{ "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": [ [ "Q0HA29-1...", "protein_xref..." ], [ "Q0HA29-1...", "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" } ], [ "Q0HA29-1", "protein_xref_uniprotkb", "Q0HA29", "ECO_0000250", "Degraded in response to injured neurite (By similarity). Degradation is caused by polyubiquitination by MYCBP2 after recognition by FBXO45 (By similarity)." ], [ "Q0HA29-1", "protein_xref_pubmed", "Q9BZQ4", "ECO_0000250", "Degraded in response to injured neurite (By similarity). Degradation is caused by polyubiquitination by MYCBP2 after recognition by FBXO45 (By similarity)." ], [ "Q0HA29-1", "protein_xref_pubmed", "Q8BNJ3", "ECO_0000250", "Degraded in response to injured neurite (By similarity). Degradation is caused by polyubiquitination by MYCBP2 after recognition by FBXO45 (By similarity)." ], [ "Q0HA29-1", "protein_xref_uniprotkb", "Q0HA29", "ECO_0000250", "Palmitoylated; palmitoylation is required for membrane association." ], [ "Q0HA29-1", "protein_xref_pubmed", "Q8BNJ3", "ECO_0000250", "Palmitoylated; palmitoylation is required for membrane association." ], [ "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." ], [ "Q9JHY7-1", "protein_xref_uniprotkb", "Q9JHY7", "ECO_0000250", "In vitro phosphorylation at Thr-117 by AURKB prevents interaction with INCENP and localization to mitotic chromosomes. Phosphorylation at Thr-48 by CK2 is critical for its mitotic and anti-apoptotic activities. Phosphorylation at Thr-34 by CDK15 is critical for its anti-apoptotic activity." ], [ "Q9JHY7-1", "protein_xref_pubmed", "O15392", "ECO_0000250", "In vitro phosphorylation at Thr-117 by AURKB prevents interaction with INCENP and localization to mitotic chromosomes. Phosphorylation at Thr-48 by CK2 is critical for its mitotic and anti-apoptotic activities. Phosphorylation at Thr-34 by CDK15 is critical for its anti-apoptotic activity." ], [ "Q9JHY7-1", "protein_xref_uniprotkb", "Q9JHY7", "ECO_0000250", "Ubiquitinated by the Cul9-RING ubiquitin-protein ligase complex, leading to its degradation. Ubiquitination is required for centrosomal targeting." ], [ "Q9JHY7-1", "protein_xref_pubmed", "O15392", "ECO_0000250", "Ubiquitinated by the Cul9-RING ubiquitin-protein ligase complex, leading to its degradation. Ubiquitination is required for centrosomal targeting." ], [ "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." ], [ "D3ZSP7-1", "protein_xref_uniprotkb", "D3ZSP7", "ECO_0000250", "Proteolytically cleaved into differently sized N- and C-terminal fragments." ], [ "D3ZSP7-1", "protein_xref_pubmed", "P53804", "ECO_0000250", "Proteolytically cleaved into differently sized N- and C-terminal fragments." ], [ "D3ZSP7-1", "protein_xref_uniprotkb", "D3ZSP7", "ECO_0000250", "Phosphorylation on Ser-397 by Akt is required for ubiquitin ligase activity." ], [ "D3ZSP7-1", "protein_xref_pubmed", "P53804", "ECO_0000250", "Phosphorylation on Ser-397 by Akt is required for ubiquitin ligase activity." ], [ "Q9JIL3-1", "protein_xref_uniprotkb", "Q9JIL3", "ECO_0000250", "Phosphorylated at Thr-188 and Thr-315 by PKR in response to RNA viruses. This phosphorylation results in the dissociation of ILF2 from the ILF2-ILF3 complex resulting in a cytoplasmic sequestration of ILF3 where it can bind to viral RNAs and impede viral replication." ], [ "Q9JIL3-1", "protein_xref_pubmed", "Q12906", "ECO_0000250", "Phosphorylated at Thr-188 and Thr-315 by PKR in response to RNA viruses. This phosphorylation results in the dissociation of ILF2 from the ILF2-ILF3 complex resulting in a cytoplasmic sequestration of ILF3 where it can bind to viral RNAs and