[ { "uniprot_canonical_ac": "P27958-1", "uniprot_ac": "P27958", "uniprot_id": "POLG_HCV77", "mass": { "chemical_mass": 327146.0, "monoisotopic_mass": 327146.0 }, "refseq": {}, "gene_names": [], "protein_names": [ { "name": "Genome polyprotein", "type": "recommended", "evidence": [ { "id": "P27958", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprotkb/P27958/entry#names_and_taxonomy" } ] }, { "name": "Capsid protein C", "type": "synonym", "evidence": [ { "id": "P27958", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprotkb/P27958/entry#names_and_taxonomy" } ] }, { "name": "Hepacivirin", "type": "synonym", "evidence": [ { "id": "P27958", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprotkb/P27958/entry#names_and_taxonomy" } ] }, { "name": "NS1", "type": "synonym", "evidence": [ { "id": "P27958", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprotkb/P27958/entry#names_and_taxonomy" } ] }, { "name": "NS2", "type": "synonym", "evidence": [ { "id": "P27958", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprotkb/P27958/entry#names_and_taxonomy" } ] }, { "name": "NS3 helicase", "type": "synonym", "evidence": [ { "id": "P27958", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprotkb/P27958/entry#names_and_taxonomy" } ] }, { "name": "NS3 protease", "type": "synonym", "evidence": [ { "id": "P27958", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprotkb/P27958/entry#names_and_taxonomy" } ] }, { "name": "NS3P", "type": "synonym", "evidence": [ { "id": "P27958", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprotkb/P27958/entry#names_and_taxonomy" } ] }, { "name": "NS5B", "type": "synonym", "evidence": [ { "id": "P27958", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprotkb/P27958/entry#names_and_taxonomy" } ] }, { "name": "Non-structural protein 2", "type": "synonym", "evidence": [ { "id": "P27958", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprotkb/P27958/entry#names_and_taxonomy" } ] }, { "name": "Viroporin p70", "type": "synonym", "evidence": [ { "id": "P27958", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprotkb/P27958/entry#names_and_taxonomy" } ] }, { "name": "gp32", "type": "synonym", "evidence": [ { "id": "P27958", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprotkb/P27958/entry#names_and_taxonomy" } ] }, { "name": "gp35", "type": "synonym", "evidence": [ { "id": "P27958", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprotkb/P27958/entry#names_and_taxonomy" } ] }, { "name": "gp68", "type": "synonym", "evidence": [ { "id": "P27958", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprotkb/P27958/entry#names_and_taxonomy" } ] }, { "name": "gp70", "type": "synonym", "evidence": [ { "id": "P27958", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprotkb/P27958/entry#names_and_taxonomy" } ] }, { "name": "p21", "type": "synonym", "evidence": [ { "id": "P27958", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprotkb/P27958/entry#names_and_taxonomy" } ] }, { "name": "p23", "type": "synonym", "evidence": [ { "id": "P27958", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprotkb/P27958/entry#names_and_taxonomy" } ] }, { "name": "p27", "type": "synonym", "evidence": [ { "id": "P27958", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprotkb/P27958/entry#names_and_taxonomy" } ] }, { "name": "p56/58", "type": "synonym", "evidence": [ { "id": "P27958", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprotkb/P27958/entry#names_and_taxonomy" } ] }, { "name": "p68", "type": "synonym", "evidence": [ { "id": "P27958", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprotkb/P27958/entry#names_and_taxonomy" } ] }, { "name": "p8", "type": "synonym", "evidence": [ { "id": "P27958", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprotkb/P27958/entry#names_and_taxonomy" } ] } ], "function": [ { "annotation": "Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (PubMed:8248148). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (By similarity). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (PubMed:21147927).", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958#function" }, { "database": "UniProtKB", "id": "P26663", "url": "https://www.uniprot.org/uniprotkb/P26663#function" }, { "database": "PubMed", "id": "21147927", "url": "https://glygen.org/publication/PubMed/21147927" }, { "database": "PubMed", "id": "8248148", "url": "https://glygen.org/publication/PubMed/8248148" } ] }, { "annotation": "Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (PubMed:25551442). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B-NS5A and NS5A-NS5B (PubMed:8035505, PubMed:8189513, PubMed:8386278). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (PubMed:30341327). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (Probable). Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (PubMed:21940894). Inhibits host antiviral proteins TBK1 and IRF3 thereby preventing the establishment of an antiviral state (By similarity). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (PubMed:16177806, PubMed:16301520). Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (PubMed:15710891).", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958#function" }, { "database": "PubMed", "id": "8035505", "url": "https://glygen.org/publication/PubMed/8035505" }, { "database": "PubMed", "id": "16177806", "url": "https://glygen.org/publication/PubMed/16177806" }, { "database": "PubMed", "id": "15269774", "url": "https://glygen.org/publication/PubMed/15269774" }, { "database": "PubMed", "id": "8189513", "url": "https://glygen.org/publication/PubMed/8189513" }, { "database": "UniProtKB", "id": "Q9WMX2", "url": "https://www.uniprot.org/uniprotkb/Q9WMX2#function" }, { "database": "PubMed", "id": "30341327", "url": "https://glygen.org/publication/PubMed/30341327" }, { "database": "PubMed", "id": "21940894", "url": "https://glygen.org/publication/PubMed/21940894" }, { "database": "PubMed", "id": "8386278", "url": "https://glygen.org/publication/PubMed/8386278" }, { "database": "PubMed", "id": "15710891", "url": "https://glygen.org/publication/PubMed/15710891" }, { "database": "PubMed", "id": "16301520", "url": "https://glygen.org/publication/PubMed/16301520" }, { "database": "PubMed", "id": "25551442", "url": "https://glygen.org/publication/PubMed/25551442" } ] }, { "annotation": "Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (PubMed:14990718, PubMed:16894197). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (PubMed:16533059, PubMed:24698129, PubMed:29505618). The interaction between E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (PubMed:25122793, PubMed:29695434). This interaction is probably promoted via the up-regulation of cellular autophagy by the virus (PubMed:29695434). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (PubMed:24838241, PubMed:25122793, PubMed:29695434). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (PubMed:12356718, PubMed:12913001, PubMed:12970454, PubMed:22767607, PubMed:28404852). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (PubMed:12913001, PubMed:22767607). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity) (PubMed:12913001, PubMed:12970454, PubMed:19182773, PubMed:20375010, PubMed:22855500, PubMed:24038151). Diffusion of the complex E1/E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity) (PubMed:12913001, PubMed:12970454, PubMed:19182773, PubMed:20375010, PubMed:24038151). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on DCs, and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (PubMed:15371595). These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (PubMed:15371595). The interaction between E2 and host amino acid transporter complex formed by SLC3A2 and SLC7A5/LAT1 may facilitate viral entry into host cell (PubMed:30341327).", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958#function" }, { "database": "PubMed", "id": "24038151", "url": "https://glygen.org/publication/PubMed/24038151" }, { "database": "PubMed", "id": "14990718", "url": "https://glygen.org/publication/PubMed/14990718" }, { "database": "PubMed", "id": "16894197", "url": "https://glygen.org/publication/PubMed/16894197" }, { "database": "PubMed", "id": "24838241", "url": "https://glygen.org/publication/PubMed/24838241" }, { "database": "PubMed", "id": "19182773", "url": "https://glygen.org/publication/PubMed/19182773" }, { "database": "UniProtKB", "id": "Q99IB8", "url": "https://www.uniprot.org/uniprotkb/Q99IB8#function" }, { "database": "PubMed", "id": "12913001", "url": "https://glygen.org/publication/PubMed/12913001" }, { "database": "PubMed", "id": "29505618", "url": "https://glygen.org/publication/PubMed/29505618" }, { "database": "PubMed", "id": "29695434", "url": "https://glygen.org/publication/PubMed/29695434" }, { "database": "PubMed", "id": "15371595", "url": "https://glygen.org/publication/PubMed/15371595" }, { "database": "UniProtKB", "id": "P26664", "url": "https://www.uniprot.org/uniprotkb/P26664#function" }, { "database": "PubMed", "id": "28404852", "url": "https://glygen.org/publication/PubMed/28404852" }, { "database": "PubMed", "id": "25122793", "url": "https://glygen.org/publication/PubMed/25122793" }, { "database": "PubMed", "id": "30341327", "url": "https://glygen.org/publication/PubMed/30341327" }, { "database": "PubMed", "id": "22855500", "url": "https://glygen.org/publication/PubMed/22855500" }, { "database": "PubMed", "id": "12356718", "url": "https://glygen.org/publication/PubMed/12356718" }, { "database": "PubMed", "id": "16533059", "url": "https://glygen.org/publication/PubMed/16533059" }, { "database": "PubMed", "id": "24698129", "url": "https://glygen.org/publication/PubMed/24698129" }, { "database": "PubMed", "id": "22767607", "url": "https://glygen.org/publication/PubMed/22767607" }, { "database": "PubMed", "id": "12970454", "url": "https://glygen.org/publication/PubMed/12970454" }, { "database": "PubMed", "id": "20375010", "url": "https://glygen.org/publication/PubMed/20375010" } ] }, { "annotation": "Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (PubMed:14990718, PubMed:16894197). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (PubMed:16533059, PubMed:24698129, PubMed:29505618). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (PubMed:24838241, PubMed:25122793, PubMed:29695434). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (PubMed:12356718, PubMed:12913001, PubMed:12970454, PubMed:22767607, PubMed:28404852). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (PubMed:12913001, PubMed:22767607). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (PubMed:22855500). Diffusion of the complex E1/E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity) (PubMed:12913001, PubMed:12970454, PubMed:19182773, PubMed:20375010, PubMed:24038151).", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958#function" }, { "database": "PubMed", "id": "24038151", "url": "https://glygen.org/publication/PubMed/24038151" }, { "database": "PubMed", "id": "14990718", "url": "https://glygen.org/publication/PubMed/14990718" }, { "database": "PubMed", "id": "16894197", "url": "https://glygen.org/publication/PubMed/16894197" }, { "database": "PubMed", "id": "24838241", "url": "https://glygen.org/publication/PubMed/24838241" }, { "database": "PubMed", "id": "19182773", "url": "https://glygen.org/publication/PubMed/19182773" }, { "database": "UniProtKB", "id": "Q99IB8", "url": "https://www.uniprot.org/uniprotkb/Q99IB8#function" }, { "database": "PubMed", "id": "12913001", "url": "https://glygen.org/publication/PubMed/12913001" }, { "database": "PubMed", "id": "29505618", "url": "https://glygen.org/publication/PubMed/29505618" }, { "database": "PubMed", "id": "29695434", "url": "https://glygen.org/publication/PubMed/29695434" }, { "database": "PubMed", "id": "28404852", "url": "https://glygen.org/publication/PubMed/28404852" }, { "database": "PubMed", "id": "25122793", "url": "https://glygen.org/publication/PubMed/25122793" }, { "database": "PubMed", "id": "22855500", "url": "https://glygen.org/publication/PubMed/22855500" }, { "database": "PubMed", "id": "12356718", "url": "https://glygen.org/publication/PubMed/12356718" }, { "database": "PubMed", "id": "16533059", "url": "https://glygen.org/publication/PubMed/16533059" }, { "database": "PubMed", "id": "24698129", "url": "https://glygen.org/publication/PubMed/24698129" }, { "database": "PubMed", "id": "22767607", "url": "https://glygen.org/publication/PubMed/22767607" }, { "database": "PubMed", "id": "12970454", "url": "https://glygen.org/publication/PubMed/12970454" }, { "database": "PubMed", "id": "20375010", "url": "https://glygen.org/publication/PubMed/20375010" } ] }, { "annotation": "Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (PubMed:12021330). