{ "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", "tags": "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. Degradation is probably caused by ubiquitination by MYCBP2 (By similarity). Ubiquitinated on threonine and/or serine residues by MYCBP2; consequences of threonine and/or serine ubiquitination are however unclear (By similarity)." ], [ "Q0HA29-1", "protein_xref_pubmed", "Q9BZQ4", "ECO_0000250", "Degraded in response to injured neurite. Degradation is probably caused by ubiquitination by MYCBP2 (By similarity). Ubiquitinated on threonine and/or serine residues by MYCBP2; consequences of threonine and/or serine ubiquitination are however unclear (By similarity)." ], [ "Q0HA29-1", "protein_xref_pubmed", "Q8BNJ3", "ECO_0000250", "Degraded in response to injured neurite. Degradation is probably caused by ubiquitination by MYCBP2 (By similarity). Ubiquitinated on threonine and/or serine residues by MYCBP2; consequences of threonine and/or serine ubiquitination are however unclear (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." ], [ "Q07969-1", "protein_xref_uniprotkb", "Q07969", "ECO_0000250", "Ubiquitinated at Lys-469 and Lys-472. Ubiquitination is induced by fatty acids such as oleic acid and leads to degradation by the proteasome (PubMed:21610069). Ubiquitination and degradation are inhibited by insulin which blocks the effect of fatty acids (By similarity)." ], [ "Q07969-1", "protein_xref_pubmed", "Q08857", "ECO_0000250", "Ubiquitinated at Lys-469 and Lys-472. Ubiquitination is induced by fatty acids such as oleic acid and leads to degradation by the proteasome (PubMed:21610069). Ubiquitination and degradation are inhibited by insulin which blocks the effect of fatty acids (By similarity)." ], [ "Q07969-1", "protein_xref_uniprotkb", "Q07969", "ECO_0000269", "Ubiquitinated at Lys-469 and Lys-472. Ubiquitination is induced by fatty acids such as oleic acid and leads to degradation by the proteasome (PubMed:21610069). Ubiquitination and degradation are inhibited by insulin which blocks the effect of fatty acids (By similarity)." ], [ "Q07969-1", "protein_xref_pubmed", "21610069", "ECO_0000269", "Ubiquitinated at Lys-469 and Lys-472. Ubiquitination is induced by fatty acids such as oleic acid and leads to degradation by the proteasome (PubMed:21610069). Ubiquitination and degradation are inhibited by insulin which blocks the effect of fatty acids (By similarity)." ], [ "Q07969-1", "protein_xref_pubmed", "P16671", "ECO_0000250", "Ubiquitinated at Lys-469 and Lys-472. Ubiquitination is induced by fatty acids such as oleic acid and leads to degradation by the proteasome (PubMed:21610069). Ubiquitination and degradation are inhibited by insulin which blocks the effect of fatty acids (By similarity)." ], [ "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", "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." ], [ "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." ], [ "P08011-1", "protein_xref_uniprotkb", "P08011", "ECO_0000269", "Peroxynitrite induces nitration at Tyr-93 which activates the enzyme." ], [ "P08011-1", "protein_xref_pubmed", "16314419", "ECO_0000269", "Peroxynitrite induces nitration at Tyr-93 which activates the enzyme." ], [ "P22002-1", "protein_xref_uniprotkb", "P22002", "ECO_0000250", "Phosphorylation by PKA at Ser-1927 activates the channel (By similarity). Elevated levels of blood glucose lead to increased phosphorylation by PKA (By similarity). Is also phosphorylated in vitro by CaM-kinase II, PKC and CGPK (PubMed:8396138)." ], [ "P22002-1", "protein_xref_pubmed", "Q01815", "ECO_0000250", "Phosphorylation