impede viral replication." ], [ "Q9JIL3-1", "protein_xref_uniprotkb", "Q9JIL3", "ECO_0000250", "Methylated by protein arginine N-methyltransferase 1." ], [ "Q9JIL3-1", "protein_xref_pubmed", "Q12906", "ECO_0000250", "Methylated by protein arginine N-methyltransferase 1." ], [ "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_0000250", "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", "Q9EQX0", "ECO_0000250", "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_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_0000250", "Methylated at Gln-271 by N6AMT1." ], [ "Q9ESR9-1", "protein_xref_pubmed", "Q9BZC7", "ECO_0000250", "Methylated at Gln-271 by N6AMT1." ], [ "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_0000250", "ENaC cleavage by furin, and subsequently by prostasin (PRSS8), leads to a stepwise increase in the open probability of the channel as a result of release of the alpha and gamma subunit inhibitory tracts, respectively. Interaction of ENaC subunit SCNN1B with BPIFA1 protects ENaC against proteolytic activation." ], [ "P37089-1", "protein_xref_pubmed", "P37088", "ECO_0000250", "ENaC cleavage by furin, and subsequently by prostasin (PRSS8), leads to a stepwise increase in the open probability of the channel as a result of release of the alpha and gamma subunit inhibitory tracts, respectively. Interaction of ENaC subunit SCNN1B with BPIFA1 protects ENaC against proteolytic activation." ], [ "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." ], [ "Q62737-1", "protein_xref_uniprotkb", "Q62737", "ECO_0000250", "Ubiquitinated at Lys-149 likely by RNF145." ], [ "Q62737-1", "protein_xref_pubmed", "Q61462", "ECO_0000250", "Ubiquitinated at Lys-149 likely by RNF145." ], [ "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." ], [ "Q62735-1", "protein_xref_uniprotkb", "Q62735", "ECO_0000250", "Sumoylated upon ligand binding." ], [ "Q62735-1", "protein_xref_pubmed", "Q96RI1", "ECO_0000250", "Sumoylated upon ligand binding." ], [ "Q62735-1", "protein_xref_uniprotkb", "Q62735", "ECO_0000250", "Acetylated by EP300. Lys-210 as is the major acetylation site for EP300; the dynamicly regulated acetylation inhibits heterodimerization with RXRA and transactivation activity. Deacetylated by SIRT1." ], [ "Q62735-1", "protein_xref_pubmed", "Q96RI1", "ECO_0000250", "Acetylated by EP300. Lys-210 as is the major acetylation site for EP300; the dynamicly regulated acetylation inhibits heterodimerization with RXRA and transactivation activity. Deacetylated by SIRT1." ], [ "Q62735-1", "protein_xref_uniprotkb", "Q62735", "ECO_0000250", "Methylation may increase transactivation of target genes." ], [ "Q62735-1", "protein_xref_pubmed", "Q96RI1", "ECO_0000250", "Methylation may increase transactivation of target genes." ], [ "Q62735-1", "protein_xref_uniprotkb", "Q62735", "ECO_0000250", "Phosphorylation by PKC/PRKCA increases transactivation activity by promoting association with PPARGC1A." ], [ "Q62735-1", "protein_xref_pubmed", "Q96RI1", "ECO_0000250", "Phosphorylation by PKC/PRKCA increases transactivation activity by promoting association with PPARGC1A." ], [ "Q9Z1Z3-1", "protein_xref_uniprotkb", "Q9Z1Z3", "ECO_0000269", "Ubiquitinated." ], [ "Q9Z1Z3-1", "protein_xref_pubmed", "11919637", "ECO_0000269", "Ubiquitinated." ], [ "O35923-1", "protein_xref_uniprotkb", "O35923", "ECO_0000250", "Phosphorylated by ATM upon irradiation-induced DNA damage. Phosphorylation by CHEK1 and CHEK2 regulates interaction with RAD51. Phosphorylation at Ser-3222 by CDK1 and CDK2 is low in S phase when recombination is active, but increases as cells progress