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (PubMed:12021330). NS4B self-interaction contributes to its function in membranous web formation (PubMed:16731940). Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3-mediated interferon signaling (PubMed:29782532). Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (PubMed:23542348).", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958#function" }, { "database": "PubMed", "id": "23542348", "url": "https://glygen.org/publication/PubMed/23542348" }, { "database": "PubMed", "id": "16731940", "url": "https://glygen.org/publication/PubMed/16731940" }, { "database": "PubMed", "id": "29782532", "url": "https://glygen.org/publication/PubMed/29782532" }, { "database": "PubMed", "id": "12021330", "url": "https://glygen.org/publication/PubMed/12021330" } ] }, { "annotation": "Ion channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (PubMed:12719519, PubMed:20824094, PubMed:27320856). Participates in virus envelopment by coordinating the encounter between NS5A and NS2-based assembly sites loaded with E1/E2 heterodimer, which subsequently leads to nucleocapsid envelopment (By similarity). Creates a pore in acidic organelles and releases Ca(2+) and H(+) in the cytoplasm of infected cells, leading to a productive viral infection (Probable) (PubMed:20824094). High levels of cytoplasmic Ca(2+) may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). The release of Ca(2+) may also activate the inflamasome leading to chronic inflammation (Probable) (PubMed:31801866). Targets also host mitochondria and induces mitochondrial depolarization (PubMed:29039530). In addition of its role as a viroporin, acts as a lipid raft adhesion factor (PubMed:27320856).", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958#function" }, { "database": "PubMed", "id": "14741348", "url": "https://glygen.org/publication/PubMed/14741348" }, { "database": "UniProtKB", "id": "Q99IB8", "url": "https://www.uniprot.org/uniprotkb/Q99IB8#function" }, { "database": "PubMed", "id": "20824094", "url": "https://glygen.org/publication/PubMed/20824094" }, { "database": "PubMed", "id": "24006444", "url": "https://glygen.org/publication/PubMed/24006444" }, { "database": "PubMed", "id": "29039530", "url": "https://glygen.org/publication/PubMed/29039530" }, { "database": "PubMed", "id": "27320856", "url": "https://glygen.org/publication/PubMed/27320856" }, { "database": "PubMed", "id": "12719519", "url": "https://glygen.org/publication/PubMed/12719519" }, { "database": "PubMed", "id": "31801866", "url": "https://glygen.org/publication/PubMed/31801866" } ] }, { "annotation": "Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (PubMed:18033802). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity) (PubMed:23799612). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (PubMed:11086025, PubMed:17881511). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (PubMed:14602201). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (PubMed:14602201).", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958#function" }, { "database": "UniProtKB", "id": "P29846", "url": "https://www.uniprot.org/uniprotkb/P29846#function" }, { "database": "PubMed", "id": "14602201", "url": "https://glygen.org/publication/PubMed/14602201" }, { "database": "UniProtKB", "id": "Q99IB8", "url": "https://www.uniprot.org/uniprotkb/Q99IB8#function" }, { "database": "PubMed", "id": "17881511", "url": "https://glygen.org/publication/PubMed/17881511" }, { "database": "UniProtKB", "id": "P26662", "url": "https://www.uniprot.org/uniprotkb/P26662#function" }, { "database": "UniProtKB", "id": "P26664", "url": "https://www.uniprot.org/uniprotkb/P26664#function" }, { "database": "PubMed", "id": "18033802", "url": "https://glygen.org/publication/PubMed/18033802" }, { "database": "PubMed", "id": "23799612", "url": "https://glygen.org/publication/PubMed/23799612" }, { "database": "PubMed", "id": "11086025", "url": "https://glygen.org/publication/PubMed/11086025" } ] }, { "annotation": "Peptide cofactor which forms a non-covalent complex with the N-terminal of NS3 serine protease (PubMed:21507982, PubMed:8189513). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (PubMed:30341327).", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958#function" }, { "database": "PubMed", "id": "8189513", "url": "https://glygen.org/publication/PubMed/8189513" }, { "database": "UniProtKB", "id": "Q9WMX2", "url": "https://www.uniprot.org/uniprotkb/Q9WMX2#function" }, { "database": "PubMed", "id": "30341327", "url": "https://glygen.org/publication/PubMed/30341327" }, { "database": "PubMed", "id": "21507982", "url": "https://glygen.org/publication/PubMed/21507982" } ] }, { "annotation": "Phosphorylated protein that is indispensable for viral replication and assembly (PubMed:27578425). Both hypo- and hyperphosphorylated states are required for the viral life cycle (By similarity). The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity). Involved in RNA-binding and especially in binding to the viral genome (Probable). Zinc is essential for RNA-binding (PubMed:20926572). Participates in the viral particle production as a result of its interaction with the viral mature core protein (By similarity). Its interaction with host VAPB may target the viral replication complex to vesicles (By similarity). Down-regulates viral IRES translation initiation (By similarity). Mediates interferon resistance, presumably by interacting with and inhibiting host EIF2AK2/PKR (PubMed:16951545). Prevents BIN1-induced apoptosis (PubMed:16530520). Acts as a transcriptional activator of some host genes important for viral replication when localized in the nucleus (By similarity). Via the interaction with host PACSIN2, modulates lipid droplet formation in order to promote virion assembly (PubMed:31801866). Modulates TNFRSF21/DR6 signaling pathway for viral propagation (PubMed:28743875).", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958#function" }, { "database": "PubMed", "id": "25683609", "url": "https://glygen.org/publication/PubMed/25683609" }, { "database": "PubMed", "id": "16530520", "url": "https://glygen.org/publication/PubMed/16530520" }, { "database": "PubMed", "id": "31801866", "url": "https://glygen.org/publication/PubMed/31801866" }, { "database": "UniProtKB", "id": "Q99IB8", "url": "https://www.uniprot.org/uniprotkb/Q99IB8#function" }, { "database": "PubMed", "id": "20926572", "url": "https://glygen.org/publication/PubMed/20926572" }, { "database": "PubMed", "id": "28743875", "url": "https://glygen.org/publication/PubMed/28743875" }, { "database": "UniProtKB", "id": "Q9WMX2", "url": "https://www.uniprot.org/uniprotkb/Q9WMX2#function" }, { "database": "UniProtKB", "id": "P26662", "url": "https://www.uniprot.org/uniprotkb/P26662#function" }, { "database": "UniProtKB", "id": "P26664", "url": "https://www.uniprot.org/uniprotkb/P26664#function" }, { "database": "PubMed", "id": "27578425", "url": "https://glygen.org/publication/PubMed/27578425" }, { "database": "PubMed", "id": "16951545", "url": "https://glygen.org/publication/PubMed/16951545" } ] }, { "annotation": "RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication (PubMed:20729191). Initiates RNA transcription/replication at a flavin adenine dinucleotide (FAD), resulting in a 5'- FAD cap on viral RNAs. In this way, recognition of viral 5' RNA by host pattern recognition receptors can be bypassed (PubMed:37407817), thereby evading activation of antiviral pathways.", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958#function" }, { "database": "PubMed", "id": "20729191", "url": "https://glygen.org/publication/PubMed/20729191" }, { "database": "PubMed", "id": "37407817", "url": "https://glygen.org/publication/PubMed/37407817" } ] } ], "disease": [ { "disease_id": "DOID:1883", "recommended_name": { "id": "DOID:1883", "resource": "Disease Ontology", "url": "https://disease-ontology.org/term/DOID:1883", "name": "hepatitis C", "description": "A viral hepatitis that results_in inflammation located_in liver, has_material_basis_in hepatitis C virus (Hepacivirus hominis), which is transmitted_by blood from an infected person enters the body of an uninfected person. The infection has_symptom fever, has_symptom fatigue, has_symptom loss of appetite, has_symptom nausea, has_symptom vomiting, has_symptom abdominal pain, has_symptom clay-colored bowel movements, has_symptom joint pain, and has_symptom jaundice." }, "synonyms": [ { "id": "DOID:1883", "resource": "Disease Ontology", "url": "https://disease-ontology.org/term/DOID:1883", "name": "NANBH", "description": "" }, { "id": "DOID:1883", "resource": "Disease Ontology", "url": "https://disease-ontology.org/term/DOID:1883", "name": "Viral hepatitis C", "description": "" }, { "id": "DOID:1883", "resource": "Disease Ontology", "url": "https://disease-ontology.org/term/DOID:1883", "name": "chronic hepatitis C", "description": "" }, { "id": "DOID:1883", "resource": "Disease Ontology", "url": "https://disease-ontology.org/term/DOID:1883", "name": "hepatitis C infection", "description": "" }, { "id": "DOID:1883", "resource": "Disease Ontology", "url": "https://disease-ontology.org/term/DOID:1883", "name": "hepatitis nonA nonB", "description": "" }, { "id": "MONDO:0005231", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0005231", "name": "hepatitis C virus infection", "description": "A viral infection caused by the hepatitis C virus." }, { "id": "MONDO:0005231", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0005231", "name": "Hepatitis C virus caused hepatitis", "description": "" }, { "id": "MONDO:0005231", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0005231", "name": "Hepatitis C virus hepatitis", "description": "" }, { "id": "MONDO:0005231", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0005231", "name": "NANBH", "description": "" }, { "id": "MONDO:0005231", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0005231", "name": "hepatitis C infection", "description": "" }, { "id": "MONDO:0005231", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0005231", "name": "hepatitis type C", "description": "" }, { "id": "MONDO:0005231", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0005231", "name": "non-A, non-B Hepatitis", "description": "" }, { "id": "MONDO:0005231", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0005231", "name": "chronic hepatitis C", "description": "" } ], "unlinked_id_list": [], "evidence": [ { "id": "GLY_000487", "database": "GlyGen", "url": "https://data.glygen.org/GLY_000487" } ] }, { "disease_id": "DOID:5082", "recommended_name": { "id": "DOID:5082", "resource": "Disease Ontology", "url": "https://disease-ontology.org/term/DOID:5082", "name": "liver cirrhosis", "description": "" }, "synonyms": [ { "id": "DOID:5082", "resource": "Disease Ontology", "url": "https://disease-ontology.org/term/DOID:5082", "name": "Cirrhosis", "description": "" }, { "id": "DOID:5082", "resource": "Disease Ontology", "url": "https://disease-ontology.org/term/DOID:5082", "name": "cirrhosis of liver", "description": "" }, { "id": "MONDO:0005155", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0005155", "name": "cirrhosis of