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P26663

- POLG_HCVBK

UniProt

P26663 - POLG_HCVBK

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Protein

Genome polyprotein

Gene
N/A
Organism
Hepatitis C virus genotype 1b (isolate BK) (HCV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Core protein packages viral RNA to form a viral nucleocapsid, and promotes virion budding. Modulates viral translation initiation by interacting with HCV IRES and 40S ribosomal subunit. Also regulates many host cellular functions such as signaling pathways and apoptosis. Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways and by inducing human STAT1 degradation. Thought to play a role in virus-mediated cell transformation leading to hepatocellular carcinomas. Interacts with, and activates STAT3 leading to cellular transformation. May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm. Also represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation. Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses NK-kappaB activation, and activates AP-1. Could mediate apoptotic pathways through association with TNF-type receptors TNFRSF1A and LTBR, although its effect on death receptor-induced apoptosis remains controversial. Enhances TRAIL mediated apoptosis, suggesting that it might play a role in immune-mediated liver cell injury. Seric core protein is able to bind C1QR1 at the T-cell surface, resulting in down-regulation of T-lymphocytes proliferation. May transactivate human MYC, Rous sarcoma virus LTR, and SV40 promoters. May suppress the human FOS and HIV-1 LTR activity. Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage. Core protein induces up-regulation of FAS promoter activity, and thereby probably contributes to the increased triglyceride accumulation in hepatocytes (steatosis) By similarity.By similarity
E1 and E2 glycoproteins form a heterodimer that is involved in virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane. E1/E2 heterodimer binds to human LDLR, CD81 and SCARB1/SR-BI receptors, but this binding is not sufficient for infection, some additional liver specific cofactors may be needed. The fusion function may possibly be carried by E1. E2 inhibits human EIF2AK2/PKR activation, preventing the establishment of an antiviral state. E2 is a 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. These interactions allow capture of circulating HCV particles by these cells and subsequent transmission to permissive cells. DCs act as sentinels in various tissues where they entrap pathogens and convey them to local lymphoid tissue or lymph node for establishment of immunity. Capture of circulating HCV particles by these SIGN+ cells may facilitate virus infection of proximal hepatocytes and lymphocyte subpopulations and may be essential for the establishment of persistent infection By similarity.By similarity
P7 seems to be a heptameric ion channel protein (viroporin) and is inhibited by the antiviral drug amantadine. Also inhibited by long-alkyl-chain iminosugar derivatives. Essential for infectivity By similarity.By similarity
Protease NS2-3 is a cysteine protease responsible for the autocatalytic cleavage of NS2-NS3. Seems to undergo self-inactivation following maturation By similarity.By similarity
NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B-NS5A and NS5A-NS5B. NS3/NS4A complex also prevents phosphorylation of human IRF3, thus preventing the establishment of dsRNA induced antiviral state. NS3 RNA helicase binds to RNA and unwinds dsRNA in the 3' to 5' direction, and likely RNA stable secondary structure in the template strand. Cleaves and inhibits the host antiviral protein MAVS By similarity.By similarity
NS4B induces a specific membrane alteration that serves as a scaffold for the virus replication complex. This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex By similarity.By similarity
NS5A is a component of the replication complex involved in RNA-binding. Its interaction with Human VAPB may target the viral replication complex to vesicles. Down-regulates viral IRES translation initiation. Mediates interferon resistance, presumably by interacting with and inhibiting human EIF2AK2/PKR. Seems to inhibit apoptosis by interacting with BIN1 and FKBP8. The hyperphosphorylated form of NS5A is an inhibitor of viral replication By similarity.By similarity
NS5B is an RNA-dependent RNA polymerase that plays an essential role in the virus replication.By similarity

Catalytic activityi

Hydrolysis of four peptide bonds in the viral precursor polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and Ser or Ala in P1'.
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation
NTP + H2O = NDP + phosphate.
ATP + H2O = ADP + phosphate.

Cofactori

Binds 1 zinc ion per NS3 protease domain.By similarity
Binds 1 zinc ion per NS5A N-terminal domain.By similarity

Enzyme regulationi

Activity of auto-protease NS2-3 is dependent on zinc ions and completely inhibited by EDTA, 1,10-phenanthroline, iodocetamide and N-ethylmaleimide. According to PubMed:9261354, completely inhibited by the serine protease inhibitors TLCK and TPCK. According to PubMed:8189501, almost completely inhibited by TPCK and slightly inhibited by TLCK. Not inhibited by antipain, aprotinin, E64, PMSF and pepstatin. Also inhibited by NS2-3 and NS4A derived peptides. Serine protease NS3 is also activated by zinc ions.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei177 – 1782Cleavage; by host signal peptidaseBy similarity
Sitei191 – 1922Cleavage; by host signal peptidaseSequence Analysis
Sitei383 – 3842Cleavage; by host signal peptidaseSequence Analysis
Sitei746 – 7472Cleavage; by host signal peptidaseBy similarity
Sitei809 – 8102Cleavage; by host signal peptidaseBy similarity
Active sitei952 – 9521For protease NS2-3 activity; shared with dimeric partnerPROSITE-ProRule annotation
Active sitei972 – 9721For protease NS2-3 activity; shared with dimeric partnerPROSITE-ProRule annotation
Active sitei993 – 9931For protease NS2-3 activity; shared with dimeric partnerPROSITE-ProRule annotation
Sitei1026 – 10272Cleavage; by protease NS2-3PROSITE-ProRule annotation
Active sitei1083 – 10831Charge relay system; for serine protease NS3 activityBy similarity
Active sitei1107 – 11071Charge relay system; for serine protease NS3 activityBy similarity
Metal bindingi1123 – 11231Zinc
Metal bindingi1125 – 11251Zinc
Active sitei1165 – 11651Charge relay system; for serine protease NS3 activityBy similarity
Metal bindingi1171 – 11711Zinc
Metal bindingi1175 – 11751Zinc
Sitei1657 – 16582Cleavage; by serine protease NS3Sequence Analysis
Sitei1711 – 17122Cleavage; by serine protease NS3Sequence Analysis
Sitei1972 – 19732Cleavage; by serine protease NS3Sequence Analysis
Metal bindingi2011 – 20111ZincBy similarity
Metal bindingi2029 – 20291ZincBy similarity
Metal bindingi2031 – 20311ZincBy similarity
Metal bindingi2052 – 20521ZincBy similarity
Sitei2419 – 24202Cleavage; by serine protease NS3Sequence Analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1230 – 12378ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATP-dependent helicase activity Source: InterPro
  3. cysteine-type endopeptidase activity Source: InterPro
  4. identical protein binding Source: IntAct
  5. ion channel activity Source: UniProtKB-KW
  6. RNA binding Source: UniProtKB-KW
  7. RNA-directed RNA polymerase activity Source: UniProtKB-KW
  8. serine-type endopeptidase activity Source: InterPro
  9. serine-type exopeptidase activity Source: InterPro
  10. structural molecule activity Source: InterPro
  11. zinc ion binding Source: InterPro

