{ "bcoid": "GLY_000317", "title": "Mouse Protein PTM Annotation (UniProtKB)", "description": "The Mouse Protein PTM Annotation (UniProtKB) dataset contains mouse [taxid:10090] PTM annotations for ...", "filename": "mouse_protein_ptm_annotation_uniprotkb.csv", "filetype": "csv", "categories": { "species": "Mus musculus", "molecule": "Protein", "tags": "PTM annotation", "file_type": "csv", "status": "Reviewed", "scope": "internal" }, "minitable": { "content": [ [ "B2RXV4-1...", "protein_xref..." ], [ "B2RXV4-1...", "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" } ], [ "B2RXV4-1", "protein_xref_uniprotkb", "B2RXV4", "", "N-Glycosylated." ], [ "B2RXV4-1", "protein_xref_pubmed", "", "", "N-Glycosylated." ], [ "Q9QYH9-1", "protein_xref_uniprotkb", "Q9QYH9", "", "The soluble form derives from the membrane form by proteolytic processing." ], [ "Q9QYH9-1", "protein_xref_pubmed", "", "", "The soluble form derives from the membrane form by proteolytic processing." ], [ "P52479-1", "protein_xref_uniprotkb", "P52479", "", "Ubiquitinated. Deubiquitinated by USP13 (By similarity)." ], [ "P52479-1", "protein_xref_pubmed", "", "", "Ubiquitinated. Deubiquitinated by USP13 (By similarity)." ], [ "P52479-1", "protein_xref_uniprotkb", "P52479", "", "Phosphorylated by ATM following DNA damage, leading to stablization and translocation it to the nucleus." ], [ "P52479-1", "protein_xref_pubmed", "", "", "Phosphorylated by ATM following DNA damage, leading to stablization and translocation it to the nucleus." ], [ "O08537-1", "protein_xref_uniprotkb", "O08537", "ECO_0000269", "Phosphorylation at Ser-87 and Ser-105 recruits NCOA1." ], [ "O08537-1", "protein_xref_pubmed", "10230404", "ECO_0000269", "Phosphorylation at Ser-87 and Ser-105 recruits NCOA1." ], [ "O08537-1", "protein_xref_pubmed", "10995228", "ECO_0000269", "Phosphorylation at Ser-87 and Ser-105 recruits NCOA1." ], [ "Q3URK3-1", "protein_xref_uniprotkb", "Q3URK3", "ECO_0000269", "Glycosylated. Interaction with OGT leads to GlcNAcylation." ], [ "Q3URK3-1", "protein_xref_pubmed", "23352454", "ECO_0000269", "Glycosylated. Interaction with OGT leads to GlcNAcylation." ], [ "Q9EP73-1", "protein_xref_uniprotkb", "Q9EP73", "ECO_0000250", "Ubiquitinated; STUB1 likely mediates polyubiquitination of PD-L1/CD274 triggering its degradation." ], [ "Q9EP73-1", "protein_xref_pubmed", "Q9NZQ7", "ECO_0000250", "Ubiquitinated; STUB1 likely mediates polyubiquitination of PD-L1/CD274 triggering its degradation." ], [ "Q8R349-1", "protein_xref_uniprotkb", "Q8R349", "", "Phosphorylated. Phosphorylation on Ser-560 occurs specifically during mitosis (By similarity)." ], [ "Q8R349-1", "protein_xref_pubmed", "", "", "Phosphorylated. Phosphorylation on Ser-560 occurs specifically during mitosis (By similarity)." ], [ "O08911-1", "protein_xref_uniprotkb", "O08911", "ECO_0000269", "Dually phosphorylated on Thr-183 and Tyr-185 by MAP2K3/MKK3 and MAP2K6/MKK6, which activates the enzyme." ], [ "O08911-1", "protein_xref_pubmed", "20004242", "ECO_0000269", "Dually phosphorylated on Thr-183 and Tyr-185 by MAP2K3/MKK3 and MAP2K6/MKK6, which activates the enzyme." ], [ "O08911-1", "protein_xref_uniprotkb", "O08911", "", "Ubiquitinated. Ubiquitination leads to degradation by the proteasome pathway (By similarity)." ], [ "O08911-1", "protein_xref_pubmed", "", "", "Ubiquitinated. Ubiquitination leads to degradation by the proteasome pathway (By similarity)." ], [ "Q8BZM0-1", "protein_xref_uniprotkb", "Q8BZM0", "ECO_0000250", "Ubiquitinated by the SCF(FBXL17) complex, leading to its degradation by the proteaseome: ubiquitination by the SCF(FBXL17) complex takes place when aberrant BTB domain dimers are formed." ], [ "Q8BZM0-1", "protein_xref_pubmed", "Q53G59", "ECO_0000250", "Ubiquitinated by the SCF(FBXL17) complex, leading to its degradation by the proteaseome: ubiquitination by the SCF(FBXL17) complex takes place when aberrant BTB domain dimers