{ "bcoid": "GLY_000768", "title": "Yeast Protein PTM Annotation (UniProtKB)", "description": "The Yeast Protein PTM Annotation (UniProtKB) dataset contains yeast [taxid:559292] PTM annotations for ...", "filename": "yeast_protein_ptm_annotation_uniprotkb.csv", "filetype": "csv", "categories": { "species": [ "Saccharomyces cerevisiae S288C" ], "molecule": [ "Protein" ], "tag": [ "PTM annotation" ], "file_type": [ "csv" ], "status": [ "Reviewed" ], "scope": [ "internal" ] }, "minitable": { "content": [ [ "P39979-1...", "protein_xref..." ], [ "P39979-1...", "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" } ], [ "P39979-1", "protein_xref_uniprotkb", "P39979", "ECO_0000305", "Autoacetylates in an intermolecular reaction." ], [ "P39979-1", "protein_xref_pubmed", "10600387", "ECO_0000305", "Autoacetylates in an intermolecular reaction." ], [ "Q08745-1", "protein_xref_uniprotkb", "Q08745", "ECO_0000269", "The N-terminus is not modified." ], [ "Q08745-1", "protein_xref_pubmed", "10601260", "ECO_0000269", "The N-terminus is not modified." ], [ "Q08743-1", "protein_xref_uniprotkb", "Q08743", "ECO_0000269", "N-glycosylated." ], [ "Q08743-1", "protein_xref_pubmed", "19756047", "ECO_0000269", "N-glycosylated." ], [ "P32913-1", "protein_xref_uniprotkb", "P32913", "ECO_0000269", "Phosphorylated on one or more serine residues." ], [ "P32913-1", "protein_xref_pubmed", "19779198", "ECO_0000269", "Phosphorylated on one or more serine residues." ], [ "P32913-1", "protein_xref_pubmed", "18407956", "ECO_0000269", "Phosphorylated on one or more serine residues." ], [ "Q04439-1", "protein_xref_uniprotkb", "Q04439", "ECO_0000269", "Phosphorylation of the TEDS site (Ser-357) is required for the polarization of the actin cytoskeleton and for ligand-induced, but not for constitutive internalization of STE2. Phosphorylation probably activates the myosin-I ATPase activity. Ser-357 is phosphorylated by YPK2 in vitro." ], [ "Q04439-1", "protein_xref_pubmed", "16478726", "ECO_0000269", "Phosphorylation of the TEDS site (Ser-357) is required for the polarization of the actin cytoskeleton and for ligand-induced, but not for constitutive internalization of STE2. Phosphorylation probably activates the myosin-I ATPase activity. Ser-357 is phosphorylated by YPK2 in vitro." ], [ "Q04432-1", "protein_xref_uniprotkb", "Q04432", "ECO_0000269", "Cys-138 is easily oxidized to sulfinic acid." ], [ "Q04432-1", "protein_xref_pubmed", "14745011", "ECO_0000269", "Cys-138 is easily oxidized to sulfinic acid." ], [ "P25376-1", "protein_xref_uniprotkb", "P25376", "ECO_0000269", "Palmitoylated by PFA4." ], [ "P25376-1", "protein_xref_pubmed", "16751107", "ECO_0000269", "Palmitoylated by PFA4." ], [ "P00724-1", "protein_xref_uniprotkb", "P00724", "ECO_0000269", "Isoform Secreted is glycosylated. Isoform Intracellular is not glycosylated." ], [ "P00724-1", "protein_xref_pubmed", "3284881", "ECO_0000269", "Isoform Secreted is glycosylated. Isoform Intracellular is not glycosylated." ], [ "P00729-1", "protein_xref_uniprotkb", "P00729", "ECO_0000269", "The four high mannose core N-glycans found in mature CPY are Man(11-15)GlcNAc(2) at Asn-124, Man(8-12)GlcNAc(2) at Asn-198, Man(9-14)GlcNAc(2) at Asn-279 and phosphorylated Man(12-17)GlcNAc(2) as well as Man(11-16)GlcNAc(2) at Asn-479." ], [ "P00729-1", "protein_xref_pubmed", "28189789", "ECO_0000269", "The four high mannose core N-glycans found in mature CPY are Man(11-15)GlcNAc(2) at