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. clathrin-mediated endocytosis of virus by host cell Source: UniProtKB-KW
  3. fusion of virus membrane with host endosome membrane Source: UniProtKB-KW
  4. induction by virus of host autophagy Source: UniProtKB-KW
  5. modulation by virus of host G1/S transition checkpoint Source: UniProtKB-KW
  6. pore formation by virus in membrane of host cell Source: UniProtKB-KW
  7. protein oligomerization Source: UniProtKB-KW
  8. regulation of transcription, DNA-templated Source: UniProtKB-KW
  9. suppression by virus of host MAVS activity Source: UniProtKB-KW
  10. suppression by virus of host STAT1 activity Source: UniProtKB-KW
  11. suppression by virus of host TRAF activity Source: UniProtKB-KW
  12. suppression by virus of host type I interferon-mediated signaling pathway Source: UniProtKB-KW
  13. transcription, DNA-templated Source: UniProtKB-KW
  14. transformation of host cell by virus Source: InterPro
  15. viral RNA genome replication Source: InterPro
  16. virion attachment to host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, Ribonucleoprotein, RNA-directed RNA polymerase, Serine protease, Thiol protease, Transferase, Viral ion channel

Keywords - Biological processi

Activation 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

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, Viral nucleoprotein, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 11 chains:
Alternative name(s):
Capsid protein C
p21
Alternative name(s):
gp32
gp35
Alternative name(s):
NS1
gp68
gp70
Protease NS2-3 (EC:3.4.22.-)
Short name:
p23
Alternative name(s):
Hepacivirin
NS3P
p70
Alternative name(s):
p8
Alternative name(s):
p27
Alternative name(s):
p56
Alternative name(s):
NS5B
p68
OrganismiHepatitis C virus genotype 1b (isolate BK) (HCV)
Taxonomic identifieri11105 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageFlaviviridaeHepacivirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000007413: Genome

Subcellular locationi

Chain Core protein p21 : Host endoplasmic reticulum membrane; Single-pass membrane protein. Host mitochondrion membrane; Single-pass type I membrane protein. Host lipid droplet
Note: The C-terminal transmembrane domain of core protein p21 contains an ER signal leading the nascent polyprotein to the ER membrane. Only a minor proportion of core protein is present in the nucleus and an unknown proportion is secreted.
Chain Core protein p19 : Virion By similarity. Host cytoplasm By similarity. Host nucleus By similarity. Secreted By similarity
Chain Envelope glycoprotein E1 : Virion membrane Curated; Single-pass type I membrane protein Curated. Host endoplasmic reticulum membrane By similarity; Single-pass type I membrane protein By similarity
Note: The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase. After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor. A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain. These events explain the final topology of the protein. ER retention of E1 is leaky and, in overexpression conditions, only a small fraction reaches the plasma membrane.
Chain Envelope glycoprotein E2 : Virion membrane Curated; Single-pass type I membrane protein Curated. Host endoplasmic reticulum membrane By similarity; Single-pass type I membrane protein By similarity
Note: The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase. After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor. A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain. These events explain the final topology of the protein. ER retention of E2 is leaky and, in overexpression conditions, only a small fraction reaches the plasma membrane.
Chain p7 : Host endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity. Host cell membrane By similarity
Note: The C-terminus of p7 membrane domain acts as a signal sequence. After cleavage by host signal peptidase, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor. Only a fraction localizes to the plasma membrane.
Chain Serine protease NS3 : Host endoplasmic reticulum membrane By similarity; Peripheral membrane protein By similarity
Note: NS3 is associated to the ER membrane through its binding to NS4A.
Chain Non-structural protein 4A : Host endoplasmic reticulum membrane Curated; Single-pass type I membrane protein Curated
Note: Host membrane insertion occurs after processing by the NS3 protease.
Chain Non-structural protein 5A : Host endoplasmic reticulum membrane By similarity; Peripheral membrane protein By similarity. Host cytoplasmhost perinuclear region By similarity. Host mitochondrion By similarity
Note: Host membrane insertion occurs after processing by the NS3 protease.
Chain RNA-directed RNA polymerase : Host endoplasmic reticulum membrane Curated; Single-pass type I membrane protein Curated
Note: Host membrane insertion occurs after processing by the NS3 protease.

GO - Cellular componenti

  1. host cell endoplasmic reticulum Source: UniProtKB-KW
  2. host cell lipid particle Source: UniProtKB-KW
  3. host cell mitochondrion Source: UniProtKB-KW
  4. host cell nucleus Source: UniProtKB-KW
  5. host cell plasma membrane Source: UniProtKB-KW
  6. integral component of membrane Source: UniProtKB-KW
  7. integral to membrane of host cell Source: UniProtKB-KW
  8. ribonucleoprotein complex Source: UniProtKB-KW
  9. viral envelope Source: UniProtKB-KW
  10. viral nucleocapsid Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2194 – 21941S → A: Loss of phosphorylation. 1 Publication
Mutagenesisi2322 – 23221P → A: Complete loss of binding to GRB2. 1 Publication
Mutagenesisi2323 – 23231P → A: Complete loss of binding to GRB2. 1 Publication
Mutagenesisi2326 – 23261P → A: Complete loss of binding to GRB2. 1 Publication

Keywords - Diseasei

Oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed; by hostBy similarity
Chaini2 – 191190Core protein p21Sequence AnalysisPRO_0000037529Add
BLAST
Chaini2 – 177176Core protein p19By similarityPRO_0000037530Add
BLAST
Propeptidei178 – 19114ER anchor for the core protein, removed in mature form by host signal peptidaseBy similarityPRO_0000037531Add
BLAST
Chaini192 – 383192Envelope glycoprotein E1Sequence AnalysisPRO_0000037532Add
BLAST
Chaini384 – 746363Envelope glycoprotein E2Sequence AnalysisPRO_0000037533Add
BLAST
Chaini747 – 80963p7By similarityPRO_0000037534Add
BLAST
Chaini810 – 1026217Protease NS2-3PROSITE-ProRule annotationPRO_0000037535Add
BLAST
Chaini1027 – 1657631Serine protease NS3PRO_0000037536Add
BLAST
Chaini1658 – 171154Non-structural protein 4APRO_0000037537Add
BLAST
Chaini1712 – 1972261Non-structural protein 4BPRO_0000037538Add
BLAST
Chaini1973 – 2419447Non-structural protein 5APRO_0000037539Add
BLAST
Chaini2420 – 3010591RNA-directed RNA polymerasePRO_0000037540Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine; by hostBy similarity
Modified residuei53 – 531Phosphoserine; by hostBy similarity
Modified residuei99 – 991Phosphoserine; by hostBy similarity
Modified residuei116 – 1161Phosphoserine; by host PKABy similarity
Glycosylationi196 – 1961N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi209 – 2091N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi234 – 2341N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi250 – 2501N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi305 – 3051N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi417 – 4171N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi423 – 4231N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi430 – 4301N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi448 – 4481N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi532 – 5321N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi540 – 5401N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi556 – 5561N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi576 – 5761N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi623 – 6231N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi645 – 6451N-linked (GlcNAc...); by hostSequence Analysis
Lipidationi1968 – 19681S-palmitoyl cysteine; by hostBy similarity
Lipidationi1972 – 19721S-palmitoyl cysteine; by hostBy similarity
Disulfide bondi2114 ↔ 2162By similarity
Modified residuei2194 – 21941Phosphoserine; by host; in p561 Publication
Modified residuei2197 – 21971Phosphoserine; by host; in p58By similarity
Modified residuei2201 – 22011Phosphoserine; by host; in p58By similarity
Modified residuei2204 – 22041Phosphoserine; by host; in p58By similarity

