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UniProtKB - O39929 (POLG_HCVED)

Entry version 164 (25 May 2022)
Sequence version 3 (23 Jan 2007)
Previous versions | rss
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Protein

Genome polyprotein

Gene
N/A
Organism
Hepatitis C virus genotype 4a (isolate ED43) (HCV)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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 (By similarity).

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).

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 TNF-induced 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 (By similarity).

Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity).

Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity).

By similarityCurated

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 (By similarity).

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 (By similarity).

E1/E2 heterodimer binds host apolipoproteins such as APOB and ApoE thereby forming a lipo-viro-particle (LVP) (By similarity).

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) (By similarity).

The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity).

E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity).

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).

By similarity

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 (By similarity).

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 (By similarity).

The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity).

This interaction is probably promoted via the up-regulation of cellular autophagy by the virus (By similarity).

E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity).

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) (By similarity).

The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity).

E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity).

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).

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 dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity).

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 (By similarity).

The interaction between E2 and host amino acid transporter complex formed by SLC3A2 and SLC7A5/LAT1 may facilitate viral entry into host cell (By similarity).

By similarity

Ion channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (By similarity).

Regulates the host cell secretory pathway, which induces the intracellular retention of viral glycoproteins and favors assembly of viral particles (By similarity).

Creates a pore in acidic organelles and releases Ca2+ and H+ in the cytoplasm of infected cells, leading to a productive viral infection (By similarity).

High levels of cytoplasmic Ca2+ may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). This ionic imbalance induces the assembly of the inflammasome complex, which triggers the maturation of pro-IL-1beta into IL-1beta through the action of caspase-1 (By similarity).

Targets also host mitochondria and induces mitochondrial depolarization (By similarity).

In addition of its role as a viroporin, acts as a lipid raft adhesion factor (By similarity).

By similarityCurated

Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (By similarity).

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 (By similarity).

By similarity

Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (By similarity).

NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B-NS5A and NS5A-NS5B (By similarity).

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 (By similarity).

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 (By similarity).

Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (By similarity).

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 (By similarity).

Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (By similarity).

By similarity

Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity).

This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity).

NS4B self-interaction contributes to its function in membranous web formation (By similarity).

Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3-mediated interferon signaling (By similarity).

Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (By similarity).

By similarity

Phosphorylated protein that is indispensable for viral replication and assembly (By similarity).

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 (By similarity).

Zinc is essential for RNA-binding (By similarity).

Participates in the viral particle production as a result of its interaction with the mature viral 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 (By similarity).

Prevents BIN1-induced apoptosis (By similarity).

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 (By similarity).

Modulates TNFRSF21/DR6 signaling pathway for viral propagation (By similarity).

By similarity

RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication.

By similarity

Miscellaneous

Viral particle assembly takes place at the surface of ER-derived membranes in close proximity to lipid droplets. NS2 associates with E1/E2 glycoproteins, NS3 and NS5A, which interacts with the viral RNA and core protein to promote genome encapsidation. The nucleocapsid buds at the ER membrane where E1/E2 glycoproteins are anchored and afterward associate with nascent lipid droplet to acquire APOE and APOC. Secretion of viral particles is probably regulated by viroporin p7.Curated
Cell culture adaptation of the virus leads to mutations in NS5A, reducing its inhibitory effect on replication.Curated
Exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding.By similarity

Caution

The core gene probably also codes for alternative reading frame proteins (ARFPs). Many functions depicted for the core protein might belong to the ARFPs.Curated

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protease NS2:
Zn2+By similarityNote: Activity of protease NS2 is dependent on zinc ions and completely inhibited by EDTA. This is probably due to the fact that NS2 protease activity needs NS3 N-terminus that binds a zinc atom (active region NS2-3).By similarity
RNA-directed RNA polymerase:
Mg2+By similarityNote: Binds 2 magnesium ion that constitute a dinuclear catalytic metal center.By similarity
Serine protease/helicase NS3:
Zn2+By similarity, Mg2+By similarityNote: Binds 1 zinc ion, which has a structural role (By similarity). The magnesium ion is essential for the helicase activity (By similarity).By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by the antiviral drug hexamethylene amiloride (By similarity). Inhibition by amantadine appears to be genotype-dependent (By similarity). Also inhibited by long-alkyl-chain iminosugar derivatives (By similarity).By similarity
Activity is up-regulated by PRK2/PKN2-mediated phosphorylation.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei952For protease NS2 activity; shared with dimeric partnerPROSITE-ProRule annotation1
Active sitei972For protease NS2 activity; shared with dimeric partnerPROSITE-ProRule annotation1
Active sitei993For protease NS2 activity; shared with dimeric partnerPROSITE-ProRule annotation1
Active sitei1083Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1107Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi1123Zinc 1; structural; required for NS3 protease activity and NS2/3 auto-cleavage activityPROSITE-ProRule annotation1
Metal bindingi1125Zinc 1; structural; required for NS3 protease activity and NS2/3 auto-cleavage activityPROSITE-ProRule annotation1
Active sitei1165Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Metal bindingi1171Zinc 1; structural; required for NS3 protease activity and NS2/3 auto-cleavage activityPROSITE-ProRule annotation1
Metal bindingi1175Zinc 1; structural; required for NS3 protease activity and NS2/3 auto-cleavage activityPROSITE-ProRule annotation1
Metal bindingi1237Magnesium 1; catalytic; for NS3 helicase activityBy similarity1
Metal bindingi1317Magnesium 1; catalytic; for NS3 helicase activityBy similarity1
Metal bindingi2029Zinc 2; structuralBy similarity1
Metal bindingi2031Zinc 2; structuralBy similarity1
Metal bindingi2052Zinc 2; structuralBy similarity1
Metal bindingi2637Magnesium 2; catalytic; for RNA-directed RNA polymerase activityBy similarity1
Metal bindingi2735Magnesium 2; catalytic; for RNA-directed RNA polymerase activityBy similarity1
Metal bindingi2736Magnesium 2; catalytic; for RNA-directed RNA polymerase activityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi1230 – 1237ATPPROSITE-ProRule annotation8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHelicase, Hydrolase, Ion channel, Multifunctional enzyme, Nucleotidyltransferase, Protease, Ribonucleoprotein, RNA-binding, RNA-directed RNA polymerase, Serine protease, Thiol protease, Transferase, Viral ion channel, Viral nucleoprotein
Biological processActivation of host autophagy by virus, Apoptosis, Clathrin-mediated endocytosis of virus by host, Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, G1/S host cell cycle checkpoint dysregulation by virus, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host MAVS by virus, Inhibition of host RLR pathway by virus, Inhibition of host STAT1 by virus, Inhibition of host TRAFs by virus, Interferon antiviral system evasion, Ion transport, Modulation of host cell cycle by virus, Transcription, Transcription regulation, Transport, Viral attachment to host cell, Viral immunoevasion, Viral penetration into host cytoplasm, Viral RNA replication, Virus endocytosis by host, Virus entry into host cell
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.4.21.98, 17004