Asn-124, Man(8-12)GlcNAc(2) at Asn-198, Man(9-14)GlcNAc(2) at Asn-279 and phosphorylated Man(12-17)GlcNAc(2) as well as Man(11-16)GlcNAc(2) at Asn-479." ], [ "P00729-1", "protein_xref_uniprotkb", "P00729", "ECO_0000269", "Enters the endoplasmic reticulum as an inactive zymogen and is modified by four N-linked core oligosaccharides, giving rise to a precursor known as P1 (67 kDa). As P1 transits through the Golgi, extension of its core oligosaccharides leads to the Golgi-modified P2 precursor (69 kDa). P2 is sorted away from secretory proteins at or beyond a late Golgi compartment and is subsequently delivered to the vacuole via a prevacuolar endosome-like compartment. Upon arrival in the vacuole, the N-terminal prosegment of P2 is cleaved by vacuolar proteases to yield the enzymatically active mature vacuolar form of CPY (61 kDa)." ], [ "P00729-1", "protein_xref_pubmed", "348476", "ECO_0000269", "Enters the endoplasmic reticulum as an inactive zymogen and is modified by four N-linked core oligosaccharides, giving rise to a precursor known as P1 (67 kDa). As P1 transits through the Golgi, extension of its core oligosaccharides leads to the Golgi-modified P2 precursor (69 kDa). P2 is sorted away from secretory proteins at or beyond a late Golgi compartment and is subsequently delivered to the vacuole via a prevacuolar endosome-like compartment. Upon arrival in the vacuole, the N-terminal prosegment of P2 is cleaved by vacuolar proteases to yield the enzymatically active mature vacuolar form of CPY (61 kDa)." ], [ "Q05473-1", "protein_xref_uniprotkb", "Q05473", "ECO_0000269", "Sumoylated upon ethanol stress." ], [ "Q05473-1", "protein_xref_pubmed", "15166219", "ECO_0000269", "Sumoylated upon ethanol stress." ], [ "P40160-1", "protein_xref_uniprotkb", "P40160", "ECO_0000269", "Autophosphorylated." ], [ "P40160-1", "protein_xref_pubmed", "12690111", "ECO_0000269", "Autophosphorylated." ], [ "P38616-1", "protein_xref_uniprotkb", "P38616", "ECO_0000269", "Extensively N-glycosylated." ], [ "P38616-1", "protein_xref_pubmed", "18434410", "ECO_0000269", "Extensively N-glycosylated." ], [ "Q03180-1", "protein_xref_uniprotkb", "Q03180", "ECO_0000269", "O-glycosylated. Extensively O-mannosylated." ], [ "Q03180-1", "protein_xref_pubmed", "9301021", "ECO_0000269", "O-glycosylated. Extensively O-mannosylated." ], [ "Q06604-1", "protein_xref_uniprotkb", "Q06604", "ECO_0000269", "Phosphorylated by CDC28." ], [ "Q06604-1", "protein_xref_pubmed", "14574415", "ECO_0000269", "Phosphorylated by CDC28." ], [ "P16522-1", "protein_xref_uniprotkb", "P16522", "ECO_0000269", "Phosphorylated by CDC28, which is required for the early mitotic activity of the APC/C in its CDC20-bound form." ], [ "P16522-1", "protein_xref_pubmed", "10871279", "ECO_0000269", "Phosphorylated by CDC28, which is required for the early mitotic activity of the APC/C in its CDC20-bound form." ], [ "Q12517-1", "protein_xref_uniprotkb", "Q12517", "ECO_0000269", "Phosphorylated." ], [ "Q12517-1", "protein_xref_pubmed", "9482745", "ECO_0000269", "Phosphorylated." ], [ "P39705-1", "protein_xref_uniprotkb", "P39705", "ECO_0000269", "Phosphorylated by CDC28." ], [ "P39705-1", "protein_xref_pubmed", "14574415", "ECO_0000269", "Phosphorylated by CDC28." ], [ "P33327-1", "protein_xref_uniprotkb", "P33327", "ECO_0000269", "Phosphorylated by a complex containing the NNK1 kinase." ], [ "P33327-1", "protein_xref_pubmed", "20489023", "ECO_0000269", "Phosphorylated