Post-translational modificationi

Specific enzymatic cleavages in vivo yield mature proteins. The structural proteins, core, E1, E2 and p7 are produced by proteolytic processing by host signal peptidases. The core protein is synthesized as a 21 kDa precursor which is retained in the ER membrane through the hydrophobic signal peptide. Cleavage by the signal peptidase releases the 19 kDa mature core protein. The other proteins (p7, NS2-3, NS3, NS4A, NS4B, NS5A and NS5B) are cleaved by the viral proteases By similarity.By similarity
Envelope E1 and E2 glycoproteins are highly N-glycosylated.By similarity
Core protein is phosphorylated by host PKC and PKA.By similarity
NS5A is phosphorylated in a basal form termed p56. p58 is a hyperphosphorylated form of p56. p56 and p58 coexist in the cell in roughly equivalent amounts. Hyperphosphorylation is dependent on the presence of NS4A. Human AKT1, RPS6KB1/p70S6K, MAP2K1/MEK1, MAP2K6/MKK6 and CSNK1A1/CKI-alpha kinases may be responsible for NS5A phosphorylation.1 Publication
NS4B is palmitoylated. This modification may play a role in its polymerization or in protein-protein interactions By similarity.By similarity
The N-terminus of a fraction of NS4B molecules seems to be relocated post-translationally from the cytoplasm to the ER lumen, with a 5th transmembrane segment. The C-terminus of NS2 may be lumenal with a fourth transmembrane segment By similarity.By similarity
Core protein is ubiquitinated; mediated by UBE3A and leading to core protein subsequent proteasomal degradation.By similarity

Keywords - PTMi

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

Interactioni

Subunit structurei

Core protein is a homomultimer that binds the C-terminal part of E1 and interacts with numerous cellular proteins. Interaction with human STAT1 SH2 domain seems to result in decreased STAT1 phosphorylation, leading to decreased IFN-stimulated gene transcription. In addition to blocking the formation of phosphorylated STAT1, the core protein also promotes ubiquitin-mediated proteasome-dependent degradation of STAT1. Interacts with, and constitutively activates human STAT3. Associates with human LTBR and TNFRSF1A receptors and possibly induces apoptosis. Binds to human SP110 isoform 3/Sp110b, HNRPK, C1QR1, YWHAE, UBE3A/E6AP, DDX3X, APOA2 and RXRA proteins. Interacts with human CREB3 nuclear transcription protein, triggering cell transformation. May interact with human p53. Also binds human cytokeratins KRT8, KRT18, KRT19 and VIM (vimentin). E1 and E2 glycoproteins form a heterodimer that binds to human LDLR, CLDN1, CD81 and SCARB1 receptors. E2 binds and inhibits human EIF2AK2/PKR. Also binds human CD209/DC-SIGN and CLEC4M/DC-SIGNR. p7 forms a homoheptamer in vitro. NS2 forms a homodimer containing a pair of composite active sites at the dimerization interface. NS2 seems to interact with all other non-structural (NS) proteins. NS4A interacts with NS3 serine protease and stabilizes its folding. NS3-NS4A complex is essential for the activation of the latter and allows membrane anchorage of NS3. NS3 interacts with human TANK-binding kinase TBK1 and MAVS. NS4B and NS5A form homodimers and seem to interact with all other non-structural (NS) proteins. NS5A also interacts with human EIF2AK2/PKR, FKBP8, GRB2, BIN1, PIK3R1, SRCAP, VAPB and with most Src-family kinases. NS5B is a homooligomer and interacts with human VAPB, HNRNPA1 and SEPT6 By similarity.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Q9WMX25EBI-6874437,EBI-6863741From a different organism.
PkmP524803EBI-6857429,EBI-647785From a different organism.
Sos1Q622452EBI-6857429,EBI-1693From a different organism.
TP53P046379EBI-6838571,EBI-366083From a different organism.

Protein-protein interaction databases

IntActiP26663. 6 interactions.
MINTiMINT-6548567.

Structurei

Secondary structure

1
3010
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi413 – 4164
Beta strandi419 – 4224
Beta strandi1031 – 10355
Helixi1039 – 104810
Beta strandi1057 – 10637
Beta strandi1068 – 10747
Beta strandi1077 – 10804
Helixi1082 – 10854
Beta strandi1090 – 10923
Beta strandi1095 – 10973
Beta strandi1100 – 11034
Turni1104 – 11074
Beta strandi1108 – 11125
Beta strandi1128 – 11336
Beta strandi1135 – 11373
Beta strandi1139 – 11446
Beta strandi1146 – 115712
Helixi1158 – 11614
Beta strandi1168 – 11703
Turni1172 – 11743
Beta strandi1176 – 118611
Beta strandi1189 – 11979
Helixi1198 – 12069
Beta strandi1224 – 12296
Beta strandi1232 – 12354
Turni1236 – 12383
Helixi1239 – 12457
Turni1246 – 12483
Beta strandi1251 – 12566
Helixi1258 – 127013
Beta strandi1271 – 12733
Beta strandi1277 – 12793
Beta strandi1290 – 12956
Helixi1296 – 13016
Beta strandi1311 – 13177
Helixi1323 – 133513
Turni1336 – 13405
Beta strandi1342 – 13509
Beta strandi1362 – 13665
Beta strandi1371 – 13755
Beta strandi1378 – 13803
Helixi1383 – 13864
Beta strandi1390 – 13934
Helixi1397 – 140913
Beta strandi1414 – 14174
Beta strandi1419 – 14213
Helixi1423 – 14253
Beta strandi1428 – 14303
Beta strandi1433 – 14364
Helixi1440 – 14434
Beta strandi1448 – 14536
Beta strandi1456 – 14638
Beta strandi1467 – 14693
Beta strandi1471 – 14788
Helixi1481 – 14888
Beta strandi1493 – 14953
Beta strandi1497 – 15037
Beta strandi1509 – 15113
Helixi1514 – 152613
Helixi1532 – 154413
Helixi1555 – 15639
Helixi1570 – 157910
Helixi1584 – 159613
Helixi1606 – 161712
Beta strandi1627 – 16293
Beta strandi1635 – 16373
Helixi1640 – 16489
Beta strandi1653 – 16564
Beta strandi1680 – 16889
Beta strandi2421 – 24255
Helixi2446 – 24494
Helixi2453 – 24553
Beta strandi2456 – 24583
Helixi2461 – 24633
Helixi2464 – 24718
Helixi2481 – 249414
Helixi2504 – 25096
Turni2519 – 25213
Helixi2524 – 25285
Helixi2532 – 254716
Beta strandi2549 – 25513
Beta strandi2555 – 25595
Beta strandi2563 – 25653
Turni2568 – 25714
Beta strandi2578 – 25814
Helixi2584 – 260623
Helixi2607 – 26093
Helixi2611 – 26133
Helixi2616 – 262914
Beta strandi2630 – 26389
Helixi2643 – 26464
Helixi2649 – 265911
Helixi2666 – 267813
Turni2679 – 26813
Beta strandi2683 – 26864
Beta strandi2688 – 26903
Beta strandi2692 – 26965
Beta strandi2701 – 27033
Helixi2706 – 272419
Beta strandi2728 – 27358
Beta strandi2738 – 27447
Helixi2748 – 276417
Beta strandi2769 – 27713
Beta strandi2776 – 27783
Helixi2779 – 27813
Beta strandi2787 – 27937
Beta strandi2795 – 27973
Beta strandi2799 – 28046
Helixi2808 – 281912
Helixi2826 – 28338
Turni2834 – 28363
Helixi2838 – 28425
Helixi2844 – 285411
Beta strandi2858 – 28603
Beta strandi2862 – 28665
Beta strandi2869 – 28735
Helixi2875 – 28773
Helixi2878 – 28869
Helixi2888 – 28914
Helixi2898 – 291114
Helixi2916 – 293318
Helixi2935 – 294410
Helixi2946 – 29483
Beta strandi2949 – 29513
Helixi2959 – 29624
Turni2967 – 29704
Beta strandi2976 – 29783
Beta strandi2979 – 29813

