{
    "bcoid": "GLY_000472",
    "title": "SARS-CoV2 Protein PTM Annotation (UniProtKB)",
    "description": "The SARS coronavirus (SARS-CoV-2 or 2019-nCoV) Protein PTM Annotation (UniProtKB) dataset contains sarscov2 ...",
    "filename": "sarscov2_protein_ptm_annotation_uniprotkb.csv",
    "filetype": "csv",
    "categories": {
        "species": [
            "SARS coronavirus (SARS-CoV-2 or 2019-nCoV)"
        ],
        "molecule": [
            "Protein"
        ],
        "tags": [
            "PTM annotation"
        ],
        "file_type": [
            "csv"
        ],
        "status": [
            "Reviewed"
        ],
        "scope": [
            "internal"
        ]
    },
    "minitable": {
        "content": [
            [
                "P0DTC7-1...",
                "protein_xref..."
            ],
            [
                "P0DTC7-1...",
                "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"
                }
            ],
            [
                "P0DTC7-1",
                "protein_xref_uniprotkb",
                "P0DTC7",
                "ECO_0000269",
                "Poly-ubiquitinated by host with K63-linked polyubiquitin chains."
            ],
            [
                "P0DTC7-1",
                "protein_xref_pubmed",
                "33473190",
                "ECO_0000269",
                "Poly-ubiquitinated by host with K63-linked polyubiquitin chains."
            ],
            [
                "P0DTC5-1",
                "protein_xref_uniprotkb",
                "P0DTC5",
                "ECO_0000250",
                "Glycosylated at N-terminus."
            ],
            [
                "P0DTC5-1",
                "protein_xref_pubmed",
                "P59596",
                "ECO_0000250",
                "Glycosylated at N-terminus."
            ],
            [
                "P0DTC3-1",
                "protein_xref_uniprotkb",
                "P0DTC3",
                "ECO_0000250",
                "Exists in both O-glycosylated and non-glycosylated forms. The glycosylated form is associated with the virion."
            ],
            [
                "P0DTC3-1",
                "protein_xref_pubmed",
                "P59632",
                "ECO_0000250",
                "Exists in both O-glycosylated and non-glycosylated forms. The glycosylated form is associated with the virion."
            ],
            [
                "P0DTC2-1",
                "protein_xref_uniprotkb",
                "P0DTC2",
                "ECO_0000269",
                "The cytoplasmic Cys-rich domain is palmitoylated. Palmitoylated spike proteins drive the formation of localized ordered cholesterol and sphingo-lipid-rich lipid nanodomains in the early Golgi, where viral budding occurs."
            ],
            [
                "P0DTC2-1",
                "protein_xref_pubmed",
                "34599882",
                "ECO_0000269",
                "The cytoplasmic Cys-rich domain is palmitoylated. Palmitoylated spike proteins drive the formation of localized ordered cholesterol and sphingo-lipid-rich lipid nanodomains in the early Golgi, where viral budding occurs."
            ],
            [
                "P0DTC2-1",
                "protein_xref_uniprotkb",
                "P0DTC2",
                "ECO_0000269",
                "O-glycosylated by host GALNT1 at the end of S1. This could reduce the efficiency of S1/S2 cleavage."
            ],
            [
                "P0DTC2-1",
                "protein_xref_pubmed",
                "34732583",
                "ECO_0000269",
                "O-glycosylated by host GALNT1 at the end of S1. This could reduce the efficiency of S1/S2 cleavage."
            ],
            [
                "P0DTC2-1",
                "protein_xref_uniprotkb",
                "P0DTC2",
                "ECO_0000269",
                "Highly decorated by heterogeneous N-linked glycans protruding from the trimer surface (PubMed:32075877, PubMed:32155444, PubMed:32929138). Highly glycosylated by host both on S1 and S2 subunits, occluding many regions across the surface of the protein (PubMed:32366695, PubMed:32363391, PubMed:32929138). Approximately 40% of the protein surface is shielded from antibody recognition by glycans, with the notable exception of the ACE2 receptor binding domain (PubMed:32929138)."