towards mitosis; this phosphorylation prevents homologous recombination-dependent repair during S phase and G2 by inhibiting RAD51 binding." ], [ "O35923-1", "protein_xref_pubmed", "P51587", "ECO_0000250", "Phosphorylated by ATM upon irradiation-induced DNA damage. Phosphorylation by CHEK1 and CHEK2 regulates interaction with RAD51. Phosphorylation at Ser-3222 by CDK1 and CDK2 is low in S phase when recombination is active, but increases as cells progress towards mitosis; this phosphorylation prevents homologous recombination-dependent repair during S phase and G2 by inhibiting RAD51 binding." ], [ "O35923-1", "protein_xref_uniprotkb", "O35923", "ECO_0000250", "Ubiquitinated in the absence of DNA damage; this does not lead to proteasomal degradation. In contrast, ubiquitination in response to DNA damage leads to proteasomal degradation." ], [ "O35923-1", "protein_xref_pubmed", "P51587", "ECO_0000250", "Ubiquitinated in the absence of DNA damage; this does not lead to proteasomal degradation. In contrast, ubiquitination in response to DNA damage leads to proteasomal degradation." ], [ "D3ZN95-1", "protein_xref_uniprotkb", "D3ZN95", "ECO_0000250", "Proteolytically cleaved at one or several PPCE--THET sites within the HCF repeats. Further cleavage of the primary N- and C-terminal chains results in a 'trimming' and accumulation of the smaller chains. Cleavage is promoted by O-glycosylation." ], [ "D3ZN95-1", "protein_xref_pubmed", "P51610", "ECO_0000250", "Proteolytically cleaved at one or several PPCE--THET sites within the HCF repeats. Further cleavage of the primary N- and C-terminal chains results in a 'trimming' and accumulation of the smaller chains. Cleavage is promoted by O-glycosylation." ], [ "D3ZN95-1", "protein_xref_uniprotkb", "D3ZN95", "ECO_0000250", "O-glycosylated. GlcNAcylation by OGT promotes proteolytic processing." ], [ "D3ZN95-1", "protein_xref_pubmed", "P51610", "ECO_0000250", "O-glycosylated. GlcNAcylation by OGT promotes proteolytic processing." ], [ "D3ZN95-1", "protein_xref_uniprotkb", "D3ZN95", "ECO_0000250", "Ubiquitinated. Lys-1818 and Lys-1819 are ubiquitinated both via 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. BAP1 mediated deubiquitination of 'Lys-48'-linked polyubiquitin chains; deubiquitination by BAP1 does not seem to stabilize the protein." ], [ "D3ZN95-1", "protein_xref_pubmed", "P51610", "ECO_0000250", "Ubiquitinated. Lys-1818 and Lys-1819 are ubiquitinated both via 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. BAP1 mediated deubiquitination of 'Lys-48'-linked polyubiquitin chains; deubiquitination by BAP1 does not seem to stabilize the protein." ], [ "Q63035-1", "protein_xref_uniprotkb", "Q63035", "ECO_0000250", "Polyubiquitinated with 'Lys-63'-linked chains, promoting the interaction with PYCARD/ASC and formation of the NLRP6 inflammasome. Deubiquitination by CYLD decreases the interaction with PYCARD/ASC." ] ] }, "readme": "Name\n - Rat Protein PTM Annotation (UniProtKB)\n\nVersion\n - v-2.2.1\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], 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/2023_10_30/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-2.2.1/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-2.2.1/reviewed/rat_protein_ptm_annotation_uniprotkb.stat.csv\n\nFields\n Name: \"uniprotkb_canonical_ac\"\n Description: \"\"\n Unique Values: \"1831\"\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: \"4344\"\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: \"2318\"", "downloadurl": "/ln2data/releases/data/v-2.2.1/reviewed/rat_protein_ptm_annotation_uniprotkb.csv" }