{ "bcoid": "GLY_000650", "title": "Fruitfly Protein PTM Annotation (UniProtKB)", "description": "The Fruitfly Protein PTM Annotation (UniProtKB) dataset contains fruitfly [taxid:7227] PTM annotations ...", "filename": "fruitfly_protein_ptm_annotation_uniprotkb.csv", "filetype": "csv", "categories": { "species": [ "Drosophila melanogaster" ], "molecule": [ "Protein" ], "tag": [ "PTM annotation" ], "file_type": [ "csv" ], "status": [ "Reviewed" ], "scope": [ "internal" ] }, "minitable": { "content": [ [ "P40797-1...", "protein_xref..." ], [ "P40797-1...", "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" } ], [ "P40797-1", "protein_xref_uniprotkb", "P40797", "ECO_0000269", "Ubiquitinated by park, leading to its degradation by the proteasome." ], [ "P40797-1", "protein_xref_pubmed", "17456438", "ECO_0000269", "Ubiquitinated by park, leading to its degradation by the proteasome." ], [ "P06607-1", "protein_xref_uniprotkb", "P06607", "ECO_0000269", "Tyrosine sulfation occurs in the female only and plays an essential functional role." ], [ "P06607-1", "protein_xref_pubmed", "3922974", "ECO_0000269", "Tyrosine sulfation occurs in the female only and plays an essential functional role." ], [ "P18475-1", "protein_xref_uniprotkb", "P18475", "ECO_0000250", "May be auto-phosphorylated on tyrosine residues." ], [ "P18475-1", "protein_xref_pubmed", "D2IYS2", "ECO_0000250", "May be auto-phosphorylated on tyrosine residues." ], [ "P00528-1", "protein_xref_uniprotkb", "P00528", "ECO_0000269", "Phosphorylated." ], [ "P00528-1", "protein_xref_pubmed", "31491385", "ECO_0000269", "Phosphorylated." ], [ "Q9V9Y9-1", "protein_xref_uniprotkb", "Q9V9Y9", "ECO_0000269", "Phosphorylated by IKKepsilon (PubMed:18796167, PubMed:26540204). Phosphorylation is required for spn-F neuronal distribution and dendrite pruning and reduces spn-F homooligomerization (PubMed:26540204). It does not lead to spn-F degradation (PubMed:18796167)." ], [ "Q9V9Y9-1", "protein_xref_pubmed", "26540204", "ECO_0000269", "Phosphorylated by IKKepsilon (PubMed:18796167, PubMed:26540204). Phosphorylation is required for spn-F neuronal distribution and dendrite pruning and reduces spn-F homooligomerization (PubMed:26540204). It does not lead to spn-F degradation (PubMed:18796167)." ], [ "Q9V9Y9-1", "protein_xref_pubmed", "18796167", "ECO_0000269", "Phosphorylated by IKKepsilon (PubMed:18796167, PubMed:26540204). Phosphorylation is required for spn-F neuronal distribution and dendrite pruning and reduces spn-F homooligomerization (PubMed:26540204). It does not lead to spn-F degradation (PubMed:18796167)." ], [ "O16844-1", "protein_xref_uniprotkb", "O16844", "ECO_0000269", "Polyubiquitinated by Ubr3, which leads to proteasomal degradation." ], [ "O16844-1", "protein_xref_pubmed", "27195754", "ECO_0000269", "Polyubiquitinated by Ubr3, which leads to proteasomal degradation." ], [ "Q24119-5", "protein_xref_uniprotkb", "Q24119", "ECO_0000269", "Ser-673 phosphorylation by PKB/Akt1 is required for nuclear targeting and transcriptional activity." ], [ "Q24119-5", "protein_xref_pubmed", "11740943", "ECO_0000269", "Ser-673 phosphorylation by PKB/Akt1 is required for nuclear targeting and transcriptional activity." ], [ "Q0KHV6-1", "protein_xref_uniprotkb", "Q0KHV6", "ECO_0000269", "Autophosphorylated on Ser-346, which activates kinase activity (PubMed:25474007, PubMed:27906179). Loss of mitochondrial membrane potential results in the precursor accumulating on the outer mitochondrial membrane (OMM) where it is activated by autophosphorylation at Ser-346 (PubMed:27906179). Autophosphorylation is sufficient and essential for selective recruitment of park to depolarized mitochondria, likely via Pink1-dependent phosphorylation of polyubiquitin chains (PubMed:25474007, PubMed:27906179)." ], [ "Q0KHV6-1", "protein_xref_pubmed", "27906179", "ECO_0000269", "Autophosphorylated on Ser-346, which activates kinase activity (PubMed:25474007, PubMed:27906179). Loss of mitochondrial