{ "bcoid": "GLY_000316", "title": "Human Protein PTM Annotation (UniProtKB)", "description": "The Human Protein PTM Annotation (UniProtKB) dataset contains human [taxid:9606] PTM annotations for ...", "filename": "human_protein_ptm_annotation_uniprotkb.csv", "filetype": "csv", "categories": { "species": "Homo sapiens", "molecule": "Protein", "tags": "PTM annotation", "file_type": "csv", "status": "Reviewed", "scope": "internal" }, "minitable": { "content": [ [ "Q8NHX9-1...", "protein_xref..." ], [ "Q8NHX9-1...", "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" } ], [ "Q8NHX9-1", "protein_xref_uniprotkb", "Q8NHX9", "ECO_0000250", "N-glycosylated." ], [ "Q8NHX9-1", "protein_xref_pubmed", "Q8BWC0", "ECO_0000250", "N-glycosylated." ], [ "Q9C0H2-1", "protein_xref_uniprotkb", "Q9C0H2", "ECO_0000269", "N-glycosylated." ], [ "Q9C0H2-1", "protein_xref_pubmed", "19159218", "ECO_0000269", "N-glycosylated." ], [ "Q9C0H2-1", "protein_xref_pubmed", "15010458", "ECO_0000269", "N-glycosylated." ], [ "Q9C0H9-5", "protein_xref_uniprotkb", "Q9C0H9", "ECO_0000269", "Tyrosine-phosphorylated in response to EGF and to cell adhesion to integrin ligands." ], [ "Q9C0H9-5", "protein_xref_pubmed", "14657239", "ECO_0000269", "Tyrosine-phosphorylated in response to EGF and to cell adhesion to integrin ligands." ], [ "P40429-1", "protein_xref_uniprotkb", "P40429", "ECO_0000269", "Phosphorylation at Ser-77 upon interferon-gamma treatment in monocytes involves a DAPK1-DAPK3 kinase cascade and is causing release from the ribosome, association with the GAIT complex and subsequent involvement in transcript-selective translation inhibition." ], [ "P40429-1", "protein_xref_pubmed", "18995835", "ECO_0000269", "Phosphorylation at Ser-77 upon interferon-gamma treatment in monocytes involves a DAPK1-DAPK3 kinase cascade and is causing release from the ribosome, association with the GAIT complex and subsequent involvement in transcript-selective translation inhibition." ], [ "P40429-1", "protein_xref_pubmed", "14567916", "ECO_0000269", "Phosphorylation at Ser-77 upon interferon-gamma treatment in monocytes involves a DAPK1-DAPK3 kinase cascade and is causing release from the ribosome, association with the GAIT complex and subsequent involvement in transcript-selective translation inhibition." ], [ "P02768-1", "protein_xref_uniprotkb", "P02768", "ECO_0000269", "Phosphorylated by FAM20C in the extracellular medium." ], [ "P02768-1", "protein_xref_pubmed", "26091039", "ECO_0000269", "Phosphorylated by FAM20C in the extracellular medium." ], [ "P02760-1", "protein_xref_uniprotkb", "P02760", "ECO_0000269", "N- and O-glycosylated. N-glycan heterogeneity at Asn-115: Hex5HexNAc4 (major), Hex6HexNAc5 (minor) and dHex1Hex6HexNAc5 (minor). N-glycan at Asn-250: Hex5HexNAc4. O-linkage of the glycosaminoglycan, chondroitin sulfate, at Ser-215 allows cross-linking between the three polypeptide chains." ], [ "P02760-1", "protein_xref_pubmed", "7682553", "ECO_0000269", "N- and O-glycosylated. N-glycan heterogeneity at Asn-115: Hex5HexNAc4 (major), Hex6HexNAc5 (minor) and dHex1Hex6HexNAc5 (minor). N-glycan at Asn-250: Hex5HexNAc4. O-linkage of the glycosaminoglycan, chondroitin sulfate, at Ser-215 allows cross-linking between the three polypeptide chains." ], [ "P02760-1", "protein_xref_pubmed", "1898736", "ECO_0000269", "N- and O-glycosylated. N-glycan heterogeneity at Asn-115: Hex5HexNAc4 (major), Hex6HexNAc5 (minor) and dHex1Hex6HexNAc5 (minor). N-glycan at Asn-250: Hex5HexNAc4. O-linkage of the glycosaminoglycan, chondroitin sulfate, at Ser-215 allows cross-linking between the three polypeptide