            ],
            [
                "P0DTC2-1",
                "protein_xref_pubmed",
                "32075877",
                "ECO_0000269",
                "Highly decorated by heterogeneous N-linked glycans protruding from the trimer surface (PubMed:32075877, PubMed:32155444, PubMed:32929138). Highly glycosylated by host both on S1 and S2 subunits, occluding many regions across the surface of the protein (PubMed:32366695, PubMed:32363391, PubMed:32929138). Approximately 40% of the protein surface is shielded from antibody recognition by glycans, with the notable exception of the ACE2 receptor binding domain (PubMed:32929138)."
            ],
            [
                "P0DTC2-1",
                "protein_xref_pubmed",
                "32929138",
                "ECO_0000269",
                "Highly decorated by heterogeneous N-linked glycans protruding from the trimer surface (PubMed:32075877, PubMed:32155444, PubMed:32929138). Highly glycosylated by host both on S1 and S2 subunits, occluding many regions across the surface of the protein (PubMed:32366695, PubMed:32363391, PubMed:32929138). Approximately 40% of the protein surface is shielded from antibody recognition by glycans, with the notable exception of the ACE2 receptor binding domain (PubMed:32929138)."
            ],
            [
                "P0DTC2-1",
                "protein_xref_pubmed",
                "32363391",
                "ECO_0000269",
                "Highly decorated by heterogeneous N-linked glycans protruding from the trimer surface (PubMed:32075877, PubMed:32155444, PubMed:32929138). Highly glycosylated by host both on S1 and S2 subunits, occluding many regions across the surface of the protein (PubMed:32366695, PubMed:32363391, PubMed:32929138). Approximately 40% of the protein surface is shielded from antibody recognition by glycans, with the notable exception of the ACE2 receptor binding domain (PubMed:32929138)."
            ],
            [
                "P0DTC2-1",
                "protein_xref_pubmed",
                "32155444",
                "ECO_0000269",
                "Highly decorated by heterogeneous N-linked glycans protruding from the trimer surface (PubMed:32075877, PubMed:32155444, PubMed:32929138). Highly glycosylated by host both on S1 and S2 subunits, occluding many regions across the surface of the protein (PubMed:32366695, PubMed:32363391, PubMed:32929138). Approximately 40% of the protein surface is shielded from antibody recognition by glycans, with the notable exception of the ACE2 receptor binding domain (PubMed:32929138)."
            ],
            [
                "P0DTC2-1",
                "protein_xref_pubmed",
                "32366695",
                "ECO_0000269",
                "Highly decorated by heterogeneous N-linked glycans protruding from the trimer surface (PubMed:32075877, PubMed:32155444, PubMed:32929138). Highly glycosylated by host both on S1 and S2 subunits, occluding many regions across the surface of the protein (PubMed:32366695, PubMed:32363391, PubMed:32929138). Approximately 40% of the protein surface is shielded from antibody recognition by glycans, with the notable exception of the ACE2 receptor binding domain (PubMed:32929138)."
            ],
            [
                "P0DTC2-1",
                "protein_xref_uniprotkb",
                "P0DTC2",
                "ECO_0000269",
                "Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into S1 and S2 by host furin or unknown proteases to yield the mature S1 and S2 proteins (PubMed:32362314, PubMed:32703818, PubMed:34159616, PubMed:34561887, PubMed:32155444). Processing between S2 and S2' occurs either by host CTSL in endosomes (PubMed:32221306, PubMed:33465165, PubMed:34159616), or by host TMPRSS2 at the cell surface (PubMed:32142651). Both cleavages are necessary for the protein to be fusion competent (PubMed:32703818, PubMed:34159616, PubMed:34561887). Cell surface activation allows the virus to enter the cell despite inhibition of the endosomal pathway by hydroxychloroquine (PubMed:33465165). The polybasic furin cleavage site is absent in SARS-CoV S (PubMed:32155444, PubMed:32362314, PubMed:33465165). It increases the dependence on TMPRSS2 expression by SARS-CoV-2 (PubMed:33465165). D614G substitution would enhance furin cleavage at the S1/S2 junction (PubMed:33417835)."