by a complex containing the NNK1 kinase." ], [ "P21182-1", "protein_xref_uniprotkb", "P21182", "ECO_0000269", "Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain." ], [ "P21182-1", "protein_xref_pubmed", "2266128", "ECO_0000269", "Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain." ], [ "P39956-1", "protein_xref_uniprotkb", "P39956", "ECO_0000269", "RAD53-dependent phosphorylated in response to DNA damage." ], [ "P39956-1", "protein_xref_pubmed", "11809875", "ECO_0000269", "RAD53-dependent phosphorylated in response to DNA damage." ], [ "P02293-1", "protein_xref_uniprotkb", "P02293", "ECO_0000269", "Sumoylation to form H2BK6su or H2BK7su, and probably also H2BK16su or H2BK17su, occurs preferentially near the telomeres and represses gene transcription." ], [ "P02293-1", "protein_xref_pubmed", "15166219", "ECO_0000269", "Sumoylation to form H2BK6su or H2BK7su, and probably also H2BK16su or H2BK17su, occurs preferentially near the telomeres and represses gene transcription." ], [ "P02293-1", "protein_xref_pubmed", "16598039", "ECO_0000269", "Sumoylation to form H2BK6su or H2BK7su, and probably also H2BK16su or H2BK17su, occurs preferentially near the telomeres and represses gene transcription." ], [ "P02293-1", "protein_xref_uniprotkb", "P02293", "ECO_0000269", "Phosphorylated by STE20 to form H2BS10ph during progression through meiotic prophase. May be correlated with chromosome condensation. H2BS10ph is also formed after H(2)O(2) treatment, and is a step leading to apoptosis." ], [ "P02293-1", "protein_xref_pubmed", "15652479", "ECO_0000269", "Phosphorylated by STE20 to form H2BS10ph during progression through meiotic prophase. May be correlated with chromosome condensation. H2BS10ph is also formed after H(2)O(2) treatment, and is a step leading to apoptosis." ], [ "P02293-1", "protein_xref_pubmed", "15970663", "ECO_0000269", "Phosphorylated by STE20 to form H2BS10ph during progression through meiotic prophase. May be correlated with chromosome condensation. H2BS10ph is also formed after H(2)O(2) treatment, and is a step leading to apoptosis." ], [ "P02293-1", "protein_xref_uniprotkb", "P02293", "ECO_0000269", "Acetylated by GCN5, a component of the SAGA complex, to form H2BK11ac and H2BK16ac. H2BK16ac can also be formed by ESA1, a component of the NuA4 histone acetyltransferase (HAT) complex. Acetylation of N-terminal lysines and particularly formation of H2BK11acK16ac has a positive effect on transcription." ], [ "P02293-1", "protein_xref_pubmed", "15186774", "ECO_0000269", "Acetylated by GCN5, a component of the SAGA complex, to form H2BK11ac and H2BK16ac. H2BK16ac can also be formed by ESA1, a component of the NuA4 histone acetyltransferase (HAT) complex. Acetylation of N-terminal lysines and particularly formation of H2BK11acK16ac has a positive effect on transcription." ], [ "P02293-1", "protein_xref_pubmed", "10777603", "ECO_0000269", "Acetylated by GCN5, a component of the SAGA complex, to form H2BK11ac and H2BK16ac. H2BK16ac can also be formed by ESA1, a component of the NuA4 histone acetyltransferase (HAT) complex. Acetylation of N-terminal lysines and particularly formation of H2BK11acK16ac has a positive effect on transcription." ], [ "P02293-1", "protein_xref_pubmed", "11545749", "ECO_0000269", "Acetylated by GCN5, a component of the SAGA complex, to form H2BK11ac and H2BK16ac. H2BK16ac can also be formed by ESA1, a component of the NuA4 histone acetyltransferase (HAT) complex. Acetylation of N-terminal lysines and particularly formation of H2BK11acK16ac has a positive effect on transcription." ], [ "P02293-1", "protein_xref_pubmed", "16598039", "ECO_0000269", "Acetylated by GCN5, a component of the SAGA complex, to form H2BK11ac and H2BK16ac. H2BK16ac can also be formed by ESA1, a component of the NuA4 histone acetyltransferase (HAT) complex. Acetylation of N-terminal lysines and particularly formation of H2BK11acK16ac has a positive effect on transcription." ], [ "P02294-1", "protein_xref_uniprotkb", "P02294", "ECO_0000269", "Acetylated by GCN5, a component of the SAGA complex, to form H2BK11ac and H2BK16ac. H2BK16ac can also be formed by ESA1, a component of the NuA4 histone acetyltransferase (HAT) complex. Acetylation of N-terminal lysines and particularly formation of H2BK11acK16ac has a positive effect on transcription." ], [ "P02294-1", "protein_xref_pubmed", "15186774", "ECO_0000269", "Acetylated by GCN5, a component of the SAGA complex, to form H2BK11ac and H2BK16ac. H2BK16ac can also be formed by ESA1, a component of the NuA4 histone acetyltransferase (HAT) complex. Acetylation of N-terminal lysines and particularly formation of H2BK11acK16ac has a positive effect on transcription." ], [ "P02294-1", "protein_xref_pubmed", "10777603", "ECO_0000269", "Acetylated by GCN5, a component of the SAGA complex, to form H2BK11ac and H2BK16ac. H2BK16ac can also be formed by ESA1, a component of the NuA4 histone acetyltransferase (HAT) complex. Acetylation of N-terminal lysines and particularly formation of H2BK11acK16ac has a positive effect on transcription." ], [ "P02294-1", "protein_xref_pubmed", "11545749", "ECO_0000269", "Acetylated by GCN5, a component of the SAGA complex, to form H2BK11ac and H2BK16ac. H2BK16ac can also be formed by ESA1, a component of the NuA4 histone acetyltransferase (HAT) complex. Acetylation of N-terminal lysines and particularly formation of H2BK11acK16ac has a positive effect on transcription." ], [ "P02294-1", "protein_xref_pubmed", "16598039", "ECO_0000269", "Acetylated by GCN5, a component of the SAGA complex, to form H2BK11ac and H2BK16ac. H2BK16ac can also be formed by ESA1, a component of the NuA4 histone acetyltransferase (HAT) complex. Acetylation of N-terminal lysines and particularly formation of H2BK11acK16ac has a positive effect on transcription." ], [ "P02294-1", "protein_xref_uniprotkb", "P02294", "ECO_0000269", "Phosphorylated by STE20 to form H2BS10ph during progression through meiotic prophase. May be correlated with chromosome condensation. H2BS10ph is also formed after H(2)O(2) treatment, and is a step leading to apoptosis." ], [ "P02294-1", "protein_xref_pubmed", "15652479", "ECO_0000269", "Phosphorylated by STE20 to form H2BS10ph during progression through meiotic prophase. May be correlated with chromosome condensation. H2BS10ph is also formed after H(2)O(2) treatment, and is a step leading to apoptosis." ], [ "P02294-1", "protein_xref_pubmed", "15970663", "ECO_0000269", "Phosphorylated by STE20 to form H2BS10ph during progression through meiotic prophase. May be correlated with chromosome condensation. H2BS10ph is also formed after H(2)O(2) treatment, and is a step leading to apoptosis." ], [ "P02294-1", "protein_xref_uniprotkb", "P02294", "ECO_0000269", "Sumoylation to form H2BK6su or H2BK7su, and probably also H2BK16su or H2BK17su, occurs preferentially near the telomeres and represses gene