liver", "description": "A disorder characterized by replacement of the liver parenchyma with fibrous tissue and regenerative nodules. It is usually caused by alcoholism, hepatitis B, and hepatitis C. Complications include the development of ascites, esophageal varices, bleeding, and hepatic encephalopathy." }, { "id": "MONDO:0005155", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0005155", "name": "cirrhosis", "description": "" } ], "unlinked_id_list": [], "evidence": [ { "id": "GLY_000487", "database": "GlyGen", "url": "https://data.glygen.org/GLY_000487" } ] }, { "disease_id": "DOID:684", "recommended_name": { "id": "DOID:684", "resource": "Disease Ontology", "url": "https://disease-ontology.org/term/DOID:684", "name": "hepatocellular carcinoma", "description": "A liver carcinoma that has_material_basis_in undifferentiated hepatocytes and located_in the liver." }, "synonyms": [ { "id": "DOID:684", "resource": "Disease Ontology", "url": "https://disease-ontology.org/term/DOID:684", "name": "Hepatoma", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "hepatocellular carcinoma", "description": "A malignant tumor that arises from hepatocytes. Hepatocellular carcinoma is relatively rare in the United States but very common in all African countries south of the Sahara and in Southeast Asia. Most cases are seen in patients over the age of 50 years, but this tumor can also occur in younger individuals and even in children. Hepatocellular carcinoma is more common in males than females and is associated with hepatitis B, hepatitis C, chronic alcohol abuse and cirrhosis. Serum elevation of alpha-fetoprotein occurs in a large percentage of patients with hepatocellular carcinoma. Grossly, hepatocellular carcinoma may present as a single mass, as multiple nodules, or as diffuse liver involvement. Microscopically, there is a wide range of differentiation from tumor to tumor (well differentiated to poorly differentiated tumors). Hepatocellular carcinomas quickly metastasize to regional lymph nodes and lung. The overall median survival of untreated liver cell carcinoma is about 4 months. The most effective treatment of hepatocellular carcinoma is complete resection of the tumor. Lately, an increasing number of tumors have been treated with liver transplantation." }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "HCC", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "cancer, hepatocellular", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "carcinoma of liver", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "carcinoma of liver cells", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "carcinoma of the liver cells", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "carcinoma, hepatocellular, malignant", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "hepatoblastoma, somatic", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "hepatocellular adenocarcinoma", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "hepatocellular cancer", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "hepatocellular cancer, somatic", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "hepatocellular carcinoma", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "hepatocellular carcinoma, childhood type, somatic", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "hepatocellular carcinoma, somatic", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "hepatoma", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "liver carcinoma", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "liver cell cancer (hepatocellular carcinoma)", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "liver cell carcinoma", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "primary carcinoma of liver cells", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "primary carcinoma of the liver cells", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "adult hepatoma", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "adult primary hepatocellular carcinoma", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "hepatocellular carcinoma", "description": "A malignant tumor that arises from hepatocytes. Hepatocellular carcinoma is relatively rare in the United States but very common in all African countries south of the Sahara and in Southeast Asia. Most cases are seen in patients over the age of 50 years, but this tumor can also occur in younger individuals and even in children. Hepatocellular carcinoma is more common in males than females and is associated with hepatitis B, hepatitis C, chronic alcohol abuse and cirrhosis. Serum elevation of alpha-fetoprotein occurs in a large percentage of patients with hepatocellular carcinoma. Grossly, hepatocellular carcinoma may present as a single mass, as multiple nodules, or as diffuse liver involvement. Microscopically, there is a wide range of differentiation from tumor to tumor (well differentiated to poorly differentiated tumors). Hepatocellular carcinomas quickly metastasize to regional lymph nodes and lung. The overall median survival of untreated liver cell carcinoma is about 4 months. The most effective treatment of hepatocellular carcinoma is complete resection of the tumor. Lately, an increasing number of tumors have been treated with liver transplantation." }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "HCC", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "cancer, hepatocellular", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "carcinoma of liver", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "carcinoma of liver cells", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "carcinoma of the liver cells", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "carcinoma, hepatocellular, malignant", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "hepatoblastoma, somatic", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "hepatocellular adenocarcinoma", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "hepatocellular cancer", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "hepatocellular cancer, somatic", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "hepatocellular carcinoma", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "hepatocellular carcinoma, childhood type, somatic", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "hepatocellular carcinoma, somatic", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "hepatoma", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "liver carcinoma", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "liver cell cancer (hepatocellular carcinoma)", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "liver cell carcinoma", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "primary carcinoma of liver cells", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "primary carcinoma of the liver cells", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "adult hepatoma", "description": "" }, { "id": "MONDO:0007256", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0007256", "name": "adult primary hepatocellular carcinoma", "description": "" }, { "id": "MIM:114550", "resource": "MIM", "url": "https://www.omim.org/entry/114550", "name": "Hepatocellular carcinoma", "description": "Hepatocellular carcinoma" } ], "unlinked_id_list": [], "evidence": [ { "id": "GLY_000487", "database": "GlyGen", "url": "https://data.glygen.org/GLY_000487" } ] } ], "snv": [], "mutagenesis": [ { "start_pos": 1083, "end_pos": 1083, "sequence_org": "H", "sequence_mut": "A", "comment": "Complete loss of NS3-NS4A, NS4A-NS4B, NS4B-NS5A and NS5A-NS5B cleavages.", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" }, { "database": "PubMed", "id": "8386278", "url": "https://glygen.org/publication/PubMed/8386278" } ] }, { "start_pos": 1165, "end_pos": 1165, "sequence_org": "S", "sequence_mut": "A", "comment": "Complete loss of NS3-NS4A, NS4A-NS4B, NS4B-NS5A and NS5A-NS5B cleavages.", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" }, { "database": "PubMed", "id": "8386278", "url": "https://glygen.org/publication/PubMed/8386278" }, { "database": "PubMed", "id": "8248148", "url": "https://glygen.org/publication/PubMed/8248148" } ] }, { "start_pos": 1968, "end_pos": 1968, "sequence_org": "C", "sequence_mut": "A", "comment": "Strong decrease in NS4B palmitoylation.", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" }, { "database": "PubMed", "id": "16731940", "url": "https://glygen.org/publication/PubMed/16731940" } ] }, { "start_pos": 1972, "end_pos": 1972, "sequence_org": "C", "sequence_mut": "A", "comment": "Slight decrease in NS4B palmitoylation.", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" }, { "database": "PubMed", "id": "16731940", "url": "https://glygen.org/publication/PubMed/16731940" } ] }, { "start_pos": 2321, "end_pos": 2321, "sequence_org": "S", "sequence_mut": "A", "comment": "Loss of phosphorylation.", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" }, { "database": "PubMed", "id": "10488152", "url": "https://glygen.org/publication/PubMed/10488152" } ] }, { "start_pos": 399, "end_pos": 399, "sequence_org": "L", "sequence_mut": "R", "comment": "Complete loss of E2 binding to host SCARB1; 5-10-fold decrease of infectivity for the viral particles.", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" }, { "database": "PubMed", "id": "22767607", "url": "https://glygen.org/publication/PubMed/22767607" } ] }, { "start_pos": 429, "end_pos": 429, "sequence_org": "C", "sequence_mut": "A", "comment": "Complete loss of infectivity.", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" }, { "database": "PubMed", "id": "22278231", "url": "https://glygen.org/publication/PubMed/22278231" } ] }, { "start_pos": 452, "end_pos": 452, "sequence_org": "C", "sequence_mut": "A", "comment": "Complete loss of infectivity. Loss of heterodimerization with E1. No effect on CD81-binding function.", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" }, { "database": "PubMed", "id": "22278231", "url": "https://glygen.org/publication/PubMed/22278231" } ] }, { "start_pos": 459, "end_pos": 459, "sequence_org": "C", "sequence_mut": "A", "comment": "Complete loss of infectivity. Loss of heterodimerization with E1. 