{
    "bcoid": "GLY_000422",
    "title": "SARS-CoV2 Protein Function (UniProtKB)",
    "description": "The SARS coronavirus (SARS-CoV-2 or 2019-nCov) Protein Function (UniProtKB) dataset contains biological ...",
    "filename": "sarscov2_protein_function_uniprotkb.csv",
    "filetype": "csv",
    "categories": {
        "species": "SARS coronavirus (SARS-CoV-2 or 2019-nCoV)",
        "molecule": "Protein",
        "tags": "Protein Function",
        "file_type": "csv",
        "status": "Reviewed",
        "scope": "internal"
    },
    "minitable": {
        "content": [
            [
                "P0DTD2-1...",
                "protein_xref..."
            ],
            [
                "P0DTC6-1...",
                "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": "evidence"
                },
                {
                    "type": "string",
                    "label": "annotation"
                }
            ],
            [
                "P0DTD2-1",
                "protein_xref_uniprotkb_fun",
                "P0DTD2",
                "",
                "Plays a role in the inhibition of host innate immune response by targeting the mitochondrial-associated adapter MAVS. Mechanistically, usurps the E3 ligase ITCH to trigger the degradation of MAVS, TRAF3, and TRAF6. In addition, causes mitochondrial elongation by triggering ubiquitination and proteasomal degradation of dynamin-like protein 1/DNM1L."
            ],
            [
                "P0DTC6-1",
                "protein_xref_uniprotkb_fun",
                "P0DTC6",
                "",
                "Disrupts cell nuclear import complex formation by tethering karyopherin alpha 2 and karyopherin beta 1 to the membrane. Retention of import factors at the ER/Golgi membrane leads to a loss of transport into the nucleus. Thereby prevents STAT1 nuclear translocation in response to interferon signaling, thus blocking the expression of interferon stimulated genes (ISGs) that display multiple antiviral activities."
            ],
            [
                "P0DTC9-1",
                "protein_xref_uniprotkb_fun",
                "P0DTC9",
                "",
                "Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication (By similarity). May modulate transforming growth factor-beta signaling by binding host smad3 (By similarity)."
            ],
            [
                "P0DTC7-1",
                "protein_xref_uniprotkb_fun",
                "P0DTC7",
                "",
                "Plays a role as antagonist of host tetherin (BST2), disrupting its antiviral effect. Acts by binding to BST2 thereby interfering with its glycosylation. May suppress small interfering RNA (siRNA). May bind to host ITGAL, thereby playing a role in attachment or modulation of leukocytes."
            ],
            [
                "P0DTD3-1",
                "protein_xref_uniprotkb_fun",
                "P0DTD3",
                "",
                "May play a role in host-virus interaction."
            ],
            [
                "P0DTC5-1",
                "protein_xref_uniprotkb_fun",
                "P0DTC5",
                "",
                "Component of the viral envelope that plays a central role in virus morphogenesis and assembly via its interactions with other viral proteins."
            ],
            [
                "P0DTC4-1",
                "protein_xref_uniprotkb_fun",
                "P0DTC4",
                "",
                "Plays a central role in virus morphogenesis and assembly. Acts as a viroporin and self-assembles in host membranes forming pentameric protein-lipid pores that allow ion transport. Also plays a role in the induction of apoptosis."
            ],
            [
                "P0DTC3-1",
                "protein_xref_uniprotkb_fun",
                "P0DTC3",
                "",
                "Forms homotetrameric potassium sensitive ion channels (viroporin) and may modulate virus release. Up-regulates expression of fibrinogen subunits FGA, FGB and FGG in host lung epithelial cells. Induces apoptosis in cell culture. Downregulates the type 1 interferon receptor by inducing serine phosphorylation within the IFN alpha-receptor subunit 1 (IFNAR1) degradation motif and increasing IFNAR1 ubiquitination."
            ],
            [
                "P0DTC2-1",
                "protein_xref_uniprotkb_fun",
                "P0DTC2",
                "",
                "Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis."