            ],
            [
                "P0DTC2-1",
                "protein_xref_pubmed",
                "32155444",
                "ECO_0000269",
                "Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into S1 and S2 by host furin or unknown proteases to yield the mature S1 and S2 proteins (PubMed:32362314, PubMed:32703818, PubMed:34159616, PubMed:34561887, PubMed:32155444). Processing between S2 and S2' occurs either by host CTSL in endosomes (PubMed:32221306, PubMed:33465165, PubMed:34159616), or by host TMPRSS2 at the cell surface (PubMed:32142651). Both cleavages are necessary for the protein to be fusion competent (PubMed:32703818, PubMed:34159616, PubMed:34561887). Cell surface activation allows the virus to enter the cell despite inhibition of the endosomal pathway by hydroxychloroquine (PubMed:33465165). The polybasic furin cleavage site is absent in SARS-CoV S (PubMed:32155444, PubMed:32362314, PubMed:33465165). It increases the dependence on TMPRSS2 expression by SARS-CoV-2 (PubMed:33465165). D614G substitution would enhance furin cleavage at the S1/S2 junction (PubMed:33417835)."
            ],
            [
                "P0DTC2-1",
                "protein_xref_uniprotkb",
                "P0DTC2",
                "ECO_0000255",
                "Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into S1 and S2 by host furin or unknown proteases to yield the mature S1 and S2 proteins (PubMed:32362314, PubMed:32703818, PubMed:34159616, PubMed:34561887, PubMed:32155444). Processing between S2 and S2' occurs either by host CTSL in endosomes (PubMed:32221306, PubMed:33465165, PubMed:34159616), or by host TMPRSS2 at the cell surface (PubMed:32142651). Both cleavages are necessary for the protein to be fusion competent (PubMed:32703818, PubMed:34159616, PubMed:34561887). Cell surface activation allows the virus to enter the cell despite inhibition of the endosomal pathway by hydroxychloroquine (PubMed:33465165). The polybasic furin cleavage site is absent in SARS-CoV S (PubMed:32155444, PubMed:32362314, PubMed:33465165). It increases the dependence on TMPRSS2 expression by SARS-CoV-2 (PubMed:33465165). D614G substitution would enhance furin cleavage at the S1/S2 junction (PubMed:33417835)."
            ],
            [
                "P0DTC2-1",
                "protein_xref_pubmed",
                "MF_04099",
                "ECO_0000255",
                "Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into S1 and S2 by host furin or unknown proteases to yield the mature S1 and S2 proteins (PubMed:32362314, PubMed:32703818, PubMed:34159616, PubMed:34561887, PubMed:32155444). Processing between S2 and S2' occurs either by host CTSL in endosomes (PubMed:32221306, PubMed:33465165, PubMed:34159616), or by host TMPRSS2 at the cell surface (PubMed:32142651). Both cleavages are necessary for the protein to be fusion competent (PubMed:32703818, PubMed:34159616, PubMed:34561887). Cell surface activation allows the virus to enter the cell despite inhibition of the endosomal pathway by hydroxychloroquine (PubMed:33465165). The polybasic furin cleavage site is absent in SARS-CoV S (PubMed:32155444, PubMed:32362314, PubMed:33465165). It increases the dependence on TMPRSS2 expression by SARS-CoV-2 (PubMed:33465165). D614G substitution would enhance furin cleavage at the S1/S2 junction (PubMed:33417835)."
            ],
            [
                "P0DTC2-1",
                "protein_xref_pubmed",
                "32142651",
                "ECO_0000269",
                "Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into S1 and S2 by host furin or unknown proteases to yield the mature S1 and S2 proteins (PubMed:32362314, PubMed:32703818, PubMed:34159616, PubMed:34561887, PubMed:32155444). Processing between S2 and S2' occurs either by host CTSL in endosomes (PubMed:32221306, PubMed:33465165, PubMed:34159616), or by host TMPRSS2 at the cell surface (PubMed:32142651). Both cleavages are necessary for the protein to be fusion competent (PubMed:32703818, PubMed:34159616, PubMed:34561887). Cell surface activation allows the virus to enter the cell despite inhibition of the endosomal pathway by hydroxychloroquine (PubMed:33465165). The polybasic furin cleavage site is absent in SARS-CoV S (PubMed:32155444, PubMed:32362314, PubMed:33465165). It increases the dependence on TMPRSS2 expression by SARS-CoV-2 (PubMed:33465165). D614G substitution would enhance furin cleavage at the S1/S2 junction (PubMed:33417835)."
