECO_0000269", "In non-muscle cells, phosphorylation by CDK1 during mitosis causes caldesmon to dissociate from microfilaments. Phosphorylation reduces caldesmon binding to actin, myosin, and calmodulin as well as its inhibition of actomyosin ATPase activity. Phosphorylation also occurs in both quiescent and dividing smooth muscle cells with similar effects on the interaction with actin and calmodulin and on microfilaments reorganization. CDK1-mediated phosphorylation promotes Schwann cell migration during peripheral nerve regeneration." ], [ "Q62736-1", "protein_xref_pubmed", "1986309", "ECO_0000269", "In non-muscle cells, phosphorylation by CDK1 during mitosis causes caldesmon to dissociate from microfilaments. Phosphorylation reduces caldesmon binding to actin, myosin, and calmodulin as well as its inhibition of actomyosin ATPase activity. Phosphorylation also occurs in both quiescent and dividing smooth muscle cells with similar effects on the interaction with actin and calmodulin and on microfilaments reorganization. CDK1-mediated phosphorylation promotes Schwann cell migration during peripheral nerve regeneration." ], [ "Q9Z1Z3-1", "protein_xref_uniprotkb", "Q9Z1Z3", "ECO_0000269", "Ubiquitinated." ], [ "Q9Z1Z3-1", "protein_xref_pubmed", "11919637", "ECO_0000269", "Ubiquitinated." ], [ "P28818-1", "protein_xref_uniprotkb", "P28818", "ECO_0000269", "Phosphorylated by PLK2, leading to ubiquitination and degradation by the proteasome." ], [ "P28818-1", "protein_xref_pubmed", "21382555", "ECO_0000269", "Phosphorylated by PLK2, leading to ubiquitination and degradation by the proteasome." ], [ "P28818-1", "protein_xref_uniprotkb", "P28818", "ECO_0000269", "Ubiquitinated and degraded following phosphorylation by PLK2." ], [ "P28818-1", "protein_xref_pubmed", "21382555", "ECO_0000269", "Ubiquitinated and degraded following phosphorylation by PLK2." ], [ "O88498-1", "protein_xref_uniprotkb", "O88498", "ECO_0000269", "Ubiquitination by TRIM2 following phosphorylation by MAPK1/MAPK3 leads to proteasomal degradation (PubMed:21478148). Conversely, deubiquitination catalyzed by USP27X stabilizes the protein (By similarity)." ], [ "O88498-1", "protein_xref_pubmed", "21478148", "ECO_0000269", "Ubiquitination by TRIM2 following phosphorylation by MAPK1/MAPK3 leads to proteasomal degradation (PubMed:21478148). Conversely, deubiquitination catalyzed by USP27X stabilizes the protein (By similarity)." ], [ "O35346-1", "protein_xref_uniprotkb", "O35346", "ECO_0000269", "Sumoylated; this enhances autophosphorylation." ], [ "O35346-1", "protein_xref_pubmed", "14500712", "ECO_0000269", "Sumoylated; this enhances autophosphorylation." ], [ "O35346-1", "protein_xref_pubmed", "16373587", "ECO_0000269", "Sumoylated; this enhances autophosphorylation." ], [ "O35346-1", "protein_xref_pubmed", "12732587", "ECO_0000269", "Sumoylated; this enhances autophosphorylation." ], [ "Q8CG08-1", "protein_xref_uniprotkb", "Q8CG08", "ECO_0000269", "N-glycosylated." ], [ "Q8CG08-1", "protein_xref_pubmed", "15618538", "ECO_0000269", "N-glycosylated." ], [ "D3ZMK9-1", "protein_xref_uniprotkb", "D3ZMK9", "ECO_0000269", "Phosphorylated by CSK on Tyr-238, Tyr-343, and Tyr-391; Tyr-391 is a primary site of phosphorylation." ], [ "D3ZMK9-1", "protein_xref_pubmed", "27116701", "ECO_0000269", "Phosphorylated by CSK on Tyr-238, Tyr-343, and Tyr-391; Tyr-391 is a primary site of phosphorylation." ], [ "P13668-1", "protein_xref_uniprotkb", "P13668", "ECO_0000269", "Many different phosphorylated forms are observed depending on specific combinations among the sites which can be phosphorylated. MAPK is responsible for the phosphorylation of stathmin in response to NGF (By similarity). Phosphorylation at Ser-16 is higher in