{ "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." ], [ "P62634-1", "protein_xref_uniprotkb", "P62634", "ECO_0000250", "Arginine methylation by PRMT1 in the Arg/Gly-rich region impedes RNA binding." ], [ "P62634-1", "protein_xref_pubmed", "P62633", "ECO_0000250", "Arginine methylation by PRMT1 in the Arg/Gly-rich region impedes RNA binding." ], [ "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", "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." ], [ "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 METTL13. Mono- and dimethylated at Lys-55 by METTL13; 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 METTL13. Mono- and dimethylated at Lys-55 by METTL13; dimethylated form is predominant." ], [ "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 METTL13." ], [ "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 METTL13." ], [ "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)." ] ] }, "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: rat_protein_masterlist.csv\n URI: https://data.glygen.org//ln2data/releases/data/v-1.11.2/reviewed/rat_protein_masterlist.csv\n Name: uniprot-proteome-rattus-norvegicus.nt\n URI: https://data.glygen.org//ln2data/releases/data/v-1.11.2/reviewed/rat_protein_ntdata.nt\n Output Subdomain\n Name: rat_protein_ptm_annotation_uniprotkb.csv\n URI: http://data.glygen.org/ln2data/releases/data/v-1.12.1/reviewed/rat_protein_ptm_annotation_uniprotkb.csv\n Name: rat_protein_ptm_annotation_uniprotkb.stat.csv\n URI: http://data.glygen.org/ln2data/releases/data/v-1.12.1/reviewed/rat_protein_ptm_annotation_uniprotkb.stat.csv", "downloadurl": "/ln2data/releases/data/v-1.12.1/reviewed/rat_protein_ptm_annotation_uniprotkb.csv" }