chains." ], [ "P02760-1", "protein_xref_pubmed", "1694784", "ECO_0000269", "N- and O-glycosylated. N-glycan heterogeneity at Asn-115: Hex5HexNAc4 (major), Hex6HexNAc5 (minor) and dHex1Hex6HexNAc5 (minor). N-glycan at Asn-250: Hex5HexNAc4. O-linkage of the glycosaminoglycan, chondroitin sulfate, at Ser-215 allows cross-linking between the three polypeptide chains." ], [ "P02760-1", "protein_xref_pubmed", "22171320", "ECO_0000269", "N- and O-glycosylated. N-glycan heterogeneity at Asn-115: Hex5HexNAc4 (major), Hex6HexNAc5 (minor) and dHex1Hex6HexNAc5 (minor). N-glycan at Asn-250: Hex5HexNAc4. O-linkage of the glycosaminoglycan, chondroitin sulfate, at Ser-215 allows cross-linking between the three polypeptide chains." ], [ "P02760-1", "protein_xref_pubmed", "6171497", "ECO_0000269", "N- and O-glycosylated. N-glycan heterogeneity at Asn-115: Hex5HexNAc4 (major), Hex6HexNAc5 (minor) and dHex1Hex6HexNAc5 (minor). N-glycan at Asn-250: Hex5HexNAc4. O-linkage of the glycosaminoglycan, chondroitin sulfate, at Ser-215 allows cross-linking between the three polypeptide chains." ], [ "P02763-1", "protein_xref_uniprotkb", "P02763", "ECO_0000269", "N-glycosylated. N-glycan heterogeneity at Asn-33: Hex5HexNAc4 (minor), Hex6HexNAc5 (major) and dHex1Hex6HexNAc5 (minor)." ], [ "P02763-1", "protein_xref_pubmed", "1567356", "ECO_0000269", "N-glycosylated. N-glycan heterogeneity at Asn-33: Hex5HexNAc4 (minor), Hex6HexNAc5 (major) and dHex1Hex6HexNAc5 (minor)." ], [ "P02763-1", "protein_xref_pubmed", "19159218", "ECO_0000269", "N-glycosylated. N-glycan heterogeneity at Asn-33: Hex5HexNAc4 (minor), Hex6HexNAc5 (major) and dHex1Hex6HexNAc5 (minor)." ], [ "P02763-1", "protein_xref_pubmed", "12754519", "ECO_0000269", "N-glycosylated. N-glycan heterogeneity at Asn-33: Hex5HexNAc4 (minor), Hex6HexNAc5 (major) and dHex1Hex6HexNAc5 (minor)." ], [ "P02763-1", "protein_xref_pubmed", "16335952", "ECO_0000269", "N-glycosylated. N-glycan heterogeneity at Asn-33: Hex5HexNAc4 (minor), Hex6HexNAc5 (major) and dHex1Hex6HexNAc5 (minor)." ], [ "P02763-1", "protein_xref_pubmed", "19838169", "ECO_0000269", "N-glycosylated. N-glycan heterogeneity at Asn-33: Hex5HexNAc4 (minor), Hex6HexNAc5 (major) and dHex1Hex6HexNAc5 (minor)." ], [ "P02763-1", "protein_xref_pubmed", "16740002", "ECO_0000269", "N-glycosylated. N-glycan heterogeneity at Asn-33: Hex5HexNAc4 (minor), Hex6HexNAc5 (major) and dHex1Hex6HexNAc5 (minor)." ], [ "P02763-1", "protein_xref_pubmed", "15253437", "ECO_0000269", "N-glycosylated. N-glycan heterogeneity at Asn-33: Hex5HexNAc4 (minor), Hex6HexNAc5 (major) and dHex1Hex6HexNAc5 (minor)." ], [ "P02763-1", "protein_xref_pubmed", "14760718", "ECO_0000269", "N-glycosylated. N-glycan heterogeneity at Asn-33: Hex5HexNAc4 (minor), Hex6HexNAc5 (major) and dHex1Hex6HexNAc5 (minor)." ], [ "P02763-1", "protein_xref_pubmed", "15084671", "ECO_0000269", "N-glycosylated. N-glycan heterogeneity at Asn-33: Hex5HexNAc4 (minor), Hex6HexNAc5 (major) and dHex1Hex6HexNAc5 (minor)." ], [ "P02763-1", "protein_xref_pubmed", "22171320", "ECO_0000269", "N-glycosylated. N-glycan heterogeneity at Asn-33: Hex5HexNAc4 (minor), Hex6HexNAc5 (major) and dHex1Hex6HexNAc5 (minor)." ], [ "P02765-1", "protein_xref_uniprotkb", "P02765", "ECO_0000269", "Phosphorylated by FAM20C in the extracellular medium." ], [ "P02765-1", "protein_xref_pubmed", "11439093", "ECO_0000269", "Phosphorylated by FAM20C in the extracellular medium." ], [ "P02765-1", "protein_xref_pubmed", "26091039", "ECO_0000269", "Phosphorylated by FAM20C in the extracellular medium." ], [ "P02765-1", "protein_xref_uniprotkb", "P02765", "ECO_0000269", "O- and