            ],
            [
                "P0DTC2-1",
                "protein_xref_uniprotkb",
                "P0DTC2",
                "ECO_0000305",
                "Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into S1 and S2 by host furin or unknown proteases to yield the mature S1 and S2 proteins (PubMed:32362314, PubMed:32703818, PubMed:34159616, PubMed:34561887, PubMed:32155444). Processing between S2 and S2' occurs either by host CTSL in endosomes (PubMed:32221306, PubMed:33465165, PubMed:34159616), or by host TMPRSS2 at the cell surface (PubMed:32142651). Both cleavages are necessary for the protein to be fusion competent (PubMed:32703818, PubMed:34159616, PubMed:34561887). Cell surface activation allows the virus to enter the cell despite inhibition of the endosomal pathway by hydroxychloroquine (PubMed:33465165). The polybasic furin cleavage site is absent in SARS-CoV S (PubMed:32155444, PubMed:32362314, PubMed:33465165). It increases the dependence on TMPRSS2 expression by SARS-CoV-2 (PubMed:33465165). D614G substitution would enhance furin cleavage at the S1/S2 junction (PubMed:33417835)."
            ],
            [
                "P0DTC2-1",
                "protein_xref_pubmed",
                "34561887",
                "ECO_0000305",
                "Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into S1 and S2 by host furin or unknown proteases to yield the mature S1 and S2 proteins (PubMed:32362314, PubMed:32703818, PubMed:34159616, PubMed:34561887, PubMed:32155444). Processing between S2 and S2' occurs either by host CTSL in endosomes (PubMed:32221306, PubMed:33465165, PubMed:34159616), or by host TMPRSS2 at the cell surface (PubMed:32142651). Both cleavages are necessary for the protein to be fusion competent (PubMed:32703818, PubMed:34159616, PubMed:34561887). Cell surface activation allows the virus to enter the cell despite inhibition of the endosomal pathway by hydroxychloroquine (PubMed:33465165). The polybasic furin cleavage site is absent in SARS-CoV S (PubMed:32155444, PubMed:32362314, PubMed:33465165). It increases the dependence on TMPRSS2 expression by SARS-CoV-2 (PubMed:33465165). D614G substitution would enhance furin cleavage at the S1/S2 junction (PubMed:33417835)."
            ],
            [
                "P0DTC2-1",
                "protein_xref_pubmed",
                "32362314",
                "ECO_0000269",
                "Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into S1 and S2 by host furin or unknown proteases to yield the mature S1 and S2 proteins (PubMed:32362314, PubMed:32703818, PubMed:34159616, PubMed:34561887, PubMed:32155444). Processing between S2 and S2' occurs either by host CTSL in endosomes (PubMed:32221306, PubMed:33465165, PubMed:34159616), or by host TMPRSS2 at the cell surface (PubMed:32142651). Both cleavages are necessary for the protein to be fusion competent (PubMed:32703818, PubMed:34159616, PubMed:34561887). Cell surface activation allows the virus to enter the cell despite inhibition of the endosomal pathway by hydroxychloroquine (PubMed:33465165). The polybasic furin cleavage site is absent in SARS-CoV S (PubMed:32155444, PubMed:32362314, PubMed:33465165). It increases the dependence on TMPRSS2 expression by SARS-CoV-2 (PubMed:33465165). D614G substitution would enhance furin cleavage at the S1/S2 junction (PubMed:33417835)."
