{ "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": [ [ "P40429-1...", "protein_xref..." ], [ "P40429-1...", "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" } ], [ "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." ], [ "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)." ], [ "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." ], [ "P17693-1", "protein_xref_uniprotkb", "P17693", "ECO_0000269", "Produced by proteolytic cleavage at the cell surface (shedding) by matrix metalloproteinase MMP2." ], [ "P17693-1", "protein_xref_pubmed", "23737137", "ECO_0000269", "Produced by proteolytic cleavage at the cell surface (shedding) by matrix metalloproteinase MMP2." ], [ "P17693-1", "protein_xref_uniprotkb", "P17693", "ECO_0000269", "N-glycosylated." ], [ "P17693-1", "protein_xref_pubmed", "11290782", "ECO_0000269", "N-glycosylated." ], [ "Q8IYD8-1", "protein_xref_uniprotkb", "Q8IYD8", "ECO_0000269", "Phosphorylated; hyperphosphorylated in response to genotoxic stress." ], [ "Q8IYD8-1", "protein_xref_pubmed", "16116422", "ECO_0000269", "Phosphorylated; hyperphosphorylated in response to genotoxic stress." ], [ "P45984-1", "protein_xref_uniprotkb", "P45984", "ECO_0000269", "Dually phosphorylated on Thr-183 and Tyr-185 by MAP2K7 and MAP2K4, which activates the enzyme. Autophosphorylated in vitro." ], [ "P45984-1", "protein_xref_pubmed", "11062067", "ECO_0000269", "Dually phosphorylated on Thr-183 and Tyr-185 by MAP2K7 and MAP2K4, which activates the enzyme. Autophosphorylated in vitro." ], [ "Q7Z5G4-1", "protein_xref_uniprotkb", "Q7Z5G4", "ECO_0000269", "Palmitoylated on Cys-69 and Cys-72; which is required for Golgi localization and interaction with GOLGA3." ], [ "Q7Z5G4-1", "protein_xref_pubmed", "14522980", "ECO_0000269", "Palmitoylated on Cys-69 and Cys-72; which is required for Golgi localization and interaction with GOLGA3." ], [ "O60830-1", "protein_xref_uniprotkb", "O60830", "ECO_0000269", "Forms one disulfide bond." ], [ "O60830-1", "protein_xref_pubmed", "27265872", "ECO_0000269", "Forms one disulfide bond." ], [ "O14579-1", "protein_xref_uniprotkb", "O14579", "ECO_0000269", "Polyubiquitinated by RCHY1 in the presence of androgen, leading to proteasomal degradation." ], [ "O14579-1", "protein_xref_pubmed", "17721809", "ECO_0000269", "Polyubiquitinated by RCHY1 in the presence of androgen, leading to proteasomal degradation." ], [ "Q7LDG7-1", "protein_xref_uniprotkb", "Q7LDG7", "ECO_0000269", "Isoform 2 is palmitoylated and myristoylated." ], [ "Q7LDG7-1", "protein_xref_pubmed", "10918068", "ECO_0000269", "Isoform 2 is palmitoylated and myristoylated." ], [ "Q05397-1", "protein_xref_uniprotkb", "Q05397", "ECO_0000269", "Phosphorylated on tyrosine residues upon activation, e.g. upon integrin signaling. Tyr-397 is the major autophosphorylation site, but other kinases can also phosphorylate this residue. Phosphorylation at Tyr-397 promotes interaction with SRC and SRC family members, leading to phosphorylation at Tyr-576, Tyr-577 and at additional tyrosine residues. FGR promotes phosphorylation at Tyr-397 and Tyr-576. FER promotes phosphorylation at Tyr-577, Tyr-861 and Tyr-925, even when cells are not adherent. Tyr-397, Tyr-576 and Ser-722 are phosphorylated only when cells are adherent. Phosphorylation at Tyr-397 is important for interaction with BMX, PIK3R1 and SHC1. Phosphorylation at Tyr-925 is important for interaction with GRB2. Dephosphorylated by PTPN11; PTPN11 is recruited to PTK2 via EPHA2 (tyrosine phosphorylated). Microtubule-induced dephosphorylation at Tyr-397 is crucial for the induction of focal adhesion disassembly; this dephosphorylation could be catalyzed by PTPN11 and regulated by ZFYVE21. Phosphorylation