membrane potential results in the precursor accumulating on the outer mitochondrial membrane (OMM) where it is activated by autophosphorylation at Ser-346 (PubMed:27906179). Autophosphorylation is sufficient and essential for selective recruitment of park to depolarized mitochondria, likely via Pink1-dependent phosphorylation of polyubiquitin chains (PubMed:25474007, PubMed:27906179)." ], [ "Q0KHV6-1", "protein_xref_pubmed", "25474007", "ECO_0000269", "Autophosphorylated on Ser-346, which activates kinase activity (PubMed:25474007, PubMed:27906179). Loss of mitochondrial membrane potential results in the precursor accumulating on the outer mitochondrial membrane (OMM) where it is activated by autophosphorylation at Ser-346 (PubMed:27906179). Autophosphorylation is sufficient and essential for selective recruitment of park to depolarized mitochondria, likely via Pink1-dependent phosphorylation of polyubiquitin chains (PubMed:25474007, PubMed:27906179)." ], [ "Q0KHV6-1", "protein_xref_uniprotkb", "Q0KHV6", "ECO_0000269", "Proteolytically cleaved (PubMed:19048081). In healthy cells, the precursor is continuously imported into mitochondria where it is proteolytically cleaved into its short form by the mitochondrial rhomboid protease rho-7 (PubMed:19048081). The short form is then released into the cytosol where it rapidly undergoes proteasome-dependent degradation (Probable). In unhealthy cells, when cellular stress conditions lead to the loss of mitochondrial membrane potential, mitochondrial import is impaired leading to the precursor accumulating on the outer mitochondrial membrane (OMM) (PubMed:27906179)." ], [ "Q0KHV6-1", "protein_xref_pubmed", "27906179", "ECO_0000269", "Proteolytically cleaved (PubMed:19048081). In healthy cells, the precursor is continuously imported into mitochondria where it is proteolytically cleaved into its short form by the mitochondrial rhomboid protease rho-7 (PubMed:19048081). The short form is then released into the cytosol where it rapidly undergoes proteasome-dependent degradation (Probable). In unhealthy cells, when cellular stress conditions lead to the loss of mitochondrial membrane potential, mitochondrial import is impaired leading to the precursor accumulating on the outer mitochondrial membrane (OMM) (PubMed:27906179)." ], [ "Q0KHV6-1", "protein_xref_pubmed", "19048081", "ECO_0000269", "Proteolytically cleaved (PubMed:19048081). In healthy cells, the precursor is continuously imported into mitochondria where it is proteolytically cleaved into its short form by the mitochondrial rhomboid protease rho-7 (PubMed:19048081). The short form is then released into the cytosol where it rapidly undergoes proteasome-dependent degradation (Probable). In unhealthy cells, when cellular stress conditions lead to the loss of mitochondrial membrane potential, mitochondrial import is impaired leading to the precursor accumulating on the outer mitochondrial membrane (OMM) (PubMed:27906179)." ], [ "Q0KHV6-1", "protein_xref_uniprotkb", "Q0KHV6", "ECO_0000305", "Proteolytically cleaved (PubMed:19048081). In healthy cells, the precursor is continuously imported into mitochondria where it is proteolytically cleaved into its short form by the mitochondrial rhomboid protease rho-7 (PubMed:19048081). The short form is then released into the cytosol where it rapidly undergoes proteasome-dependent degradation (Probable). In unhealthy cells, when cellular stress conditions lead to the loss of mitochondrial membrane potential, mitochondrial import is impaired leading to the precursor accumulating on the outer mitochondrial membrane (OMM) (PubMed:27906179)." ], [ "Q0KHV6-1", "protein_xref_pubmed", "19048081", "ECO_0000305", "Proteolytically cleaved (PubMed:19048081). In healthy cells, the precursor is continuously imported into mitochondria where it is proteolytically cleaved into its short form by the mitochondrial rhomboid protease rho-7 (PubMed:19048081). The short form is then released into the