            ],
            [
                "P0DTC2-1",
                "protein_xref_pubmed",
                "33465165",
                "ECO_0000269",
                "Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into S1 and S2 by host furin or unknown proteases to yield the mature S1 and S2 proteins (PubMed:32362314, PubMed:32703818, PubMed:34159616, PubMed:34561887, PubMed:32155444). Processing between S2 and S2' occurs either by host CTSL in endosomes (PubMed:32221306, PubMed:33465165, PubMed:34159616), or by host TMPRSS2 at the cell surface (PubMed:32142651). Both cleavages are necessary for the protein to be fusion competent (PubMed:32703818, PubMed:34159616, PubMed:34561887). Cell surface activation allows the virus to enter the cell despite inhibition of the endosomal pathway by hydroxychloroquine (PubMed:33465165). The polybasic furin cleavage site is absent in SARS-CoV S (PubMed:32155444, PubMed:32362314, PubMed:33465165). It increases the dependence on TMPRSS2 expression by SARS-CoV-2 (PubMed:33465165). D614G substitution would enhance furin cleavage at the S1/S2 junction (PubMed:33417835)."
            ],
            [
                "P0DTC2-1",
                "protein_xref_pubmed",
                "33417835",
                "ECO_0000269",
                "Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into S1 and S2 by host furin or unknown proteases to yield the mature S1 and S2 proteins (PubMed:32362314, PubMed:32703818, PubMed:34159616, PubMed:34561887, PubMed:32155444). Processing between S2 and S2' occurs either by host CTSL in endosomes (PubMed:32221306, PubMed:33465165, PubMed:34159616), or by host TMPRSS2 at the cell surface (PubMed:32142651). Both cleavages are necessary for the protein to be fusion competent (PubMed:32703818, PubMed:34159616, PubMed:34561887). Cell surface activation allows the virus to enter the cell despite inhibition of the endosomal pathway by hydroxychloroquine (PubMed:33465165). The polybasic furin cleavage site is absent in SARS-CoV S (PubMed:32155444, PubMed:32362314, PubMed:33465165). It increases the dependence on TMPRSS2 expression by SARS-CoV-2 (PubMed:33465165). D614G substitution would enhance furin cleavage at the S1/S2 junction (PubMed:33417835)."
            ],
            [
                "P0DTC2-1",
                "protein_xref_pubmed",
                "34159616",
                "ECO_0000269",
                "Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into S1 and S2 by host furin or unknown proteases to yield the mature S1 and S2 proteins (PubMed:32362314, PubMed:32703818, PubMed:34159616, PubMed:34561887, PubMed:32155444). Processing between S2 and S2' occurs either by host CTSL in endosomes (PubMed:32221306, PubMed:33465165, PubMed:34159616), or by host TMPRSS2 at the cell surface (PubMed:32142651). Both cleavages are necessary for the protein to be fusion competent (PubMed:32703818, PubMed:34159616, PubMed:34561887). Cell surface activation allows the virus to enter the cell despite inhibition of the endosomal pathway by hydroxychloroquine (PubMed:33465165). The polybasic furin cleavage site is absent in SARS-CoV S (PubMed:32155444, PubMed:32362314, PubMed:33465165). It increases the dependence on TMPRSS2 expression by SARS-CoV-2 (PubMed:33465165). D614G substitution would enhance furin cleavage at the S1/S2 junction (PubMed:33417835)."
            ],
            [
                "P0DTC2-1",
                "protein_xref_pubmed",
                "32221306",
                "ECO_0000269",
                "Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into S1 and S2 by host furin or unknown proteases to yield the mature S1 and S2 proteins (PubMed:32362314, PubMed:32703818, PubMed:34159616, PubMed:34561887, PubMed:32155444). Processing between S2 and S2' occurs either by host CTSL in endosomes (PubMed:32221306, PubMed:33465165, PubMed:34159616), or by host TMPRSS2 at the cell surface (PubMed:32142651). Both cleavages are necessary for the protein to be fusion competent (PubMed:32703818, PubMed:34159616, PubMed:34561887). Cell surface activation allows the virus to enter the cell despite inhibition of the endosomal pathway by hydroxychloroquine (PubMed:33465165). The polybasic furin cleavage site is absent in SARS-CoV S (PubMed:32155444, PubMed:32362314, PubMed:33465165). It increases the dependence on TMPRSS2 expression by SARS-CoV-2 (PubMed:33465165). D614G substitution would enhance furin cleavage at the S1/S2 junction (PubMed:33417835)."