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A1QX-ray2.40A/B/C1027-1215[»]
1BT7NMR-A1027-1206[»]
1C2PX-ray1.90A/B2422-2989[»]
1CSJX-ray2.80A/B2420-2950[»]
1CU1X-ray2.50A/B1029-1657[»]
1GX5X-ray1.70A2420-2955[»]
1GX6X-ray1.85A2420-2950[»]
1JXPX-ray2.20A/B1027-1206[»]
C/D1678-1691[»]
1NHUX-ray2.00A/B2420-2989[»]
1NHVX-ray2.90A/B2420-2989[»]
1NS3X-ray2.80A/B1029-1206[»]
C/D1678-1689[»]
1OS5X-ray2.20A2420-2989[»]
1QUVX-ray2.50A2420-2989[»]
2AWZX-ray2.15A/B2420-2989[»]
2AX0X-ray2.00A/B2420-2989[»]
2AX1X-ray2.10A/B2420-2989[»]
2BRKX-ray2.30A2420-2955[»]
2BRLX-ray2.40A2420-2955[»]
2DXSX-ray2.20A/B2420-2963[»]
2GIQX-ray1.65A/B2421-2981[»]
2GIRX-ray1.90A/B2421-2981[»]
2HAIX-ray1.58A2420-2988[»]
2HWHX-ray2.30A/B2422-2989[»]
2HWIX-ray2.00A/B2422-2989[»]
2I1RX-ray2.20A/B2422-2989[»]
2JC0X-ray2.20A/B2420-2989[»]
2JC1X-ray2.00A/B2420-2989[»]
2O5DX-ray2.20A/B2422-2989[»]
2WCXX-ray2.00A2420-2955[»]
2WHOX-ray2.00A/B2420-2955[»]
2WRMX-ray1.95A2420-2955[»]
2XWYX-ray2.53A2420-2955[»]
2ZKUX-ray1.95A/B/C/D2420-2989[»]
3BR9X-ray2.30A/B2420-2989[»]
3BSAX-ray2.30A/B2420-2989[»]
3BSCX-ray2.65A/B2420-2989[»]
3CDEX-ray2.10A/B2420-2989[»]
3CIZX-ray1.87A/B2421-2989[»]
3CJ0X-ray1.90A/B2421-2989[»]
3CJ2X-ray1.75A/B2421-2989[»]
3CJ3X-ray1.87A/B2421-2989[»]
3CJ4X-ray2.07A/B2421-2989[»]
3CJ5X-ray1.92A/B2421-2989[»]
3CO9X-ray2.10A/B2420-2989[»]
3CVKX-ray2.31A/B2420-2989[»]
3CWJX-ray2.40A/B2420-2989[»]
3D28X-ray2.30A/B2420-2989[»]
3D5MX-ray2.20A/B2420-2989[»]
3E51X-ray1.90A/B2420-2989[»]
3FQKX-ray2.20A/B2421-2989[»]
3FRZX-ray1.86A2420-2989[»]
3G86X-ray2.20A/B2421-2989[»]
3GYNX-ray2.15A/B2420-2989[»]
3H2LX-ray1.90A/B2420-2989[»]
3H59X-ray2.10A/B2421-2989[»]
3H5SX-ray2.00A/B2421-2989[»]
3H5UX-ray1.95A/B2421-2989[»]
3H98X-ray1.90A/B2421-2989[»]
3IGVX-ray2.60A/B2420-2989[»]
3MF5X-ray2.00A/B2421-2989[»]
3UA7X-ray1.50E/F2321-2331[»]
3UDLX-ray2.17A/B/C/D2420-2989[»]
3VQSX-ray1.90A/B/C/D2420-2989[»]
4A92X-ray2.73A/B1029-1657[»]
A/B1678-1690[»]
4B6EX-ray2.46A/B1029-1657[»]
4B6FX-ray2.89A/B1029-1657[»]
4B71X-ray2.50A/B1029-1657[»]
4B73X-ray2.50A/B1029-1657[»]
4B74X-ray2.18A/B1029-1657[»]
4B75X-ray2.53A/B1029-1655[»]
4B76X-ray2.14A/B1029-1657[»]
4DGVX-ray1.80A412-423[»]
4DGYX-ray1.80A412-423[»]
4EO6X-ray1.79A/B2422-2989[»]
4EO8X-ray1.80A/B2422-2989[»]
4IH5X-ray1.90A/B2421-2989[»]
4IH6X-ray2.20A/B2421-2989[»]
4IH7X-ray2.30A/B2421-2989[»]
4K8BX-ray2.80C/D1678-1689[»]
4KAIX-ray2.30A/B2420-2989[»]
4KB7X-ray1.85A/B2420-2989[»]
4KBIX-ray2.06A/B2420-2989[»]
4KE5X-ray2.11A/B2420-2989[»]
4MIAX-ray2.80A/B2421-2989[»]
4MIBX-ray2.30A/B2421-2989[»]
4MK7X-ray2.80A/B2421-2989[»]
4MK8X-ray2.09A/B2421-2989[»]
4MK9X-ray2.05A/B2421-2989[»]
4MKAX-ray2.05A/B2421-2989[»]
4MKBX-ray1.90A/B2421-2989[»]
8OHMX-ray2.30A1216-1650[»]
ProteinModelPortaliP26663.
SMRiP26663. Positions 2-45, 902-1026, 1029-1657, 1973-2003, 2008-2170, 2420-2983.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26663.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 168167CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini190 – 358169LumenalSequence AnalysisAdd
BLAST
Topological domaini380 – 725346LumenalSequence AnalysisAdd
BLAST
Topological domaini747 – 75711LumenalSequence AnalysisAdd
BLAST
Topological domaini779 – 7824CytoplasmicSequence Analysis
Topological domaini804 – 81310LumenalSequence Analysis
Topological domaini835 – 88147CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini903 – 92826LumenalSequence AnalysisAdd
BLAST
Topological domaini950 – 1657708CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini1679 – 1805127CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini1827 – 18282LumenalSequence Analysis
Topological domaini1850 – 18501CytoplasmicSequence Analysis
Topological domaini1872 – 188110LumenalSequence Analysis
Topological domaini1903 – 197270CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini2003 – 2989987CytoplasmicSequence AnalysisAdd
BLAST

Intramembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Intramembranei1973 – 200230By similarityAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei169 – 18921HelicalSequence AnalysisAdd
BLAST
Transmembranei359 – 37921HelicalSequence AnalysisAdd
BLAST
Transmembranei726 – 74621HelicalSequence AnalysisAdd
BLAST
Transmembranei758 – 77821HelicalSequence AnalysisAdd
BLAST
Transmembranei783 – 80321HelicalSequence AnalysisAdd
BLAST
Transmembranei814 – 83421HelicalSequence AnalysisAdd
BLAST
Transmembranei882 – 90221HelicalSequence AnalysisAdd
BLAST
Transmembranei929 – 94921HelicalSequence AnalysisAdd
BLAST
Transmembranei1658 – 167821HelicalSequence AnalysisAdd
BLAST
Transmembranei1806 – 182621HelicalSequence AnalysisAdd
BLAST
Transmembranei1829 – 184921HelicalSequence AnalysisAdd
BLAST
Transmembranei1851 – 187121HelicalSequence AnalysisAdd
BLAST
Transmembranei1882 – 190221HelicalSequence AnalysisAdd
BLAST
Transmembranei2990 – 301021HelicalBy similarityAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini903 – 1026124Peptidase C18PROSITE-ProRule annotationAdd
BLAST
Domaini1217 – 1369153Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2633 – 2751119RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 5958Interaction with DDX3XBy similarityAdd
BLAST
Regioni2 – 2322Interaction with STAT1By similarityAdd
BLAST
Regioni122 – 17352Interaction with APOA2By similarityAdd
BLAST
Regioni148 – 23689Interaction with FKBP8Add
BLAST
Regioni150 – 15910Mitochondrial targeting signalBy similarity
Regioni164 – 1674Important for lipid droplets localizationBy similarity
Regioni265 – 29632Fusion peptideSequence AnalysisAdd
BLAST
Regioni385 – 41127HVR1Add
BLAST
Regioni475 – 4817HVR2
Regioni482 – 49413CD81-binding 1Sequence AnalysisAdd
BLAST
Regioni522 – 55332CD81-binding 2Sequence AnalysisAdd
BLAST
Regioni660 – 67112PKR/eIF2-alpha phosphorylation homology domain (PePHD)Add
BLAST
Regioni1679 – 169012NS3-binding (by NS4A)Sequence AnalysisAdd
BLAST
Regioni2120 – 2332213Transcriptional activationSequence AnalysisAdd
BLAST
Regioni2120 – 220889FKBP8-bindingSequence AnalysisAdd
BLAST
Regioni2200 – 225051Basal phosphorylationBy similarityAdd
BLAST
Regioni2210 – 227566PKR-bindingSequence AnalysisAdd
BLAST
Regioni2210 – 224940ISDRAdd
BLAST
Regioni2249 – 230658NS4B-bindingSequence AnalysisAdd
BLAST
Regioni2351 – 241969Basal phosphorylationBy similarityAdd
BLAST
Regioni2354 – 237724V3Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi5 – 139Nuclear localization signalSequence Analysis
Motifi38 – 436Nuclear localization signalSequence Analysis
Motifi58 – 647Nuclear localization signalSequence Analysis
Motifi66 – 716Nuclear localization signalSequence Analysis
Motifi1316 – 13194DECH box
Motifi2322 – 23254SH3-bindingSequence Analysis
Motifi2327 – 23359Nuclear localization signalSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi796 – 8038Poly-Leu
Compositional biasi1432 – 14354Poly-Val
Compositional biasi2282 – 232746Pro-richAdd
BLAST
Compositional biasi2995 – 29984Poly-Leu

Domaini

The transmembrane regions of envelope E1 and E2 glycoproteins are involved in heterodimer formation, ER localization, and assembly of these proteins. Envelope E2 glycoprotein contain two highly variable regions called hypervariable region 1 and 2 (HVR1 and HVR2). E2 also contain two segments involved in CD81-binding. HVR1 is implicated in the SCARB1-mediated cell entry. HVR2 and CD81-binding regions may be involved in sensitivity and/or resistance to IFN-alpha therapy By similarity.By similarity
The N-terminus of NS5A acts as membrane anchor. 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 PKR By similarity. The C-terminus of NS5A contains a variable region called variable region 3 (V3). ISDR and V3 may be involved in sensitivity and/or resistance to IFN-alpha therapy.By similarity
The SH3-binding domain of NS5A is involved in the interaction with human Bin1, GRB2 and Src-family kinases.
The N-terminal one-third of serine protease NS3 contains the protease activity. This region contains a zinc atom that does not belong to the active site, but may play a structural rather than a catalytic role. This region is essential for the activity of protease NS2-3, maybe by contributing to the folding of the latter. The helicase activity is located in the C-terminus of NS3.