            ],
            [
                "P0DTC2-1",
                "protein_xref_uniprotkb_fun",
                "P0DTC2",
                "",
                "mediates fusion of the virion and cellular membranes by acting as a class I viral fusion protein. Under the current model, the protein has at least three conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes."
            ],
            [
                "P0DTC2-1",
                "protein_xref_uniprotkb_fun",
                "P0DTC2",
                "",
                "May down-regulate host tetherin (BST2) by lysosomal degradation, thereby counteracting its antiviral activity."
            ],
            [
                "P0DTC2-1",
                "protein_xref_uniprotkb_fun",
                "P0DTC2",
                "32075877",
                "attaches the virion to the cell membrane by interacting with host receptor, initiating the infection. Binding to human ACE2 receptor and internalization of the virus into the endosomes of the host cell induces conformational changes in the Spike glycoprotein (PubMed:32142651, PubMed:32075877, PubMed:32155444). Uses also human TMPRSS2 for priming in human lung cells which is an essential step for viral entry (PubMed:32142651). Can be alternatively processed by host furin (PubMed:32362314). Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and activate membranes fusion within endosomes."
            ],
            [
                "P0DTC2-1",
                "protein_xref_uniprotkb_fun",
                "P0DTC2",
                "32142651",
                "attaches the virion to the cell membrane by interacting with host receptor, initiating the infection. Binding to human ACE2 receptor and internalization of the virus into the endosomes of the host cell induces conformational changes in the Spike glycoprotein (PubMed:32142651, PubMed:32075877, PubMed:32155444). Uses also human TMPRSS2 for priming in human lung cells which is an essential step for viral entry (PubMed:32142651). Can be alternatively processed by host furin (PubMed:32362314). Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and activate membranes fusion within endosomes."
            ],
            [
                "P0DTC2-1",
                "protein_xref_uniprotkb_fun",
                "P0DTC2",
                "32155444",
                "attaches the virion to the cell membrane by interacting with host receptor, initiating the infection. Binding to human ACE2 receptor and internalization of the virus into the endosomes of the host cell induces conformational changes in the Spike glycoprotein (PubMed:32142651, PubMed:32075877, PubMed:32155444). Uses also human TMPRSS2 for priming in human lung cells which is an essential step for viral entry (PubMed:32142651). Can be alternatively processed by host furin (PubMed:32362314). Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and activate membranes fusion within endosomes."
            ],
            [
                "P0DTC2-1",
                "protein_xref_uniprotkb_fun",
                "P0DTC2",
                "32362314",
                "attaches the virion to the cell membrane by interacting with host receptor, initiating the infection. Binding to human ACE2 receptor and internalization of the virus into the endosomes of the host cell induces conformational changes in the Spike glycoprotein (PubMed:32142651, PubMed:32075877, PubMed:32155444). Uses also human TMPRSS2 for priming in human lung cells which is an essential step for viral entry (PubMed:32142651). Can be alternatively processed by host furin (PubMed:32362314). Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and activate membranes fusion within endosomes."
            ],
            [
                "P0DTC1-1",
                "protein_xref_uniprotkb_fun",
                "P0DTC1",
                "",
                "May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses."
            ],
            [
                "P0DTC1-1",
                "protein_xref_uniprotkb_fun",
                "P0DTC1",
                "",
                "May participate in viral replication by acting as a ssRNA-binding protein."
            ],
            [
                "P0DTC1-1",
                "protein_xref_uniprotkb_fun",
                "P0DTC1",
                "",
                "Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers."
            ],
            [
                "P0DTC1-1",
                "protein_xref_uniprotkb_fun",
                "P0DTC1",
                "",
                "Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling."
            ],
            [
                "P0DTC1-1",
                "protein_xref_uniprotkb_fun",
                "P0DTC1",
                "",
                "Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication."
            ],
            [
                "P0DTC1-1",
                "protein_xref_uniprotkb_fun",
                "P0DTC1",
                "",
                "Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response."
            ],
            [
                "P0DTC1-1",
                "protein_xref_uniprotkb_fun",
                "P0DTC1",
                "",
                "Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers."
            ],
            [
                "P0DTC1-1",
                "protein_xref_uniprotkb_fun",
                "P0DTC1",
                "",
                "Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein."