            ],
            [
                "P0DTC2-1",
                "protein_xref_pubmed",
                "32703818",
                "ECO_0000269",
                "Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into S1 and S2 by host furin or unknown proteases to yield the mature S1 and S2 proteins (PubMed:32362314, PubMed:32703818, PubMed:34159616, PubMed:34561887, PubMed:32155444). Processing between S2 and S2' occurs either by host CTSL in endosomes (PubMed:32221306, PubMed:33465165, PubMed:34159616), or by host TMPRSS2 at the cell surface (PubMed:32142651). Both cleavages are necessary for the protein to be fusion competent (PubMed:32703818, PubMed:34159616, PubMed:34561887). Cell surface activation allows the virus to enter the cell despite inhibition of the endosomal pathway by hydroxychloroquine (PubMed:33465165). The polybasic furin cleavage site is absent in SARS-CoV S (PubMed:32155444, PubMed:32362314, PubMed:33465165). It increases the dependence on TMPRSS2 expression by SARS-CoV-2 (PubMed:33465165). D614G substitution would enhance furin cleavage at the S1/S2 junction (PubMed:33417835)."
            ],
            [
                "P0DTC1-1",
                "protein_xref_uniprotkb",
                "P0DTC1",
                "ECO_0000250",
                "Specific enzymatic cleavages in vivo by its own proteases yield mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically processed."
            ],
            [
                "P0DTC1-1",
                "protein_xref_pubmed",
                "P0C6X7",
                "ECO_0000250",
                "Specific enzymatic cleavages in vivo by its own proteases yield mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically processed."
            ],
            [
                "P0DTC9-1",
                "protein_xref_uniprotkb",
                "P0DTC9",
                "ECO_0000255",
                "ADP-ribosylated. The ADP-ribosylation is retained in the virion during infection."
            ],
            [
                "P0DTC9-1",
                "protein_xref_pubmed",
                "MF_04096",
                "ECO_0000255",
                "ADP-ribosylated. The ADP-ribosylation is retained in the virion during infection."
            ],
            [
                "P0DTC9-1",
                "protein_xref_uniprotkb",
                "P0DTC9",
                "ECO_0000269",
                "Phosphorylated on serine residues by host GSK3A and GSK3B (PubMed:34593624, PubMed:35728038). This promotes the solubility of homodimers that would otherwise aggregate (PubMed:32974389). Host phosphatase would dephosphorylate the protein during assembly at M bound membranes (PubMed:32974389)."
            ],
            [
                "P0DTC9-1",
                "protein_xref_pubmed",
                "34593624",
                "ECO_0000269",
                "Phosphorylated on serine residues by host GSK3A and GSK3B (PubMed:34593624, PubMed:35728038). This promotes the solubility of homodimers that would otherwise aggregate (PubMed:32974389). Host phosphatase would dephosphorylate the protein during assembly at M bound membranes (PubMed:32974389)."
            ],
            [
                "P0DTC9-1",
                "protein_xref_pubmed",
                "35728038",
                "ECO_0000269",
                "Phosphorylated on serine residues by host GSK3A and GSK3B (PubMed:34593624, PubMed:35728038). This promotes the solubility of homodimers that would otherwise aggregate (PubMed:32974389). Host phosphatase would dephosphorylate the protein during assembly at M bound membranes (PubMed:32974389)."
            ],
            [
                "P0DTC9-1",
                "protein_xref_uniprotkb",
                "P0DTC9",
                "ECO_0000305",
                "Phosphorylated on serine residues by host GSK3A and GSK3B (PubMed:34593624, PubMed:35728038). This promotes the solubility of homodimers that would otherwise aggregate (PubMed:32974389). Host phosphatase would dephosphorylate the protein during assembly at M bound membranes (PubMed:32974389)."