by PKA at Ser-1927 activates the channel (By similarity). Elevated levels of blood glucose lead to increased phosphorylation by PKA (By similarity). Is also phosphorylated in vitro by CaM-kinase II, PKC and CGPK (PubMed:8396138)." ], [ "P22002-1", "protein_xref_uniprotkb", "P22002", "ECO_0000269", "Phosphorylation by PKA at Ser-1927 activates the channel (By similarity). Elevated levels of blood glucose lead to increased phosphorylation by PKA (By similarity). Is also phosphorylated in vitro by CaM-kinase II, PKC and CGPK (PubMed:8396138)." ], [ "P22002-1", "protein_xref_pubmed", "8396138", "ECO_0000269", "Phosphorylation by PKA at Ser-1927 activates the channel (By similarity). Elevated levels of blood glucose lead to increased phosphorylation by PKA (By similarity). Is also phosphorylated in vitro by CaM-kinase II, PKC and CGPK (PubMed:8396138)." ], [ "Q02294-1", "protein_xref_uniprotkb", "Q02294", "ECO_0000269", "Phosphorylated in vitro by CaM-kinase II, PKA, PKC and CGPK." ], [ "Q02294-1", "protein_xref_pubmed", "8125957", "ECO_0000269", "Phosphorylated in vitro by CaM-kinase II, PKA, PKC and CGPK." ], [ "Q9R1N3-1", "protein_xref_uniprotkb", "Q9R1N3", "ECO_0000269", "N-glycosylated." ], [ "Q9R1N3-1", "protein_xref_pubmed", "11053051", "ECO_0000269", "N-glycosylated." ], [ "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." ], [ "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." ], [ "P00176-1", "protein_xref_uniprotkb", "P00176", "ECO_0000269", "Phosphorylation is accompanied by a decrease in enzyme activity." ], [ "P00176-1", "protein_xref_pubmed", "2583091", "ECO_0000269", "Phosphorylation is accompanied by a decrease in enzyme activity." ], [ "P32301-1", "protein_xref_uniprotkb", "P32301", "ECO_0000250", "N-glycosylation enhances cell surface expression and lengthens receptor half-life by preventing degradation in the ER." ], [ "P32301-1", "protein_xref_pubmed", "P43220", "ECO_0000250", "N-glycosylation enhances cell surface expression and lengthens receptor half-life by preventing degradation in the ER." ], [ "Q9QYH7-1", "protein_xref_uniprotkb", "Q9QYH7", "ECO_0000269", "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-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-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", "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." ], [ "Q6MFZ5-1", "protein_xref_uniprotkb", "Q6MFZ5", "ECO_0000250", "Autoubiquitinated." ], [ "Q6MFZ5-1", "protein_xref_pubmed", "Q9HCM9", "ECO_0000250", "Autoubiquitinated." ], [ "P62630-1", "protein_xref_uniprotkb", "P62630", "ECO_0000250", "ISGylated." ], [ "P62630-1", "protein_xref_pubmed", "P68104", "ECO_0000250", "ISGylated." ], [ "P62630-1", "protein_xref_uniprotkb", "P62630", "ECO_0000250", "Trimethylated at Lys-79 by EEF1AKMT1. Methylated at Lys-165 by EEF1AKMT3, methylation by EEF1AKMT3 is dynamic as well as inducible by stress conditions, such as ER-stress, and plays a regulatory role on mRNA translation. Trimethylated at Lys-318 by EEF1AKMT2. Mono-, di-, and trimethylated at Lys-36 by EEF1AKMT4; trimethylated form is predominant. Methylation by EEF1AKMT4 contributes to the fine-tuning of translation rates for a subset of tRNAs. Trimethylated at Gly-2 by EEF1AKNMT. Mono- and dimethylated at Lys-55 by EEF1AKNMT; dimethylated form is predominant." ], [ "P62630-1", "protein_xref_pubmed", "P68104", "ECO_0000250", "Trimethylated at Lys-79 by EEF1AKMT1. Methylated at Lys-165 by EEF1AKMT3, methylation by EEF1AKMT3 is dynamic as well as inducible by stress conditions, such as ER-stress, and plays a regulatory