Protein family/group databases

MEROPS protease database

More...MEROPSi		S29.001

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 11 chains:
Core protein precursor
Alternative name(s):
Capsid protein C
p23
Mature core protein
Alternative name(s):
p21
Envelope glycoprotein E1
Alternative name(s):
gp32
gp35
Envelope glycoprotein E2
Alternative name(s):
NS1
gp68
gp70
Viroporin p7
Protease NS2 (EC:3.4.22.-By similarity)
Short name:
p23
Alternative name(s):
Non-structural protein 2
Short name:
NS2
Serine protease/helicase NS3 (EC:3.4.21.98By similarity, EC:3.6.1.15By similarity, EC:3.6.4.13By similarity)
Alternative name(s):
Hepacivirin
NS3 helicaseBy similarity
NS3 proteaseBy similarity
NS3P
Viroporin p70
Non-structural protein 4A
Short name:
NS4A
Alternative name(s):
p8
Non-structural protein 4B
Short name:
NS4B
Alternative name(s):
p27
Non-structural protein 5A
Short name:
NS5A
Alternative name(s):
p56/58
RNA-directed RNA polymerase (EC:2.7.7.48By similarity)
Alternative name(s):
NS5B
p68
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHepatitis C virus genotype 4a (isolate ED43) (HCV)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri356418 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiViruses › Riboviria › Orthornavirae › Kitrinoviricota › Flasuviricetes › Amarillovirales › Flaviviridae › Hepacivirus ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>Virus hostiHomo sapiens (Human) [TaxID: 9606]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000007415 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Genome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini2 – 168CytoplasmicSequence analysisAdd BLAST167
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei169 – 189HelicalSequence analysisAdd BLAST21
Topological domaini190 – 358LumenalBy similarityAdd BLAST169
Transmembranei359 – 379HelicalBy similarityAdd BLAST21
Topological domaini380 – 725LumenalBy similarityAdd BLAST346
Transmembranei726 – 746HelicalBy similarityAdd BLAST21
Topological domaini747 – 757LumenalBy similarityAdd BLAST11
Transmembranei758 – 778HelicalBy similarityAdd BLAST21
Topological domaini779 – 782CytoplasmicSequence analysis4
Transmembranei783 – 803HelicalBy similarityAdd BLAST21
Topological domaini804 – 813LumenalBy similarity10
Transmembranei814 – 834HelicalBy similarityAdd BLAST21
Topological domaini835 – 881CytoplasmicBy similarityAdd BLAST47
Transmembranei882 – 902HelicalBy similarityAdd BLAST21
Topological domaini903 – 928LumenalBy similarityAdd BLAST26
Transmembranei929 – 949HelicalBy similarityAdd BLAST21
Topological domaini950 – 1657CytoplasmicBy similarityAdd BLAST708
Transmembranei1658 – 1678HelicalSequence analysisAdd BLAST21
Topological domaini1679 – 1805CytoplasmicSequence analysisAdd BLAST127
Transmembranei1806 – 1826HelicalSequence analysisAdd BLAST21
Topological domaini1827 – 1828LumenalBy similarity2
Transmembranei1829 – 1849HelicalSequence analysisAdd BLAST21
Topological domaini1850CytoplasmicSequence analysis1
Transmembranei1851 – 1871HelicalSequence analysisAdd BLAST21
Topological domaini1872 – 1881LumenalSequence analysis10
Transmembranei1882 – 1902HelicalSequence analysisAdd BLAST21
Topological domaini1903 – 1972CytoplasmicSequence analysisAdd BLAST70
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei1973 – 2002By similarityAdd BLAST30
Topological domaini2003 – 2987CytoplasmicBy similarityAdd BLAST985
Transmembranei2988 – 3008HelicalBy similarityAdd BLAST21

Keywords - Cellular componenti

Capsid protein, Host cell membrane, Host cytoplasm, Host endoplasmic reticulum, Host lipid droplet, Host membrane, Host mitochondrion, Host nucleus, Membrane, Viral envelope protein, Virion