cytosol where it rapidly undergoes proteasome-dependent degradation (Probable). In unhealthy cells, when cellular stress conditions lead to the loss of mitochondrial membrane potential, mitochondrial import is impaired leading to the precursor accumulating on the outer mitochondrial membrane (OMM) (PubMed:27906179)." ], [ "P33450-1", "protein_xref_uniprotkb", "P33450", "ECO_0000269", "Phosphorylated by fj on Ser/Thr of cadherin domains (PubMed:18635802). Phosphorylation by fj enhances binding to ds (PubMed:20434335). Phosphorylated in the cytoplasmic domain in a dco-dependent manner which is promoted by ds (PubMed:19574458)." ], [ "P33450-1", "protein_xref_pubmed", "18635802", "ECO_0000269", "Phosphorylated by fj on Ser/Thr of cadherin domains (PubMed:18635802). Phosphorylation by fj enhances binding to ds (PubMed:20434335). Phosphorylated in the cytoplasmic domain in a dco-dependent manner which is promoted by ds (PubMed:19574458)." ], [ "P33450-1", "protein_xref_pubmed", "19574458", "ECO_0000269", "Phosphorylated by fj on Ser/Thr of cadherin domains (PubMed:18635802). Phosphorylation by fj enhances binding to ds (PubMed:20434335). Phosphorylated in the cytoplasmic domain in a dco-dependent manner which is promoted by ds (PubMed:19574458)." ], [ "P33450-1", "protein_xref_pubmed", "20434335", "ECO_0000269", "Phosphorylated by fj on Ser/Thr of cadherin domains (PubMed:18635802). Phosphorylation by fj enhances binding to ds (PubMed:20434335). Phosphorylated in the cytoplasmic domain in a dco-dependent manner which is promoted by ds (PubMed:19574458)." ], [ "P33450-1", "protein_xref_uniprotkb", "P33450", "ECO_0000269", "Proteolytically cleaved to yield stably associated N- and C-terminal fragments (PubMed:19574458). The C-terminal fragment is processed further to release a 68 kDa mitochondrial fragment, Ft-mito (PubMed:25215488)." ], [ "P33450-1", "protein_xref_pubmed", "25215488", "ECO_0000269", "Proteolytically cleaved to yield stably associated N- and C-terminal fragments (PubMed:19574458). The C-terminal fragment is processed further to release a 68 kDa mitochondrial fragment, Ft-mito (PubMed:25215488)." ], [ "P33450-1", "protein_xref_pubmed", "19574458", "ECO_0000269", "Proteolytically cleaved to yield stably associated N- and C-terminal fragments (PubMed:19574458). The C-terminal fragment is processed further to release a 68 kDa mitochondrial fragment, Ft-mito (PubMed:25215488)." ], [ "P02572-1", "protein_xref_uniprotkb", "P02572", "ECO_0000269", "Oxidation of Met-45 by Mical to form methionine sulfoxide promotes actin filament depolymerization. Methionine sulfoxide is produced stereospecifically, but it is not known whether the (S)-S-oxide or the (R)-S-oxide is produced." ], [ "P02572-1", "protein_xref_pubmed", "22116028", "ECO_0000269", "Oxidation of Met-45 by Mical to form methionine sulfoxide promotes actin filament depolymerization. Methionine sulfoxide is produced stereospecifically, but it is not known whether the (S)-S-oxide or the (R)-S-oxide is produced." ], [ "P02572-1", "protein_xref_uniprotkb", "P02572", "ECO_0000250", "N-terminal cleavage of acetylated cysteine of immature actin by ACTMAP." ], [ "P02572-1", "protein_xref_pubmed", "P68134", "ECO_0000250", "N-terminal cleavage of acetylated cysteine of immature actin by ACTMAP." ], [ "P35415-1", "protein_xref_uniprotkb", "P35415", "ECO_0000269", "The more-acidic and less-abundant isoform is phosphorylated." ], [ "P35415-1", "protein_xref_pubmed", "18327897", "ECO_0000269", "The more-acidic and less-abundant isoform is phosphorylated." ], [ "P26019-1", "protein_xref_uniprotkb", "P26019", "ECO_0000269", "In embryos, a cleaved form of 130 kDa is produced up to cycle 14 and then disappears." ], [ "P26019-1", "protein_xref_pubmed", "7592543", "ECO_0000269", "In embryos, a cleaved form of 130 kDa is produced up to cycle 14 and then disappears." ], [ "P36193-1", "protein_xref_uniprotkb", "P36193", "ECO_0000269", "O-glycosylated (PubMed:8325867, PubMed:9888811, PubMed:9736738). O-glycosylation is essential for full biological activity (PubMed:8325867)." ], [ "P36193-1", "protein_xref_pubmed", "8325867", "ECO_0000269", "O-glycosylated (PubMed:8325867, PubMed:9888811, PubMed:9736738). O-glycosylation is essential for full biological activity (PubMed:8325867)." ], [ "P36193-1", "protein_xref_pubmed", "9736738", "ECO_0000269", "O-glycosylated (PubMed:8325867, PubMed:9888811, PubMed:9736738). O-glycosylation is essential for full biological activity (PubMed:8325867)." ], [ "P36193-1", "protein_xref_pubmed", "9888811", "ECO_0000269", "O-glycosylated (PubMed:8325867, PubMed:9888811, PubMed:9736738). O-glycosylation is essential for full biological activity (PubMed:8325867)." ], [ "Q9VS59-1", "protein_xref_uniprotkb", "Q9VS59", "ECO_0000269", "Polyubiquitinated via 'Lys-63'-linked ubiquitin by Hyd, promoting interaction with rel." ], [ "Q9VS59-1", "protein_xref_pubmed", "32950464", "ECO_0000269", "Polyubiquitinated via 'Lys-63'-linked ubiquitin by Hyd, promoting interaction with rel." ], [ "B5A5T4-1", "protein_xref_uniprotkb", "B5A5T4", "ECO_0000269", "N-glycosylated." ], [ "B5A5T4-1", "protein_xref_pubmed", "18635795", "ECO_0000269", "N-glycosylated." ], [ "Q8IPH9-1", "protein_xref_uniprotkb", "Q8IPH9", "ECO_0000269", "Phosphorylated. Phosphorylation of Ser-54 and Ser-79 is required for the interaction with 14-3-3-zeta but not with that of Slo." ], [ "Q8IPH9-1", "protein_xref_pubmed", "10230800", "ECO_0000269", "Phosphorylated. Phosphorylation of Ser-54 and Ser-79 is required for the interaction with 14-3-3-zeta but not with that of Slo." ], [ "M9NDE3-1", "protein_xref_uniprotkb", "M9NDE3", "ECO_0000269", "N-glycosylated." ], [ "M9NDE3-1", "protein_xref_pubmed", "25982676", "ECO_0000269", "N-glycosylated." ], [ "M9NDE3-1", "protein_xref_uniprotkb", "M9NDE3", "ECO_0000269", "May be proteolytically cleaved in the extracellular domain." ], [ "M9NDE3-1", "protein_xref_pubmed", "25982676", "ECO_0000269", "May be proteolytically cleaved in the extracellular domain." ], [ "P08111-1", "protein_xref_uniprotkb", "P08111", "ECO_0000269", "Phosphorylated by aPKC which lowers lipid affinity and promotes dissociation from the cell cortex (PubMed:26481050). In developing oocytes, aPKC-mediated phosphorylation restricts activity to the oocyte posterior and is required for oocyte polarity formation (PubMed:18094021, PubMed:18327897)." ], [ "P08111-1", "protein_xref_pubmed", "26481050", "ECO_0000269", "Phosphorylated by aPKC which lowers lipid affinity and promotes dissociation from the cell cortex (PubMed:26481050). In developing oocytes, aPKC-mediated phosphorylation restricts activity to the oocyte posterior and is required for oocyte polarity formation (PubMed:18094021, PubMed:18327897)." ], [ "P08111-1", "protein_xref_pubmed", "18094021", "ECO_0000269", "Phosphorylated by aPKC which lowers lipid affinity and promotes dissociation from the cell cortex (PubMed:26481050). In developing oocytes, aPKC-mediated phosphorylation restricts activity to the oocyte posterior and is required for oocyte polarity formation (PubMed:18094021, PubMed:18327897)." ], [ "P08111-1", "protein_xref_pubmed", "18327897", "ECO_0000269", "Phosphorylated by aPKC which lowers lipid affinity and promotes dissociation from the cell cortex (PubMed:26481050). In developing oocytes, aPKC-mediated phosphorylation restricts activity to the oocyte posterior and is required for oocyte polarity formation (PubMed:18094021, PubMed:18327897)." ], [ "Q9VJN9-1", "protein_xref_uniprotkb", "Q9VJN9", "ECO_0000269", "Undergoes cleavage in the male during mating with a cleaved product detected in the ejaculatory duct and/or bulb of males by 8-10 minutes after the start of mating (PubMed:17116868). Further cleavage occurs in the mated female (PubMed:15979005). May undergo cleavage in a two-step process where it is first cleaved by Sems, making it susceptible to activational cleavage which may be carried out by another