Sequence similaritiesi

Belongs to the hepacivirus polyprotein family.Curated
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 peptidase C18 domain.PROSITE-ProRule annotation
Contains 1 peptidase S29 domain.Curated
Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3-binding, Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011492. DEAD_Flavivir.
IPR002521. HCV_core_C.
IPR002522. HCV_core_N.
IPR002519. HCV_env.
IPR002531. HCV_NS1.
IPR002518. HCV_NS2.
IPR000745. HCV_NS4a.
IPR001490. HCV_NS4b.
IPR002868. HCV_NS5a.
IPR013193. HCV_NS5a_1B_dom.
IPR024350. HCV_NS5a_C.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR013192. NS5A_1a.
IPR027417. P-loop_NTPase.
IPR004109. Peptidase_S29.
IPR007094. RNA-dir_pol_PSvirus.
IPR002166. RNA_pol_HCV.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF07652. Flavi_DEAD. 1 hit.
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.
[Graphical view]
ProDomiPD001388. HCV_env. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00487. DEXDc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiPS51693. HCV_NS2_PRO. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P26663-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSTNPKPQRK TKRNTNRRPQ DVKFPGGGQI VGGVYLLPRR GPRLGVRAPR
60 70 80 90 100
KTSERSQPRG RRQPIPKARR PEGRTWAQPG YPWPLYGNEG LGWAGWLLSP
110 120 130 140 150
RGSRPSWGPT DPRRRSRNLG KVIDTLTCGF ADLMGYIPLV GAPLGGAARA
160 170 180 190 200
LAHGVRVLED GVNYATGNLP GCSFSIFLLA LLSCLTTPAS AYEVHNVSGI
210 220 230 240 250
YHVTNDCSNA SIVYEAADLI MHTPGCVPCV REGNSSRCWV ALTPTLAARN
260 270 280 290 300
VTIPTTTIRR HVDLLVGAAA FCSAMYVGDL CGSVFLVSQL FTFSPRRHVT
310 320 330 340 350
LQDCNCSIYP GHVSGHRMAW DMMMNWSPTT ALVVSQLLRI PQAVVDMVAG
360 370 380 390 400
AHWGVLAGLA YYSMAGNWAK VLIVMLLFAG VDGDTHVTGG AQAKTTNRLV
410 420 430 440 450
SMFASGPSQK IQLINTNGSW HINRTALNCN DSLQTGFLAA LFYTHSFNSS
460 470 480 490 500
GCPERMAQCR TIDKFDQGWG PITYAESSRS DQRPYCWHYP PPQCTIVPAS
510 520 530 540 550
EVCGPVYCFT PSPVVVGTTD RFGVPTYRWG ENETDVLLLN NTRPPQGNWF
560 570 580 590 600
GCTWMNSTGF TKTCGGPPCN IGGVGNNTLT CPTDCFRKHP EATYTKCGSG
610 620 630 640 650
PWLTPRCMVD YPYRLWHYPC TVNFTIFKVR MYVGGVEHRL NAACNWTRGE
660 670 680 690 700
RCDLEDRDRP ELSPLLLSTT EWQVLPCSFT TLPALSTGLI HLHQNIVDVQ
710 720 730 740 750
YLYGIGSAVV SFAIKWEYVL LLFLLLADAR VCACLWMMLL IAQAEAALEN
760 770 780 790 800
LVVLNSASVA GAHGILSFLV FFCAAWYIKG RLVPGATYAL YGVWPLLLLL
810 820 830 840 850
LALPPRAYAM DREMAASCGG AVFVGLVLLT LSPYYKVFLA RLIWWLQYFT
860 870 880 890 900
TRAEADLHVW IPPLNARGGR DAIILLMCAV HPELIFDITK LLIAILGPLM
910 920 930 940 950
VLQAGITRVP YFVRAQGLIH ACMLVRKVAG GHYVQMAFMK LGALTGTYIY
960 970 980 990 1000
NHLTPLRDWP RAGLRDLAVA VEPVVFSDME TKIITWGADT AACGDIILGL
1010 1020 1030 1040 1050
PVSARRGKEI LLGPADSLEG RGLRLLAPIT AYSQQTRGLL GCIITSLTGR
1060 1070 1080 1090 1100
DKNQVEGEVQ VVSTATQSFL ATCVNGVCWT VYHGAGSKTL AAPKGPITQM
1110 1120 1130 1140 1150
YTNVDQDLVG WPKPPGARSL TPCTCGSSDL YLVTRHADVI PVRRRGDSRG
1160 1170 1180 1190 1200
SLLSPRPVSY LKGSSGGPLL CPFGHAVGIF RAAVCTRGVA KAVDFVPVES
1210 1220 1230 1240 1250
METTMRSPVF TDNSSPPAVP QSFQVAHLHA PTGSGKSTKV PAAYAAQGYK
1260 1270 1280 1290 1300
VLVLNPSVAA TLGFGAYMSK AHGIDPNIRT GVRTITTGAP VTYSTYGKFL
1310 1320 1330 1340 1350
ADGGCSGGAY DIIICDECHS TDSTTILGIG TVLDQAETAG ARLVVLATAT
1360 1370 1380 1390 1400
PPGSVTVPHP NIEEVALSNT GEIPFYGKAI PIEAIRGGRH LIFCHSKKKC
1410 1420 1430 1440 1450
DELAAKLSGL GINAVAYYRG LDVSVIPTIG DVVVVATDAL MTGYTGDFDS
1460 1470 1480 1490 1500
VIDCNTCVTQ TVDFSLDPTF TIETTTVPQD AVSRSQRRGR TGRGRRGIYR
1510 1520 1530 1540 1550
FVTPGERPSG MFDSSVLCEC YDAGCAWYEL TPAETSVRLR AYLNTPGLPV
1560 1570 1580 1590 1600
CQDHLEFWES VFTGLTHIDA HFLSQTKQAG DNFPYLVAYQ ATVCARAQAP
1610 1620 1630 1640 1650
PPSWDQMWKC LIRLKPTLHG PTPLLYRLGA VQNEVTLTHP ITKYIMACMS
1660 1670 1680 1690 1700
ADLEVVTSTW VLVGGVLAAL AAYCLTTGSV VIVGRIILSG RPAIVPDREL
1710 1720 1730 1740 1750
LYQEFDEMEE CASHLPYIEQ GMQLAEQFKQ KALGLLQTAT KQAEAAAPVV
1760 1770 1780 1790 1800
ESKWRALETF WAKHMWNFIS GIQYLAGLST LPGNPAIASL MAFTASITSP
1810 1820 1830 1840 1850
LTTQSTLLFN ILGGWVAAQL APPSAASAFV GAGIAGAAVG SIGLGKVLVD
1860 1870 1880 1890 1900
ILAGYGAGVA GALVAFKVMS GEMPSTEDLV NLLPAILSPG ALVVGVVCAA
1910 1920 1930 1940 1950
ILRRHVGPGE GAVQWMNRLI AFASRGNHVS PTHYVPESDA AARVTQILSS
1960 1970 1980 1990 2000
LTITQLLKRL HQWINEDCST PCSGSWLRDV WDWICTVLTD FKTWLQSKLL
2010 2020 2030 2040 2050
PQLPGVPFFS CQRGYKGVWR GDGIMQTTCP CGAQITGHVK NGSMRIVGPK
2060 2070 2080 2090 2100
TCSNTWHGTF PINAYTTGPC TPSPAPNYSR ALWRVAAEEY VEVTRVGDFH
2110 2120 2130 2140 2150
YVTGMTTDNV KCPCQVPAPE FFSEVDGVRL HRYAPACRPL LREEVTFQVG
2160 2170 2180 2190 2200
LNQYLVGSQL PCEPEPDVAV LTSMLTDPSH ITAETAKRRL ARGSPPSLAS
2210 2220 2230 2240 2250
SSASQLSAPS LKATCTTHHV SPDADLIEAN LLWRQEMGGN ITRVESENKV
2260 2270 2280 2290 2300
VVLDSFDPLR AEEDEREVSV PAEILRKSKK FPAAMPIWAR PDYNPPLLES
2310 2320 2330 2340 2350
WKDPDYVPPV VHGCPLPPIK APPIPPPRRK RTVVLTESSV SSALAELATK
2360 2370 2380 2390 2400
TFGSSESSAV DSGTATALPD QASDDGDKGS DVESYSSMPP LEGEPGDPDL
2410 2420 2430 2440 2450
SDGSWSTVSE EASEDVVCCS MSYTWTGALI TPCAAEESKL PINALSNSLL
2460 2470 2480 2490 2500
RHHNMVYATT SRSAGLRQKK VTFDRLQVLD DHYRDVLKEM KAKASTVKAK
2510 2520 2530 2540 2550
LLSVEEACKL TPPHSAKSKF GYGAKDVRNL SSKAVNHIHS VWKDLLEDTV
2560 2570 2580 2590 2600
TPIDTTIMAK NEVFCVQPEK GGRKPARLIV FPDLGVRVCE KMALYDVVST
2610 2620 2630 2640 2650
LPQVVMGSSY GFQYSPGQRV EFLVNTWKSK KNPMGFSYDT RCFDSTVTEN
2660 2670 2680 2690 2700
DIRVEESIYQ CCDLAPEARQ AIKSLTERLY IGGPLTNSKG QNCGYRRCRA
2710 2720 2730 2740 2750
SGVLTTSCGN TLTCYLKASA ACRAAKLQDC TMLVNGDDLV VICESAGTQE
2760 2770 2780 2790 2800
DAASLRVFTE AMTRYSAPPG DPPQPEYDLE LITSCSSNVS VAHDASGKRV
2810 2820 2830 2840 2850
YYLTRDPTTP LARAAWETAR HTPVNSWLGN IIMYAPTLWA RMILMTHFFS
2860 2870 2880 2890 2900
ILLAQEQLEK ALDCQIYGAC YSIEPLDLPQ IIERLHGLSA FSLHSYSPGE
2910 2920 2930 2940 2950
INRVASCLRK LGVPPLRVWR HRARSVRARL LSQGGRAATC GKYLFNWAVK
2960 2970 2980 2990 3000
TKLKLTPIPA ASRLDLSGWF VAGYSGGDIY HSLSRARPRW FMLCLLLLSV
3010
GVGIYLLPNR
Length:3,010
Mass (Da):327,194
Last modified:January 23, 2007 - v3
Checksum:iF8422D5ECCFDFD9C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M58335 Genomic RNA. Translation: AAA72945.1.
PIRiA38465. GNWVTC.