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Keywords - Diseasei

Oncogene

Chemistry databases

DrugCentral

More...DrugCentrali		O39929

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved; by hostBy similarity
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004509002 – 3008Genome polyproteinAdd BLAST3007
ChainiPRO_00000455322 – 191Core protein precursorAdd BLAST190
ChainiPRO_00000455332 – 177Mature core proteinAdd BLAST176
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000045534178 – 191ER anchor for the core protein, removed in mature form by host signal peptidaseAdd BLAST14
ChainiPRO_0000045535192 – 383Envelope glycoprotein E1Add BLAST192
ChainiPRO_0000045536384 – 746Envelope glycoprotein E2Add BLAST363
ChainiPRO_0000045537747 – 809Viroporin p7Add BLAST63
ChainiPRO_0000045538810 – 1026Protease NS2PROSITE-ProRule annotationAdd BLAST217
ChainiPRO_00000455391027 – 1657Serine protease/helicase NS3Add BLAST631
ChainiPRO_00000455401658 – 1711Non-structural protein 4AAdd BLAST54
ChainiPRO_00000455411712 – 1972Non-structural protein 4BAdd BLAST261
ChainiPRO_00000455421973 – 2417Non-structural protein 5AAdd BLAST445
ChainiPRO_00000455432418 – 3008RNA-directed RNA polymeraseAdd BLAST591

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserine; by hostBy similarity1
Modified residuei53Phosphoserine; by hostBy similarity1
Modified residuei99Phosphoserine; by hostBy similarity1
Modified residuei116Phosphoserine; by hostBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi196N-linked (GlcNAc...) asparagine; by hostBy similarity1
Glycosylationi209N-linked (GlcNAc...) asparagine; by hostBy similarity1
Glycosylationi234N-linked (GlcNAc...) asparagine; by hostBy similarity1
Glycosylationi305N-linked (GlcNAc...) asparagine; by hostBy similarity1
Glycosylationi417N-linked (GlcNAc...) (high mannose) asparagine; by hostBy similarity1
Glycosylationi423N-linked (GlcNAc...) (high mannose) asparagine; by hostBy similarity1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi429 ↔ 553By similarity
Glycosylationi430N-linked (GlcNAc...) (high mannose) asparagine; by hostBy similarity1
Glycosylationi448N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi452 ↔ 459By similarity
Glycosylationi476N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi487 ↔ 495By similarity
Disulfide bondi504 ↔ 509By similarity
Glycosylationi533N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi557N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi565 ↔ 570By similarity
Disulfide bondi581 ↔ 585By similarity
Disulfide bondi597 ↔ 620By similarity
Disulfide bondi607 ↔ 644By similarity
Glycosylationi623N-linked (GlcNAc...) (high mannose) asparagine; by hostBy similarity1
Glycosylationi645N-linked (GlcNAc...) (high mannose) asparagine; by hostBy similarity1
Disulfide bondi652 ↔ 677By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi922S-palmitoyl cysteine; by hostBy similarity1
Lipidationi1972S-palmitoyl cysteine; by hostBy similarity1
Modified residuei2194Phosphoserine; by hostBy similarity1
Modified residuei2197Phosphoserine; by hostBy similarity1
Modified residuei2201Phosphoserine; by hostBy similarity1
Modified residuei2204Phosphoserine; by hostBy similarity1
Modified residuei2207Phosphoserine; by hostBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki2347Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei2446Phosphoserine; by hostBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Specific enzymatic cleavages in vivo yield mature proteins (By similarity). The structural proteins, core, E1, E2 and p7 are produced by proteolytic processing by host signal peptidases (By similarity). 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 (By similarity). Autoprocessing between NS2 and NS3 is mediated by the NS2 cysteine protease catalytic domain and regulated by the NS3 N-terminal domain (By similarity).By similarity
Phosphorylated by host PKC and PKA.By similarity
Ubiquitinated; mediated by UBE3A and leading to core protein subsequent proteasomal degradation.By similarity
Highly N-glycosylated.By similarity
Highly N-glycosylated.By similarity
Palmitoylation is required for NS2/3 autoprocessing and E2 recruitment to membranes.By similarity
Palmitoylated. This modification may play a role in its polymerization or in protein-protein interactions.By similarity
Phosphorylated on serines in a basal form termed p56 (By similarity). p58 is a hyperphosphorylated form of p56 (By similarity). p56 and p58 coexist in the cell in roughly equivalent amounts (By similarity). Hyperphosphorylation is dependent on the presence of NS4A (By similarity). Host CSNK1A1/CKI-alpha or RPS6KB1 kinases may be responsible for NS5A phosphorylation (By similarity).By similarity
Tyrosine phosphorylation is essential for the interaction with host SRC.By similarity
The N-terminus is phosphorylated by host PRK2/PKN2.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei177 – 178Cleavage; by host signal peptide peptidaseBy similarity2
Sitei191 – 192Cleavage; by host signal peptidaseBy similarity2
Sitei383 – 384Cleavage; by host signal peptidaseBy similarity2
Sitei746 – 747Cleavage; by host signal peptidase2
Sitei809 – 810Cleavage; by host signal peptidase2
Sitei1026 – 1027Cleavage; by protease NS2PROSITE-ProRule annotation2
Sitei1657 – 1658Cleavage; by serine protease NS3By similarity2
Sitei1711 – 1712Cleavage; by serine protease NS3By similarity2
Sitei1972 – 1973Cleavage; by serine protease NS3By similarity2
Sitei2417 – 2418Cleavage; by serine protease NS3By similarity2

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Isopeptide bond, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

PRoteomics IDEntifications database

More...PRIDEi		O39929

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homooligomer (By similarity).

Interacts with E1 (via C-terminus) (By similarity).

Interacts with the non-structural protein 5A (By similarity).

Interacts (via N-terminus) with host STAT1 (via SH2 domain); this interaction results in decreased STAT1 phosphorylation and ubiquitin-mediated proteasome-dependent STAT1 degradation, leading to decreased IFN-stimulated gene transcription (By similarity).

Interacts with host STAT3; this interaction constitutively activates STAT3 (By similarity).

Interacts with host LTBR receptor (By similarity).

Interacts with host TNFRSF1A receptor and possibly induces apoptosis (By similarity).

Interacts with host HNRPK (By similarity).

Interacts with host YWHAE (By similarity).

Interacts with host UBE3A/E6AP (By similarity).

Interacts with host DDX3X (By similarity).

Interacts with host APOA2 (By similarity).