N-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans. N-glycan at Asn-156: Hex5HexNAc4; N-glycan heterogeneity at Asn-176: Hex5HexNAc4 (major) and Hex6HexNAc5 (minor)." ], [ "P02765-1", "protein_xref_pubmed", "19159218", "ECO_0000269", "O- and N-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans. N-glycan at Asn-156: Hex5HexNAc4; N-glycan heterogeneity at Asn-176: Hex5HexNAc4 (major) and Hex6HexNAc5 (minor)." ], [ "P02765-1", "protein_xref_pubmed", "12754519", "ECO_0000269", "O- and N-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans. N-glycan at Asn-156: Hex5HexNAc4; N-glycan heterogeneity at Asn-176: Hex5HexNAc4 (major) and Hex6HexNAc5 (minor)." ], [ "P02765-1", "protein_xref_pubmed", "16335952", "ECO_0000269", "O- and N-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans. N-glycan at Asn-156: Hex5HexNAc4; N-glycan heterogeneity at Asn-176: Hex5HexNAc4 (major) and Hex6HexNAc5 (minor)." ], [ "P02765-1", "protein_xref_pubmed", "19838169", "ECO_0000269", "O- and N-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans. N-glycan at Asn-156: Hex5HexNAc4; N-glycan heterogeneity at Asn-176: Hex5HexNAc4 (major) and Hex6HexNAc5 (minor)." ], [ "P02765-1", "protein_xref_pubmed", "16740002", "ECO_0000269", "O- and N-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans. N-glycan at Asn-156: Hex5HexNAc4; N-glycan heterogeneity at Asn-176: Hex5HexNAc4 (major) and Hex6HexNAc5 (minor)." ], [ "P02765-1", "protein_xref_pubmed", "14760718", "ECO_0000269", "O- and N-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans. N-glycan at Asn-156: Hex5HexNAc4; N-glycan heterogeneity at Asn-176: Hex5HexNAc4 (major) and Hex6HexNAc5 (minor)." ], [ "P02765-1", "protein_xref_pubmed", "19139490", "ECO_0000269", "O- and N-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans. N-glycan at Asn-156: Hex5HexNAc4; N-glycan heterogeneity at Asn-176: Hex5HexNAc4 (major) and Hex6HexNAc5 (minor)." ], [ "P02765-1", "protein_xref_pubmed", "22171320", "ECO_0000269", "O- and N-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans. N-glycan at Asn-156: Hex5HexNAc4; N-glycan heterogeneity at Asn-176: Hex5HexNAc4 (major) and Hex6HexNAc5 (minor)." ], [ "P02766-1", "protein_xref_uniprotkb", "P02766", "ECO_0000269", "Not glycosylated under normal conditions. Following unfolding, caused for example by variant AMYL-TTR 'Gly-38', the cryptic Asn-118 site is exposed and glycosylated by STT3B-containing OST complex, leading to its degradation by the ER-associated degradation (ERAD) pathway." ], [ "P02766-1", "protein_xref_pubmed", "16335952", "ECO_0000269", "Not glycosylated under normal conditions. Following unfolding, caused for example by variant AMYL-TTR 'Gly-38', the cryptic Asn-118 site is exposed and glycosylated by STT3B-containing OST complex, leading to its degradation by the ER-associated degradation (ERAD) pathway." ], [ "P02766-1", "protein_xref_pubmed", "19167329", "ECO_0000269", "Not glycosylated under normal conditions. Following unfolding, caused for example by variant AMYL-TTR 'Gly-38', the cryptic Asn-118 site is exposed and glycosylated by STT3B-containing OST complex, leading to its degradation by the ER-associated degradation (ERAD) pathway." ], [ "P02766-1", "protein_xref_pubmed", "14760718", "ECO_0000269", "Not glycosylated under normal conditions. Following unfolding, caused for example by variant AMYL-TTR 'Gly-38', the cryptic Asn-118 site is exposed and glycosylated by STT3B-containing OST complex, leading to its degradation by the ER-associated degradation (ERAD) pathway." ], [ "Q9BZG2-1", "protein_xref_uniprotkb", "Q9BZG2", "ECO_0000305", "Glycosylated." ], [ "Q9BZG2-1", "protein_xref_pubmed", "15219672", "ECO_0000305", "Glycosylated." ], [ "Q14566-1", "protein_xref_uniprotkb", "Q14566", "ECO_0000269", "O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner." ], [ "Q14566-1", "protein_xref_pubmed", "22967762", "ECO_0000269", "O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner." ], [ "Q6ZMG9-1", "protein_xref_uniprotkb", "Q6ZMG9", "ECO_0000250", "Acetylated. Deacetylation by SIRT3 increases enzyme activity and promotes mitochondrial ceramide accumulation." ], [ "Q6ZMG9-1", "protein_xref_pubmed", "Q8C172", "ECO_0000250", "Acetylated. Deacetylation by SIRT3 increases enzyme activity and promotes mitochondrial ceramide accumulation." ], [ "Q6ZMG9-1", "protein_xref_uniprotkb", "Q6ZMG9", "ECO_0000269", "Phosphorylated at the C-terminus by CK2." ], [ "Q6ZMG9-1", "protein_xref_pubmed", "26887952", "ECO_0000269", "Phosphorylated at the C-terminus by CK2." ], [ "Q96BT3-1", "protein_xref_uniprotkb", "Q96BT3", "ECO_0000269", "Dynamically phosphorylated at Ser-47 and probably also other sites during the cell cycle. Phosphorylated at Ser-47 during G2 phase, metaphase and anaphase, but not during telophase or G1 phase." ], [ "Q96BT3-1", "protein_xref_pubmed", "21529714", "ECO_0000269", "Dynamically phosphorylated at Ser-47 and probably also other sites during the cell cycle. Phosphorylated at Ser-47 during G2 phase, metaphase and anaphase, but not during telophase or G1 phase." ], [ "Q99519-1", "protein_xref_uniprotkb", "Q99519", "ECO_0000269", "N-glycosylated." ], [ "Q99519-1", "protein_xref_pubmed", "19159218", "ECO_0000269", "N-glycosylated." ], [ "Q99519-1", "protein_xref_pubmed", "9480870", "ECO_0000269", "N-glycosylated." ], [ "Q99519-1", "protein_xref_pubmed", "8985184", "ECO_0000269", "N-glycosylated." ], [ "Q96RU2-1", "protein_xref_uniprotkb", "Q96RU2", "ECO_0000269", "Phosphorylated upon DNA damage at Ser-67 and Ser-714, by ATM or ATR (PubMed:16901786). Phosphorylated by PRKD1 (PubMed:24623306)." ], [ "Q96RU2-1", "protein_xref_pubmed", "24623306", "ECO_0000269", "Phosphorylated upon DNA damage at Ser-67 and Ser-714, by ATM or ATR (PubMed:16901786). Phosphorylated by PRKD1 (PubMed:24623306)." ], [ "Q96RU2-1", "protein_xref_pubmed", "16901786", "ECO_0000269", "Phosphorylated upon DNA damage at Ser-67 and Ser-714, by ATM or ATR (PubMed:16901786). Phosphorylated by PRKD1 (PubMed:24623306)." ], [ "Q13641-1", "protein_xref_uniprotkb", "Q13641", "ECO_0000269", "Highly glycosylated." ], [ "Q13641-1", "protein_xref_pubmed", "19159218", "ECO_0000269", "Highly glycosylated." ], [ "Q13641-1", "protein_xref_pubmed", "24582434", "ECO_0000269", "Highly glycosylated." ], [ "Q9Y5A9-1", "protein_xref_uniprotkb", "Q9Y5A9", "ECO_0000269", "Ubiquitinated by the SCF(SKP2) complex, leading to its degradation." ], [ "Q9Y5A9-1", "protein_xref_pubmed", "32267835", "ECO_0000269", "Ubiquitinated by the SCF(SKP2) complex, leading to its degradation." ], [ "Q9Y294-1", "protein_xref_uniprotkb", "Q9Y294", "ECO_0000269", "Phosphorylated by TLK1 and TLK2. Highly phosphorylated in S-phase and at lower levels in M-phase. TLK2-mediated phosphorylation at Ser-192 prevents proteasome-dependent degradation." ], [ "Q9Y294-1", "protein_xref_pubmed", "11470414", "ECO_0000269", "Phosphorylated by TLK1 and TLK2. Highly phosphorylated in S-phase and at lower levels in M-phase. TLK2-mediated phosphorylation at Ser-192 prevents proteasome-dependent degradation." ], [ "Q9Y294-1", "protein_xref_pubmed", "20016786", "ECO_0000269", "Phosphorylated by TLK1 and TLK2. Highly phosphorylated in S-phase and at lower levels in