78% loss of CD81-binding function.", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" }, { "database": "PubMed", "id": "22278231", "url": "https://glygen.org/publication/PubMed/22278231" } ] }, { "start_pos": 486, "end_pos": 486, "sequence_org": "C", "sequence_mut": "A", "comment": "Complete loss of infectivity. No effect on CD81-binding function. Loss of heterodimerization with E1.", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" }, { "database": "PubMed", "id": "22278231", "url": "https://glygen.org/publication/PubMed/22278231" } ] }, { "start_pos": 494, "end_pos": 494, "sequence_org": "C", "sequence_mut": "A", "comment": "Complete loss of infectivity and CD81-binding function. Loss of heterodimerization with E1.", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" }, { "database": "PubMed", "id": "22278231", "url": "https://glygen.org/publication/PubMed/22278231" } ] }, { "start_pos": 503, "end_pos": 503, "sequence_org": "C", "sequence_mut": "A", "comment": "Complete loss of infectivity and CD81-binding function.", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" }, { "database": "PubMed", "id": "22278231", "url": "https://glygen.org/publication/PubMed/22278231" } ] }, { "start_pos": 508, "end_pos": 508, "sequence_org": "C", "sequence_mut": "A", "comment": "Complete loss of infectivity and CD81-binding function.", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" }, { "database": "PubMed", "id": "22278231", "url": "https://glygen.org/publication/PubMed/22278231" } ] }, { "start_pos": 552, "end_pos": 552, "sequence_org": "C", "sequence_mut": "A", "comment": "Complete loss of infectivity.", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" }, { "database": "PubMed", "id": "22278231", "url": "https://glygen.org/publication/PubMed/22278231" } ] }, { "start_pos": 564, "end_pos": 564, "sequence_org": "C", "sequence_mut": "A", "comment": "Complete loss of infectivity and CD81-binding function.", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" }, { "database": "PubMed", "id": "22278231", "url": "https://glygen.org/publication/PubMed/22278231" } ] }, { "start_pos": 569, "end_pos": 569, "sequence_org": "C", "sequence_mut": "A", "comment": "Complete loss of infectivity. No effect on CD81-binding function. Loss of heterodimerization with E1.", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" }, { "database": "PubMed", "id": "22278231", "url": "https://glygen.org/publication/PubMed/22278231" } ] }, { "start_pos": 581, "end_pos": 581, "sequence_org": "C", "sequence_mut": "A", "comment": "Complete loss of infectivity. No effect on CD81-binding function. Loss of heterodimerization with E1.", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" }, { "database": "PubMed", "id": "22278231", "url": "https://glygen.org/publication/PubMed/22278231" } ] }, { "start_pos": 585, "end_pos": 585, "sequence_org": "C", "sequence_mut": "A", "comment": "Complete loss of infectivity. No effect on CD81-binding function. Loss of heterodimerization with E1.", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" }, { "database": "PubMed", "id": "22278231", "url": "https://glygen.org/publication/PubMed/22278231" } ] }, { "start_pos": 597, "end_pos": 597, "sequence_org": "C", "sequence_mut": "A", "comment": "Complete loss of infectivity. Reduced CD81-binding function.", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" }, { "database": "PubMed", "id": "22278231", "url": "https://glygen.org/publication/PubMed/22278231" } ] }, { "start_pos": 607, "end_pos": 607, "sequence_org": "C", "sequence_mut": "A", "comment": "Complete loss of infectivity. Complete loss of E2 expression probably due to the disruption of the global conformation of the protein.", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" }, { "database": "PubMed", "id": "22278231", "url": "https://glygen.org/publication/PubMed/22278231" } ] }, { "start_pos": 620, "end_pos": 620, "sequence_org": "C", "sequence_mut": "A", "comment": "Complete loss of infectivity. Reduced CD81-binding function.", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" }, { "database": "PubMed", "id": "22278231", "url": "https://glygen.org/publication/PubMed/22278231" } ] }, { "start_pos": 644, "end_pos": 644, "sequence_org": "C", "sequence_mut": "A", "comment": "Complete loss of infectivity. Complete loss of E2 expression probably due to the disruption of the global conformation of the protein.", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" }, { "database": "PubMed", "id": "22278231", "url": "https://glygen.org/publication/PubMed/22278231" } ] }, { "start_pos": 652, "end_pos": 652, "sequence_org": "C", "sequence_mut": "A", "comment": "Complete loss of infectivity. Reduced heterodimerization with E1. No effect on CD81-binding function.", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" }, { "database": "PubMed", "id": "22278231", "url": "https://glygen.org/publication/PubMed/22278231" } ] }, { "start_pos": 677, "end_pos": 677, "sequence_org": "C", "sequence_mut": "A", "comment": "Complete loss of infectivity. Reduced heterodimerization with E1. No effect on CD81-binding function.", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" }, { "database": "PubMed", "id": "22278231", "url": "https://glygen.org/publication/PubMed/22278231" } ] }, { "start_pos": 720, "end_pos": 720, "sequence_org": "V", "sequence_mut": "L", "comment": "Increases processing between E2 and p7.", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" }, { "database": "PubMed", "id": "15722527", "url": "https://glygen.org/publication/PubMed/15722527" } ] }, { "start_pos": 779, "end_pos": 779, "sequence_org": "K", "sequence_mut": "I", "comment": "Virus can no longer infect chimpanzee.", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" }, { "database": "PubMed", "id": "14504405", "url": "https://glygen.org/publication/PubMed/14504405" } ] }, { "start_pos": 781, "end_pos": 781, "sequence_org": 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"id": "16862121", "url": "https://glygen.org/publication/PubMed/16862121" } ] }, { "start_pos": 993, "end_pos": 993, "sequence_org": "C", "sequence_mut": "A", "comment": "Complete loss of NS2-NS3 cleavage.", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" }, { "database": "PubMed", "id": "8248148", "url": "https://glygen.org/publication/PubMed/8248148" }, { "database": "PubMed", "id": "16862121", "url": "https://glygen.org/publication/PubMed/16862121" } ] } ], "expression_tissue": [], "expression_disease": [], "species": [ { "name": "Hepatitis C virus (isolate H77)", "taxid": 63746, "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "common_name": "HCV", "glygen_name": "HCV-H77", "reference_species": "Hepatitis C virus (isolate H77) [63746]" } ], "gene": [ { "name": "", "url": "https://www.uniprot.org/uniprotkb/P27958", "locus": {} } ], "crossref": [ { "id": 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"https://www.ebi.ac.uk/interpro/entry/pfam/PF01538", "database": "Pfam", "categories": [ "Protein Classification", "Other" ] }, { "id": "PF01539", "url": "https://www.ebi.ac.uk/interpro/entry/pfam/PF01539", "database": "Pfam", "categories": [ "Protein Classification", "Other" ] }, { "id": "PF01542", "url": "https://www.ebi.ac.uk/interpro/entry/pfam/PF01542", "database": "Pfam", "categories": [ "Protein Classification", "Other" ] }, { "id": "PF01543", "url": "https://www.ebi.ac.uk/interpro/entry/pfam/PF01543", "database": "Pfam", "categories": [ "Protein Classification", "Other" ] }, { "id": "PF01560", "url": "https://www.ebi.ac.uk/interpro/entry/pfam/PF01560", "database": "Pfam", "categories": [ "Protein Classification", "Other" ] }, { "id": "PF02907", "url": "https://www.ebi.ac.uk/interpro/entry/pfam/PF02907", "database": "Pfam", "categories": [ "Protein Classification", "Other" ] }, { "id": "PF07652", "url": "https://www.ebi.ac.uk/interpro/entry/pfam/PF07652", "database": "Pfam", "categories": [ "Protein Classification", "Other" ] }, { "id": "PF08300", "url": "https://www.ebi.ac.uk/interpro/entry/pfam/PF08300", "database": "Pfam", "categories": [ "Protein Classification", "Other" ] }, { "id": "PF08301", "url": "https://www.ebi.ac.uk/interpro/entry/pfam/PF08301", "database": "Pfam", "categories": [ "Protein Classification", "Other" ] }, { "id": "PF12941", "url": "https://www.ebi.ac.uk/interpro/entry/pfam/PF12941", "database": "Pfam", "categories": [ "Protein Classification", "Other" ] }, { "id": "PF22027", "url": "https://www.ebi.ac.uk/interpro/entry/pfam/PF22027", "database": "Pfam", "categories": [ "Protein Classification", "Other" ] }, { "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958", "database": "UniProtKB", "categories": [ "Protein" ] }, { "id": "P27958-1", "url": "https://www.uniprot.org/uniprotkb/P27958-1", "database": "UniProtKB", "categories": [ "Protein" ] }, { "id": "hcv", "url": "https://www.viprbrc.org/brc/home.spg?decorator=flavi_hcv", "database": "ViPR", "categories": [ "Organism-specific" ] } ], "sequence": { "sequence": "MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKARRPEGRTWAQPGYPWPLYGNEGCGWAGWLLSPRGSRPSWGPTDPRRRSRNLGKVIDTLTCGFADLMGYIPLVGAPLGGAARALAHGVRVLEDGVNYATGNLPGCSFSIFLLALLSCLTVPASAYQVRNSSGLYHVTNDCPNSSVVYEAADAILHTPGCVPCVREGNASRCWVAVTPTVATRDGKLPTTQLRRHIDLLVGSATLCSALYVGDLCGSVFLVGQLFTFSPRHHWTTQDCNCSIYPGHITGHRMAWNMMMNWSPTAALVVAQLLRIPQAIMDMIAGAHWGVLAGIKYFSMVGNWAKVLVVLLLFAGVDAETHVTGGNAGRTTAGLVGLLTPGAKQNIQLINTNGSWHINSTALNCNESLNTGWLAGLFYQHKFNSSGCPERLASCRRLTDFAQGWGPISYANGSGLDERPYCWHYPPRPCGIVPAKSVCGPVYCFTPSPVVVGTTDRSGAPTYSWGANDTDVFVLNNTRPPLGNWFGCTWMNSTGFTKVCGAPPCVIGGVGNNTLLCPTDCFRKYPEATYSRCGSGPRITPRCMVDYPYRLWHYPCTINYTIFKVRMYVGGVEHRLEAACNWTRGERCDLEDRDRSELSPLLLSTTQWQVLPCSFTTLPALSTGLIHLHQNIVDVQYLYGVGSSIASWAIKWEYVVLLFLLLADARVCSCLWMMLLISQAEAALENLVILNAASLAGTHGLVSFLVFFCFAWYLKGRWVPGAVYALYGMWPLLLLLLALPQRAYALDTEVAASCGGVVLVGLMALTLSPYYKRYISWCMWWLQYFLTRVEAQLHVWVPPLNVRGGRDAVILLTCVVHPALVFDITKLLLAIFGPLWILQASLLKVPYFVRVQGLLRICALARKIAGGHYVQMAIIKLGALTGTCVYNHLAPLRDWAHNGLRDLAVAVEPVVFSRMETKLITWGADTAACGDIINGLPVSARRGQEILLGPADGMVSKGWRLLAPITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVSTATQTFLATCINGVCWTVYHGAGTRTIASPKGPVIQTYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPTGHAVGLFRAAVCTRGVAKAVDFIPVENLETTMRSPVFTDNSSPPAVPQSFQVAHLHAPTGSGKSTKVPAAYAAKGYKVLVLNPSVAATLGFGAYMSKAHGVDPNIRTGVRTITTGSPITYSTYGKFLADAGCSGGAYDIIICDECHSTDATSISGIGTVLDQAETAGARLVVLATATPPGSVTVSHPNIEEVALSTTGEIPFYGKAIPLEVIKGGRHLIFCHSKKKCDELAAKLVALGINAVAYYRGLDVSVIPTSGDVVVVSTDALMTGFTGDFDSVIDCNTCVTQTVDFSLDPTFTIETTTLPQDAVSRTQRRGRTGRGKPGIYRFVAPGERPSGMFDSSVLCECYDAGCAWYELTPAETTVRLRAYMNTPGLPVCQDHLGFWEGVFTGLTHIDAHFLSQTKQSGENFPYLVAYQATVCARAQAPPPSWDQMRKCLIRLKPTLHGPTPLLYRLGAVQNEVTLTHPITKYIMTCMSADLEVVTSTWVLVGGVLAALAAYCLSTGCVVIVGRIVLSGKPAIIPDREVLYQEFDEMEECSQHLPYIEQGMMLAEQFKQKALGLLQTASRHAEVITPAVQTNWQKLEVFWAKHMWNFISGIQYLAGLSTLPGNPAIASLMAFTAAVTSPLTTGQTLLFNILGGWVAAQLAAPGAATAFVGAGLAGAALDSVGLGKVLVDILAGYGAGVAGALVAFKIMSGEVPSTEDLVNLLPAILSPGALAVGVVFASILRRRVGPGEGAVQWMNRLIAFASRGNHVSPTHYVPESDAAARVTAILSSLTVTQLLRRLHQWISSECTTPCSGSWLRDIWDWICEVLSDFKTWLKAKLMPQLPGIPFVSCQRGYRGVWRGDGIMHTRCHCGAEITGHVKNGTMRIVGPRTCKNMWSGTFFINAYTTGPCTPLPAPNYKFALWRVSAEEYVEIRRVGDFHYVSGMTTDNLKCPCQIPSPEFFTELDGVRLHRFAPPCKPLLREEVSFRVGLHEYPVGSQLPCEPEPDVAVLTSMLTDPSHITAEAAGRRLARGSPPSMASSSASQLSAPSLKATCTANHDSPDAELIEANLLWRQEMGGNITRVESENKVVILDSFDPLVAEEDEREVSVPAEILRKSRRFAPALPVWARPDYNPLLVETWKKPDYEPPVVHGCPLPPPRSPPVPPPRKKRTVVLTESTLPTALAELATKSFGSSSTSGITGDNTTTSSEPAPSGCPPDSDVESYSSMPPLEGEPGDPDLSDGSWSTVSSGADTEDVVCCSMSYSWTGALVTPCAAEEQKLPINALSNSLLRHHNLVYSTTSRSACQRKKKVTFDRLQVLDSHYQDVLKEVKAAASKVKANLLSVEEACSLAPPHSAKSKFGYGAKDVRCHARKAVAHINSVWKDLLEDSVTPIDTTIMAKNEVFCVQPEKGGRKPARLIVFPDLGVRVCEKMALYDVVSKLPLAVMGSSYGFQYSPGQRVEFLVQAWKSKKTPMGLSYDTRCFDSTVTESDIRTEEAIYQCCDLDPQARVAIKSLTERLYVGGPLTNSRGENCGYRRCRASRVLTTSCGNTLTRYIKARAACRAAGLQDCTMLVCGDDLVVICESAGVQEDAASLRAFTEAMTRYSAPPGDPPQPEYDLELITSCSSNVSVAHDGAGKRVYYLTRDPTTPLARAAWETARHTPVNSWLGNIIMFAPTLWARMILMTHFFSVLIARDQLEQALNCEIYGACYSIEPLDLPPIIQRLHGLSAFSLHSYSPGEINRVAACLRKLGVPPLRAWRHRAWSVRARLLARGGKAAICGKYLFNWAVRTKLKLTPITAAGRLDLSGWFTAGYSGGDIYHSVSHARPRWFWFCLLLLAAGVGIYLLPNR", "length": 3011, "header": "sp|P27958-1|POLG_HCV77 Isoform 1 of Genome polyprotein OS=Hepatitis C virus (isolate H77) OX=63746 GN= PE=1 SV=3 CANONICAL=P27958-1" }, "isoforms": [ { "isoform_ac": "P27958-1", "url": "https://www.uniprot.org/uniprotkb/P27958/entry#P27958-1", "sequence": { "sequence": "MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKARRPEGRTWAQPGYPWPLYGNEGCGWAGWLLSPRGSRPSWGPTDPRRRSRNLGKVIDTLTCGFADLMGYIPLVGAPLGGAARALAHGVRVLEDGVNYATGNLPGCSFSIFLLALLSCLTVPASAYQVRNSSGLYHVTNDCPNSSVVYEAADAILHTPGCVPCVREGNASRCWVAVTPTVATRDGKLPTTQLRRHIDLLVGSATLCSALYVGDLCGSVFLVGQLFTFSPRHHWTTQDCNCSIYPGHITGHRMAWNMMMNWSPTAALVVAQLLRIPQAIMDMIAGAHWGVLAGIKYFSMVGNWAKVLVVLLLFAGVDAETHVTGGNAGRTTAGLVGLLTPGAKQNIQLINTNGSWHINSTALNCNESLNTGWLAGLFYQHKFNSSGCPERLASCRRLTDFAQGWGPISYANGSGLDERPYCWHYPPRPCGIVPAKSVCGPVYCFTPSPVVVGTTDRSGAPTYSWGANDTDVFVLNNTRPPLGNWFGCTWMNSTGFTKVCGAPPCVIGGVGNNTLLCPTDCFRKYPEATYSRCGSGPRITPRCMVDYPYRLWHYPCTINYTIFKVRMYVGGVEHRLEAACNWTRGERCDLEDRDRSELSPLLLSTTQWQVLPCSFTTLPALSTGLIHLHQNIVDVQYLYGVGSSIASWAIKWEYVVLLFLLLADARVCSCLWMMLLISQAEAALENLVILNAASLAGTHGLVSFLVFFCFAWYLKGRWVPGAVYALYGMWPLLLLLLALPQRAYALDTEVAASCGGVVLVGLMALTLSPYYKRYISWCMWWLQYFLTRVEAQLHVWVPPLNVRGGRDAVILLTCVVHPALVFDITKLLLAIFGPLWILQASLLKVPYFVRVQGLLRICALARKIAGGHYVQMAIIKLGALTGTCVYNHLAPLRDWAHNGLRDLAVAVEPVVFSRMETKLITWGADTAACGDIINGLPVSARRGQEILLGPADGMVSKGWRLLAPITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVSTATQTFLATCINGVCWTVYHGAGTRTIASPKGPVIQTYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPTGHAVGLFRAAVCTRGVAKAVDFIPVENLETTMRSPVFTDNSSPPAVPQSFQVAHLHAPTGSGKSTKVPAAYAAKGYKVLVLNPSVAATLGFGAYMSKAHGVDPNIRTGVRTITTGSPITYSTYGKFLADAGCSGGAYDIIICDECHSTDATSISGIGTVLDQAETAGARLVVLATATPPGSVTVSHPNIEEVALSTTGEIPFYGKAIPLEVIKGGRHLIFCHSKKKCDELAAKLVALGINAVAYYRGLDVSVIPTSGDVVVVSTDALMTGFTGDFDSVIDCNTCVTQTVDFSLDPTFTIETTTLPQDAVSRTQRRGRTGRGKPGIYRFVAPGERPSGMFDSSVLCECYDAGCAWYELTPAETTVRLRAYMNTPGLPVCQDHLGFWEGVFTGLTHIDAHFLSQTKQSGENFPYLVAYQATVCARAQAPPPSWDQMRKCLIRLKPTLHGPTPLLYRLGAVQNEVTLTHPITKYIMTCMSADLEVVTSTWVLVGGVLAALAAYCLSTGCVVIVGRIVLSGKPAIIPDREVLYQEFDEMEECSQHLPYIEQGMMLAEQFKQKALGLLQTASRHAEVITPAVQTNWQKLEVFWAKHMWNFISGIQYLAGLSTLPGNPAIASLMAFTAAVTSPLTTGQTLLFNILGGWVAAQLAAPGAATAFVGAGLAGAALDSVGLGKVLVDILAGYGAGVAGALVAFKIMSGEVPSTEDLVNLLPAILSPGALAVGVVFASILRRRVGPGEGAVQWMNRLIAFASRGNHVSPTHYVPESDAAARVTAILSSLTVTQLLRRLHQWISSECTTPCSGSWLRDIWDWICEVLSDFKTWLKAKLMPQLPGIPFVSCQRGYRGVWRGDGIMHTRCHCGAEITGHVKNGTMRIVGPRTCKNMWSGTFFINAYTTGPCTPLPAPNYKFALWRVSAEEYVEIRRVGDFHYVSGMTTDNLKCPCQIPSPEFFTELDGVRLHRFAPPCKPLLREEVSFRVGLHEYPVGSQLPCEPEPDVAVLTSMLTDPSHITAEAAGRRLARGSPPSMASSSASQLSAPSLKATCTANHDSPDAELIEANLLWRQEMGGNITRVESENKVVILDSFDPLVAEEDEREVSVPAEILRKSRRFAPALPVWARPDYNPLLVETWKKPDYEPPVVHGCPLPPPRSPPVPPPRKKRTVVLTESTLPTALAELATKSFGSSSTSGITGDNTTTSSEPAPSGCPPDSDVESYSSMPPLEGEPGDPDLSDGSWSTVSSGADTEDVVCCSMSYSWTGALVTPCAAEEQKLPINALSNSLLRHHNLVYSTTSRSACQRKKKVTFDRLQVLDSHYQDVLKEVKAAASKVKANLLSVEEACSLAPPHSAKSKFGYGAKDVRCHARKAVAHINSVWKDLLEDSVTPIDTTIMAKNEVFCVQPEKGGRKPARLIVFPDLGVRVCEKMALYDVVSKLPLAVMGSSYGFQYSPGQRVEFLVQAWKSKKTPMGLSYDTRCFDSTVTESDIRTEEAIYQCCDLDPQARVAIKSLTERLYVGGPLTNSRGENCGYRRCRASRVLTTSCGNTLTRYIKARAACRAAGLQDCTMLVCGDDLVVICESAGVQEDAASLRAFTEAMTRYSAPPGDPPQPEYDLELITSCSSNVSVAHDGAGKRVYYLTRDPTTPLARAAWETARHTPVNSWLGNIIMFAPTLWARMILMTHFFSVLIARDQLEQALNCEIYGACYSIEPLDLPPIIQRLHGLSAFSLHSYSPGEINRVAACLRKLGVPPLRAWRHRAWSVRARLLARGGKAAICGKYLFNWAVRTKLKLTPITAAGRLDLSGWFTAGYSGGDIYHSVSHARPRWFWFCLLLLAAGVGIYLLPNR", "length": 