Cross-referencesi

Web resourcesi

euHCVdb

The European HCV database

Virus Pathogen Resource

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M58335 Genomic RNA. Translation: AAA72945.1 .
PIRi A38465. GNWVTC.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A1Q X-ray 2.40 A/B/C 1027-1215 [» ]
1BT7 NMR - A 1027-1206 [» ]
1C2P X-ray 1.90 A/B 2422-2989 [» ]
1CSJ X-ray 2.80 A/B 2420-2950 [» ]
1CU1 X-ray 2.50 A/B 1029-1657 [» ]
1GX5 X-ray 1.70 A 2420-2955 [» ]
1GX6 X-ray 1.85 A 2420-2950 [» ]
1JXP X-ray 2.20 A/B 1027-1206 [» ]
C/D 1678-1691 [» ]
1NHU X-ray 2.00 A/B 2420-2989 [» ]
1NHV X-ray 2.90 A/B 2420-2989 [» ]
1NS3 X-ray 2.80 A/B 1029-1206 [» ]
C/D 1678-1689 [» ]
1OS5 X-ray 2.20 A 2420-2989 [» ]
1QUV X-ray 2.50 A 2420-2989 [» ]
2AWZ X-ray 2.15 A/B 2420-2989 [» ]
2AX0 X-ray 2.00 A/B 2420-2989 [» ]
2AX1 X-ray 2.10 A/B 2420-2989 [» ]
2BRK X-ray 2.30 A 2420-2955 [» ]
2BRL X-ray 2.40 A 2420-2955 [» ]
2DXS X-ray 2.20 A/B 2420-2963 [» ]
2GIQ X-ray 1.65 A/B 2421-2981 [» ]
2GIR X-ray 1.90 A/B 2421-2981 [» ]
2HAI X-ray 1.58 A 2420-2988 [» ]
2HWH X-ray 2.30 A/B 2422-2989 [» ]
2HWI X-ray 2.00 A/B 2422-2989 [» ]
2I1R X-ray 2.20 A/B 2422-2989 [» ]
2JC0 X-ray 2.20 A/B 2420-2989 [» ]
2JC1 X-ray 2.00 A/B 2420-2989 [» ]
2O5D X-ray 2.20 A/B 2422-2989 [» ]
2WCX X-ray 2.00 A 2420-2955 [» ]
2WHO X-ray 2.00 A/B 2420-2955 [» ]
2WRM X-ray 1.95 A 2420-2955 [» ]
2XWY X-ray 2.53 A 2420-2955 [» ]
2ZKU X-ray 1.95 A/B/C/D 2420-2989 [» ]
3BR9 X-ray 2.30 A/B 2420-2989 [» ]
3BSA X-ray 2.30 A/B 2420-2989 [» ]
3BSC X-ray 2.65 A/B 2420-2989 [» ]
3CDE X-ray 2.10 A/B 2420-2989 [» ]
3CIZ X-ray 1.87 A/B 2421-2989 [» ]
3CJ0 X-ray 1.90 A/B 2421-2989 [» ]
3CJ2 X-ray 1.75 A/B 2421-2989 [» ]
3CJ3 X-ray 1.87 A/B 2421-2989 [» ]
3CJ4 X-ray 2.07 A/B 2421-2989 [» ]
3CJ5 X-ray 1.92 A/B 2421-2989 [» ]
3CO9 X-ray 2.10 A/B 2420-2989 [» ]
3CVK X-ray 2.31 A/B 2420-2989 [» ]
3CWJ X-ray 2.40 A/B 2420-2989 [» ]
3D28 X-ray 2.30 A/B 2420-2989 [» ]
3D5M X-ray 2.20 A/B 2420-2989 [» ]
3E51 X-ray 1.90 A/B 2420-2989 [» ]
3FQK X-ray 2.20 A/B 2421-2989 [» ]
3FRZ X-ray 1.86 A 2420-2989 [» ]
3G86 X-ray 2.20 A/B 2421-2989 [» ]
3GYN X-ray 2.15 A/B 2420-2989 [» ]
3H2L X-ray 1.90 A/B 2420-2989 [» ]
3H59 X-ray 2.10 A/B 2421-2989 [» ]
3H5S X-ray 2.00 A/B 2421-2989 [» ]
3H5U X-ray 1.95 A/B 2421-2989 [» ]
3H98 X-ray 1.90 A/B 2421-2989 [» ]
3IGV X-ray 2.60 A/B 2420-2989 [» ]
3MF5 X-ray 2.00 A/B 2421-2989 [» ]
3UA7 X-ray 1.50 E/F 2321-2331 [» ]
3UDL X-ray 2.17 A/B/C/D 2420-2989 [» ]
3VQS X-ray 1.90 A/B/C/D 2420-2989 [» ]
4A92 X-ray 2.73 A/B 1029-1657 [» ]
A/B 1678-1690 [» ]
4B6E X-ray 2.46 A/B 1029-1657 [» ]
4B6F X-ray 2.89 A/B 1029-1657 [» ]
4B71 X-ray 2.50 A/B 1029-1657 [» ]
4B73 X-ray 2.50 A/B 1029-1657 [» ]
4B74 X-ray 2.18 A/B 1029-1657 [» ]
4B75 X-ray 2.53 A/B 1029-1655 [» ]
4B76 X-ray 2.14 A/B 1029-1657 [» ]
4DGV X-ray 1.80 A 412-423 [» ]
4DGY X-ray 1.80 A 412-423 [» ]
4EO6 X-ray 1.79 A/B 2422-2989 [» ]
4EO8 X-ray 1.80 A/B 2422-2989 [» ]
4IH5 X-ray 1.90 A/B 2421-2989 [» ]
4IH6 X-ray 2.20 A/B 2421-2989 [» ]
4IH7 X-ray 2.30 A/B 2421-2989 [» ]
4K8B X-ray 2.80 C/D 1678-1689 [» ]
4KAI X-ray 2.30 A/B 2420-2989 [» ]
4KB7 X-ray 1.85 A/B 2420-2989 [» ]
4KBI X-ray 2.06 A/B 2420-2989 [» ]
4KE5 X-ray 2.11 A/B 2420-2989 [» ]
4MIA X-ray 2.80 A/B 2421-2989 [» ]
4MIB X-ray 2.30 A/B 2421-2989 [» ]
4MK7 X-ray 2.80 A/B 2421-2989 [» ]
4MK8 X-ray 2.09 A/B 2421-2989 [» ]
4MK9 X-ray 2.05 A/B 2421-2989 [» ]
4MKA X-ray 2.05 A/B 2421-2989 [» ]
4MKB X-ray 1.90 A/B 2421-2989 [» ]
8OHM X-ray 2.30 A 1216-1650 [» ]
ProteinModelPortali P26663.
SMRi P26663. Positions 2-45, 902-1026, 1029-1657, 1973-2003, 2008-2170, 2420-2983.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P26663. 6 interactions.
MINTi MINT-6548567.