            ],
            [
                "P0DTC9-1",
                "protein_xref_pubmed",
                "32974389",
                "ECO_0000305",
                "Phosphorylated on serine residues by host GSK3A and GSK3B (PubMed:34593624, PubMed:35728038). This promotes the solubility of homodimers that would otherwise aggregate (PubMed:32974389). Host phosphatase would dephosphorylate the protein during assembly at M bound membranes (PubMed:32974389)."
            ],
            [
                "P0DTC9-1",
                "protein_xref_uniprotkb",
                "P0DTC9",
                "ECO_0000269",
                "Proteolytically cleaved by host CASP6. The cleavage leads to two fragments and facilitates viral replication by inhibiting host IFN signaling. The two fragments may interact with IRF3 inhibiting its nuclear translocation after activation and reduce the expression of IFNB and IFN-stimulated genes."
            ],
            [
                "P0DTC9-1",
                "protein_xref_pubmed",
                "35922005",
                "ECO_0000269",
                "Proteolytically cleaved by host CASP6. The cleavage leads to two fragments and facilitates viral replication by inhibiting host IFN signaling. The two fragments may interact with IRF3 inhibiting its nuclear translocation after activation and reduce the expression of IFNB and IFN-stimulated genes."
            ],
            [
                "P0DTC8-1",
                "protein_xref_uniprotkb",
                "P0DTC8",
                "ECO_0000269",
                "Glycosylated by the host when secreted via the conventional pathway. The glycosylated form cannot bind IL17A and would not participate in the cytokine storm."
            ],
            [
                "P0DTC8-1",
                "protein_xref_pubmed",
                "36689483",
                "ECO_0000269",
                "Glycosylated by the host when secreted via the conventional pathway. The glycosylated form cannot bind IL17A and would not participate in the cytokine storm."
            ],
            [
                "P0DTD1-1",
                "protein_xref_uniprotkb",
                "P0DTD1",
                "ECO_0000250",
                "Specific enzymatic cleavages in vivo by its own proteases yield mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically processed."
            ],
            [
                "P0DTD1-1",
                "protein_xref_pubmed",
                "P0C6X7",
                "ECO_0000250",
                "Specific enzymatic cleavages in vivo by its own proteases yield mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically processed."
            ]
        ]
    },
    "readme": "Name\n   - SARS-CoV2 Protein PTM Annotation (UniProtKB)\n\nVersion\n   - v-2.1.1\n\nCreated on\n  - 2020-04-19T11:44:49.318101\n\nModified on\n   - 2022-09-26T09:05:56.474034\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]\n\nAuthors\n   - Maria Martin [martin@ebi.ac.uk], Preethi Vasudev [pvasudev@ebi.ac.uk]\n\nChecksum\n   - \n\nUsability Domain\n   - The SARS coronavirus (SARS-CoV-2 or 2019-nCoV) Protein PTM Annotation (UniProtKB) dataset contains sarscov2 [taxid:2697049] PTM annotations for UniProtKB canonical accessions. The annotation is the curated statements of mainly about glycosylation and phosphorylation. The dataset is derived form 2020-01 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 sequences and 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-sars-cov-2.nt\n      URI: /data/shared/glyds/downloads/ebi/2023_02/uniprot-proteome-sars-cov-2.nt\n   Output Subdomain\n      Name: sarscov2_protein_ptm_annotation_uniprotkb.csv\n      URI: https:/data.glygen.org/ln2releases/data/v-2.1.1/reviewed/sarscov2_protein_ptm_annotation_uniprotkb.csv\n      Name: sarscov2_protein_ptm_annotation_uniprotkb.stat.csv\n      URI: https:/data.glygen.org/ln2releases/data/v-2.1.1/reviewed/sarscov2_protein_ptm_annotation_uniprotkb.stat.csv\n\nFields\n      Name: \"uniprotkb_canonical_ac\"\n     Description: \"\"\n      Unique Values: \"8\"\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: \"34\"\n      Name: \"eco_id\"\n     Description: \"Evidence & Conclusion Ontology (ECO) identifier\"\n      Unique Values: \"4\"\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: \"12\"",
    "downloadurl": "/ln2data/releases/data/v-2.1.1/reviewed/sarscov2_protein_ptm_annotation_uniprotkb.csv"
}