protease or by autocleavage (PubMed:24514904)." ], [ "Q9VJN9-1", "protein_xref_pubmed", "24514904", "ECO_0000269", "Undergoes cleavage in the male during mating with a cleaved product detected in the ejaculatory duct and/or bulb of males by 8-10 minutes after the start of mating (PubMed:17116868). Further cleavage occurs in the mated female (PubMed:15979005). May undergo cleavage in a two-step process where it is first cleaved by Sems, making it susceptible to activational cleavage which may be carried out by another protease or by autocleavage (PubMed:24514904)." ], [ "Q9VJN9-1", "protein_xref_pubmed", "15979005", "ECO_0000269", "Undergoes cleavage in the male during mating with a cleaved product detected in the ejaculatory duct and/or bulb of males by 8-10 minutes after the start of mating (PubMed:17116868). Further cleavage occurs in the mated female (PubMed:15979005). May undergo cleavage in a two-step process where it is first cleaved by Sems, making it susceptible to activational cleavage which may be carried out by another protease or by autocleavage (PubMed:24514904)." ], [ "Q9VJN9-1", "protein_xref_pubmed", "17116868", "ECO_0000269", "Undergoes cleavage in the male during mating with a cleaved product detected in the ejaculatory duct and/or bulb of males by 8-10 minutes after the start of mating (PubMed:17116868). Further cleavage occurs in the mated female (PubMed:15979005). May undergo cleavage in a two-step process where it is first cleaved by Sems, making it susceptible to activational cleavage which may be carried out by another protease or by autocleavage (PubMed:24514904)." ], [ "P15372-1", "protein_xref_uniprotkb", "P15372", "ECO_0000269", "Phosphorylated, but does not undergo light-induced phosphorylation." ], [ "P15372-1", "protein_xref_pubmed", "1905538", "ECO_0000269", "Phosphorylated, but does not undergo light-induced phosphorylation." ], [ "P28466-1", "protein_xref_uniprotkb", "P28466", "ECO_0000250", "Palmitoleoylated by porcupine. The lipid group functions as a sorting signal, targeting the ligand to polarized vesicles that transport Wnt5 to unique sites at the cell surface. Depalmitoleoylated by notum, leading to inhibit Wnt signaling pathway." ], [ "P28466-1", "protein_xref_pubmed", "P09615", "ECO_0000250", "Palmitoleoylated by porcupine. The lipid group functions as a sorting signal, targeting the ligand to polarized vesicles that transport Wnt5 to unique sites at the cell surface. Depalmitoleoylated by notum, leading to inhibit Wnt signaling pathway." ], [ "P28466-1", "protein_xref_uniprotkb", "P28466", "ECO_0000269", "Glycosylated, glycosylation is stimulated by porcupine at the ER." ], [ "P28466-1", "protein_xref_pubmed", "11821428", "ECO_0000269", "Glycosylated, glycosylation is stimulated by porcupine at the ER." ], [ "P28465-1", "protein_xref_uniprotkb", "P28465", "ECO_0000250", "Palmitoleoylated by porcupine. The lipid group functions as a sorting signal, targeting the ligand to polarized vesicles that transport Wnt2 to unique sites at the cell surface. Depalmitoleoylated by notum, leading to inhibit Wnt signaling pathway." ], [ "P28465-1", "protein_xref_pubmed", "P09615", "ECO_0000250", "Palmitoleoylated by porcupine. The lipid group functions as a sorting signal, targeting the ligand to polarized vesicles that transport Wnt2 to unique sites at the cell surface. Depalmitoleoylated by notum, leading to inhibit Wnt signaling pathway." ], [ "Q24311-1", "protein_xref_uniprotkb", "Q24311", "ECO_0000269", "Neddylated (PubMed:12183637, PubMed:18493598). Deneddylated via its interaction with the COP9 signalosome (CSN) complex (PubMed:12183637)." ], [ "Q24311-1", "protein_xref_pubmed", "12183637", "ECO_0000269", "Neddylated (PubMed:12183637, PubMed:18493598). Deneddylated via its interaction with the COP9 signalosome (CSN) complex (PubMed:12183637)." ], [ "Q24311-1", "protein_xref_pubmed", "18493598", "ECO_0000269", "Neddylated (PubMed:12183637, PubMed:18493598). Deneddylated via