are formed." ], [ "Q8BZM1-1", "protein_xref_uniprotkb", "Q8BZM1", "ECO_0000250", "Phosphorylated on tyrosine residues." ], [ "Q8BZM1-1", "protein_xref_pubmed", "Q92990", "ECO_0000250", "Phosphorylated on tyrosine residues." ], [ "Q4VC33-1", "protein_xref_uniprotkb", "Q4VC33", "ECO_0000250", "Autoubiquitinated as component of the CTLH E3 ubiquitin-protein ligase complex (in vitro)." ], [ "Q4VC33-1", "protein_xref_pubmed", "Q7L5Y9", "ECO_0000250", "Autoubiquitinated as component of the CTLH E3 ubiquitin-protein ligase complex (in vitro)." ], [ "P50429-1", "protein_xref_uniprotkb", "P50429", "", "The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity." ], [ "P50429-1", "protein_xref_pubmed", "", "", "The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity." ], [ "Q99LV7-1", "protein_xref_uniprotkb", "Q99LV7", "", "N-glycosylated." ], [ "Q99LV7-1", "protein_xref_pubmed", "", "", "N-glycosylated." ], [ "P50427-1", "protein_xref_uniprotkb", "P50427", "ECO_0000250", "The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity." ], [ "P50427-1", "protein_xref_pubmed", "P08842", "ECO_0000250", "The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity." ], [ "Q7M729-1", "protein_xref_uniprotkb", "Q7M729", "", "N-glycosylated." ], [ "Q7M729-1", "protein_xref_pubmed", "", "", "N-glycosylated." ], [ "Q7M729-1", "protein_xref_uniprotkb", "Q7M729", "", "Contains an interchain disulfide bond with SCN2A." ], [ "Q7M729-1", "protein_xref_pubmed", "", "", "Contains an interchain disulfide bond with SCN2A." ], [ "Q6T3U4-1", "protein_xref_uniprotkb", "Q6T3U4", "", "Highly glycosylated." ], [ "Q6T3U4-1", "protein_xref_pubmed", "", "", "Highly glycosylated." ], [ "O88668-1", "protein_xref_uniprotkb", "O88668", "", "N-glycosylated." ], [ "O88668-1", "protein_xref_pubmed", "", "", "N-glycosylated." ], [ "Q8BGW0-1", "protein_xref_uniprotkb", "Q8BGW0", "ECO_0000269", "Phosphorylated on Tyr residues quickly after TCR stimulation." ], [ "Q8BGW0-1", "protein_xref_pubmed", "19597498", "ECO_0000269", "Phosphorylated on Tyr residues quickly after TCR stimulation." ], [ "Q8BGW0-1", "protein_xref_pubmed", "19597499", "ECO_0000269", "Phosphorylated on Tyr residues quickly after TCR stimulation." ], [ "Q6PDM2-1", "protein_xref_uniprotkb", "Q6PDM2", "", "Phosphorylated by CLK1, CLK2, CLK3 and CLK4. Phosphorylated by SRPK1 at multiple serines in its RS domain via a directional (C-terminal to N-terminal) and a dual-track mechanism incorporating both processive phosphorylation (in which the kinase stays attached to the substrate after each round of phosphorylation) and distributive phosphorylation steps (in which the kinase and substrate dissociate after each phosphorylation event). The RS domain of SRSF1 binds to a docking groove in the large lobe of the kinase domain of SRPK1 and this induces certain structural changes in SRPK1 and/or RRM 2 domain of SRSF1, allowing RRM 2 to bind the kinase and initiate phosphorylation. The cycles continue for several phosphorylation steps in a processive manner (steps 1-8) until the last few phosphorylation steps (approximately steps 9-12). During that time, a mechanical stress induces the unfolding of the beta-4 motif in RRM 2, which then docks at the docking groove of SRPK1. This also signals RRM 2 to begin to dissociate, which facilitates SRSF1 dissociation after phosphorylation is completed (By similarity)." ], [ "Q6PDM2-1", "protein_xref_pubmed", "", "", "Phosphorylated by CLK1, CLK2, CLK3 and CLK4. Phosphorylated by SRPK1 at multiple serines in its RS domain via a directional (C-terminal to N-terminal) and a dual-track mechanism incorporating both processive phosphorylation (in which the kinase stays attached to the substrate after each round of phosphorylation) and distributive phosphorylation steps (in which the kinase and substrate dissociate after each phosphorylation event). The RS domain of SRSF1 binds to a docking groove in the large