            ],
            [
                "P0DTC1-1",
                "protein_xref_uniprotkb_fun",
                "P0DTC1",
                "",
                "Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation."
            ],
            [
                "P0DTC1-1",
                "protein_xref_uniprotkb_fun",
                "P0DTC1",
                "",
                "Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes."
            ],
            [
                "P0DTC1-1",
                "protein_xref_uniprotkb_fun",
                "P0DTC1",
                "32198291",
                "Cleaves the C-terminus of replicase polyprotein at 11 sites (By similarity) (PubMed:32198291, PubMed:32272481). Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''-phosphate (ADRP) (By similarity)."
            ],
            [
                "P0DTC1-1",
                "protein_xref_uniprotkb_fun",
                "P0DTC1",
                "32272481",
                "Cleaves the C-terminus of replicase polyprotein at 11 sites (By similarity) (PubMed:32198291, PubMed:32272481). Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''-phosphate (ADRP) (By similarity)."
            ],
            [
                "P0DTD1-1",
                "protein_xref_uniprotkb_fun",
                "P0DTD1",
                "",
                "May participate in viral replication by acting as a ssRNA-binding protein."
            ],
            [
                "P0DTD1-1",
                "protein_xref_uniprotkb_fun",
                "P0DTD1",
                "",
                "Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein."
            ],
            [
                "P0DTD1-1",
                "protein_xref_uniprotkb_fun",
                "P0DTD1",
                "",
                "May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses."
            ],
            [
                "P0DTD1-1",
                "protein_xref_uniprotkb_fun",
                "P0DTD1",
                "",
                "Mn(2+)-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond."
            ],
            [
                "P0DTD1-1",
                "protein_xref_uniprotkb_fun",
                "P0DTD1",
                "",
                "Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation."
            ],
            [
                "P0DTD1-1",
                "protein_xref_uniprotkb_fun",
                "P0DTD1",
                "",
                "Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes."
            ],
            [
                "P0DTD1-1",
                "protein_xref_uniprotkb_fun",
                "P0DTD1",
                "",
                "Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response."
            ],
            [
                "P0DTD1-1",
                "protein_xref_uniprotkb_fun",
                "P0DTD1",
                "",
                "Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling."
            ],
            [
                "P0DTD1-1",
                "protein_xref_uniprotkb_fun",
                "P0DTD1",
                "",
                "Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium."
            ],
            [
                "P0DTD1-1",
                "protein_xref_uniprotkb_fun",
                "P0DTD1",
                "",
                "Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication."
            ],
            [
                "P0DTD1-1",
                "protein_xref_uniprotkb_fun",
                "P0DTD1",
                "",
                "Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system."
            ],
            [
                "P0DTD1-1",
                "protein_xref_uniprotkb_fun",
                "P0DTD1",
                "",
                "Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. Acts as a proofreading exoribonuclease for RNA replication, thereby lowering The sensitivity of the virus to RNA mutagens."
            ],
            [
                "P0DTD1-1",
                "protein_xref_uniprotkb_fun",
                "P0DTD1",
                "32277040",
                "Plays a role in viral RNA synthesis (PubMed:32358203, PubMed:32277040). Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers (By similarity)."
            ],
            [
                "P0DTD1-1",
                "protein_xref_uniprotkb_fun",
                "P0DTD1",
                "32358203",
                "Plays a role in viral RNA synthesis (PubMed:32358203, PubMed:32277040). Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers (By similarity)."
            ],
            [
                "P0DTD1-1",
                "protein_xref_uniprotkb_fun",
                "P0DTD1",
                "32277040",
                "Plays a role in viral RNA synthesis (PubMed:32358203, PubMed:32277040). Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers (By similarity)."
            ],
            [
                "P0DTD1-1",
                "protein_xref_uniprotkb_fun",
                "P0DTD1",
                "32358203",
                "Plays a role in viral RNA synthesis (PubMed:32358203, PubMed:32277040). Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers (By similarity)."
            ],
            [
                "P0DTD1-1",
                "protein_xref_uniprotkb_fun",
                "P0DTD1",
                "",
                "Responsible for replication and transcription of the viral RNA genome."