role on mRNA translation. Trimethylated at Lys-318 by EEF1AKMT2. Mono-, di-, and trimethylated at Lys-36 by EEF1AKMT4; trimethylated form is predominant. Methylation by EEF1AKMT4 contributes to the fine-tuning of translation rates for a subset of tRNAs. Trimethylated at Gly-2 by EEF1AKNMT. Mono- and dimethylated at Lys-55 by EEF1AKNMT; dimethylated form is predominant." ], [ "P62630-1", "protein_xref_uniprotkb", "P62630", "ECO_0000250", "Phosphorylated by TXK. Phosphorylation by PASK increases translation efficiency. Phosphorylated by ROCK2." ], [ "P62630-1", "protein_xref_pubmed", "P68104", "ECO_0000250", "Phosphorylated by TXK. Phosphorylation by PASK increases translation efficiency. Phosphorylated by ROCK2." ], [ "P62632-1", "protein_xref_uniprotkb", "P62632", "ECO_0000250", "Trimethylated at Lys-165 by EEF1AKMT3. Mono-, di-, and trimethylated at Lys-36 by EEF1AKMT4; trimethylated form is predominant. Methylation by EEF1AKMT4 contributes to the fine-tuning of translation rates for a subset of tRNAs. Trimethylated at the N-terminus and dimethylated at Lys-55 by EEF1AKNMT." ], [ "P62632-1", "protein_xref_pubmed", "Q05639", "ECO_0000250", "Trimethylated at Lys-165 by EEF1AKMT3. Mono-, di-, and trimethylated at Lys-36 by EEF1AKMT4; trimethylated form is predominant. Methylation by EEF1AKMT4 contributes to the fine-tuning of translation rates for a subset of tRNAs. Trimethylated at the N-terminus and dimethylated at Lys-55 by EEF1AKNMT." ], [ "Q9Z272-1", "protein_xref_uniprotkb", "Q9Z272", "ECO_0000269", "Phosphorylated on tyrosine residues by PTK2/FAK1 and SRC in growing fibroblasts (PubMed:10938112). Phosphorylation at Tyr-392 is induced by activation of Ephrin-B1/EFNB1 and catalyzed by SRC family kinases. It is required for the interaction with NCK2 and for GIT1 recruitment to synapses in hippocampal neurons (PubMed:17310244)." ], [ "Q9Z272-1", "protein_xref_pubmed", "17310244", "ECO_0000269", "Phosphorylated on tyrosine residues by PTK2/FAK1 and SRC in growing fibroblasts (PubMed:10938112). Phosphorylation at Tyr-392 is induced by activation of Ephrin-B1/EFNB1 and catalyzed by SRC family kinases. It is required for the interaction with NCK2 and for GIT1 recruitment to synapses in hippocampal neurons (PubMed:17310244)." ], [ "Q9Z272-1", "protein_xref_pubmed", "10938112", "ECO_0000269", "Phosphorylated on tyrosine residues by PTK2/FAK1 and SRC in growing fibroblasts (PubMed:10938112). Phosphorylation at Tyr-392 is induced by activation of Ephrin-B1/EFNB1 and catalyzed by SRC family kinases. It is required for the interaction with NCK2 and for GIT1 recruitment to synapses in hippocampal neurons (PubMed:17310244)." ], [ "P26433-1", "protein_xref_uniprotkb", "P26433", "ECO_0000250", "Phosphorylated by PKA, which inhibits activity (PubMed:9933588). Phosphorylation at Ser-661 by SGK1 is associated with increased abundance at the cell membrane (By similarity)." ], [ "P26433-1", "protein_xref_pubmed", "P26432", "ECO_0000250", "Phosphorylated by PKA, which inhibits activity (PubMed:9933588). Phosphorylation at Ser-661 by SGK1 is associated with increased abundance at the cell membrane (By similarity)." ], [ "P26433-1", "protein_xref_uniprotkb", "P26433", "ECO_0000269", "Phosphorylated by PKA, which inhibits activity (PubMed:9933588). Phosphorylation at Ser-661 by SGK1 is associated with increased abundance at the cell membrane (By similarity)." ], [ "P26433-1", "protein_xref_pubmed", "9933588", "ECO_0000269", "Phosphorylated by PKA, which inhibits activity (PubMed:9933588). Phosphorylation at Ser-661 by SGK1 is associated with increased