M-phase. TLK2-mediated phosphorylation at Ser-192 prevents proteasome-dependent degradation." ], [ "Q9Y295-1", "protein_xref_uniprotkb", "Q9Y295", "ECO_0000269", "Sumoylated by UBE2I in response to MEKK1-mediated stimuli." ], [ "Q9Y295-1", "protein_xref_pubmed", "17709345", "ECO_0000269", "Sumoylated by UBE2I in response to MEKK1-mediated stimuli." ], [ "Q9Y295-1", "protein_xref_uniprotkb", "Q9Y295", "ECO_0000269", "Hydroxylated (with S stereochemistry) at C-3 of Lys-22 by JMJD7; this modification hinders trypsin-catalyzed proteolysis in vitro." ], [ "Q9Y295-1", "protein_xref_pubmed", "29915238", "ECO_0000269", "Hydroxylated (with S stereochemistry) at C-3 of Lys-22 by JMJD7; this modification hinders trypsin-catalyzed proteolysis in vitro." ], [ "Q9Y295-1", "protein_xref_uniprotkb", "Q9Y295", "ECO_0000269", "Phosphorylated at Thr-100 by STK16." ], [ "Q9Y295-1", "protein_xref_pubmed", "18184589", "ECO_0000269", "Phosphorylated at Thr-100 by STK16." ], [ "Q9Y295-1", "protein_xref_uniprotkb", "Q9Y295", "ECO_0000250", "Polyubiquitinated; this modification induces proteolytic degradation and is impaired by interaction with ZC3H15." ], [ "Q9Y295-1", "protein_xref_pubmed", "P32233", "ECO_0000250", "Polyubiquitinated; this modification induces proteolytic degradation and is impaired by interaction with ZC3H15." ], [ "P61289-1", "protein_xref_uniprotkb", "P61289", "ECO_0000269", "Phosphorylated by MAP3K3 (By similarity). Phosphorylation at Ser-247 promotes its association with CCAR2." ], [ "P61289-1", "protein_xref_pubmed", "25361978", "ECO_0000269", "Phosphorylated by MAP3K3 (By similarity). Phosphorylation at Ser-247 promotes its association with CCAR2." ], [ "P61289-1", "protein_xref_uniprotkb", "P61289", "ECO_0000250", "Phosphorylated by MAP3K3 (By similarity). Phosphorylation at Ser-247 promotes its association with CCAR2." ], [ "P61289-1", "protein_xref_pubmed", "P61290", "ECO_0000250", "Phosphorylated by MAP3K3 (By similarity). Phosphorylation at Ser-247 promotes its association with CCAR2." ], [ "P61289-1", "protein_xref_uniprotkb", "P61289", "ECO_0000269", "Acetylation at the major site Lys-195 is important for oligomerization and ability to degrade its target substrates. Deacetylated by SIRT1." ], [ "P61289-1", "protein_xref_pubmed", "SIPE5468F94A72A33A3", "ECO_0000269", "Acetylation at the major site Lys-195 is important for oligomerization and ability to degrade its target substrates. Deacetylated by SIRT1." ] ] }, "readme": "Name\n - Human Protein PTM Annotation (UniProtKB)\n\nVersion\n - 1.10.6\n\nCreated on\n - 2019-11-30T13:58:37.032006\n\nModified on\n - 2020-04-11T11:28:33.003978\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 Human Protein PTM Annotation (UniProtKB) dataset contains human [taxid:9606] 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-homo-sapiens.nt\n URI: https://data.glygen.org/ln2wwwdata/reviewed/uniprot-proteome-homo-sapiens.nt\n Name: human_protein_masterlist.csv\n URI: https://data.glygen.org/ln2wwwdata/reviewed/human_protein_masterlist.csv\n Output Subdomain\n Name: human_protein_ptm_annotation_uniprotkb.csv\n URI: http://data.glygen.org/ln2wwwdata/reviewed/human_protein_ptm_annotation_uniprotkb.csv\n Name: human_protein_ptm_annotation_uniprotkb.stat.csv\n URI: http://data.glygen.org/ln2wwwdata/reviewed/human_protein_ptm_annotation_uniprotkb.stat.csv\n\nFields\n Name: \"glytoucan_ac\"\n Description: \"Unique accession assigned to the registered glycan structure in GlyTouCan database\"\n Unique Values: \"123404\"", "downloadurl": "/ln2data/releases/data/v-1.10.6/reviewed/human_protein_ptm_annotation_uniprotkb.csv" }