Interacts with host RXRA protein (By similarity).

Interacts with host SP110 isoform 3/Sp110b; this interaction sequesters the transcriptional corepressor SP110 away from the nucleus (By similarity).

Interacts with host CREB3 nuclear transcription protein; this interaction triggers cell transformation (By similarity).

Interacts with host ACY3 (By similarity).

Interacts with host C1QR1 (By similarity).

Interacts with host RBM24; this interaction, which enhances the interaction of the mature core protein with 5'-UTR, may inhibit viral translation and favor replication (By similarity).

Interacts with host EIF2AK2/PKR; this interaction induces the autophosphorylation of EIF2AK2 (By similarity). Part of the viral assembly initiation complex composed of NS2, E1, E2, NS3, NS4A, NS5A and the mature core protein (By similarity).

By similarity

Forms a heterodimer with envelope glycoprotein E2 (By similarity).

Interacts with mature core protein (By similarity).

Interacts with protease NS2 (By similarity). The heterodimer E1/E2 interacts with host CLDN1; this interaction plays a role in viral entry into host cell (By similarity).

Interacts with host SPSB2 (via C-terminus) (By similarity). Part of the viral assembly initiation complex composed of NS2, E1, E2, NS3, NS4A, NS5A and the mature core protein (By similarity).

By similarity

Forms a heterodimer with envelope glycoprotein E1 (By similarity).

Interacts with host CD81 and SCARB1 receptors; these interactions play a role in viral entry into host cell (By similarity).

Interacts with host EIF2AK2/PKR; this interaction inhibits EIF2AK2 and probably allows the virus to evade the innate immune response (By similarity).

Interacts with host CD209/DC-SIGN and CLEC4M/DC-SIGNR (By similarity). Interact with host SPCS1; this interaction is essential for viral particle assembly (By similarity).

Interacts with protease NS2 (By similarity). The heterodimer E1/E2 interacts with host CLDN1; this interaction plays a role in viral entry into host cell (By similarity). Part of the viral assembly initiation complex composed of NS2, E1, E2, NS3, NS4A, NS5A and the mature core protein (By similarity).

Interacts with host SLC3A2/4F2hc; the interaction may facilitate viral entry into host cell (By similarity).

Interacts with human PLSCR1 (By similarity).

By similarity

Homohexamer (By similarity). Homoheptamer (By similarity).

Interacts with protease NS2 (By similarity).

By similarity

Homodimer (By similarity).

Interacts with host SPCS1; this interaction is essential for viral particle assembly (By similarity).

Interacts with envelope glycoprotein E1 (By similarity).

Interacts with envelope glycoprotein E2 (By similarity).

Interacts with viroporin p7 (By similarity).

Interacts with serine protease/helicase NS3 (By similarity). Part of the replication complex composed of NS2, NS3, NS4A, NS4B, NS5A and the RNA-directed RNA polymerase embedded in an ER-derived membranous web (By similarity). Part of the viral assembly initiation complex composed of NS2, E1, E2, NS3, NS4A, NS5A and the mature core protein (By similarity).

By similarity

Interacts with protease NS2 (By similarity).

Interacts with non-structural protein 4A; this interaction stabilizes the folding of NS3 serine protease (By similarity). NS3-NS4A interaction is essential for NS3 activation and allows membrane anchorage of the latter (By similarity). NS3/NS4A complex also prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity).

Interacts with host MAVS; this interaction leads to the cleavage and inhibition of host MAVS (By similarity).

Interacts with host TICAM1; this interaction leads to the cleavage and inhibition of host TICAM1 (By similarity).

Interacts with host TANK-binding kinase/TBK1; this interaction results in the inhibition of the association between TBK1 and IRF3, which leads to the inhibition of IRF3 activation (By similarity).

Interacts with host RBM24 (By similarity). Part of the replication complex composed of NS2, NS3, NS4A, NS4B, NS5A and the RNA-directed RNA polymerase embedded in an ER-derived membranous web (By similarity). Part of the viral assembly initiation complex composed of NS2, E1, E2, NS3, NS4A, NS5A and the mature core protein (By similarity).

By similarity

Interacts with NS3 serine protease; this interaction stabilizes the folding of NS3 serine protease (By similarity). NS3-NS4A interaction is essential for NS3 activation and allows membrane anchorage of the latter (By similarity).

Interacts with non-structural protein 5A (via N-terminus) (By similarity). Part of the replication complex composed of NS2, NS3, NS4A, NS4B, NS5A and the RNA-directed RNA polymerase embedded in an ER-derived membranous web (By similarity). Part of the viral assembly initiation complex composed of NS2, E1, E2, NS3, NS4A, NS5A and the mature core protein (By similarity).

By similarity

Homomultimer (By similarity).

Interacts with non-structural protein NS5A (By similarity).

Interacts with host PLA2G4C; this interaction likely initiates the recruitment of replication complexes to lipid droplets (By similarity).

Interacts with host STING; this interaction disrupts the interaction between STING and TBK1 thereby suppressing the interferon signaling (By similarity). Part of the replication complex composed of NS2, NS3, NS4A, NS4B, NS5A and the RNA-directed RNA polymerase embedded in an ER-derived membranous web (By similarity).

By similarity

Monomer (By similarity). Homodimer; dimerization is required for RNA-binding (By similarity).

Interacts with mature core protein (By similarity).

Interacts (via N-terminus) with non-structural protein 4A (By similarity).

Interacts with non-structural protein 4B (By similarity).

Interacts with RNA-directed RNA polymerase (By similarity). Part of the viral assembly initiation complex composed of NS2, E1, E2, NS3, NS4A, NS5A and the mature core protein (By similarity). Part of the replication complex composed of NS2, NS3, NS4A, NS4B, NS5A and the RNA-directed RNA polymerase (By similarity).

Interacts with host GRB2 (By similarity).