3011, "header": "sp|P27958-1|POLG_HCV77 Isoform 1 of Genome polyprotein OS=Hepatitis C virus (isolate H77) OX=63746 GN= PE=1 SV=3 CANONICAL=P27958-1" }, "locus": {} } ], "glycosylation": [ { "glytoucan_ac": "", "type": "O-linked", "subtype": "", "prediction_tool_list": [ { "label": "isoglyp", "url": "https://github.com/jonmohl/ISOGlyP" } ], "site_category": "predicted", "site_category_dict": { "predicted": true }, "site_seq": "", "relation": "attached", "comment": "", "icn3d_view": {}, "start_pos": 110, "start_aa": "Thr", "end_pos": 110, "end_aa": "Thr", "residue": "Thr", "site_lbl": "Thr110", "evidence": [ { "id": "GLY_001154", "database": "GlyGen", "url": "https://data.glygen.org/GLY_001154" } ] }, { "glytoucan_ac": "", "type": "N-linked", "subtype": "", "prediction_tool_list": [], "site_category": "reported", "site_category_dict": { "reported": true }, "site_seq": "N", "relation": "attached", "comment": "N-linked (GlcNAc...) asparagine", "icn3d_view": {}, "start_pos": 196, 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by host", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "site_lbl": "Ser53" }, { "start_pos": 99, "end_pos": 99, "kinase_uniprot_canonical_ac": "", "kinase_gene_name": "", "residue": "Ser", "comment": "Phosphoserine; by host", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "site_lbl": "Ser99" } ], "glycation": [], "keywords": [ "enzyme", "glycoprotein", "glycoprotein_reported", "glycoprotein_reported_with_glycan", "glycoprotein_predicted" ], "publication": [ { "title": "Analysis of the glycosylation sites of hepatitis C virus (HCV) glycoprotein E1 and the influence of E1 glycans on the formation of the HCV glycoprotein complex.", "journal": "The Journal of general virology", "date": "1999", "authors": "Meunier JC, Fournillier A, Choukhi A, Cahour A, Cocquerel L, Dubuisson J, Wychowski C", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958#ptm_processing" }, { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "10211957", "url": "https://glygen.org/publication/PubMed/10211957" } ] }, { "title": "Inhibition of the interferon-inducible protein kinase PKR by HCV E2 protein.", "journal": "Science", "date": "1999", "authors": "Taylor D R, Shi S T, Romano P R, Barber G N, Lai M M", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "10390359", "url": "https://glygen.org/publication/PubMed/10390359" } ] }, { "title": "Identification of the major phosphorylation site of the hepatitis C virus H strain NS5A protein as serine 2321.", "journal": "The Journal of biological chemistry", "date": "1999", "authors": "Reed KE, Rice CM", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "10488152", "url": "https://glygen.org/publication/PubMed/10488152" } ] }, { "title": "Hepatitis C virus NS5A protein modulates transcription through a novel cellular transcription factor SRCAP.", "journal": "J. Biol. Chem.", "date": "2000", "authors": "Ghosh AK, Majumder M, Steele R, Yaciuk P, Chrivia J, Ray R, Ray RB", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "10702287", "url": "https://glygen.org/publication/PubMed/10702287" } ] }, { "title": "Properties of the hepatitis C virus core protein: a structural protein that modulates cellular processes.", "journal": "J. Viral Hepat.", "date": "2000", "authors": "McLauchlan J", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "10718937", "url": "https://glygen.org/publication/PubMed/10718937" } ] }, { "title": "Charged residues in the transmembrane domains of hepatitis C virus glycoproteins play a major role in the processing, subcellular localization, and assembly of these envelope proteins.", "journal": "J. Virol.", "date": "2000", "authors": "Cocquerel L, Wychowski C, Minner F, Penin F, Dubuisson J", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "10729138", "url": "https://glygen.org/publication/PubMed/10729138" } ] }, { "title": "Interaction between complement receptor gC1qR and hepatitis C virus core protein inhibits T-lymphocyte proliferation.", "journal": "The Journal of clinical investigation", "date": "2000-11", "authors": "Kittlesen D J, Chianese-Bullock K A, Yao Z Q, Braciale T J, Hahn Y S", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "11086025", "url": "https://glygen.org/publication/PubMed/11086025" } ] }, { "title": "The transmembrane domain of the hepatitis C virus E2 glycoprotein is required for correct folding of the E1 glycoprotein and native complex formation.", "journal": "Virology", "date": "2001", "authors": "Patel J, Patel A H, McLauchlan J", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "11145889", "url": "https://glygen.org/publication/PubMed/11145889" } ] }, { "title": "Conservation of the conformation and positive charges of hepatitis C virus E2 envelope glycoprotein hypervariable region 1 points to a role in cell attachment.", "journal": "J. Virol.", "date": "2001", "authors": "Penin F, Combet C, Germanidis G, Frainais P O, Del\u00e9age G, Pawlotsky J M", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "11356980", "url": "https://glygen.org/publication/PubMed/11356980" } ] }, { "title": "Synthesis of a novel hepatitis C virus protein by ribosomal frameshift.", "journal": "EMBO J.", "date": "2001", "authors": "Xu Z, Choi J, Yen T S, Lu W, Strohecker A, Govindarajan S, Chien D, Selby M J, Ou J", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "11447125", "url": "https://glygen.org/publication/PubMed/11447125" } ] }, { "title": "Functional analysis of hepatitis C virus E2 glycoproteins and virus-like particles reveals structural dissimilarities between different forms of E2.", "journal": "The Journal of general virology", "date": "2001-08", "authors": "Owsianka Ania, Clayton Reginald F, Loomis-Price Lawrence D, McKeating Jane A, Patel Arvind H", "evidence": [ { "database": "IEDB", "id": "51371", "url": "https://www.iedb.org/epitope/51371" } ], "reference": [ { "type": "PubMed", "id": "11457993", "url": "https://glygen.org/publication/PubMed/11457993" } ] }, { "title": "Determinants for membrane association of the hepatitis C virus RNA-dependent RNA polymerase.", "journal": "J. Biol. Chem.", "date": "2001", "authors": "Schmidt-Mende J, Bieck E, Hugle T, Penin F, Rice C M, Blum H E, Moradpour D", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "11557752", "url": "https://glygen.org/publication/PubMed/11557752" } ] }, { "title": "The domains required to direct core proteins of hepatitis C virus and GB virus-B to lipid droplets share common features with plant oleosin proteins.", "journal": "J. Biol. Chem.", "date": "2002", "authors": "Hope R Graham, Murphy Denis J, McLauchlan John", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "11706032", "url": "https://glygen.org/publication/PubMed/11706032" } ] }, { "title": "An amino-terminal amphipathic alpha-helix mediates membrane association of the hepatitis C virus nonstructural protein 5A.", "journal": "J. Biol. Chem.", "date": "2002", "authors": "Brass Volker, Bieck Elke, Montserret Roland, W\u00f6lk Benno, Hellings Jan Albert, Blum Hubert E, Penin Fran\u00e7ois, Moradpour Darius", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "11744739", "url": "https://glygen.org/publication/PubMed/11744739" } ] }, { "title": "Hepatitis C virus (HCV) NS5A binds RNA-dependent RNA polymerase (RdRP) NS5B and modulates RNA-dependent RNA polymerase activity.", "journal": "J. Biol. Chem.", "date": "2002", "authors": "Shirota Yukihiro, Luo Hong, Qin Weiping, Kaneko Shuichi, Yamashita Tatsuya, Kobayashi Kenichi, Murakami Seishi", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "11801599", "url": "https://glygen.org/publication/PubMed/11801599" } ] }, { "title": "Solution structure and backbone dynamics of an engineered arginine-rich subdomain 2 of the hepatitis C virus NS3 RNA helicase.", "journal": "J. Mol. Biol.", "date": "2001", "authors": "Liu D, Wang Y S, Gesell J J, Wyss D F", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "11846566", "url": "https://glygen.org/publication/PubMed/11846566" } ] }, { "title": "Subcellular localization and topology of the p7 polypeptide of hepatitis C virus.", "journal": "J. Virol.", "date": "2002", "authors": "Carr\u00e8re-Kremer S\u00e9verine, Montpellier-Pala Claire, Cocquerel Laurence, Wychowski Czeslaw, Penin Fran\u00e7ois, Dubuisson Jean", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "11907211", "url": "https://glygen.org/publication/PubMed/11907211" } ] }, { "title": "Mapping and characterization of B cell linear epitopes in the conservative regions of hepatitis C virus envelope glycoproteins.", "journal": "Journal of viral hepatitis", "date": "2002-05", "authors": "Olenina L V, Nikolaeva L I, Sobolev B N, Blokhina N P, Archakov A I, Kolesanova E F", "evidence": [ { "database": "IEDB", "id": "2899", "url": "https://www.iedb.org/epitope/2899" }, { "database": "IEDB", "id": "38404", "url": "https://www.iedb.org/epitope/38404" }, { "database": "IEDB", "id": "39697", "url": "https://www.iedb.org/epitope/39697" }, { "database": "IEDB", "id": "61621", "url": "https://www.iedb.org/epitope/61621" }, { "database": "IEDB", "id": "63882", "url": "https://www.iedb.org/epitope/63882" } ], "reference": [ { "type": "PubMed", "id": "12010504", "url": "https://glygen.org/publication/PubMed/12010504" } ] }, { "title": "Expression of hepatitis C virus proteins induces distinct membrane alterations including a candidate viral replication complex.", "journal": "Journal of virology", "date": "2002-06", "authors": "Egger Denise, W\u00f6lk Benno, Gosert Rainer, Bianchi Leonardo, Blum Hubert E, Moradpour Darius, Bienz Kurt", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "12021330", "url": "https://glygen.org/publication/PubMed/12021330" } ] }, { "title": "Topological changes in the transmembrane domains of hepatitis C virus envelope glycoproteins.", "journal": "EMBO J.", "date": "2002", "authors": "Cocquerel Laurence, Op de Beeck Anne, Lambot Michel, Roussel Juliette, Delgrange David, Pillez Andr\u00e9, Wychowski Czeslaw, Penin Fran\u00e7ois, Dubuisson Jean", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "12065403", "url": "https://glygen.org/publication/PubMed/12065403" } ] }, { "title": "Structural features of envelope proteins on hepatitis C virus-like particles as determined by anti-envelope monoclonal antibodies and CD81 binding.", "journal": "Virology", "date": "2002-06-20", "authors": "Triyatni Miriam, Vergalla John, Davis Anthony R, Hadlock Kenneth G, Foung Steven K H, Liang T Jake", "evidence": [ { "database": "IEDB", "id": "51371", "url": "https://www.iedb.org/epitope/51371" }, { "database": "IEDB", "id": "61037", "url": "https://www.iedb.org/epitope/61037" } ], "reference": [ { "type": "PubMed", "id": "12093180", "url": "https://glygen.org/publication/PubMed/12093180" } ] }, { "title": "The human scavenger receptor class B type I is a novel candidate receptor for the hepatitis C virus.", "journal": "The EMBO journal", "date": "2002-10-01", "authors": "Scarselli Elisa, Ansuini Helenia, Cerino Raffaele, Roccasecca Rosa Maria, Acali Stefano, Filocamo Gessica, Traboni Cinzia, Nicosia Alfredo, Cortese Riccardo, Vitelli Alessandra", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "12356718", "url": "https://glygen.org/publication/PubMed/12356718" } ] }, { "title": "Pyrrolidine-5,5-trans-lactams. 