abundance at the cell membrane (By similarity)." ], [ "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_0000250", "Autophosphorylated." ], [ "Q00972-1", "protein_xref_pubmed", "O14874", "ECO_0000250", "Autophosphorylated." ], [ "O70276-1", "protein_xref_uniprotkb", "O70276", "ECO_0000250", "Palmitoylation by LRAT regulates ligand binding specificity; the palmitoylated form (membrane form) specifically binds all-trans-retinyl-palmitate, while the soluble unpalmitoylated form binds all-trans-retinol (vitamin A)." ], [ "O70276-1", "protein_xref_pubmed", "Q28175", "ECO_0000250", "Palmitoylation by LRAT regulates ligand binding specificity; the palmitoylated form (membrane form) specifically binds all-trans-retinyl-palmitate, while the soluble unpalmitoylated form binds all-trans-retinol (vitamin A)." ], [ "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." ], [ "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", "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_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", "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", "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)." ], [ "P08733-1", "protein_xref_uniprotkb", "P08733", "ECO_0000250", "N-terminus is methylated by METTL11A/NTM1." ], [ "P08733-1", "protein_xref_pubmed", "P51667", "ECO_0000250", "N-terminus is methylated by METTL11A/NTM1." ], [ "P08733-1", "protein_xref_uniprotkb", "P08733", "ECO_0000269", "Phosphorylated by MYLK3 and MYLK2; promotes cardiac muscle contraction and function (By similarity) (PubMed:17885681). Dephosphorylated by PPP1CB complexed to PPP1R12B (PubMed:16431080). The phosphorylated form in adult is expressed as gradients across the heart from endocardium (low phosphorylation) to epicardium (high phosphorylation); regulates cardiac torsion and workload distribution (By similarity)." ], [ "P08733-1", "protein_xref_pubmed", "16431080", "ECO_0000269", "Phosphorylated by MYLK3 and MYLK2; promotes cardiac muscle contraction and function (By similarity) (PubMed:17885681). Dephosphorylated by PPP1CB complexed to PPP1R12B (PubMed:16431080). The phosphorylated form in adult is expressed as gradients across the heart from endocardium (low phosphorylation) to epicardium (high phosphorylation); regulates cardiac torsion and workload distribution (By similarity)." ], [ "P08733-1", "protein_xref_pubmed", "17885681", "ECO_0000269", "Phosphorylated by MYLK3 and MYLK2; promotes cardiac muscle contraction and function (By similarity) (PubMed:17885681). Dephosphorylated by PPP1CB complexed to PPP1R12B (PubMed:16431080). The phosphorylated form in adult is expressed as gradients across the heart from endocardium (low phosphorylation) to epicardium (high phosphorylation); regulates cardiac torsion and workload distribution (By similarity)." ], [ "P08733-1", "protein_xref_uniprotkb", "P08733", "ECO_0000250", "Phosphorylated by MYLK3 and MYLK2; promotes cardiac muscle contraction and function (By similarity) (PubMed:17885681). Dephosphorylated by PPP1CB complexed to PPP1R12B (PubMed:16431080). The phosphorylated form in adult is expressed as gradients across the heart from endocardium (low phosphorylation) to epicardium (high phosphorylation); regulates cardiac torsion and workload distribution (By similarity)." ] ] }, "readme": "Name\n - Rat Protein PTM Annotation (UniProtKB)\n\nVersion\n - 1.11.2\n\nCreated on\n - 2019-11-30T14:07:14.445471\n\nModified on\n - 2020-04-10T12:14:03.498068\n\nCreated by\n - Jeet Vora [jeetvora@gwu.edu], Rahi Navelkar [rsn13@gwu.edu], Robel Kahsay [rykahsay@gwu.edu], Xavier Holmes [xavierh@email.gwu.edu], Karina Martinez [karinamartinez@gwu.edu], Amanda Bell [amandab2140@gwu.edu], Jonathon Keeney [keeneyjg@gwu.edu], Millicent Quartey [mquartey@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/GW-HIVE/glygen-backend-integration/blob/master/pipeline/integrator/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/ln2wwwdata/reviewed/uniprot-proteome-rattus-norvegicus.nt\n Name: rat_protein_masterlist.csv\n URI: https://data.glygen.org/ln2wwwdata/reviewed/rat_protein_masterlist.csv\n Output Subdomain\n Name: rat_protein_ptm_annotation_uniprotkb.csv\n URI: http://data.glygen.org/ln2wwwdata/reviewed/rat_protein_ptm_annotation_uniprotkb.csv\n Name: rat_protein_ptm_annotation_uniprotkb.stat.csv\n URI: http://data.glygen.org/ln2wwwdata/reviewed/rat_protein_ptm_annotation_uniprotkb.stat.csv\n\nFields\n Name: \"uniprotkb_canonical_ac\"\n Description: \"\"\n Unique Values: \"16\"\n Name: \"motif_start\"\n Description: \"\"\n Unique Values: \"23\"\n Name: \"filter_flags\"\n Description: \"Filter tags/flags assigned to the mutation entries that have passed the mutation filter criteria\"\n Unique Values: \"19\"\n Name: \"sift_prediction\"\n Description: \"The SIFT qualitative prediction is derived from this score such that substitutions with a score < 0.05 are called 'deleterious' and all others are called 'tolerated\"\n Unique Values: \"3\"\n Name: \"somatic_status\"\n Description: \"The status of the variant whether it is germline (somatic status =0) or somatic (somatic status =1) variant\"\n Unique Values: \"1\"\n Name: \"chr_pos\"\n Description: \"Chromosome Position of a gene\"\n Unique Values: \"19\"\n Name: \"chr_id\"\n Description: \"\"\n Unique Values: \"10\"\n Name: \"dbsnp_id\"\n Description: \"\"A reference SNP ID number\"\n Unique Values: \"19\"\n Name: \"evidence_ECO:0000313\"\n Description: \"A type of evidence that is imported information used in an automatic assertion\"\n Unique Values: \"1\"\n Name: \"xref_id\"\n Description: \"ID of the X-ref\"\n Unique Values: \"19\"\n Name: \"mim_id\"\n Description: \"Disease ID from the OMIM database\"\n Unique Values: \"1\"\n Name: \"description\"\n Description: \"\"\n Unique Values: \"1\"\n Name: \"begin_aa_pos\"\n Description: \"Start position of the amino acid in the sequence of a protein in UniProtKB\"\n Unique Values: \"18\"\n Name: \"cytogenic_band\"\n Description: \"One of the subregions of a chromosome visible microscopically after special staining\"\n Unique Values: \"14\"\n Name: \"aa_pos\"\n Description: \"Position of the amino acid in canonical sequence of protein in the UniProtKB database\"\n Unique Values: \"18\"\n Name: \"ref_aa\"\n Description: \"Reference amino acid residue\"\n Unique Values: \"9\"\n Name: \"sift_score\"\n Description: \"SIFT predicts whether an amino acid substitution is likely to affect protein function based on sequence homology and the physico-chemical similarity between the alternate amino acids. The data we provide for each amino acid substitution is a score and a qualitative prediction (either 'tolerated' or 'deleterious'). The score is the normalized probability that the amino acid change is tolerated so scores nearer zero are more likely to be deleterious. The qualitative prediction is derived from this score such that substitutions with a score < 0.05 are called 'deleterious' and all others are called 'tolerated\"\n Unique Values: \"10\"\n Name: \"alt_motif\"\n Description: \"Altered motif\"\n Unique Values: \"24\"\n Name: \"disease_xrefs\"\n Description: \"\"\n Unique Values: \"1\"\n Name: \"polyphen_score\"\n Description: \"The score assigned to a amino acid substitution by a tool called as PolyPhen (=Polymorphism Phenotyping) which predicts possible impact of an amino acid substitution on the structure and function of a human protein using straightforward physical and comparative considerations. The PolyPhen score ranges from 0.0 (tolerated) to 1.0 (deleterious). Variants with scores of 0.0 are predicted to be benign. Values closer to 1.0 are more confidently predicted to be deleterious\"\n Unique Values: \"1\"\n Name: \"polyphen_prediction\"\n Description: \"\"The PolyPhen prediction values are - greater than 0.908 - \"\"Probably Damaging\"\"; greater than 0.446 and less than or equal to 0.908 - \"\"Possibly Damaging\"\"; less than or equal to 0.446 - \"\"Benign\"\"\"\n Unique Values: \"1\"\n Name: \"is_known_glycoprotein\"\n Description: \"Yes or no flag to denote if a protein is experimentally proven glycoprotein\"\n Unique Values: \"1\"\n Name: \"alt_nt\"\n Description: \"Alternative nucleotide\"\n Unique Values: \"1\"\n Name: \"protein_name\"\n Description: \"Protein name in the UniProtKB\"\n Unique Values: \"16\"\n Name: \"disease_evidence_ECO:0000313\"\n Description: \"The evidence that could be a PMID or a ClinVar ID that associates disease with the variant\"\n Unique Values: \"1\"\n Name: \"effect\"\n Description: \"The effect on glycosylation or N-sequon due to variation at site of glycosylated amino acid.\"\n Unique Values: \"3\"\n Name: \"end_aa_pos\"\n Description: \"End position of the amino acid in the sequence of a protein in UniProtKB\"\n Unique Values: \"18\"\n Name: \"mutation_type\"\n Description: \"Denotes whether mutation was reported with reference to amino acid or nucleotide\"\n Unique Values: \"1\"\n Name: \"disease_description\"\n Description: \"The disease description and/or definition \"\n Unique Values: \"1\"\n Name: \"do_id\"\n Description: \"Disease Ontology identifier\"\n Unique Values: \"1\"\n Name: \"evidence_ECO:0000269\"\n Description: \"A type of experimental evidence that is used in a manual assertion. Usually the values are PMIDs\"\n Unique Values: \"1\"\n Name: \"ref_nt\"\n Description: \"Reference nucleotide\"\n Unique Values: \"4\"\n Name: \"disease\"\n Description: \"The disease name for the cell line\"\n Unique Values: \"1\"\n Name: \"alt_aa\"\n Description: \"Altered amino acid residue\"\n Unique Values: \"10\"\n Name: \"cosmic_id\"\n Description: \"Legacy mutation identifier (COSM) in Catalogue of Somatic Mutations in Cancer (COSMIC) represents existing COSM mutation identifiers. This identifier remains the same between different assemblies (GRCh37 and GRCh38). All the COSM ids at the same genomic location have been collapsed into one representative COSM id. These ids are maintained to help track existing mutations\"\n Unique Values: \"1\"\n Name: \"ref_motif\"\n Description: \"Reference motif\"\n Unique Values: \"20\"\n Name: \"xref_key\"\n Description: \"Source key associated to the xref_id\"\n Unique Values: \"2\"\n Name: \"minor_allelic_frequency\"\n Description: \"\"\n Unique Values: \"1\"\n Name: \"gene_name\"\n Description: \"\"Official gene name/symbol assigned to the gene. Human gene name/symbol are approved by the HUGO Gene Nomenclature Committee (HGNC) and mouse gene name are approved by the Mouse Genome Informatics (MGI)\"\n Unique Values: \"17\"\n Name: \"disease_evidence_ECO:0000269\"\n Description: \"The PMID evidence for the association of the disease with the variant.\"\n Unique Values: \"1\"", "downloadurl": "/ln2data/releases/data/v-1.11.2/reviewed/rat_protein_ptm_annotation_uniprotkb.csv" }