Interacts with host BIN1 (By similarity).

Interacts with host PIK3R1 (By similarity).

Interacts with host SRCAP (By similarity).

Interacts with host FKBP8 (By similarity).

Interacts with host VAPB (By similarity).

Interacts with host EIF2AK2/PKR; this interaction leads to disruption of EIF2AK2 dimerization by NS5A and probably allows the virus to evade the innate immune response (By similarity).

Interacts (via N-terminus) with host PACSIN2 (via N-terminus); this interaction attenuates protein kinase C alpha-mediated phosphorylation of PACSIN2 by disrupting the interaction between PACSIN2 and PRKCA (By similarity).

Interacts (via N-terminus) with host SRC kinase (via SH2 domain) (By similarity).

Interacts with most Src-family kinases (By similarity).

Interacts with host IFI27 and SKP2; promotes the ubiquitin-mediated proteasomal degradation of NS5A (By similarity).

Interacts with host GPS2 (By similarity).

Interacts with host TNFRSF21; this interaction allows the modulation by the virus of JNK, p38 MAPK, STAT3, and Akt signaling pathways in a DR6-dependent manner (By similarity).

Interacts (via N-terminus) with host CIDEB (via N-terminus); this interaction seems to regulate the association of HCV particles with APOE (By similarity).

Interacts with host CHKA/Choline Kinase-alpha; CHKA bridges host PI4KA and NS5A and potentiates NS5A-stimulated PI4KA activity, which then facilitates the targeting of the ternary complex to the ER for viral replication (By similarity).

Interacts with host SPSB2 (via C-terminus); this interaction targets NS5A for ubiquitination and degradation (By similarity).

Interacts with host RAB18; this interaction may promote the association of NS5A and other replicase components with lipid droplets (By similarity).

By similarity

Homooligomer (By similarity).

Interacts with non-structural protein 5A (By similarity).

Interacts with host VAPB (By similarity).

Interacts with host PRK2/PKN2 (By similarity).

Interacts with host HNRNPA1 and SEPT6; these interactions facilitate viral replication (By similarity). Part of the replication complex composed of NS2, NS3, NS4A, NS4B, NS5A and the RNA-directed RNA polymerase (By similarity).

By similarity

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		O39929

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

13008
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		O39929

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		O39929

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini903 – 1026Peptidase C18PROSITE-ProRule annotationAdd BLAST124
Domaini1027 – 1208Peptidase S29PROSITE-ProRule annotationAdd BLAST182
Domaini1217 – 1369Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST153
Domaini2631 – 2749RdRp catalyticPROSITE-ProRule annotationAdd BLAST119

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni2 – 75DisorderedBy similarityAdd BLAST74
Regioni2 – 59Interaction with DDX3XBy similarityAdd BLAST58
Regioni2 – 58Interaction with EIF2AK2/PKRBy similarityAdd BLAST57
Regioni2 – 23Interaction with STAT1By similarityAdd BLAST22
Regioni112 – 152Important for endoplasmic reticulum and mitochondrial localizationBy similarityAdd BLAST41
Regioni122 – 173Interaction with APOA2By similarityAdd BLAST52
Regioni164 – 167Important for lipid droplets localizationBy similarity4
Regioni265 – 296Important for fusionBy similarityAdd BLAST32
Regioni385 – 412HVR1By similarityAdd BLAST28
Regioni475 – 479HVR2By similarity5
Regioni481 – 494CD81-binding 1By similarityAdd BLAST14
Regioni545 – 552CD81-binding 2By similarity8
Regioni660 – 671PKR/eIF2-alpha phosphorylation homology domain (PePHD)By similarityAdd BLAST12
Regioni904 – 1206Protease NS2-3By similarityAdd BLAST303
Regioni929 – 949Interaction with host SCPS1By similarityAdd BLAST21
Regioni1486 – 1498RNA-bindingBy similarityAdd BLAST13
Regioni1679 – 1690NS3-bindingBy similarityAdd BLAST12
Regioni2120 – 2329Transcriptional activationSequence analysisAdd BLAST210
Regioni2120 – 2208FKBP8-bindingBy similarityAdd BLAST89
Regioni2135 – 2139Interaction with non-structural protein 4ABy similarity5
Regioni2189 – 2435Interaction with host SKP2By similarityAdd BLAST247
Regioni2210 – 2272Interaction with EIF2AK2/PKRBy similarityAdd BLAST63
Regioni2210 – 2245ISDRBy similarityAdd BLAST36
Regioni2245 – 2303NS4B-bindingSequence analysisAdd BLAST59
Regioni2296 – 2373V3Add BLAST78
Regioni2346 – 2406DisorderedSequence analysisAdd BLAST61

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi5 – 13Nuclear localization signalBy similarity9
Motifi38 – 43Nuclear localization signalBy similarity6
Motifi58 – 64Nuclear localization signalBy similarity7
Motifi66 – 71Nuclear localization signalBy similarity6
Motifi1316 – 1319DECH boxBy similarity4
Motifi2319 – 2322SH3-bindingSequence analysis4
Motifi2324 – 2332Nuclear localization signalBy similarity9

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi47 – 69Basic and acidic residuesSequence analysisAdd BLAST23
Compositional biasi2349 – 2373Polar residuesSequence analysisAdd BLAST25