lobe of the kinase domain of SRPK1 and this induces certain structural changes in SRPK1 and/or RRM 2 domain of SRSF1, allowing RRM 2 to bind the kinase and initiate phosphorylation. The cycles continue for several phosphorylation steps in a processive manner (steps 1-8) until the last few phosphorylation steps (approximately steps 9-12). During that time, a mechanical stress induces the unfolding of the beta-4 motif in RRM 2, which then docks at the docking groove of SRPK1. This also signals RRM 2 to begin to dissociate, which facilitates SRSF1 dissociation after phosphorylation is completed (By similarity)." ], [ "Q6PDM2-1", "protein_xref_uniprotkb", "Q6PDM2", "", "Asymmetrically dimethylated at arginines, probably by PRMT1, methylation promotes localization to nuclear speckles." ], [ "Q6PDM2-1", "protein_xref_pubmed", "", "", "Asymmetrically dimethylated at arginines, probably by PRMT1, methylation promotes localization to nuclear speckles." ], [ "Q499E6-1", "protein_xref_uniprotkb", "Q499E6", "ECO_0000250", "Phosphorylated on serines by CK2 kinase." ], [ "Q499E6-1", "protein_xref_pubmed", "Q9NX04", "ECO_0000250", "Phosphorylated on serines by CK2 kinase." ], [ "P62631-1", "protein_xref_uniprotkb", "P62631", "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." ], [ "P62631-1", "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." ], [ "Q9QZD9-1", "protein_xref_uniprotkb", "Q9QZD9", "ECO_0000255", "Phosphorylated by TGF-beta type II receptor." ], [ "Q9QZD9-1", "protein_xref_pubmed", "MF_03008", "ECO_0000255", "Phosphorylated by TGF-beta type II receptor." ], [ "Q9WVL4-1", "protein_xref_uniprotkb", "Q9WVL4", "ECO_0000250", "Farnesylation is required for full activity." ], [ "Q9WVL4-1", "protein_xref_pubmed", "P28327", "ECO_0000250", "Farnesylation is required for full activity." ], [ "Q9WVL4-1", "protein_xref_uniprotkb", "Q9WVL4", "", "Autophosphorylated, Ser-21 is a minor site of autophosphorylation compared to Ser-491 and Thr-492. Phosphorylation at Ser-21 is regulated by light and activated by cAMP." ], [ "Q9WVL4-1", "protein_xref_pubmed", "", "", "Autophosphorylated, Ser-21 is a minor site of autophosphorylation compared to Ser-491 and Thr-492. Phosphorylation at Ser-21 is regulated by light and activated by cAMP." ], [ "Q9WVL3-1", "protein_xref_uniprotkb", "Q9WVL3", "ECO_0000269", "Glycosylation at Asn-331 and Asn-344 is required for proper trafficking to the cell surface, and augments protein stability." ], [ "Q9WVL3-1", "protein_xref_pubmed", "23376777", "ECO_0000269", "Glycosylation at Asn-331 and Asn-344 is required for proper trafficking to the cell surface, and augments protein stability." ], [ "Q9WVL3-1", "protein_xref_pubmed", "19349973", "ECO_0000269", "Glycosylation at Asn-331 and Asn-344 is required for proper trafficking to the cell surface, and augments protein stability." ], [ "Q9WVL3-1", "protein_xref_pubmed", "19656770", "ECO_0000269", "Glycosylation at Asn-331 and Asn-344 is required for proper trafficking to the cell surface, and augments protein stability." ], [ "P56931-1", "protein_xref_uniprotkb", "P56931", "", "Phosphorylated by CDK2 and cyclin A-CDK2 in the S-phase." ], [ "P56931-1", "protein_xref_pubmed", "", "", "Phosphorylated by CDK2 and cyclin A-CDK2 in the S-phase." ], [ "Q9QUN7-1", "protein_xref_uniprotkb", "Q9QUN7", "ECO_0000250", "Glycosylation of Asn-442 is critical for secretion of the N-terminal ectodomain of TLR2." ], [ "Q9QUN7-1", "protein_xref_pubmed", "O60603", "ECO_0000250", "Glycosylation of Asn-442 is critical for secretion of the N-terminal ectodomain of TLR2." ], [ "Q9QUN7-1", "protein_xref_uniprotkb", "Q9QUN7", "ECO_0000269", "Ubiquitinated at Lys-754 by PPP1R11, leading to its degradation. Deubiquitinated by USP2." ], [ "Q9QUN7-1", "protein_xref_pubmed", "27805901", "ECO_0000269", "Ubiquitinated at Lys-754 by PPP1R11, leading to its degradation. Deubiquitinated by USP2." ], [ "Q9QUN3-1", "protein_xref_uniprotkb", "Q9QUN3", "ECO_0000269", "Following BCR activation, phosphorylated on tyrosine residues by SYK and LYN. When phosphorylated, serves as a scaffold to assemble downstream targets of antigen activation, including PLCG1, VAV1, GRB2 and NCK1. Phosphorylation of Tyr-84, Tyr-178 and Tyr-189 facilitates PLCG1 binding. Phosphorylation of Tyr-72 facilitates VAV1 and NCK1 binding. Phosphorylation is required for both Ca(2+) and MAPK signaling pathways (By similarity). Phosphorylation of Tyr-96 is required for the binding of BTK." ], [ "Q9QUN3-1", "protein_xref_pubmed", "9705962", "ECO_0000269", "Following BCR activation, phosphorylated on tyrosine residues by SYK and LYN. When phosphorylated, serves as a scaffold to assemble downstream targets of antigen activation, including PLCG1, VAV1, GRB2 and NCK1. Phosphorylation of Tyr-84, Tyr-178 and Tyr-189 facilitates PLCG1 binding. Phosphorylation of Tyr-72 facilitates VAV1 and NCK1 binding. Phosphorylation is required for both Ca(2+) and MAPK signaling pathways (By similarity). Phosphorylation of Tyr-96 is required for the binding of BTK." ], [ "Q91Z67-1", "protein_xref_uniprotkb", "Q91Z67", "", "Methylation at Arg-927 is required for the stimulation of cell migration, dimerization and localization at the plasma membrane protrusions." ], [ "Q91Z67-1", "protein_xref_pubmed", "", "", "Methylation at Arg-927 is required for the stimulation of cell migration, dimerization and localization at the plasma membrane protrusions." ], [ "Q91YI1-1", "protein_xref_uniprotkb", "Q91YI1", "ECO_0000250", "Phosphorylated by ULK1, ULK2 and mTOR. Phosphorylation status depends on nutrient-rich conditions; dephosphorylated during starvation or following treatment with rapamycin. ULK1-mediated phosphorylation of ATG13 at Ser-354 is required for efficient clearance of depolarized mitochondria." ], [ "Q91YI1-1", "protein_xref_pubmed", "O75143", "ECO_0000250", "Phosphorylated by ULK1, ULK2 and mTOR. Phosphorylation status depends on nutrient-rich conditions; dephosphorylated during starvation or following treatment with rapamycin. ULK1-mediated phosphorylation of ATG13 at Ser-354 is required for efficient clearance of depolarized mitochondria." ], [ "Q91YI0-1", "protein_xref_uniprotkb", "Q91YI0", "", "Acetylation modifies enzyme activity in response to alterations of extracellular nutrient availability. Acetylation increased with trichostin A (TCA) or with nicotinamide (NAM). Glucose increases acetylation by about a factor of 3 with decreasing enzyme activity. Acetylation on Lys-288 is decreased on the addition of extra amino acids resulting in activation of enzyme activity (By similarity)." ], [ "Q91YI0-1", "protein_xref_pubmed", "", "", "Acetylation modifies enzyme activity in response to alterations of extracellular nutrient availability. Acetylation increased with trichostin A (TCA) or with nicotinamide (NAM). Glucose increases acetylation by about a factor of 3 with decreasing enzyme activity. Acetylation on Lys-288 is decreased on the addition of extra amino acids resulting in activation of enzyme activity (By similarity)." ], [ "Q91YI4-1", "protein_xref_uniprotkb", "Q91YI4", "", "The ubiquitination status appears to regulate the formation and trafficking of beta-arrestin-GPCR complexes and signaling. Ubiquitination appears to occur GPCR-specific. Ubiquitinated by MDM2; the ubiquitination is required for rapid internalization of ADRB2. Deubiquitinated by USP33; the deubiquitination leads to a dissociation of the beta-arrestin-GPCR complex. Stimulation of a class A GPCR, such as ADRB2, induces transient ubiquitination and subsequently promotes association with USP33. Stimulation of a class B GPCR promotes a sustained ubiquitination (By similarity)." ], [ "Q91YI4-1", "protein_xref_pubmed", "", "", "The ubiquitination status appears to regulate the formation and trafficking of beta-arrestin-GPCR complexes and