2. The use of X-ray crystal structure data in the optimization of P3 and P4 substituents.", "journal": "Org. Lett.", "date": "2002", "authors": "Andrews David M, Chaignot Helene, Coomber Barry A, Good Andrew C, Hind S Lucy, Johnson Martin R, Jones Paul S, Mills Gail, Robinson J Ed, Skarzynski Tadeusz, Slater Martin J, Somers Donald O'N", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "12465917", "url": "https://glygen.org/publication/PubMed/12465917" } ] }, { "title": "The p7 protein of hepatitis C virus forms an ion channel that is blocked by the antiviral drug, Amantadine.", "journal": "FEBS Lett.", "date": "2003", "authors": "Griffin Stephen D C, Beales Lucy P, Clarke Dean S, Worsfold Oliver, Evans Stephen D, Jaeger Joachim, Harris Mark P G, Rowlands David J", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "12560074", "url": "https://glygen.org/publication/PubMed/12560074" } ] }, { "title": "Protein-protein interactions between hepatitis C virus nonstructural proteins.", "journal": "J. Virol.", "date": "2003", "authors": "Dimitrova Maria, Imbert Isabelle, Kieny Marie Paule, Schuster Catherine", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "12692242", "url": "https://glygen.org/publication/PubMed/12692242" } ] }, { "title": "Topology of the membrane-associated hepatitis C virus protein NS4B.", "journal": "J. Virol.", "date": "2003", "authors": "Lundin Marika, Monn\u00e9 Magnus, Widell Anders, Von Heijne Gunnar, Persson Mats A A", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "12692244", "url": "https://glygen.org/publication/PubMed/12692244" } ] }, { "title": "Identification of the hepatitis C virus RNA replication complex in Huh-7 cells harboring subgenomic replicons.", "journal": "J. Virol.", "date": "2003", "authors": "Gosert Rainer, Egger Denise, Lohmann Volker, Bartenschlager Ralf, Blum Hubert E, Bienz Kurt, Moradpour Darius", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "12692249", "url": "https://glygen.org/publication/PubMed/12692249" } ] }, { "title": "The hepatitis C virus p7 protein forms an ion channel that is inhibited by long-alkyl-chain iminosugar derivatives.", "journal": "Proceedings of the National Academy of Sciences of the United States of America", "date": "2003-05-13", "authors": "Pavlovi\u0107 Davor, Neville David C A, Argaud Olivier, Blumberg Baruch, Dwek Raymond A, Fischer Wolfgang B, Zitzmann Nicole", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "12719519", "url": "https://glygen.org/publication/PubMed/12719519" } ] }, { "title": "Cell entry of hepatitis C virus requires a set of co-receptors that include the CD81 tetraspanin and the SR-B1 scavenger receptor.", "journal": "The Journal of biological chemistry", "date": "2003-10-24", "authors": "Bartosch Birke, Vitelli Alessandra, Granier Christelle, Goujon Caroline, Dubuisson Jean, Pascale Simona, Scarselli Elisa, Cortese Riccardo, Nicosia Alfredo, Cosset Fran\u00e7ois-Lo\u00efc", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "12913001", "url": "https://glygen.org/publication/PubMed/12913001" } ] }, { "title": "CD81-dependent binding of hepatitis C virus E1E2 heterodimers.", "journal": "Journal of virology", "date": "2003-10", "authors": "Cocquerel Laurence, Kuo Chiung-Chi, Dubuisson Jean, Levy Shoshana", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "12970454", "url": "https://glygen.org/publication/PubMed/12970454" } ] }, { "title": "The p7 polypeptide of hepatitis C virus is critical for infectivity and contains functionally important genotype-specific sequences.", "journal": "Proceedings of the National Academy of Sciences of the United States of America", "date": "2003", "authors": "Sakai A, Claire MS, Faulk K, Govindarajan S, Emerson SU, Purcell RH, Bukh J", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "14504405", "url": "https://glygen.org/publication/PubMed/14504405" } ] }, { "title": "Induction of FAS ligand expression in a human hepatoblastoma cell line by HCV core protein.", "journal": "Virus research", "date": "2003-11", "authors": "Ruggieri A, Murdolo M, Rapicetta M", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", 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"title": "Attachment and Postattachment Receptors Important for Hepatitis C Virus Infection and Cell-to-Cell Transmission.", "journal": "Journal of virology", "date": "2017-07-01", "authors": "Fan Huahao, Qiao Luhua, Kang Kyung-Don, Fan Junfen, Wei Wensheng, Luo Guangxiang", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "28404852", "url": "https://glygen.org/publication/PubMed/28404852" } ] }, { "title": "Hepatitis C Virus Exploits Death Receptor 6-mediated Signaling Pathway to Facilitate Viral Propagation.", "journal": "Scientific reports", "date": "2017", "authors": "Luong TTD, Tran GVQ, Shin DJ, Lim YS, Hwang SB", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "28743875", "url": "https://glygen.org/publication/PubMed/28743875" } ] }, { "title": "Hepatitis C virus p7 induces mitochondrial depolarization of isolated liver mitochondria.", "journal": "Molecular medicine reports", "date": "2017-12", "authors": "You Deok-Gyun, Lee Hye-Ra, Kim Won-Ki, Kim Hyung Jung, Lee Gi Young, Yoo Young Do", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "29039530", "url": "https://glygen.org/publication/PubMed/29039530" } ] }, { "title": "A protein coevolution method uncovers critical features of the Hepatitis C Virus fusion mechanism.", "journal": "PLoS pathogens", "date": "2018-03", "authors": "Douam Florian, Fusil Floriane, Enguehard Margot, Dib Linda, Nadalin Francesca, Schwaller Lo\u00efc, Hrebikova Gabriela, Mancip Jimmy, Mailly Laurent, Montserret Roland, Ding Qiang, Maisse Carine, Carlot Emilie, Xu Ke, Verhoeyen Els, Baumert Thomas F, Ploss Alexander, Carbone Alessandra, Cosset Fran\u00e7ois-Lo\u00efc, Lavillette Dimitri", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "29505618", "url": "https://glygen.org/publication/PubMed/29505618" } ] }, { "title": "Regulation of Apolipoprotein E Trafficking by Hepatitis C Virus-Induced Autophagy.", "journal": "Journal of virology", "date": "2018-07-15", "authors": "Kim Ja Yeon, Ou Jing-Hsiung James", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "29695434", "url": "https://glygen.org/publication/PubMed/29695434" } ] }, { "title": "Hepatitis C virus NS4B induces the degradation of TRIF to inhibit TLR3-mediated interferon signaling pathway.", "journal": "PLoS pathogens", "date": "2018-05", "authors": "Liang Yisha, Cao Xuezhi, Ding Qiang, Zhao Yanan, He Zhenliang, Zhong Jin", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "29782532", "url": "https://glygen.org/publication/PubMed/29782532" } ] }, { "title": "Hepatitis C Virus Modulates Solute carrier family 3 member 2 for Viral Propagation.", "journal": "Scientific reports", "date": "2018-10-19", "authors": "Nguyen Ngan N T, Lim Yun-Sook, Nguyen Lap P, Tran Si C, Luong Trang T D, Nguyen Tram T T, Pham Hang T, Mai Han N, Choi Jae-Woong, Han Sang-Seop, Hwang Soon B", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "30341327", "url": "https://glygen.org/publication/PubMed/30341327" } ] }, { "title": "SPSB2 inhibits hepatitis C virus replication by targeting NS5A for ubiquitination and degradation.", "journal": "PLoS ONE", "date": "2019", "authors": "Wang M, Wang Y, Liu Y, Wang H, Xin X, Li J, Hao Y, Han L, Yu F, Zheng C, Shen C", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "31344133", "url": "https://glygen.org/publication/PubMed/31344133" } ] }, { "title": "Palmitoylation of Hepatitis C Virus NS2 Regulates Its Subcellular Localization and NS2-NS3 Autocleavage.", "journal": "Journal of virology", "date": "2019", "authors": "Wu MJ, Shanmugam S, Welsch C, Yi M", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "31597774", "url": "https://glygen.org/publication/PubMed/31597774" } ] }, { "title": "PACSIN2 Interacts with Nonstructural Protein 5A and Regulates Hepatitis C Virus Assembly.", "journal": "Journal of virology", "date": "2020", "authors": "Nguyen LP, Tran SC, Suetsugu S, Lim YS, Hwang SB", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "31801866", "url": "https://glygen.org/publication/PubMed/31801866" } ] }, { "title": "Viroporins and inflammasomes: A key to understand virus-induced inflammation.", "journal": "Int. J. Biochem. Cell Biol.", "date": "2020", "authors": "Farag N S, Breitinger U, Breitinger H G, El Azizi M A", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "32156572", "url": "https://glygen.org/publication/PubMed/32156572" } ] }, { "title": "A conserved epitope III on hepatitis C virus E2 protein has alternate conformations facilitating cell binding or virus neutralization.", "journal": "Proceedings of the National Academy of Sciences of the United States of America", "date": "2021-07-13", "authors": "Deng Lu, Hernandez Nancy, Zhong Lilin, Holcomb David D, Yan Hailing, Virata Maria Luisa, Tarafdar Sreya, Xu Yanqun, He Yong, Struble Evi, Alter Harvey J, Zhang Pei", "evidence": [ { "database": "IEDB", "id": "1597553", "url": "https://www.iedb.org/epitope/1597553" } ], "reference": [ { "type": "PubMed", "id": "34260404", "url": "https://glygen.org/publication/PubMed/34260404" } ] }, { "title": "Hepatitis C virus RNA is 5'-capped with flavin adenine dinucleotide.", "journal": "Nature", "date": "2023-07", "authors": "Sherwood Anna V, Rivera-Rangel Lizandro R, Ryberg Line A, Larsen Helena S, Anker Klara M, Costa Rui, V\u00e5gb\u00f8 Cathrine B, Jakljevi\u010d Eva, Pham Long V, Fernandez-Antunez Carlota, Indrisiunaite Gabriele, Podolska-Charlery Agnieszka, Grothen Julius E R, Langvad Nicklas W, Fossat Nicolas, Offersgaard Anna, Al-Chaer Amal, Nielsen Louise, Ku\u015bnierczyk Anna, S\u00f8lund Christina, Weis Nina, Gottwein Judith M, Holmbeck Kenn, Bottaro Sandro, Ramirez Santseharay, Bukh Jens, Scheel Troels K H, Vinther Jeppe", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "37407817", "url": "https://glygen.org/publication/PubMed/37407817" } ] }, { "title": "Reverse vaccinology approach for identification of epitopes from E1 protein as peptide vaccine against HCV: A proof of concept.", "journal": "Vaccine", "date": "2024-10-24", "authors": "Meshram Rohan, Kolte Baban, Gacche Rajesh", "evidence": [ { "database": "IEDB", "id": "2266086", "url": "https://www.iedb.org/epitope/2266086" }, { "database": "IEDB", "id": "2266330", "url": "https://www.iedb.org/epitope/2266330" }, { "database": "IEDB", "id": "2266337", "url": "https://www.iedb.org/epitope/2266337" }, { "database": "IEDB", "id": "2266375", "url": "https://www.iedb.org/epitope/2266375" } ], "reference": [ { "type": "PubMed", "id": "38971664", "url": "https://glygen.org/publication/PubMed/38971664" } ] }, { "title": "Expression and identification of hepatitis C virus polyprotein cleavage products.", "journal": "Journal of virology", "date": "1993", "authors": "Grakoui A, Wychowski C, Lin C, Feinstone SM, Rice CM", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "7679746", "url": "https://glygen.org/publication/PubMed/7679746" } ] }, { "title": "A central region in the hepatitis C virus NS4A protein allows