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The transmembrane regions of envelope E1 and E2 glycoproteins are involved in heterodimer formation, ER localization, and assembly of these proteins.By similarity
The transmembrane regions of envelope E1 and E2 glycoproteins are involved in heterodimer formation, ER localization, and assembly of these proteins (By similarity). Envelope E2 glycoprotein contain two highly variable regions called hypervariable region 1 and 2 (HVR1 and HVR2) (By similarity). E2 also contain two segments involved in CD81-binding (By similarity). HVR1 is implicated in the SCARB1-mediated cell entry and probably acts as a regulator of the association of particles with lipids (By similarity).By similarity
The N-terminus of NS3 is required for the catalytic activity of protease NS2 (By similarity). The minimal catalytic region includes the C-terminus of NS2 and the N-terminus NS3 protease domain (active region NS2-3) (By similarity).By similarity
The N-terminal one-third contains the protease activity (By similarity). This region contains a zinc atom that does not belong to the active site, but may play a structural rather than a catalytic role (By similarity). This region is essential for the activity of protease NS2, maybe by contributing to the folding of the latter (By similarity). The NTPase/helicase activity is located in the twothirds C-terminus of NS3, this domain contains the NTPase and RNA-binding regions (By similarity).By similarity
Contains a glycine zipper region that critically contributes to the biogenesis of functional ER-derived replication organelles.By similarity
The N-terminus of NS5A acts as membrane anchor (By similarity). The central part of NS5A contains a variable region called interferon sensitivity determining region (ISDR) and seems to be intrinsically disordered and interacts with NS5B and host EIF2AK2 (By similarity). The C-terminus of NS5A contains a variable region called variable region 3 (V3) (By similarity). ISDR and V3 may be involved in sensitivity and/or resistance to IFN-alpha therapy (By similarity). The C-terminus contains a nuclear localization signal (By similarity). The SH3-binding domain is involved in the interaction with host BIN1, GRB2 and Src-family kinases (By similarity).By similarity

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the hepacivirus polyprotein family.Curated

Keywords - Domaini

SH3-binding, Transmembrane, Transmembrane helix

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.20.1280.150, 1 hit
2.20.25.210, 1 hit
2.20.25.220, 1 hit
2.30.30.710, 1 hit
2.40.10.10, 1 hit
3.30.70.270, 2 hits
3.40.50.300, 2 hits
4.10.710.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR043502, DNA/RNA_pol_sf
IPR002521, HCV_Core_C
IPR044896, HCV_core_chain_A
IPR002522, HCV_core_N
IPR002519, HCV_Env
IPR002531, HCV_NS1
IPR002518, HCV_NS2
IPR042205, HCV_NS2_C
IPR042209, HCV_NS2_N
IPR000745, HCV_NS4a
IPR001490, HCV_NS4b
IPR002868, HCV_NS5a
IPR013192, HCV_NS5A_1a
IPR013193, HCV_NS5a_1B_dom
IPR038568, HCV_NS5A_1B_sf
IPR024350, HCV_NS5a_C
IPR014001, Helicase_ATP-bd
IPR001650, Helicase_C
IPR004109, NS3_Peptidase_S29
IPR038170, NS5A_1a_sf
IPR027417, P-loop_NTPase
IPR009003, Peptidase_S1_PA
IPR043504, Peptidase_S1_PA_chymotrypsin
IPR043128, Rev_trsase/Diguanyl_cyclase
IPR007094, RNA-dir_pol_PSvirus
IPR002166, RNA_pol_HCV

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01543, HCV_capsid, 1 hit
PF01542, HCV_core, 1 hit
PF01539, HCV_env, 1 hit
PF01560, HCV_NS1, 1 hit
PF01538, HCV_NS2, 1 hit
PF01006, HCV_NS4a, 1 hit
PF01001, HCV_NS4b, 1 hit
PF01506, HCV_NS5a, 1 hit
PF08300, HCV_NS5a_1a, 1 hit
PF08301, HCV_NS5a_1b, 1 hit
PF12941, HCV_NS5a_C, 1 hit
PF02907, Peptidase_S29, 1 hit
PF00998, RdRP_3, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00487, DEXDc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50494, SSF50494, 1 hit
SSF52540, SSF52540, 2 hits
SSF56672, SSF56672, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51693, HCV_NS2_PRO, 1 hit
PS51192, HELICASE_ATP_BIND_1, 1 hit
PS51194, HELICASE_CTER, 1 hit
PS51822, HV_PV_NS3_PRO, 1 hit
PS50507, RDRP_SSRNA_POS, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