on tyrosine residues is enhanced by NTN1 (By similarity)." ], [ "Q05397-1", "protein_xref_pubmed", "19339212", "ECO_0000269", "Phosphorylated on tyrosine residues upon activation, e.g. upon integrin signaling. Tyr-397 is the major autophosphorylation site, but other kinases can also phosphorylate this residue. Phosphorylation at Tyr-397 promotes interaction with SRC and SRC family members, leading to phosphorylation at Tyr-576, Tyr-577 and at additional tyrosine residues. FGR promotes phosphorylation at Tyr-397 and Tyr-576. FER promotes phosphorylation at Tyr-577, Tyr-861 and Tyr-925, even when cells are not adherent. Tyr-397, Tyr-576 and Ser-722 are phosphorylated only when cells are adherent. Phosphorylation at Tyr-397 is important for interaction with BMX, PIK3R1 and SHC1. Phosphorylation at Tyr-925 is important for interaction with GRB2. Dephosphorylated by PTPN11; PTPN11 is recruited to PTK2 via EPHA2 (tyrosine phosphorylated). Microtubule-induced dephosphorylation at Tyr-397 is crucial for the induction of focal adhesion disassembly; this dephosphorylation could be catalyzed by PTPN11 and regulated by ZFYVE21. Phosphorylation on tyrosine residues is enhanced by NTN1 (By similarity)." ], [ "Q05397-1", "protein_xref_uniprotkb", "Q05397", "ECO_0000250", "Phosphorylated on tyrosine residues upon activation, e.g. upon integrin signaling. Tyr-397 is the major autophosphorylation site, but other kinases can also phosphorylate this residue. Phosphorylation at Tyr-397 promotes interaction with SRC and SRC family members, leading to phosphorylation at Tyr-576, Tyr-577 and at additional tyrosine residues. FGR promotes phosphorylation at Tyr-397 and Tyr-576. FER promotes phosphorylation at Tyr-577, Tyr-861 and Tyr-925, even when cells are not adherent. Tyr-397, Tyr-576 and Ser-722 are phosphorylated only when cells are adherent. Phosphorylation at Tyr-397 is important for interaction with BMX, PIK3R1 and SHC1. Phosphorylation at Tyr-925 is important for interaction with GRB2. Dephosphorylated by PTPN11; PTPN11 is recruited to PTK2 via EPHA2 (tyrosine phosphorylated). Microtubule-induced dephosphorylation at Tyr-397 is crucial for the induction of focal adhesion disassembly; this dephosphorylation could be catalyzed by PTPN11 and regulated by ZFYVE21. Phosphorylation on tyrosine residues is enhanced by NTN1 (By similarity)." ], [ "Q05397-1", "protein_xref_pubmed", "P34152", "ECO_0000250", "Phosphorylated on tyrosine residues upon activation, e.g. upon integrin signaling. Tyr-397 is the major autophosphorylation site, but other kinases can also phosphorylate this residue. Phosphorylation at Tyr-397 promotes interaction with SRC and SRC family members, leading to phosphorylation at Tyr-576, Tyr-577 and at additional tyrosine residues. FGR promotes phosphorylation at Tyr-397 and Tyr-576. FER promotes phosphorylation at Tyr-577, Tyr-861 and Tyr-925, even when cells are not adherent. Tyr-397, Tyr-576 and Ser-722 are phosphorylated only when cells are adherent. Phosphorylation at Tyr-397 is important for interaction with BMX, PIK3R1 and SHC1. Phosphorylation at Tyr-925 is important for interaction with GRB2. Dephosphorylated by PTPN11; PTPN11 is recruited to PTK2 via EPHA2 (tyrosine phosphorylated). Microtubule-induced dephosphorylation at Tyr-397 is crucial for the induction of focal adhesion disassembly; this dephosphorylation could be catalyzed by PTPN11 and regulated by ZFYVE21. Phosphorylation on tyrosine residues is enhanced by NTN1 (By similarity)." ], [ "Q05397-1", "protein_xref_pubmed", "15561106", "ECO_0000269", "Phosphorylated on tyrosine residues upon activation, e.g. upon integrin signaling. Tyr-397 is the major autophosphorylation