formation of an active NS3-NS4A serine proteinase complex in vivo and in vitro.", "journal": "J. Virol.", "date": "1995", "authors": "Lin C, Thomson J A, Rice C M", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "7769699", "url": "https://glygen.org/publication/PubMed/7769699" } ] }, { "title": "Kinetic and structural analyses of hepatitis C virus polyprotein processing.", "journal": "Journal of virology", "date": "1994", "authors": "Bartenschlager R, Ahlborn-Laake L, Mous J, Jacobsen H", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "8035505", "url": "https://glygen.org/publication/PubMed/8035505" } ] }, { "title": "Both NS3 and NS4A are required for proteolytic processing of hepatitis C virus nonstructural proteins.", "journal": "Journal of virology", "date": "1994", "authors": "Failla C, Tomei L, De Francesco R", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "8189513", "url": "https://glygen.org/publication/PubMed/8189513" } ] }, { "title": "A second hepatitis C virus-encoded proteinase.", "journal": "Proceedings of the National Academy of Sciences of the United States of America", "date": "1993", "authors": "Grakoui A, McCourt DW, Wychowski C, Feinstone SM, Rice CM", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "8248148", "url": "https://glygen.org/publication/PubMed/8248148" } ] }, { "title": "Characterization of the hepatitis C virus-encoded serine proteinase: determination of proteinase-dependent polyprotein cleavage sites.", "journal": "Journal of virology", "date": "1993", "authors": "Grakoui A, McCourt DW, Wychowski C, Feinstone SM, Rice CM", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "8386278", "url": "https://glygen.org/publication/PubMed/8386278" } ] }, { "title": "Interaction between hepatitis C virus core protein and E1 envelope protein.", "journal": "J. Virol.", "date": "1996", "authors": "Lo S Y, Selby M J, Ou J H", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "8764026", "url": "https://glygen.org/publication/PubMed/8764026" } ] }, { "title": "Crystal structure of the hepatitis C virus NS3 protease domain complexed with a synthetic NS4A cofactor peptide.", "journal": "Cell", "date": "1996", "authors": "Kim JL, Morgenstern KA, Lin C, Fox T, Dwyer MD, Landro JA, Chambers SP, Markland W, Lepre CA, O'Malley ET, Harbeson SL, Rice CM, Murcko MA, Caron PR, Thomson JA", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "8861917", "url": "https://glygen.org/publication/PubMed/8861917" } ] }, { "title": "Characterization of the nuclear localization signal and subcellular distribution of hepatitis C virus nonstructural protein NS5A.", "journal": "Gene", "date": "1996", "authors": "Ide Y, Zhang L, Chen M, Inchauspe G, Bahl C, Sasaguri Y, Padmanabhan R", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "8982089", "url": "https://glygen.org/publication/PubMed/8982089" } ] }, { "title": "Hepatitis C virus core protein shows a cytoplasmic localization and associates to cellular lipid storage droplets.", "journal": "Proc. Natl. Acad. Sci. U.S.A.", "date": "1997", "authors": "Barba G, Harper F, Harada T, Kohara M, Goulinet S, Matsuura Y, Eder G, Schaff Z, Chapman M J, Miyamura T, Br\u00e9chot C", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "9037030", "url": "https://glygen.org/publication/PubMed/9037030" } ] }, { "title": "Structure of the hepatitis C virus RNA helicase domain.", "journal": "Nat. Struct. Biol.", "date": "1997", "authors": "Yao N, Hesson T, Cable M, Hong Z, Kwong A D, Le H V, Weber P C", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "9187654", "url": "https://glygen.org/publication/PubMed/9187654" } ] }, { "title": "Transmission of hepatitis C by intrahepatic inoculation with transcribed RNA.", "journal": "Science", "date": "1997", "authors": "Kolykhalov A A, Agapov E V, Blight K J, Mihalik K, Feinstone S M, Rice C M", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "9228008", "url": "https://glygen.org/publication/PubMed/9228008" } ] }, { "title": "Transcripts from a single full-length cDNA clone of hepatitis C virus are infectious when directly transfected into the liver of a chimpanzee.", "journal": "Proc. Natl. Acad. Sci. U.S.A.", "date": "1997", "authors": "Yanagi M, Purcell RH, Emerson SU, Bukh J", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "9238047", "url": "https://glygen.org/publication/PubMed/9238047" } ] }, { "title": "Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding.", "journal": "Structure", "date": "1998", "authors": "Kim J L, Morgenstern K A, Griffith J P, Dwyer M D, Thomson J A, Murcko M A, Lin C, Caron P R", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "reference": [ { "type": "PubMed", "id": "9493270", "url": "https://glygen.org/publication/PubMed/9493270" } ] }, { "title": "Inefficient recognition of autologous viral sequences by intrahepatic hepatitis C virus-specific cytotoxic T lymphocytes in chronically infected subjects.", "journal": "Virology", "date": "1998-11-10", "authors": "Giuggio V M, Bonkovsky H L, Smith J, Rothman A L", "evidence": [ { "database": "IEDB", "id": "12926", "url": "https://www.iedb.org/epitope/12926" }, { "database": "IEDB", "id": "53437", "url": "https://www.iedb.org/epitope/53437" } ], "reference": [ { "type": "PubMed", "id": "9813209", "url": "https://glygen.org/publication/PubMed/9813209" } ] } ], "pathway": [], "orthologs": [ { "uniprot_canonical_ac": "P26662-1", "protein_name": "Genome polyprotein", "gene_name": "", "tax_id": 11116, "organism": "Hepatitis C virus (isolate Japanese)", "sequence": { "sequence": "MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKARRPEGRTWAQPGYPWPLYGNEGMGWAGWLLSPRGSRPSWGPTDPRRRSRNLGKVIDTLTCGFADLMGYIPLVGAPLGGAARALAHGVRVLEDGVNYATGNLPGCSFSIFLLALLSCLTIPASAYEVRNVSGIYHVTNDCSNSSIVYEAADMIMHTPGCVPCVRESNFSRCWVALTPTLAARNSSIPTTTIRRHVDLLVGAAALCSAMYVGDLCGSVFLVSQLFTFSPRRYETVQDCNCSIYPGHVSGHRMAWDMMMNWSPTTALVVSQLLRIPQAVVDMVAGAHWGVLAGLAYYSMVGNWAKVLIVMLLFAGVDGHTHVTGGRVASSTQSLVSWLSQGPSQKIQLVNTNGSWHINRTALNCNDSLQTGFIAALFYAHRFNASGCPERMASCRPIDEFAQGWGPITHDMPESSDQRPYCWHYAPRPCGIVPASQVCGPVYCFTPSPVVVGTTDRFGAPTYSWGENETDVLLLSNTRPPQGNWFGCTWMNSTGFTKTCGGPPCNIGGVGNNTLVCPTDCFRKHPEATYTKCGSGPWLTPRCMVDYPYRLWHYPCTVNFTVFKVRMYVGGVEHRLNAACNWTRGERCDLEDRDRSELSPLLLSTTEWQILPCSFTTLPALSTGLIHLHRNIVDVQYLYGIGSAVVSFAIKWEYILLLFLLLADARVCACLWMMLLIAQAEATLENLVVLNAASVAGAHGLLSFLVFFCAAWYIKGRLVPGAAYALYGVWPLLLLLLALPPRAYAMDREMAASCGGAVFVGLVLLTLSPYYKVFLARLIWWLQYFITRAEAHLQVWVPPLNVRGGRDAIILLTCAVHPELIFDITKLLLAILGPLMVLQAGITRVPYFVRAQGLIRACMLVRKVAGGHYVQMAFMKLAALTGTYVYDHLTPLRDWAHAGLRDLAVAVEPVVFSDMETKLITWGADTAACGDIISGLPVSARRGKEILLGPADSFGEQGWRLLAPITAYSQQTRGLLGCIITSLTGRDKNQVDGEVQVLSTATQSFLATCVNGVCWTVYHGAGSKTLAGPKGPITQMYTNVDQDLVGWPAPPGARSMTPCTCGSSDLYLVTRHADVVPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPSGHVVGIFRAAVCTRGVAKAVDFIPVESMETTMRSPVFTDNSSPPAVPQTFQVAHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGAYMSKAHGIEPNIRTGVRTITTGGPITYSTYCKFLADGGCSGGAYDIIICDECHSTDSTTILGIGTVLDQAETAGARLVVLATATPPGSITVPHPNIEEVALSNTGEIPFYGKAIPIEAIKGGRHLIFCHSKKKCDELAAKLTGLGLNAVAYYRGLDVSVIPTSGDVVVVATDALMTGFTGDFDSVIDCNTCVTQTVDFSLDPTFTIETTTLPQDAVSRAQRRGRTGRGRSGIYRFVTPGERPSGMFDSSVLCECYDAGCAWYELTPAETSVRLRAYLNTPGLPVCQDHLEFWESVFTGLTHIDAHFLSQTKQAGDNLPYLVAYQATVCARAQAPPPSWDQMWKCLIRLKPTLHGPTPLLYRLGAVQNEVTLTHPITKYIMACMSADLEVVTSTWVLVGGVLAALAAYCLTTGSVVIVGRIILSGRPAVIPDREVLYQEFDEMEECASHLPYIEQGMQLAEQFKQKALGLLQTATKQAEAAAPVVESKWRALEVFWAKHMWNFISGIQYLAGLSTLPGNPAIASLMAFTASITSPLTTQNTLLFNILGGWVAAQLAPPSAASAFVGAGIAGAAVGSIGLGKVLVDILAGYGAGVAGALVAFKVMSGEMPSTEDLVNLLPAILSPGALVVGVVCAAILRRHVGPGEGAVQWMNRLIAFASRGNHVSPTHYVPESDAAARVTQILSSLTITQLLKRLHQWINEDCSTPCSGSWLKDVWDWICTVLSDFKTWLQSKLLPRLPGLPFLSCQRGYKGVWRGDGIMQTTCPCGAQITGHVKNGSMRIVGPKTCSNTWHGTFPINAYTTGPCTPSPAPNYSRALWRVAAEEYVEVTRVGDFHYVTGMTTDNVKCPCQVPAPEFFTEVDGVRLHRYAPVCKPLLREEVVFQVGLNQYLVGSQLPCEPEPDVAVLTSMLTDPSHITAETAKRRLARGSPPSLASSSASQLSAPSLKATCTTHHDSPDADLIEANLLWRQEMGGNITRVESENKVVILDSFDPIRAVEDEREISVPAEILRKPRKFPPALPIWARPDYNPPLLESWKDPDYVPPVVHGCPLPSTKAPPIPPPRRKRTVVLTESTVSSALAELATKTFGSSGSSAVDSGTATGPPDQASDDGDKGSDVESYSSMPPLEGEPGDPDLSDGSWSTVSGEAGEDVVCCSMSYTWTGALITPCAAEESKLPINPLSNSLLRHHSMVYSTTSRSASLRQKKVTFDRLQVLDDHYRDVLKEMKAKASTVKARLLSIEEACKLTPPHSAKSKFGYGAKDVRSLSSRAVNHIRSVWEDLLEDTETPIDTTIMAKNEVFCVQPEKGGRKPARLIVFPDLGVRVCEKMALYDVVSTLPQAVMGPSYGFQYSPGQRVEFLVNTWKSKKCPMGFSYDTRCFDSTVTENDIRTEESIYQCCDLAPEARQAIRSLTERLYVGGPLTNSKGQNCGYRRCRASGVLTTSCGNTLTCYLKATAACRAAKLQDCTMLVNGDDLVVICESAGTQEDAAALRAFTEAMTRYSAPPGDPPQPEYDLELITSCSSNVSVAHDASGKRVYYLTRDPTTPLARAAWETVRHTPVNSWLGNIIMYAPTLWARMILMTHFFSILLAQEQLEKALDCQIYGACYSIEPLDLPQIIERLHGLSAFSLHSYSPGEINRVASCLRKLGVPPLRVWRHRARSVRAKLLSQGGRAATCGKYLFNWAVKTKLKLTPIPAASQLDLSGWFVAGYNGGDIYHSLSRARPRWFMLCLLLLSVGVGIYLLPNR", "length": 3010 }, "evidence": [ { "id": "GLY_000258", "url": "https://data.glygen.org/GLY_000258", "database": "GlyGen" } ], "glygen_name": "HCV-Japanese", "common_name": "HCV" } ], "go_annotation": { "categories": [ { "name": "Biological Process", "total": 24, "go_terms": [ { "name": "negative regulation of protein secretion", "id": "GO:0050709", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0050709", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "translocation of peptides or proteins into host cell cytoplasm", "id": "GO:0044053", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0044053", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "negative regulation of transcription by RNA polymerase II", "id": "GO:0000122", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0000122", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "DNA-templated transcription", "id": "GO:0006351", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0006351", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "proteolysis", "id": "GO:0006508", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0006508", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "monoatomic ion transmembrane transport", "id": "GO:0034220", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0034220", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "symbiont-mediated transformation of host cell", "id": "GO:0019087", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0019087", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "symbiont-mediated suppression of host type I interferon-mediated signaling pathway", "id": "GO:0039502", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0039502", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity", "id": "GO:0039563", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0039563", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "positive regulation of cytokinesis", "id": "GO:0032467", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0032467", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "symbiont-mediated activation of host autophagy", "id": "GO:0039520", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0039520", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "viral RNA genome replication", "id": "GO:0039694", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0039694", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "positive regulation of hexokinase activity", "id": "GO:1903301", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:1903301", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "viral translational frameshifting", "id": "GO:0075523", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0075523", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity", "id": "GO:0039545", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0039545", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint", "id": "GO:0039645", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0039645", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "fusion of virus membrane with host endosome membrane", "id": "GO:0039654", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0039654", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "clathrin-dependent endocytosis of virus by host cell", "id": "GO:0075512", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0075512", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "entry