transcription." ], [ "P02294-1", "protein_xref_pubmed", "15166219", "ECO_0000269", "Sumoylation to form H2BK6su or H2BK7su, and probably also H2BK16su or H2BK17su, occurs preferentially near the telomeres and represses gene transcription." ], [ "P02294-1", "protein_xref_pubmed", "16598039", "ECO_0000269", "Sumoylation to form H2BK6su or H2BK7su, and probably also H2BK16su or H2BK17su, occurs preferentially near the telomeres and represses gene transcription." ], [ "P32266-1", "protein_xref_uniprotkb", "P32266", "ECO_0000269", "Cleavage of the transit peptide by mitochondrial processing protease (MPP) produces a long integral membrane form of MGM1 (l-MGM1). Further processing by the rhomboid protease PCP1 produces a short peripheral membrane form of MGM1 (s-MGM1). Both isoforms are required for full activity." ], [ "P32266-1", "protein_xref_pubmed", "15096522", "ECO_0000269", "Cleavage of the transit peptide by mitochondrial processing protease (MPP) produces a long integral membrane form of MGM1 (l-MGM1). Further processing by the rhomboid protease PCP1 produces a short peripheral membrane form of MGM1 (s-MGM1). Both isoforms are required for full activity." ], [ "P29465-1", "protein_xref_uniprotkb", "P29465", "ECO_0000269", "Glycosylated." ], [ "P29465-1", "protein_xref_pubmed", "9760183", "ECO_0000269", "Glycosylated." ], [ "P29465-1", "protein_xref_uniprotkb", "P29465", "ECO_0000269", "Palmitoylated by PFA4; required for proper export from the ER." ], [ "P29465-1", "protein_xref_pubmed", "16818716", "ECO_0000269", "Palmitoylated by PFA4; required for proper export from the ER." ], [ "P24482-1", "protein_xref_uniprotkb", "P24482", "ECO_0000269", "Phosphorylated in a cell cycle dependent manner during late G1 phase. Phosphorylation may facilitate the interaction with POL2 or the activity of DNA polymerase II. Phosphorylation is independent of DNA replication but dependent upon CDC28 in vivo. Both Ser-141 and Ser-613 are phosphorylated in vivo, but in vitro only Ser-141 is phosphorylated by CDC28." ], [ "P24482-1", "protein_xref_pubmed", "14747467", "ECO_0000269", "Phosphorylated in a cell cycle dependent manner during late G1 phase. Phosphorylation may facilitate the interaction with POL2 or the activity of DNA polymerase II. Phosphorylation is independent of DNA replication but dependent upon CDC28 in vivo. Both Ser-141 and Ser-613 are phosphorylated in vivo, but in vitro only Ser-141 is phosphorylated by CDC28." ], [ "P53720-1", "protein_xref_uniprotkb", "P53720", "ECO_0000269", "N-glycosylated." ], [ "P53720-1", "protein_xref_pubmed", "19756047", "ECO_0000269", "N-glycosylated." ], [ "P43497-1", "protein_xref_uniprotkb", "P43497", "ECO_0000269", "Extensively O-glycosylated." ], [ "P43497-1", "protein_xref_pubmed", "7768807", "ECO_0000269", "Extensively O-glycosylated." ], [ "Q12167-1", "protein_xref_uniprotkb", "Q12167", "ECO_0000269", "N-glycosylated. Glycosylation is important for correct localization of the protein." ], [ "Q12167-1", "protein_xref_pubmed", "19756047", "ECO_0000269", "N-glycosylated. Glycosylation is important for correct localization of the protein." ], [ "P10664-1", "protein_xref_uniprotkb", "P10664", "ECO_0000269", "N-terminally acetylated by acetyltransferase NatA." ], [ "P10664-1", "protein_xref_pubmed", "1544921", "ECO_0000269", "N-terminally acetylated by acetyltransferase NatA." ], [ "P47050-1", "protein_xref_uniprotkb", "P47050", "ECO_0000269", "Neddylated. HRT1-binding