site, but other kinases can also phosphorylate this residue. Phosphorylation at Tyr-397 promotes interaction with SRC and SRC family members, leading to phosphorylation at Tyr-576, Tyr-577 and at additional tyrosine residues. FGR promotes phosphorylation at Tyr-397 and Tyr-576. FER promotes phosphorylation at Tyr-577, Tyr-861 and Tyr-925, even when cells are not adherent. Tyr-397, Tyr-576 and Ser-722 are phosphorylated only when cells are adherent. Phosphorylation at Tyr-397 is important for interaction with BMX, PIK3R1 and SHC1. Phosphorylation at Tyr-925 is important for interaction with GRB2. Dephosphorylated by PTPN11; PTPN11 is recruited to PTK2 via EPHA2 (tyrosine phosphorylated). Microtubule-induced dephosphorylation at Tyr-397 is crucial for the induction of focal adhesion disassembly; this dephosphorylation could be catalyzed by PTPN11 and regulated by ZFYVE21. Phosphorylation on tyrosine residues is enhanced by NTN1 (By similarity)." ], [ "Q05397-1", "protein_xref_pubmed", "18006843", "ECO_0000269", "Phosphorylated on tyrosine residues upon activation, e.g. upon integrin signaling. Tyr-397 is the major autophosphorylation site, but other kinases can also phosphorylate this residue. Phosphorylation at Tyr-397 promotes interaction with SRC and SRC family members, leading to phosphorylation at Tyr-576, Tyr-577 and at additional tyrosine residues. FGR promotes phosphorylation at Tyr-397 and Tyr-576. FER promotes phosphorylation at Tyr-577, Tyr-861 and Tyr-925, even when cells are not adherent. Tyr-397, Tyr-576 and Ser-722 are phosphorylated only when cells are adherent. Phosphorylation at Tyr-397 is important for interaction with BMX, PIK3R1 and SHC1. Phosphorylation at Tyr-925 is important for interaction with GRB2. Dephosphorylated by PTPN11; PTPN11 is recruited to PTK2 via EPHA2 (tyrosine phosphorylated). Microtubule-induced dephosphorylation at Tyr-397 is crucial for the induction of focal adhesion disassembly; this dephosphorylation could be catalyzed by PTPN11 and regulated by ZFYVE21. Phosphorylation on tyrosine residues is enhanced by NTN1 (By similarity)." ], [ "Q05397-1", "protein_xref_pubmed", "12387730", "ECO_0000269", "Phosphorylated on tyrosine residues upon activation, e.g. upon integrin signaling. Tyr-397 is the major autophosphorylation site, but other kinases can also phosphorylate this residue. Phosphorylation at Tyr-397 promotes interaction with SRC and SRC family members, leading to phosphorylation at Tyr-576, Tyr-577 and at additional tyrosine residues. FGR promotes phosphorylation at Tyr-397 and Tyr-576. FER promotes phosphorylation at Tyr-577, Tyr-861 and Tyr-925, even when cells are not adherent. Tyr-397, Tyr-576 and Ser-722 are phosphorylated only when cells are adherent. Phosphorylation at Tyr-397 is important for interaction with BMX, PIK3R1 and SHC1. Phosphorylation at Tyr-925 is important for interaction with GRB2. Dephosphorylated by PTPN11; PTPN11 is recruited to PTK2 via EPHA2 (tyrosine phosphorylated). Microtubule-induced dephosphorylation at Tyr-397 is crucial for the induction of focal adhesion disassembly; this dephosphorylation could be catalyzed by PTPN11 and regulated by ZFYVE21. Phosphorylation on tyrosine residues is enhanced by NTN1 (By similarity)." ], [ "Q05397-1", "protein_xref_pubmed", "17431114", "ECO_0000269", "Phosphorylated on tyrosine residues upon activation, e.g. upon integrin signaling. Tyr-397 is the major autophosphorylation site, but other kinases can also phosphorylate this residue. Phosphorylation at Tyr-397 promotes interaction with SRC and SRC family members, leading to phosphorylation at Tyr-576, Tyr-577 and at additional tyrosine residues. FGR promotes phosphorylation at Tyr-397 