O39929-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSTNPKPQRK TKRNTNRRPM DVKFPGGGQI VGGVYLLPRR GPRLGVRATR 
        60         70         80         90        100
KTSERSQPRG RRQPIPKARR PEGRSWAQPG YPWPLYGNEG CGWAGWLLSP 
       110        120        130        140        150
RGSRPSWGPN DPRGRSRNLG KVIDTLTCGF ADLMGYIPLV GAPVGSVARA 
       160        170        180        190        200
LAHGVRALED GINYATGNLP GCSFSIFLLA LLSCLTVPAS AVNYRNVSGI 
       210        220        230        240        250
YHVTNDCPNS SIVYEADHHI MHLPGCVPCV REGNQSRCWV ALTPTVAAPY 
       260        270        280        290        300
IGAPLESLRS HVDLMVGAAT VCSGLYIGDL CGGLFLVGQM FSFRPRRHWT 
       310        320        330        340        350
TQDCNCSIYT GHITGHRMAW DMMMNWSPTT TLVLAQVMRI PTTLVDLLSG 
       360        370        380        390        400
GHWGVLVGVA YFSMQANWAK VILVLFLFAG VDAETHVSGA AVGRSTAGLA 
       410        420        430        440        450
NLFSSGSKQN LQLINSNGSW HINRTALNCN DSLNTGFLAS LFYTHKFNSS 
       460        470        480        490        500
GCSERLACCK SLDSYGQGWG PLGVANISGS SDDRPYCWHY APRPCGIVPA 
       510        520        530        540        550
SSVCGPVYCF TPSPVVVGTT DHVGVPTYTW GENETDVFLL NSTRPPHGAW 
       560        570        580        590        600
FGCVWMNSTG FTKTCGAPPC EVNTNNGTWH CPTDCFRKHP ETTYAKCGSG 
       610        620        630        640        650
PWITPRCLID YPYRLWHFPC TANFSVFNIR TFVGGIEHRM QAACNWTRGE 
       660        670        680        690        700
VCGLEHRDRV ELSPLLLTTT AWQILPCSFT TLPALSTGLI HLHQNIVDVQ 
       710        720        730        740        750
YLYGVGSAVV SWALKWEYVV LAFLLLADAR VSAYLWMMFM VSQVEAALSN 
       760        770        780        790        800
LININAASAA GAQGFWYAIL FICIVWHVKG RFPAAAAYAA CGLWPCFLLL 
       810        820        830        840        850
LMLPERAYAY DQEVAGSLGG AIVVMLTILT LSPHYKLWLA RGLWWIQYFI 
       860        870        880        890        900
ARTEAVLHVY IPSFNVRGPR DSVIVLAVLV CPDLVFDITK YLLAILGPLH 
       910        920        930        940        950
ILQASLLRIP YFVRAQALVK ICSLLRGVVY GKYFQMVVLK SRGLTGTYIY 
       960        970        980        990       1000
DHLTPMSDWP PYGLRDLAVA LEPVVFTPME KKVIVWGADT AACGDIIRGL 
      1010       1020       1030       1040       1050
PVSARLGNEI LLGPADTETS KGWRLLAPIT AYAQQTRGLF STIVTSLTGR 
      1060       1070       1080       1090       1100
DTNENCGEVQ VLSTATQSFL GTAVNGVMWT VYHGAGAKTI SGPKGPVNQM 
      1110       1120       1130       1140       1150
YTNVDQDLVG WPAPPGVRSL APCTCGSADL YLVTRHADVI PVRRRGDTRG 
      1160       1170       1180       1190       1200
ALLSPRPISI LKGSSGGPLL CPMGHRAGIF RAAVCTRGVA KAVDFVPVES 
      1210       1220       1230       1240       1250
LETTMRSPVF TDNSTPPAVP QTYQVAHLHA PTGSGKSTKV PAAHAAQGYK 
      1260       1270       1280       1290       1300
VLVLNPSVAA TLGFGVYMSK AYGIDPNIRS GVRTITTGAP ITYSTYGKFL 
      1310       1320       1330       1340       1350
ADGGCSGGAY DIIICDECYS TDSTTILGIG TVLDQAETAG VRLTVLATAT 
      1360       1370       1380       1390       1400
PPGSVTTPHS NIEEVALPTT GEIPFYGKAI PLELIKGGRH LIFCHSKKKC 
      1410       1420       1430       1440       1450
DELARQLTSL GLNAVAYYRG LDVSVIPTSG DVVVCATDAL MTGFTGDFDS 
      1460       1470       1480       1490       1500
VIDCNTSVIQ TVDFSLDPTF SIEITTVPQD AVSRSQRRGR TGRGRLGTYR 
      1510       1520       1530       1540       1550
YVTPGERPSG MFDTAELCEC YDAGCAWYEL TPAETTTRLK AYFDTPGLPV 
      1560       1570       1580       1590       1600
CQDHLEFWES VFTGLTHIDG HFLSQTKQSG ENFPYLVAYQ ATVSAKVWLA 
      1610       1620       1630       1640       1650
PPSWDTMWKC LIRLKPTLHG PTPLLYRLGS VQNEVVLTHP ITKYIMACMS 
      1660       1670       1680       1690       1700
ADLEVVTSTW VLVGGVLAAL AAYCLSVGSV VIVGRVVLSG QPAVIPDREV 
      1710       1720       1730       1740       1750
LYQQFDEMEE CSKHLPLVEH GLQLAEQFKQ KALGLLNFAG KQAQEATPVI 
      1760       1770       1780       1790       1800
QSNFAKLEQF WANDMWNFIS GIQYLAGLST LPGNPAIASL MSFTAAVTSP 
      1810       1820       1830       1840       1850
LTTQQTLLFN ILGGWVASQI RDSDASTAFV VSGLAGAAVG SVGLGKILVD 
      1860       1870       1880       1890       1900
ILPGYGAGVR GAVVTFKIMS GEMPSTEDLV NLLPAILSPG ALVVEVVCPA 
      1910       1920       1930       1940       1950
ILRRHVGPGE GAVQWMNRLI AFASRGNHVS PTHYVPESDA ARRVTTILSS 
      1960       1970       1980       1990       2000
LTVTSLLRRL HKWINEDCST PCAESWLWEV WDWVLHVLSD FKTCLKAKFV 
      2010       2020       2030       2040       2050
PLMPGIPLLS WPRGYKGEWR GDGVMHTTCP CGADLAGHIK NGSMRITGPK 
      2060       2070       2080       2090       2100
TCSNTWHGTF PINAYTTGPG VPIPAPNYKF ALWRVSAEDY VEVRRVGDFH 
      2110       2120       2130       2140       2150
YVTGVTQDNI KFPCQVPAPE LFTEVDGIRI HRHAPKCKPL LRDEVSFSVG 
      2160       2170       2180       2190       2200
LNSFVVGSQL PCEPEPDVAV LTSMLTDPSH ITAESARRRL ARGSRPSLAS 
      2210       2220       2230       2240       2250
SSASQLSPRL LQATCTAPHD SPGTDLLEAN LLWGSTATRV ETDEKVIILD 
      2260       2270       2280       2290       2300
SFESCVAEQN DDREVSVAAE ILRPTKKFPP ALPIWARPDY NPPLTETWKQ 
      2310       2320       2330       2340       2350
QDYQAPTVHG CALPPAKQPP VPSPRRKRTV QLTESVVSTA LAELAAKTFG 
      2360       2370       2380       2390       2400
QSEPSSDRDT DLTTPTETTD SGPIVVDDAS DDGSYSSMPP LEGEPGDPDL 
      2410       2420       2430       2440       2450
TSDSWSTVSG SEDVVCCSMS YSWTGALVTP CAAEESKLPI SPLSNSLLRH 
      2460       2470       2480       2490       2500
HNMVYATTTR SAVTRQKKVT FDRLQVVDST YNEVLKEIKA RASRVKPRLL 
      2510       2520       2530       2540       2550
TTEEACDLTP PHSARSKFGY GKKDVRSHSR KAINHISSVW KDLLDDNNTP 
      2560       2570       2580       2590       2600
IPTTIMAKNE VFAVNPAKGG RKPARLIVYP DLGSRVCEKR ALHDVIKKTA 
      2610       2620       2630       2640       2650
LAVMGAAYGF QYSPAQRVEF LLTAWKSKND PMGFSYDTRC FDSTVTEKDI 
      2660       2670       2680       2690       2700
RVEEEVYQCC DLEPEARKVI TALTDRLYVG GPMHNSKGDL CGYRRCRATG 
      2710       2720       2730       2740       2750
VYTTSFGNTL TCYLKATAAI RAAALRDCTM LVCGDDLVVI AESDGVEEDN 
      2760       2770       2780       2790       2800
RALRAFTEAM TRYSAPPGDA PQPAYDLELI TSCSSNVSVA HDVTGKKVYY 
      2810       2820       2830       2840       2850
LTRDPETPLA RAVWETVRHT PVNSWLGNII VYAPTIWVRM ILMTHFFSIL 
      2860       2870       2880       2890       2900
QSQEALEKAL DFDMYGVTYS ITPLDLPAII QRLHGLSAFT LHGYSPHELN 
      2910       2920       2930       2940       2950
RVAGALRKLG VPPLRAWRHR ARAVRAKLIA QGGRAKICGI YLFNWAVKTK 
      2960       2970       2980       2990       3000
LKLTPLPAAA KLDLSGWFTV GAGGGDIYHS MSHARPRYLL LCLLILTVGV 