the developing axons from hippocampal neurons and seems to be required for neuron polarization." ], [ "P13668-1", "protein_xref_pubmed", "16982419", "ECO_0000269", "Many different phosphorylated forms are observed depending on specific combinations among the sites which can be phosphorylated. MAPK is responsible for the phosphorylation of stathmin in response to NGF (By similarity). Phosphorylation at Ser-16 is higher in the developing axons from hippocampal neurons and seems to be required for neuron polarization." ], [ "P35411-1", "protein_xref_uniprotkb", "P35411", "ECO_0000269", "This protein is not N-glycosylated which is unusual for G-protein-coupled receptors." ], [ "P35411-1", "protein_xref_pubmed", "8047298", "ECO_0000269", "This protein is not N-glycosylated which is unusual for G-protein-coupled receptors." ], [ "Q04940-1", "protein_xref_uniprotkb", "Q04940", "ECO_0000269", "Phosphorylation is activated by calcium, phospholipids, and diacylglycerol. Phosphorylation inhibits binding to calmodulin both in the presence and absence of calcium." ], [ "Q04940-1", "protein_xref_pubmed", "8454596", "ECO_0000269", "Phosphorylation is activated by calcium, phospholipids, and diacylglycerol. Phosphorylation inhibits binding to calmodulin both in the presence and absence of calcium." ], [ "Q04940-1", "protein_xref_pubmed", "8080473", "ECO_0000269", "Phosphorylation is activated by calcium, phospholipids, and diacylglycerol. Phosphorylation inhibits binding to calmodulin both in the presence and absence of calcium." ], [ "Q9WVT0-1", "protein_xref_uniprotkb", "Q9WVT0", "ECO_0000269", "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." ], [ "Q9WVT0-1", "protein_xref_pubmed", "16882675", "ECO_0000269", "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." ], [ "Q9WVT0-1", "protein_xref_pubmed", "11973329", "ECO_0000269", "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." ], [ "Q9WVT0-1", "protein_xref_uniprotkb", "Q9WVT0", "ECO_0000269", "Highly glycosylated." ], [ "Q9WVT0-1", "protein_xref_pubmed", "16882675", "ECO_0000269", "Highly glycosylated." ], [ "Q9WVT0-1", "protein_xref_pubmed", "10391944", "ECO_0000269", "Highly glycosylated." ], [ "Q5FVQ0-1", "protein_xref_uniprotkb", "Q5FVQ0", "ECO_0000269", "N-glycosylated. N-glycosylation is not required for proper iron and zinc transport." ], [ "Q5FVQ0-1", "protein_xref_pubmed", "22898811", "ECO_0000269", "N-glycosylated. N-glycosylation is not required for proper iron and zinc transport." ], [ "Q63772-1", "protein_xref_uniprotkb", "Q63772", "ECO_0000305", "Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation. These residues are essential for the binding of calcium (Probable)." ], [ "Q63772-1", "protein_xref_pubmed", "9163328", "ECO_0000305", "Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation. These residues are essential for the binding of calcium (Probable)." ], [ "P11497-1", "protein_xref_uniprotkb", "P11497", "ECO_0000305", "The biotin cofactor is covalently attached to the central biotinyl-binding domain and is required for the catalytic activity." ], [ "P11497-1", "protein_xref_pubmed", "2567668", "ECO_0000305", "The biotin cofactor is covalently attached to the central biotinyl-binding domain and is required for the catalytic activity." ], [ "P11497-1", "protein_xref_uniprotkb", "P11497", "ECO_0000269", "Phosphorylation at Ser-79 by AMPK inactivates enzyme activity. Phosphorylated in vitro at Ser-1200 and Ser-1215 by AMPK; the relevance of phosphorylation of these sites in vivo is however unclear." ], [ "P11497-1", "protein_xref_pubmed", "2900138", "ECO_0000269", "Phosphorylation at Ser-79 by AMPK inactivates enzyme activity. Phosphorylated in vitro at Ser-1200 and Ser-1215 by AMPK; the relevance