{ "bcoid": "GLY_000421", "title": "SARS-CoV1 Protein Function (UniProtKB)", "description": "The SARS coronavirus (SARS-CoV-1) Protein Function (UniProtKB) dataset contains biological function annotation ...", "filename": "sarscov1_protein_function_uniprotkb.csv", "filetype": "csv", "categories": { "species": "SARS coronavirus (SARS-CoV-1)", "molecule": "Protein", "tags": "Protein Function", "file_type": "csv", "status": "Reviewed", "scope": "internal" }, "minitable": { "content": [ [ "P59596-1...", "protein_xref..." ], [ "P59594-1...", "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" } ], [ "P59596-1", "protein_xref_uniprotkb_fun", "P59596", "", "Component of the viral envelope that plays a central role in virus morphogenesis and assembly via its interactions with other viral proteins." ], [ "P59594-1", "protein_xref_uniprotkb_fun", "P59594", "", "May down-regulate host tetherin (BST2) by lysosomal degradation, thereby counteracting its antiviral activity." ], [ "P59594-1", "protein_xref_uniprotkb_fun", "P59594", "", "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." ], [ "P59594-1", "protein_xref_uniprotkb_fun", "P59594", "", "Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis." ], [ "P59594-1", "protein_xref_uniprotkb_fun", "P59594", "", "attaches the virion to the cell membrane by interacting with host receptor, initiating the infection (By similarity). Binding to human ACE2 and CLEC4M/DC-SIGNR receptors and internalization of the virus into the endosomes of the host cell induces conformational changes in the S glycoprotein. Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and activate membranes fusion within endosomes." ], [ "P0C6U8-1", "protein_xref_uniprotkb_fun", "P0C6U8", "", "Plays an essential role in viral replication by forming a homodimer that binds single-stranded RNA." ], [ "P0C6U8-1", "protein_xref_uniprotkb_fun", "P0C6U8", "23943763", "Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:23943763). Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:23943763, PubMed:24410069). 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 (PubMed:24991833)." ], [ "P0C6U8-1", "protein_xref_uniprotkb_fun", "P0C6U8", "24410069", "Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:23943763). Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:23943763, PubMed:24410069). 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 (PubMed:24991833)." ], [ "P0C6U8-1", "protein_xref_uniprotkb_fun", "P0C6U8", "24991833", "Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:23943763). Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:23943763, PubMed:24410069). 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 (PubMed:24991833)." ], [ "P0C6U8-1", "protein_xref_uniprotkb_fun", "P0C6U8", "17692280", "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 (PubMed:17692280). Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:23943763). Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:24410069, PubMed:23943763). Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3 (PubMed:19369340, PubMed:24622840). Prevents also host NF-kappa-B signaling (PubMed:19369340, PubMed:24622840)." ], [ "P0C6U8-1", "protein_xref_uniprotkb_fun", "P0C6U8", "19369340", "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 (PubMed:17692280). Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:23943763). Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:24410069, PubMed:23943763). Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3 (PubMed:19369340, PubMed:24622840). Prevents also host NF-kappa-B signaling (PubMed:19369340, PubMed:24622840)." ], [ "P0C6U8-1", "protein_xref_uniprotkb_fun", "P0C6U8", "23943763", "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 (PubMed:17692280). Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:23943763). Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:24410069, PubMed:23943763). Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3 (PubMed:19369340, PubMed:24622840). Prevents also host NF-kappa-B signaling (PubMed:19369340, PubMed:24622840)." ], [ "P0C6U8-1", "protein_xref_uniprotkb_fun", "P0C6U8", "24410069", "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 (PubMed:17692280). Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:23943763). Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:24410069, PubMed:23943763). Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3 (PubMed:19369340, PubMed:24622840). Prevents also host NF-kappa-B signaling (PubMed:19369340, PubMed:24622840)." ], [ "P0C6U8-1", "protein_xref_uniprotkb_fun", "P0C6U8", "24622840", "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 (PubMed:17692280). Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:23943763). Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:24410069, PubMed:23943763). Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3 (PubMed:19369340, PubMed:24622840). Prevents also host NF-kappa-B signaling (PubMed:19369340, PubMed:24622840)." ], [ "P0C6U8-1", "protein_xref_uniprotkb_fun", "P0C6U8", "", "Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein." ], [ "P0C6U8-1", "protein_xref_uniprotkb_fun", "P0C6U8", "23943763", "Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:23943763, PubMed:24410069). Alone appears incapable to induce membrane curvature, but together with nsp3 is able to induce paired membranes (PubMed:23943763). Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:23943763, PubMed:24410069)." ], [ "P0C6U8-1", "protein_xref_uniprotkb_fun", "P0C6U8", "24410069", "Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:23943763, PubMed:24410069). Alone appears incapable to induce membrane curvature, but together with nsp3 is able to induce paired membranes (PubMed:23943763). Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:23943763, PubMed:24410069)." ], [ "P0C6U8-1", "protein_xref_uniprotkb_fun", "P0C6U8", "19640993", "May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2 (PubMed:19640993). Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses (PubMed:19640993)." ], [ "P0C6U8-1", "protein_xref_uniprotkb_fun", "P0C6U8", "", "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." ], [ "P0C6U8-1", "protein_xref_uniprotkb_fun", "P0C6U8", "23035226", "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 (PubMed:23035226). May disrupt nuclear pore function by binding and displacing host NUP93 (PubMed:30943371)." ], [ "P0C6U8-1", "protein_xref_uniprotkb_fun", "P0C6U8", "30943371", "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 (PubMed:23035226). May disrupt nuclear pore function by binding and displacing host NUP93 (PubMed:30943371)." ], [ "P0C6U8-1", "protein_xref_uniprotkb_fun", "P0C6U8", "", "Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''-phosphate (ADRP). May cleave host ATP6V1G1 thereby modifying host vacuoles intracellular pH." ], [ "P0C6U8-1", "protein_xref_uniprotkb_fun", "P0C6U8", "", "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." ], [ "P0C6U8-1", "protein_xref_uniprotkb_fun", "P0C6U8", "", "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." ], [ "P59595-1", "protein_xref_uniprotkb_fun", "P59595", "17210170", "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 (PubMed:17210170). May modulate transforming growth factor-beta signaling by binding host SMAD3 (PubMed:18055455)." ], [ "P59595-1", "protein_xref_uniprotkb_fun", "P59595", "18055455", "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 (PubMed:17210170). May modulate transforming growth factor-beta signaling by binding host SMAD3 (PubMed:18055455)." ], [ "Q80H93-1", "protein_xref_uniprotkb_fun", "Q80H93", "", "Non-structural protein which is dispensable for virus replication in cell culture." ], [ "P59635-1", "protein_xref_uniprotkb_fun", "P59635", "", "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." ], [ "P59633-1", "protein_xref_uniprotkb_fun", "P59633", "", "Induces host cell G0/G1 arrest and apoptosis." ], [ "P59632-1", "protein_xref_uniprotkb_fun", "P59632", "", "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." ], [ "P59637-1", "protein_xref_uniprotkb_fun", "P59637", "", "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 (By similarity). Activates the host NLRP3 inflammasome, leading to IL-1beta overproduction." ], [ "P59636-1", "protein_xref_uniprotkb_fun", "P59636", "", "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." ], [ "P0C6X7-1", "protein_xref_uniprotkb_fun", "P0C6X7", "", "Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein." ], [ "P0C6X7-1", "protein_xref_uniprotkb_fun", "P0C6X7", "18417574", "Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs (PubMed:18417574, PubMed:22022266,PubMed:20421945). N7-methyl guanosine cap is a prerequisite for binding of nsp16 (PubMed:18417574). Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system (PubMed:18417574, PubMed:22022266,PubMed:20421945)." ], [ "P0C6X7-1", "protein_xref_uniprotkb_fun", "P0C6X7", "22022266PubMed:20421945", "Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs (PubMed:18417574, PubMed:22022266,PubMed:20421945). N7-methyl guanosine cap is a prerequisite for binding of nsp16 (PubMed:18417574). Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system (PubMed:18417574, PubMed:22022266,PubMed:20421945)." ], [ "P0C6X7-1", "protein_xref_uniprotkb_fun", "P0C6X7", "", "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." ], [ "P0C6X7-1", "protein_xref_uniprotkb_fun", "P0C6X7", "19640993", "May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2 (PubMed:19640993). Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses (PubMed:19640993)." ], [ "P0C6X7-1", "protein_xref_uniprotkb_fun", "P0C6X7", "24410069", "Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:24991833, PubMed:24410069). Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:24991833, PubMed:24410069). 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 (PubMed:24991833)." ], [ "P0C6X7-1", "protein_xref_uniprotkb_fun", "P0C6X7", "24991833", "Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:24991833, PubMed:24410069). Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:24991833, PubMed:24410069). 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 (PubMed:24991833)." ], [ "P0C6X7-1", "protein_xref_uniprotkb_fun", "P0C6X7", "16549795", "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 (PubMed:16549795, PubMed:20421945, PubMed:22635272). Acts as a proofreading exoribonuclease for RNA replication, thereby lowering The sensitivity of the virus to RNA mutagens (PubMed:23966862, PubMed:29511076, PubMed:21593585)." ], [ "P0C6X7-1", "protein_xref_uniprotkb_fun", "P0C6X7", "20421945", "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 (PubMed:16549795, PubMed:20421945, PubMed:22635272). Acts as a proofreading exoribonuclease for RNA replication, thereby lowering The sensitivity of the virus to RNA mutagens (PubMed:23966862, PubMed:29511076, PubMed:21593585)." ], [ "P0C6X7-1", "protein_xref_uniprotkb_fun", "P0C6X7", "21593585", "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 (PubMed:16549795, PubMed:20421945, PubMed:22635272). Acts as a proofreading exoribonuclease for RNA replication, thereby lowering The sensitivity of the virus to RNA mutagens (PubMed:23966862, PubMed:29511076, PubMed:21593585)." ], [ "P0C6X7-1", "protein_xref_uniprotkb_fun", "P0C6X7", "22635272", "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 (PubMed:16549795, PubMed:20421945, PubMed:22635272). Acts as a proofreading exoribonuclease for RNA replication, thereby lowering The sensitivity of the virus to RNA mutagens (PubMed:23966862, PubMed:29511076, PubMed:21593585)." ], [ "P0C6X7-1", "protein_xref_uniprotkb_fun", "P0C6X7", "23966862", "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 (PubMed:16549795, PubMed:20421945, PubMed:22635272). Acts as a proofreading exoribonuclease for RNA replication, thereby lowering The sensitivity of the virus to RNA mutagens (PubMed:23966862, PubMed:29511076, PubMed:21593585)." ], [ "P0C6X7-1", "protein_xref_uniprotkb_fun", "P0C6X7", "29511076", "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 (PubMed:16549795, PubMed:20421945, PubMed:22635272). Acts as a proofreading exoribonuclease for RNA replication, thereby lowering The sensitivity of the virus to RNA mutagens (PubMed:23966862, PubMed:29511076, PubMed:21593585)." ], [ "P0C6X7-1", "protein_xref_uniprotkb_fun", "P0C6X7", "", "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." ], [ "P0C6X7-1", "protein_xref_uniprotkb_fun", "P0C6X7", "23943763", "Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:23943763). Alone appears incapable to induce membrane curvature, but together with nsp3 is able to induce paired membranes. Nsp3, nsp4 and nsp6 together are sufficient to form DMV." ], [ "P0C6X7-1", "protein_xref_uniprotkb_fun", "P0C6X7", "16828802", "Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (PubMed:28158275, PubMed:18045871). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'-cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (PubMed:16828802). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (PubMed:28158275, PubMed:18045871)." ], [ "P0C6X7-1", "protein_xref_uniprotkb_fun", "P0C6X7", "18045871", "Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (PubMed:28158275, PubMed:18045871). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'-cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (PubMed:16828802). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (PubMed:28158275, PubMed:18045871)." ], [ "P0C6X7-1", "protein_xref_uniprotkb_fun", "P0C6X7", "28158275", "Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (PubMed:28158275, PubMed:18045871). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'-cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (PubMed:16828802). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (PubMed:28158275, PubMed:18045871)." ], [ "P0C6X7-1", "protein_xref_uniprotkb_fun", "P0C6X7", "16306590", "Responsible for the cleavages located at the N-terminus of the replicase polyprotein (PubMed:16306590). In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates (PubMed:16306590, PubMed:17692280). Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:23943763). Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:24410069). Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3 (PubMed:19369340, PubMed:24622840). Prevents also host NF-kappa-B signaling (PubMed:19369340, PubMed:24622840)." ], [ "P0C6X7-1", "protein_xref_uniprotkb_fun", "P0C6X7", "17692280", "Responsible for the cleavages located at the N-terminus of the replicase polyprotein (PubMed:16306590). In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates (PubMed:16306590, PubMed:17692280). Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:23943763). Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:24410069). Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3 (PubMed:19369340, PubMed:24622840). Prevents also host NF-kappa-B signaling (PubMed:19369340, PubMed:24622840)." ], [ "P0C6X7-1", "protein_xref_uniprotkb_fun", "P0C6X7", "19369340", "Responsible for the cleavages located at the N-terminus of the replicase polyprotein (PubMed:16306590). In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates (PubMed:16306590, PubMed:17692280). Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:23943763). Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:24410069). Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3 (PubMed:19369340, PubMed:24622840). Prevents also host NF-kappa-B signaling (PubMed:19369340, PubMed:24622840)." ], [ "P0C6X7-1", "protein_xref_uniprotkb_fun", "P0C6X7", "23943763", "Responsible for the cleavages located at the N-terminus of the replicase polyprotein (PubMed:16306590). In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates (PubMed:16306590, PubMed:17692280). Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:23943763). Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:24410069). Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3 (PubMed:19369340, PubMed:24622840). Prevents also host NF-kappa-B signaling (PubMed:19369340, PubMed:24622840)." ], [ "P0C6X7-1", "protein_xref_uniprotkb_fun", "P0C6X7", "24410069", "Responsible for the cleavages located at the N-terminus of the replicase polyprotein (PubMed:16306590). In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates (PubMed:16306590, PubMed:17692280). Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:23943763). Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:24410069). Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3 (PubMed:19369340, PubMed:24622840). Prevents also host NF-kappa-B signaling (PubMed:19369340, PubMed:24622840)." ], [ "P0C6X7-1", "protein_xref_uniprotkb_fun", "P0C6X7", "24622840", "Responsible for the cleavages located at the N-terminus of the replicase polyprotein (PubMed:16306590). In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates (PubMed:16306590, PubMed:17692280). Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:23943763). Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:24410069). Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3 (PubMed:19369340, PubMed:24622840). Prevents also host NF-kappa-B signaling (PubMed:19369340, PubMed:24622840)." ], [ "P0C6X7-1", "protein_xref_uniprotkb_fun", "P0C6X7", "", "Plays an essential role in viral replication by forming a homodimer that binds single-stranded RNA." ], [ "P0C6X7-1", "protein_xref_uniprotkb_fun", "P0C6X7", "", "Responsible for replication and transcription of the viral RNA genome." ], [ "P0C6X7-1", "protein_xref_uniprotkb_fun", "P0C6X7", "", "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." ], [ "P0C6X7-1", "protein_xref_uniprotkb_fun", "P0C6X7", "", "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." ], [ "P0C6X7-1", "protein_xref_uniprotkb_fun", "P0C6X7", "", "Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''-phosphate (ADRP). May cleave host ATP6V1G1 thereby modifying host vacuoles intracellular pH." ], [ "P0C6X7-1", "protein_xref_uniprotkb_fun", "P0C6X7", "23035226", "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 (PubMed:23035226). May disrupt nuclear pore function by binding and displacing host NUP93 (PubMed:30943371)." ], [ "P0C6X7-1", "protein_xref_uniprotkb_fun", "P0C6X7", "30943371", "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 (PubMed:23035226). May disrupt nuclear pore function by binding and displacing host NUP93 (PubMed:30943371)." ], [ "P59634-1", "protein_xref_uniprotkb_fun", "P59634", "", "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." ] ] }, "readme": "Name\n - SARS-CoV1 Protein Function (UniProtKB)\n\nVersion\n - 1.11.2\n\nCreated on\n - 2020-04-02T23:52:06.244702\n\nModified on\n - 2020-04-09T18:41:33.892961\n\nCreated by\n - Jeet Vora [jeetvora@gwu.edu], Rahi Navelkar [rsn13@gwu.edu], Robel Kahsay [rykahsay@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 SARS coronavirus (SARS-CoV-1) Protein Function (UniProtKB) dataset contains biological function annotation for sarscov1 [taxid:694009] 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-coronavirus.nt\n URI: https:/data.glygen.org/ln2downloads/ebi/2021_04/uniprot-proteome-sars-coronavirus.nt\n Output Subdomain\n Name: sarscov1_protein_function_uniprotkb.csv\n URI: https:/data.glygen.org/ln2releases/data/v-1.12.3/reviewed/sarscov1_protein_function_uniprotkb.csv\n Name: sarscov1_protein_function_uniprotkb.stat.csv\n URI: https:/data.glygen.org/ln2releases/data/v-1.12.3/reviewed/sarscov1_protein_function_uniprotkb.stat.csv\n\nFields\n Name: \"uniprotkb_canonical_ac\"\n Description: \"\"\n Unique Values: \"12\"\n Name: \"xref_key\"\n Description: \"Source key associated to the xref_id\"\n Unique Values: \"1\"\n Name: \"xref_id\"\n Description: \"ID of the X-ref\"\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: \"24\"\n Name: \"annotation\"\n Description: \"Function annotation from UniProtKB|RefSeq database\"\n Unique Values: \"32\"", "downloadurl": "/ln2data/releases/data/v-1.12.3/reviewed/sarscov1_protein_function_uniprotkb.csv" }