is necessary for RUB1/NEDD8 modification of RTT101. The modification enhances ubiquitin-ligase activity." ], [ "P47050-1", "protein_xref_pubmed", "14519104", "ECO_0000269", "Neddylated. HRT1-binding is necessary for RUB1/NEDD8 modification of RTT101. The modification enhances ubiquitin-ligase activity." ], [ "Q06628-1", "protein_xref_uniprotkb", "Q06628", "ECO_0000269", "Phosphorylated; hyperphosphorylated by the TORC1 kinase complex to repress the induction of autophagy in nutrient-replete conditions (PubMed:10995454, PubMed:19995911, PubMed:19805182, PubMed:22447937, PubMed:22727621, PubMed:29698392). Starvation and TOR inactivation results in ATG13 partial dephosphorylation leading to ATG1-binding (PubMed:10995454). Rephosphorylated by ATG1 during prolonged nitrogen starvation (PubMed:21490424). Also phosphorylated by PKA (PubMed:17699586, PubMed:19805182, PubMed:21078689). PKA phosphorylation regulates the association of ATG13 with the PAS (PubMed:21900499). Within this regulatory network, mitochondrial respiratory deficiency suppresses autophagic flux (PubMed:21468027). Hyperphosphorylation in rich medium is impaired in the absence of VAC8 (PubMed:10837477). Dephosphorylation is dependent on FAR11 (PubMed:22782902)." ] ] }, "readme": "Name\n - Yeast Protein PTM Annotation (UniProtKB)\n\nVersion\n - v-2.4.1\n\nCreated on\n - 2022-08-31T10:58:38.192589\n\nModified on\n - 2023-09-11T19:19:45\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], Luke Johnson [luke.johnson@email.gwu.edu], Urnisha Bhuiyan [sbhuiyan28@email.gwu.edu], Cyrus Au-Yeung [cyruschauyeung@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 Yeast Protein PTM Annotation (UniProtKB) dataset contains yeast [taxid:559292] PTM annotations for UniProtKB canonical accessions. The annotation is the curated statements of mainly about glycosylation and phosphorylation. If you use this dataset please give proper attribution to EMBL-EBI-UniProtKB and GlyGen\n\nDescription Domain\n Keywords\n - ptm annotation\n - glycosylation\n - phosphorylation\n\n Pipeline Steps\n - Step-1: The script extracts the ptm annotation strings from the triplestore for the UniProtKB canonical sequnces asnd extracts as a dataset in a csv format\n\nExecution Domain\n Scripts - https://github.com/glygener/glygen-backend-integration/blob/master/dataset-maker/make-protein-dataset.py\n\n\n Software Prerequisites\n Name: Python\n Version: 2.7.5\n URI: https://www.python.org/download/releases/2.7.5/\n\nI/O Domain\n Input Subdomain\n Name: uniprot-proteome-saccharomyces-cerevisiae.nt\n URI: https:/data.glygen.org/ln2downloads/ebi/2024_02_13/uniprot-proteome-saccharomyces-cerevisiae.nt\n Output Subdomain\n Name: yeast_protein_ptm_annotation_uniprotkb.csv\n URI: https:/data.glygen.org/ln2releases/data/v-2.4.1/reviewed/yeast_protein_ptm_annotation_uniprotkb.csv\n Name: yeast_protein_ptm_annotation_uniprotkb.stat.csv\n URI: https:/data.glygen.org/ln2releases/data/v-2.4.1/reviewed/yeast_protein_ptm_annotation_uniprotkb.stat.csv\n\nFields\n Name: \"uniprotkb_canonical_ac\"\n Description: \"\"\n Unique Values: \"544\"\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: \"1188\"\n Name: \"eco_id\"\n Description: \"Evidence & Conclusion Ontology (ECO) identifier\"\n Unique Values: \"3\"\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: \"387\"", "downloadurl": "/ln2data/releases/data/v-2.4.1/reviewed/yeast_protein_ptm_annotation_uniprotkb.csv" }