of phosphorylation of these sites in vivo is however unclear." ], [ "P11497-1", "protein_xref_pubmed", "9029219", "ECO_0000269", "Phosphorylation at Ser-79 by AMPK inactivates enzyme activity. Phosphorylated in vitro at Ser-1200 and Ser-1215 by AMPK; the relevance of phosphorylation of these sites in vivo is however unclear." ], [ "P11497-1", "protein_xref_pubmed", "1346520", "ECO_0000269", "Phosphorylation at Ser-79 by AMPK inactivates enzyme activity. Phosphorylated in vitro at Ser-1200 and Ser-1215 by AMPK; the relevance of phosphorylation of these sites in vivo is however unclear." ], [ "P11497-1", "protein_xref_pubmed", "1974251", "ECO_0000269", "Phosphorylation at Ser-79 by AMPK inactivates enzyme activity. Phosphorylated in vitro at Ser-1200 and Ser-1215 by AMPK; the relevance of phosphorylation of these sites in vivo is however unclear." ], [ "P60192-1", "protein_xref_uniprotkb", "P60192", "ECO_0000269", "Phosphorylated by CSNK1D/CK1." ], [ "P60192-1", "protein_xref_pubmed", "11283605", "ECO_0000269", "Phosphorylated by CSNK1D/CK1." ], [ "P09951-1", "protein_xref_uniprotkb", "P09951", "ECO_0000269", "Substrate of different protein kinases. Phosphorylation, including phosphorylation at Ser-9, promotes synapsin-1 dissociation from synaptic vesicles, regulates its rate of dispersion, and controls the kinetics of vesicle pool turnover (PubMed:10571231, PubMed:11685225)." ], [ "P09951-1", "protein_xref_pubmed", "11685225", "ECO_0000269", "Substrate of different protein kinases. Phosphorylation, including phosphorylation at Ser-9, promotes synapsin-1 dissociation from synaptic vesicles, regulates its rate of dispersion, and controls the kinetics of vesicle pool turnover (PubMed:10571231, PubMed:11685225)." ], [ "P09951-1", "protein_xref_pubmed", "10571231", "ECO_0000269", "Substrate of different protein kinases. Phosphorylation, including phosphorylation at Ser-9, promotes synapsin-1 dissociation from synaptic vesicles, regulates its rate of dispersion, and controls the kinetics of vesicle pool turnover (PubMed:10571231, PubMed:11685225)." ], [ "Q8VH46-1", "protein_xref_uniprotkb", "Q8VH46", "ECO_0000269", "Phosphorylated on tyrosine residues." ] ] }, "readme": "Name\n - Rat Protein PTM Annotation (UniProtKB)\n\nVersion\n - v-2.4.1\n\nCreated on\n - 2019-11-30T14:07:14.445471\n\nModified on\n - 2022-09-26T09:05:27.733591\n\nCreated by\n - Jeet Vora [jeetvora@gwu.edu], Robel Kahsay [rykahsay@gwu.edu], Karina Martinez [karinamartinez@gwu.edu], Luke Johnson [luke.johnson@email.gwu.edu], Urnisha Bhuiyan [sbhuiyan28@email.gwu.edu], Cyrus Au-Yeung [cyruschauyeung@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 Rat Protein PTM Annotation (UniProtKB) dataset contains rat [taxid:10116] 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 sequnces asnd 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-rattus-norvegicus.nt\n URI: https:/data.glygen.org/ln2downloads/ebi/2024_02_13/uniprot-proteome-rattus-norvegicus.nt\n Output Subdomain\n Name: rat_protein_ptm_annotation_uniprotkb.csv\n URI: https:/data.glygen.org/ln2releases/data/v-2.4.1/reviewed/rat_protein_ptm_annotation_uniprotkb.csv\n Name: rat_protein_ptm_annotation_uniprotkb.stat.csv\n URI: https:/data.glygen.org/ln2releases/data/v-2.4.1/reviewed/rat_protein_ptm_annotation_uniprotkb.stat.csv\n\nFields\n Name: \"uniprotkb_canonical_ac\"\n Description: \"\"\n Unique Values: \"574\"\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: \"1363\"\n Name: \"eco_id\"\n Description: \"Evidence & Conclusion Ontology (ECO) identifier\"\n Unique Values: \"3\"\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: \"564\"", "downloadurl": "/ln2data/releases/data/v-2.4.1/reviewed/rat_protein_ptm_annotation_uniprotkb.csv" }