            ],
            [
                "P0DTD1-1",
                "protein_xref_uniprotkb_fun",
                "P0DTD1",
                "32198291",
                "Cleaves the C-terminus of replicase polyprotein at 11 sites (PubMed:32321856). Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN] (PubMed:32198291, PubMed:32272481). Also able to bind an ADP-ribose-1''-phosphate (ADRP) (By similarity) (PubMed:32198291, PubMed:32272481)."
            ],
            [
                "P0DTD1-1",
                "protein_xref_uniprotkb_fun",
                "P0DTD1",
                "32272481",
                "Cleaves the C-terminus of replicase polyprotein at 11 sites (PubMed:32321856). Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN] (PubMed:32198291, PubMed:32272481). Also able to bind an ADP-ribose-1''-phosphate (ADRP) (By similarity) (PubMed:32198291, PubMed:32272481)."
            ],
            [
                "P0DTD1-1",
                "protein_xref_uniprotkb_fun",
                "P0DTD1",
                "32321856",
                "Cleaves the C-terminus of replicase polyprotein at 11 sites (PubMed:32321856). Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN] (PubMed:32198291, PubMed:32272481). Also able to bind an ADP-ribose-1''-phosphate (ADRP) (By similarity) (PubMed:32198291, PubMed:32272481)."
            ],
            [
                "P0DTC8-1",
                "protein_xref_uniprotkb_fun",
                "P0DTC8",
                "",
                "May play a role in host-virus interaction."
            ]
        ]
    },
    "readme": "Name\n   - SARS-CoV2 Protein Function (UniProtKB)\n\nVersion\n   - 1.7.10\n\nCreated on\n  - 2020-04-03T11:46:41.584409\n\nModified on\n   - 2020-04-10T12:25:10.311615\n\nCreated by\n   - Jeet Vora [jeetvora@gwu.edu], Rahi Navelkar [rsn13@gwu.edu], Robel Kahsay [rykahsay@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 Function (UniProtKB) dataset contains biological function annotation for sarscov2 [taxid:2697049] protein accesions from the UniProtKB database. The dataset is derived from 2020-01 UniProtKB release. If you use this dataset please provide proper attribution to EMBL-EBI-UniProtKB and GlyGen\n\nDescription Domain\n   Keywords\n   - protein function\n   - UniProtKB\n\n   Pipeline Steps\n   - Step-1: The script loads the UniProtKB function annotations triplestore containing triples from nt file and extracts the data as a csv dataset\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-sars-cov-2.nt\n      URI: https://data.glygen.org/ln2wwwdata/source/uniprot-proteome-sars-cov-2.nt\n      Name: sarscov2_protein_masterlist.csv\n      URI: https://data.glygen.org/ln2wwwdata/reviewed/sarscov2_protein_masterlist.csv\n   Output Subdomain\n      Name: sarscov2_protein_function_uniprotkb.csv\n      URI: http://data.glygen.org/ln2wwwdata/reviewed/sarscov2_protein_function_uniprotkb.csv\n      Name: sarscov2_protein_function_uniprotkb.stat.csv\n      URI: http://data.glygen.org/ln2wwwdata/reviewed/sarscov2_protein_function_uniprotkb.stat.csv\n\nFields\n      Name: \"uniprotkb_canonical_ac\"\n     Description: \"\"\n      Unique Values: \"12\"\n      Name: \"evidence\"\n     Description: \"NCBI PubMed Id (PMID) or DOI (Digital Object Identifier) as evidence for the entry/annotation\"\n      Unique Values: \"10\"\n      Name: \"annotation\"\n     Description: \"Function annotation from UniProtKB|RefSeq database\"\n      Unique Values: \"30\"\n      Name: \"xref_id\"\n     Description: \"ID of the X-ref\"\n      Unique Values: \"12\"\n      Name: \"xref_key\"\n     Description: \"Source key associated to the  xref_id\"\n      Unique Values: \"1\"",
    "downloadurl": "/ln2data/releases/data/v-1.7.10/reviewed/sarscov2_protein_function_uniprotkb.csv"
}