GIFLLPAR
Length:3,008
Mass (Da):327,599
Last modified:January 23, 2007 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i8E7FC932E27C406F
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
Y11604 Genomic RNA Translation: CAA72338.1

Protein sequence database of the Protein Information Resource

More...PIRi		PQ0804

NCBI Reference Sequences

More...RefSeqi		YP_001469632.1, NC_009825.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		11027168

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		vg:11027168

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Virus Pathogen Resource

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11604 Genomic RNA Translation: CAA72338.1
PIRiPQ0804
RefSeqiYP_001469632.1, NC_009825.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6P6ZX-ray2.29A1030-1208[»]
A1678-1688[»]
BMRBiO39929
SMRiO39929
ModBaseiSearch...
PDBe-KBiSearch...

Chemistry databases

BindingDBiO39929
DrugCentraliO39929

Protein family/group databases

MEROPSiS29.001

Proteomic databases

PRIDEiO39929

Genome annotation databases

GeneIDi11027168
KEGGivg:11027168

Organism-specific databases

European Hepatitis C Virus Database

More...euHCVdbi		Y11604

Enzyme and pathway databases

BRENDAi3.4.21.98, 17004

Family and domain databases

Gene3Di1.20.1280.150, 1 hit
2.20.25.210, 1 hit
2.20.25.220, 1 hit
2.30.30.710, 1 hit
2.40.10.10, 1 hit
3.30.70.270, 2 hits
3.40.50.300, 2 hits
4.10.710.10, 1 hit
InterProiView protein in InterPro
IPR043502, DNA/RNA_pol_sf
IPR002521, HCV_Core_C
IPR044896, HCV_core_chain_A
IPR002522, HCV_core_N
IPR002519, HCV_Env
IPR002531, HCV_NS1
IPR002518, HCV_NS2
IPR042205, HCV_NS2_C
IPR042209, HCV_NS2_N
IPR000745, HCV_NS4a
IPR001490, HCV_NS4b
IPR002868, HCV_NS5a
IPR013192, HCV_NS5A_1a
IPR013193, HCV_NS5a_1B_dom
IPR038568, HCV_NS5A_1B_sf
IPR024350, HCV_NS5a_C
IPR014001, Helicase_ATP-bd
IPR001650, Helicase_C
IPR004109, NS3_Peptidase_S29
IPR038170, NS5A_1a_sf
IPR027417, P-loop_NTPase
IPR009003, Peptidase_S1_PA
IPR043504, Peptidase_S1_PA_chymotrypsin
IPR043128, Rev_trsase/Diguanyl_cyclase
IPR007094, RNA-dir_pol_PSvirus
IPR002166, RNA_pol_HCV
PfamiView protein in Pfam
PF01543, HCV_capsid, 1 hit
PF01542, HCV_core, 1 hit
PF01539, HCV_env, 1 hit
PF01560, HCV_NS1, 1 hit
PF01538, HCV_NS2, 1 hit
PF01006, HCV_NS4a, 1 hit
PF01001, HCV_NS4b, 1 hit
PF01506, HCV_NS5a, 1 hit
PF08300, HCV_NS5a_1a, 1 hit
PF08301, HCV_NS5a_1b, 1 hit
PF12941, HCV_NS5a_C, 1 hit
PF02907, Peptidase_S29, 1 hit
PF00998, RdRP_3, 1 hit
SMARTiView protein in SMART
SM00487, DEXDc, 1 hit
SUPFAMiSSF50494, SSF50494, 1 hit
SSF52540, SSF52540, 2 hits
SSF56672, SSF56672, 1 hit
PROSITEiView protein in PROSITE
PS51693, HCV_NS2_PRO, 1 hit
PS51192, HELICASE_ATP_BIND_1, 1 hit
PS51194, HELICASE_CTER, 1 hit
PS51822, HV_PV_NS3_PRO, 1 hit
PS50507, RDRP_SSRNA_POS, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPOLG_HCVED
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O39929
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: January 23, 2007
Last modified: May 25, 2022
This is version 164 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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