and Tyr-576. FER promotes phosphorylation at Tyr-577, Tyr-861 and Tyr-925, even when cells are not adherent. Tyr-397, Tyr-576 and Ser-722 are phosphorylated only when cells are adherent. Phosphorylation at Tyr-397 is important for interaction with BMX, PIK3R1 and SHC1. Phosphorylation at Tyr-925 is important for interaction with GRB2. Dephosphorylated by PTPN11; PTPN11 is recruited to PTK2 via EPHA2 (tyrosine phosphorylated). Microtubule-induced dephosphorylation at Tyr-397 is crucial for the induction of focal adhesion disassembly; this dephosphorylation could be catalyzed by PTPN11 and regulated by ZFYVE21. Phosphorylation on tyrosine residues is enhanced by NTN1 (By similarity)." ], [ "Q05397-1", "protein_xref_pubmed", "21454698", "ECO_0000269", "Phosphorylated on tyrosine residues upon activation, e.g. upon integrin signaling. Tyr-397 is the major autophosphorylation site, but other kinases can also phosphorylate this residue. Phosphorylation at Tyr-397 promotes interaction with SRC and SRC family members, leading to phosphorylation at Tyr-576, Tyr-577 and at additional tyrosine residues. FGR promotes phosphorylation at Tyr-397 and Tyr-576. FER promotes phosphorylation at Tyr-577, Tyr-861 and Tyr-925, even when cells are not adherent. Tyr-397, Tyr-576 and Ser-722 are phosphorylated only when cells are adherent. Phosphorylation at Tyr-397 is important for interaction with BMX, PIK3R1 and SHC1. Phosphorylation at Tyr-925 is important for interaction with GRB2. Dephosphorylated by PTPN11; PTPN11 is recruited to PTK2 via EPHA2 (tyrosine phosphorylated). Microtubule-induced dephosphorylation at Tyr-397 is crucial for the induction of focal adhesion disassembly; this dephosphorylation could be catalyzed by PTPN11 and regulated by ZFYVE21. Phosphorylation on tyrosine residues is enhanced by NTN1 (By similarity)." ], [ "Q05397-1", "protein_xref_pubmed", "17395594", "ECO_0000269", "Phosphorylated on tyrosine residues upon activation, e.g. upon integrin signaling. Tyr-397 is the major autophosphorylation site, but other kinases can also phosphorylate this residue. Phosphorylation at Tyr-397 promotes interaction with SRC and SRC family members, leading to phosphorylation at Tyr-576, Tyr-577 and at additional tyrosine residues. FGR promotes phosphorylation at Tyr-397 and Tyr-576. FER promotes phosphorylation at Tyr-577, Tyr-861 and Tyr-925, even when cells are not adherent. Tyr-397, Tyr-576 and Ser-722 are phosphorylated only when cells are adherent. Phosphorylation at Tyr-397 is important for interaction with BMX, PIK3R1 and SHC1. Phosphorylation at Tyr-925 is important for interaction with GRB2. Dephosphorylated by PTPN11; PTPN11 is recruited to PTK2 via EPHA2 (tyrosine phosphorylated). Microtubule-induced dephosphorylation at Tyr-397 is crucial for the induction of focal adhesion disassembly; this dephosphorylation could be catalyzed by PTPN11 and regulated by ZFYVE21. Phosphorylation on tyrosine residues is enhanced by NTN1 (By similarity)." ], [ "Q6P1M3-1", "protein_xref_uniprotkb", "Q6P1M3", "ECO_0000269", "Phosphorylated at Ser-653 by PRKCI. Phosphorylation is enhanced during cell polarization induced by calcium. Phosphorylation may occur during the cell-cell contact-induced cell polarization and may contribute to the segregation of LLGL2 from the PRKCI/aPKC and PARD6B/Par-6 complex." ], [ "Q6P1M3-1", "protein_xref_pubmed", "12725730", "ECO_0000269", "Phosphorylated at Ser-653 by PRKCI. Phosphorylation is enhanced during cell polarization induced by calcium. Phosphorylation may occur during the cell-cell contact-induced cell polarization and may contribute to the segregation of LLGL2 from the PRKCI/aPKC and PARD6B/Par-6 complex." ], [ "O43597-1", "protein_xref_uniprotkb", "O43597", "ECO_0000269", "Cleaved at Pro-144 by the prolyl endopeptidase FAP (seprase) activity (in vitro)." ], [ "O43597-1", "protein_xref_pubmed", "21288888", "ECO_0000269", "Cleaved at Pro-144 by the prolyl endopeptidase FAP (seprase) activity (in vitro)." ], [ "P33778-1", "protein_xref_uniprotkb", "P33778", "ECO_0000269", "Lactylated in macrophages by EP300/P300 by using lactoyl-CoA directly derived from endogenous or exogenous lactate, leading to stimulates gene transcription." ], [ "P33778-1", "protein_xref_pubmed", "31645732", "ECO_0000269", "Lactylated in macrophages by EP300/P300 by using lactoyl-CoA directly derived from endogenous or exogenous lactate, leading to stimulates gene transcription." ], [ "P33778-1", "protein_xref_uniprotkb", "P33778", "ECO_0000250", "GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121. It fluctuates in response to extracellular glucose, and associates with transcribed genes (By similarity)." ], [ "P33778-1", "protein_xref_pubmed", "P62807", "ECO_0000250", "GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121. It fluctuates in response to extracellular glucose, and associates with transcribed genes (By similarity)." ], [ "P33778-1", "protein_xref_uniprotkb", "P33778", "ECO_0000269", "Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes." ], [ "P33778-1", "protein_xref_pubmed", "21925322", "ECO_0000269", "Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes." ], [ "P33778-1", "protein_xref_uniprotkb", "P33778", "ECO_0000250", "Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription (By similarity). Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation. Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination." ], [ "P33778-1", "protein_xref_pubmed", "Q64475", "ECO_0000250", "Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription (By similarity). Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation. Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination." ], [ "P33778-1", "protein_xref_uniprotkb", "P33778", "ECO_0000269", "Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription (By similarity). Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation. Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination." ], [ "P33778-1", "protein_xref_pubmed", "12757711", "ECO_0000269", "Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription (By similarity). Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation. Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination." ], [ "P33778-1", "protein_xref_pubmed", "11709551", "ECO_0000269", "Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription (By similarity). Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation. Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination." ], [ "P33778-1", "protein_xref_uniprotkb", "P33778", "ECO_0000269", "Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. It also functions cooperatively with the FACT dimer to stimulate elongation by RNA polymerase II. H2BK120Ub also acts as a regulator of mRNA splicing: deubiquitination by USP49 is required for efficient cotranscriptional splicing of a large set of exons." ], [ "P33778-1", "protein_xref_pubmed", "11709551", "ECO_0000269", "Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. It also functions cooperatively with the FACT dimer to stimulate elongation by RNA polymerase II. H2BK120Ub also acts as a regulator of mRNA splicing: deubiquitination by USP49 is required for efficient cotranscriptional splicing of a large set of exons." ], [ "P01042-1", "protein_xref_uniprotkb", "P01042", "ECO_0000269", "Phosphorylated by FAM20C in the extracellular medium." ], [ "P01042-1", "protein_xref_pubmed", "26091039", "ECO_0000269", "Phosphorylated by FAM20C in the extracellular medium." ], [ "P01042-1", "protein_xref_uniprotkb", "P01042", "ECO_0000269", "Hydroxylation of Pro-383 occurs prior to the release of bradykinin." ], [ "P01042-1", "protein_xref_pubmed", "3366244", "ECO_0000269", "Hydroxylation of Pro-383 occurs prior to the release of bradykinin." ], [ "P01042-1", "protein_xref_pubmed", "3182782", "ECO_0000269", "Hydroxylation of Pro-383 occurs prior to the release of bradykinin." ], [ "P01042-1", "protein_xref_uniprotkb", "P01042", "ECO_0000269", "N- and O-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans." ], [ "P01042-1", "protein_xref_pubmed", "19159218", "ECO_0000269", "N- and O-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans." ], [ "P01042-1", "protein_xref_pubmed", "3484703", "ECO_0000269", "N- and O-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans." ], [ "P01042-1", "protein_xref_pubmed", "12754519", "ECO_0000269", "N- and O-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans." ], [ "P01042-1", "protein_xref_pubmed", "16335952", "ECO_0000269", "N- and O-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans." ], [ "P01042-1", "protein_xref_pubmed", "19838169", "ECO_0000269", "N- and O-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans." ], [ "P01042-1", "protein_xref_pubmed", "14760718", "ECO_0000269", "N- and O-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans." ], [ "P01042-1", "protein_xref_pubmed", "19139490", "ECO_0000269", "N- and O-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans." ], [ "P09693-1", "protein_xref_uniprotkb", "P09693", "ECO_0000250", "Phosphorylated on Tyr residues after T-cell receptor triggering by LCK in association with CD4/CD8." ], [ "P09693-1", "protein_xref_pubmed", "P04234", "ECO_0000250", "Phosphorylated on Tyr residues after T-cell receptor triggering by LCK in association with CD4/CD8." ], [ "P09693-1", "protein_xref_uniprotkb", "P09693", "ECO_0000269", "Phosphorylated on Tyr residues after T-cell receptor triggering by LCK in association with CD4/CD8 (PubMed:2470098). Phosphorylated also by PKC; leading to the TCR complex down-regulation (PubMed:8187769)." ], [ "P09693-1", "protein_xref_pubmed", "2470098", "ECO_0000269", "Phosphorylated on Tyr residues after T-cell receptor triggering by LCK in association with CD4/CD8 (PubMed:2470098). Phosphorylated also by PKC; leading to the TCR complex down-regulation (PubMed:8187769)." ], [ "P09693-1", "protein_xref_pubmed", "8187769", "ECO_0000269", "Phosphorylated on Tyr residues after T-cell receptor triggering by LCK in association with CD4/CD8 (PubMed:2470098). Phosphorylated also by PKC; leading to the TCR complex down-regulation (PubMed:8187769)." ], [ "Q6ZWK4-1", "protein_xref_uniprotkb", "Q6ZWK4", "ECO_0000269", "Phosphorylated. Phosphorylation on Tyr-132 and Tyr-141 occurs in a erythropoietin (EPO)-dependent manner (PubMed:25092874)." ], [ "Q6ZWK4-1", "protein_xref_pubmed", "25092874", "ECO_0000269", "Phosphorylated. Phosphorylation on Tyr-132 and Tyr-141 occurs in a erythropoietin (EPO)-dependent manner (PubMed:25092874)." ] ] }, "readme": "Name\n - Human Protein PTM Annotation (UniProtKB)\n\nVersion\n - 1.11.2\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], 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 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//ln2releases/data/v-1.11.2/reviewed/human_protein_ntdata.nt\n Name: human_protein_masterlist.csv\n URI: https://data.glygen.org//ln2releases/data/v-1.11.2/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", "downloadurl": "/ln2data/releases/data/v-1.12.1/reviewed/human_protein_ptm_annotation_uniprotkb.csv" }