signaling. Ubiquitination appears to occur GPCR-specific. Ubiquitinated by MDM2; the ubiquitination is required for rapid internalization of ADRB2. Deubiquitinated by USP33; the deubiquitination leads to a dissociation of the beta-arrestin-GPCR complex. Stimulation of a class A GPCR, such as ADRB2, induces transient ubiquitination and subsequently promotes association with USP33. Stimulation of a class B GPCR promotes a sustained ubiquitination (By similarity)." ], [ "Q91YI4-1", "protein_xref_uniprotkb", "Q91YI4", "", "Phosphorylated at Thr-383 in the cytoplasm; probably dephosphorylated at the plasma membrane. The phosphorylation does not regulate internalization and recycling of ADRB2, interaction with clathrin or AP2B1 (By similarity)." ], [ "Q91YI4-1", "protein_xref_pubmed", "", "", "Phosphorylated at Thr-383 in the cytoplasm; probably dephosphorylated at the plasma membrane. The phosphorylation does not regulate internalization and recycling of ADRB2, interaction with clathrin or AP2B1 (By similarity)." ], [ "Q91YI4-1", "protein_xref_uniprotkb", "Q91YI4", "", "Hydroxylation by PHD2 modulates the rate of internalization by slowing down recruitment to the plasma membrane and inhibiting subsequent co-internalization with class A receptors." ], [ "Q91YI4-1", "protein_xref_pubmed", "", "", "Hydroxylation by PHD2 modulates the rate of internalization by slowing down recruitment to the plasma membrane and inhibiting subsequent co-internalization with class A receptors." ], [ "Q9WUZ9-1", "protein_xref_uniprotkb", "Q9WUZ9", "ECO_0000269", "N-glycosylated; high-mannose type." ], [ "Q9WUZ9-1", "protein_xref_pubmed", "21074248", "ECO_0000269", "N-glycosylated; high-mannose type." ] ] }, "readme": "Name\n - Mouse Protein PTM Annotation (UniProtKB)\n\nVersion\n - 1.8.24\n\nCreated on\n - 2019-11-30T14:05:28.986536\n\nModified on\n - 2020-04-10T12:47:48.210199\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]\n\nAuthors\n - Maria Martin [martin@ebi.ac.uk], Preethi Vasudev [pvasudev@ebi.ac.uk]\n\nChecksum\n - \n\nUsability Domain\n - The Mouse Protein PTM Annotation (UniProtKB) dataset contains mouse [taxid:10090] 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-mus-musculus.nt\n URI: https://data.glygen.org/ln2data/releases/data/v-1.8.24/reviewed/uniprot-proteome-mus-musculus.nt\n Name: mouse_protein_masterlist.csv\n URI: https://data.glygen.org/ln2data/releases/data/v-1.8.24/reviewed/mouse_protein_masterlist.csv\n Output Subdomain\n Name: mouse_protein_ptm_annotation_uniprotkb.csv\n URI: http://data.glygen.org/ln2data/releases/data/v-1.8.24/reviewed/mouse_protein_ptm_annotation_uniprotkb.csv\n Name: mouse_protein_ptm_annotation_uniprotkb.stat.csv\n URI: http://data.glygen.org/ln2data/releases/data/v-1.8.24/reviewed/mouse_protein_ptm_annotation_uniprotkb.stat.csv\n\nFields\n Name: \"src_xref_key\"\n Description: \"Source Xref key\"\n Unique Values: \"1\"\n Name: \"xref_id\"\n Description: \"ID of the X-ref\"\n Unique Values: \"119\"\n Name: \"title\"\n Description: \"Title of the published article in the journal\"\n Unique Values: \"119\"\n Name: \"src_xref_id\"\n Description: \"Source X-ref ID\"\n Unique Values: \"120\"\n Name: \"journal_name\"\n Description: \"The name of the journal in which the article is published\"\n Unique Values: \"49\"\n Name: \"authors\"\n Description: \"NA\"\n Unique Values: \"118\"\n Name: \"publication_date\"\n Description: \"Contains the full date on which the issue of the journal was published. Sourced from MEDLINE/PubMed data element(fields) description.\"\n Unique Values: \"117\"\n Name: \"glytoucan_ac\"\n Description: \"Unique accession assigned to the registered glycan structure in GlyTouCan database\"\n Unique Values: \"115\"\n Name: \"xref_key\"\n Description: \"Source key associated to the xref_id\"\n Unique Values: \"1\"", "downloadurl": "/ln2data/releases/data/v-1.8.24/reviewed/mouse_protein_ptm_annotation_uniprotkb.csv" }