its interaction with the COP9 signalosome (CSN) complex (PubMed:12183637)." ], [ "P07140-1", "protein_xref_uniprotkb", "P07140", "ECO_0000269", "Proteolytic cleavage into the 16 kDa subunit and the 55 kDa subunits originates from the hydrophilic peptide, aa 148-180, and is associated with excretion out of the cell." ], [ "P07140-1", "protein_xref_pubmed", "2975507", "ECO_0000269", "Proteolytic cleavage into the 16 kDa subunit and the 55 kDa subunits originates from the hydrophilic peptide, aa 148-180, and is associated with excretion out of the cell." ], [ "P07140-1", "protein_xref_uniprotkb", "P07140", "ECO_0000269", "Neither N-glycosylation nor dimerization is required for enzyme activity or substrate specificity, but protects the protein against proteolytic digestion." ], [ "P07140-1", "protein_xref_pubmed", "1730712", "ECO_0000269", "Neither N-glycosylation nor dimerization is required for enzyme activity or substrate specificity, but protects the protein against proteolytic digestion." ], [ "P54367-1", "protein_xref_uniprotkb", "P54367", "ECO_0000269", "Phosphorylated. The dephosphorylated kinase is active in the cytoplasm while the active kinase in the nucleus is phosphorylated." ], [ "P54367-1", "protein_xref_pubmed", "8832407", "ECO_0000269", "Phosphorylated. The dephosphorylated kinase is active in the cytoplasm while the active kinase in the nucleus is phosphorylated." ], [ "P54360-1", "protein_xref_uniprotkb", "P54360", "ECO_0000269", "Proteolytically cleaved to yield a secreted protein." ], [ "P54360-1", "protein_xref_pubmed", "14757640", "ECO_0000269", "Proteolytically cleaved to yield a secreted protein." ], [ "P33438-1", "protein_xref_uniprotkb", "P33438", "ECO_0000269", "About four tyrosines are sulfated." ], [ "P33438-1", "protein_xref_pubmed", "2108864", "ECO_0000269", "About four tyrosines are sulfated." ], [ "Q7K4Z4-1", "protein_xref_uniprotkb", "Q7K4Z4", "ECO_0000269", "Caspase-mediated cleavage is required for activation and function; upon immune stimulation, peptidoglycans (PGN) induce proteolytic cleavage by caspases such as Dredd leading to its ubiquitination." ], [ "Q7K4Z4-1", "protein_xref_pubmed", "20122400", "ECO_0000269", "Caspase-mediated cleavage is required for activation and function; upon immune stimulation, peptidoglycans (PGN) induce proteolytic cleavage by caspases such as Dredd leading to its ubiquitination." ], [ "Q7K4Z4-1", "protein_xref_uniprotkb", "Q7K4Z4", "ECO_0000269", "Phosphorylated." ] ] }, "readme": "Name\n - Fruitfly Protein PTM Annotation (UniProtKB)\n\nVersion\n - v-2.2.1\n\nCreated on\n - 2022-08-31T10:58:38.192589\n\nModified on\n - 2022-09-26T09:08:12.662574\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 Fruitfly Protein PTM Annotation (UniProtKB) dataset contains fruitfly [taxid:7227] PTM annotations for UniProtKB canonical accessions. The annotation is the curated statements of mainly about glycosylation and phosphorylation. If you use this dataset please give proper attribution to EMBL-EBI-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-drosophila-melanogaster.nt\n URI: https:/data.glygen.org/ln2downloads/ebi/2023_10_30/uniprot-proteome-drosophila-melanogaster.nt\n Output Subdomain\n Name: fruitfly_protein_ptm_annotation_uniprotkb.csv\n URI: https:/data.glygen.org/ln2releases/data/v-2.2.1/reviewed/fruitfly_protein_ptm_annotation_uniprotkb.csv\n Name: fruitfly_protein_ptm_annotation_uniprotkb.stat.csv\n URI: https:/data.glygen.org/ln2releases/data/v-2.2.1/reviewed/fruitfly_protein_ptm_annotation_uniprotkb.stat.csv\n\nFields\n Name: \"uniprotkb_canonical_ac\"\n Description: \"\"\n Unique Values: \"255\"\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: \"588\"\n Name: \"eco_id\"\n Description: \"Evidence & Conclusion Ontology (ECO) identifier\"\n Unique Values: \"6\"\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: \"254\"", "downloadurl": "/ln2data/releases/data/v-2.2.1/reviewed/fruitfly_protein_ptm_annotation_uniprotkb.csv" }