receptor-mediated virion attachment to host cell", "id": "GO:0098670", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0098670", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "adhesion receptor-mediated virion attachment to host cell", "id": "GO:0098671", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0098671", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "viral capsid assembly", "id": "GO:0019069", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0019069", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "symbiont-mediated suppression of host TRAF-mediated signal transduction", "id": "GO:0039527", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0039527", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "symbiont-mediated perturbation of host cellular process", "id": "GO:0044068", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0044068", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT activity", "id": "GO:0039562", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0039562", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" } ] }, { "name": "Cellular Component", "total": 11, "go_terms": [ { "name": "host cell nucleus", "id": "GO:0042025", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0042025", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "endoplasmic reticulum-Golgi intermediate compartment membrane", "id": "GO:0033116", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0033116", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "viral envelope", "id": "GO:0019031", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0019031", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "ribonucleoprotein complex", "id": "GO:1990904", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:1990904", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "viral nucleocapsid", "id": "GO:0019013", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0019013", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "host cell perinuclear region of cytoplasm", "id": "GO:0044220", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0044220", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "virion membrane", "id": "GO:0055036", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0055036", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "host cell plasma membrane", "id": "GO:0020002", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0020002", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "host cell endoplasmic reticulum membrane", "id": "GO:0044167", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0044167", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "host cell lipid droplet", "id": "GO:0044186", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0044186", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "host cell mitochondrial membrane", "id": "GO:0044191", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0044191", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" } ] }, { "name": "Molecular Function", "total": 13, "go_terms": [ { "name": "RNA-directed RNA polymerase activity", "id": "GO:0003968", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0003968", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "RNA binding", "id": "GO:0003723", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0003723", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "serine-type endopeptidase activity", "id": "GO:0004252", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0004252", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "ATP binding", "id": "GO:0005524", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005524", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "zinc ion binding", "id": "GO:0008270", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0008270", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "SH3 domain binding", "id": "GO:0017124", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0017124", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "ATP hydrolysis activity", "id": "GO:0016887", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0016887", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "structural molecule activity", "id": "GO:0005198", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005198", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "channel activity", "id": "GO:0015267", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0015267", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "kinase binding", "id": "GO:0019900", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0019900", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "cysteine-type endopeptidase activity", "id": "GO:0004197", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0004197", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "RNA helicase activity", "id": "GO:0003724", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0003724", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" }, { "name": "Toll-like receptor 2 binding", "id": "GO:0035663", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0035663", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "pmid": "" } ] } ] }, "pro_annotation": [], "site_annotation": [ { "start_pos": 1213, "end_pos": 1215, "annotation": "n_glycosylation_sequon" }, { "start_pos": 196, "end_pos": 198, "annotation": "n_glycosylation_sequon" }, { "start_pos": 2041, "end_pos": 2043, "annotation": "n_glycosylation_sequon" }, { "start_pos": 209, "end_pos": 211, "annotation": "n_glycosylation_sequon" }, { "start_pos": 2240, "end_pos": 2242, "annotation": "n_glycosylation_sequon" }, { "start_pos": 234, "end_pos": 236, "annotation": "n_glycosylation_sequon" }, { "start_pos": 2364, "end_pos": 2366, "annotation": "n_glycosylation_sequon" }, { "start_pos": 2789, "end_pos": 2791, "annotation": "n_glycosylation_sequon" }, { "start_pos": 305, "end_pos": 307, "annotation": "n_glycosylation_sequon" }, { "start_pos": 325, "end_pos": 327, "annotation": "n_glycosylation_sequon" }, { "start_pos": 417, "end_pos": 419, "annotation": "n_glycosylation_sequon" }, { "start_pos": 423, "end_pos": 425, "annotation": "n_glycosylation_sequon" }, { "start_pos": 430, "end_pos": 432, "annotation": "n_glycosylation_sequon" }, { "start_pos": 448, "end_pos": 450, "annotation": "n_glycosylation_sequon" }, { "start_pos": 476, "end_pos": 478, "annotation": "n_glycosylation_sequon" }, { "start_pos": 532, "end_pos": 534, "annotation": "n_glycosylation_sequon" }, { "start_pos": 540, "end_pos": 542, "annotation": "n_glycosylation_sequon" }, { "start_pos": 556, "end_pos": 558, "annotation": "n_glycosylation_sequon" }, { "start_pos": 576, "end_pos": 578, "annotation": "n_glycosylation_sequon" }, { "start_pos": 623, "end_pos": 625, "annotation": "n_glycosylation_sequon" }, { "start_pos": 645, "end_pos": 647, "annotation": "n_glycosylation_sequon" } ], "ptm_annotation": [ { "annotation": "Highly N-glycosylated.", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" }, { "database": "PubMed", "id": "14990718", "url": "https://glygen.org/publication/PubMed/14990718" }, { "database": "PubMed", "id": "18187336", "url": "https://glygen.org/publication/PubMed/18187336" } ] }, { "annotation": "Palmitoylated. This modification may play a role in its polymerization or in protein-protein interactions.", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" }, { "database": "PubMed", "id": "16731940", "url": "https://glygen.org/publication/PubMed/16731940" } ] }, { "annotation": "Palmitoylation is required for NS2/3 autoprocessing and E2 recruitment to membranes.", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" }, { "database": "PubMed", "id": "31597774", "url": "https://glygen.org/publication/PubMed/31597774" } ] }, { "annotation": "Specific enzymatic cleavages in vivo yield mature proteins (PubMed:15722527, PubMed:8035505, PubMed:8189513, PubMed:8386278). The structural proteins, core, E1, E2 and p7 are produced by proteolytic processing by host signal peptidases (PubMed:15247249). The core protein precursor is synthesized as a 23 kDa, which is retained in the ER membrane through the hydrophobic signal peptide (By similarity). Cleavage by the signal peptidase releases the 21 kDa mature core protein (By similarity). The cleavage of the core protein precursor occurs between aminoacids 176 and 188 but the exact cleavage site is not known (By similarity). Some degraded forms of the core protein appear as well during the course of infection (By similarity). The other proteins (p7, NS2, NS3, NS4A, NS4B, NS5A and NS5B) are cleaved by the viral proteases (PubMed:15247249, PubMed:7679746, PubMed:8035505, PubMed:8189513, PubMed:8386278). Autoprocessing between NS2 and NS3 is mediated by the NS2 cysteine protease catalytic domain and regulated by the NS3 N-terminal domain (By similarity).", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" }, { "database": "PubMed", "id": "8035505", "url": "https://glygen.org/publication/PubMed/8035505" }, { "database": "PubMed", "id": "7679746", "url": "https://glygen.org/publication/PubMed/7679746" }, { "database": "PubMed", "id": "15247249", "url": "https://glygen.org/publication/PubMed/15247249" }, { "database": "PubMed", "id": "8386278", "url": "https://glygen.org/publication/PubMed/8386278" }, { "database": "PubMed", "id": "15722527", "url": "https://glygen.org/publication/PubMed/15722527" }, { "database": "PubMed", "id": "8189513", "url": "https://glygen.org/publication/PubMed/8189513" } ] }, { "annotation": "The N-terminus is phosphorylated by host PRK2/PKN2.", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" }, { "database": "PubMed", "id": "15364941", "url": "https://glygen.org/publication/PubMed/15364941" } ] }, { "annotation": "Ubiquitinated (PubMed:25683609, PubMed:27194766). Ubiquitination, most probably at Lys-2350, mediated by host IFI27 and SKP2 leads to proteasomal degradation, restricting viral infection (PubMed:27194766). Ubiquitination by host TRIM22 leads to interruption of viral replication (PubMed:25683609).", "evidence": [ { "database": "UniProtKB", "id": "P27958", "url": "https://www.uniprot.org/uniprotkb/P27958" }, { "database": "PubMed", "id": "27194766", "url": "https://glygen.org/publication/PubMed/27194766" }, { "database": "PubMed", "id": "25683609", "url": "https://glygen.org/publication/PubMed/25683609" } ] } ], "interactions": [], "reactions": [], "reaction_participants": [], "reaction_enzymes": [], "biomarkers": [], "structures": [], "lectin_list": [], "domain_list": [ { "evidence": [ { "id": "P27958", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "ann_type": "Motif_Annotation", "uniprotkb_annotation": "DECH box", "eco_id": "ECO_0000250", "start_pos": 1316, "end_pos": 1319, "start_aa": "Asp", "end_aa": "His", "glycosite_overlap": "" }, { "evidence": [ { "id": "P27958", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprotkb/P27958" }, { "id": "PRU00541", "database": "PROSITE", "url": "https://prosite.expasy.org/PRU00541" } ], "ann_type": "Domain_Extent_Annotation", "uniprotkb_annotation": "Helicase ATP-binding", "eco_id": "ECO_0000255", "start_pos": 1217, "end_pos": 1369, "start_aa": "Pro", "end_aa": "Thr", "glycosite_overlap": "" }, { "evidence": [ { "id": "P27958", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprotkb/P27958" } ], "ann_type": "Motif_Annotation", "uniprotkb_annotation": "Nuclear localization signal", "eco_id": "ECO_0000250", "start_pos": 5, "end_pos": 13, "start_aa": "Pro", "end_aa": "Arg", "glycosite_overlap": "" }, { "evidence": [ { "id": "P27958", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprotkb/P27958" }, { "id": "PRU01030", "database": "PROSITE", "url": "https://prosite.expasy.org/PRU01030" } ], "ann_type": "Domain_Extent_Annotation", "uniprotkb_annotation": "Peptidase C18", "eco_id": "ECO_0000255", "start_pos": 899, "end_pos": 1026, "start_aa": "Leu", "end_aa": "Leu", 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