Chemistry

BindingDBi P26663.
ChEMBLi CHEMBL6040.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

euHCVdbi M58335.

Miscellaneous databases

EvolutionaryTracei P26663.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR011492. DEAD_Flavivir.
IPR002521. HCV_core_C.
IPR002522. HCV_core_N.
IPR002519. HCV_env.
IPR002531. HCV_NS1.
IPR002518. HCV_NS2.
IPR000745. HCV_NS4a.
IPR001490. HCV_NS4b.
IPR002868. HCV_NS5a.
IPR013193. HCV_NS5a_1B_dom.
IPR024350. HCV_NS5a_C.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR013192. NS5A_1a.
IPR027417. P-loop_NTPase.
IPR004109. Peptidase_S29.
IPR007094. RNA-dir_pol_PSvirus.
IPR002166. RNA_pol_HCV.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF07652. Flavi_DEAD. 1 hit.
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.
[Graphical view ]
ProDomi PD001388. HCV_env. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00487. DEXDc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEi PS51693. HCV_NS2_PRO. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Structure and organization of the hepatitis C virus genome isolated from human carriers."
    Takamizawa A., Mori C., Fuke I., Manabe S., Murakami S., Fujita J., Onishi E., Andoh T., Yoshida I., Okayama H.
    J. Virol. 65:1105-1113(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Non-structural protein 3 of hepatitis C virus inhibits phosphorylation mediated by cAMP-dependent protein kinase."
    Borowski P., Heiland M., Oehlmann K., Becker B., Korneteky L.
    Eur. J. Biochem. 237:611-618(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1487-1500.
  3. "Biosynthesis and biochemical properties of the hepatitis C virus core protein."
    Santolini E., Migliaccio G., La Monica N.
    J. Virol. 68:3631-3641(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, RNA-BINDING ACTIVITY OF CORE PROTEIN.
  4. "In vitro study of the NS2-3 protease of hepatitis C virus."
    Pieroni L., Santolini E., Fipaldini C., Pacini L., Migliaccio G., La Monica N.
    J. Virol. 71:6373-6380(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF PROTEASE NS2-3.
  5. "Control of PKR protein kinase by hepatitis C virus nonstructural 5A protein: molecular mechanisms of kinase regulation."
    Gale M.J. Jr., Blakely C.M., Kwieciszewski B., Tan S.-L., Dossett M., Tang N.M., Korth M.J., Polyak S.J., Gretch D.R., Katze M.G.
    Mol. Cell. Biol. 18:5208-5218(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF NS5A.
  6. "NS5A, a nonstructural protein of hepatitis C virus, binds growth factor receptor-bound protein 2 adaptor protein in a Src homology 3 domain/ligand-dependent manner and perturbs mitogenic signaling."
    Tan S.-L., Nakao H., He Y., Vijaysri S., Neddermann P., Jacobs B.L., Mayer B.J., Katze M.G.
    Proc. Natl. Acad. Sci. U.S.A. 96:5533-5538(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION OF NS5A WITH HUMAN GRB2, MUTAGENESIS OF PRO-2322; PRO-2323 AND PRO-2326.
  7. "Ser(2194) is a highly conserved major phosphorylation site of the hepatitis C virus nonstructural protein NS5A."
    Katze M.G., Kwieciszewski B., Goodlett D.R., Blakely C.M., Neddermann P., Tan S.-L., Aebersold R.
    Virology 278:501-513(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF SER-2194.
  8. "In vitro characterization of a purified NS2/3 protease variant of hepatitis C virus."
    Thibeault D., Maurice R., Pilote L., Lamarre D., Pause A.
    J. Biol. Chem. 276:46678-46684(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF PROTEASE NS2-3.
  9. "Subversion of cell signaling pathways by hepatitis C virus nonstructural 5A protein via interaction with Grb2 and P85 phosphatidylinositol 3-kinase."
    He Y., Nakao H., Tan S.-L., Polyak S.J., Neddermann P., Vijaysri S., Jacobs B.L., Katze M.G.
    J. Virol. 76:9207-9217(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION OF NS5A WITH HUMAN PIK3R1.
  10. "Mutations within the CD81-binding sites and hypervariable region 2 of the envelope 2 protein: correlation with treatment response in hepatitis C virus-infected patients."
    Hofmann W.P., Sarrazin C., Kronenberger B., Schonberger B., Bruch K., Zeuzem S.
    J. Infect. Dis. 187:982-987(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAINS CD81-BINDING AND HVR2.
  11. "High-throughput screening of the yeast kinome: identification of human serine/threonine protein kinases that phosphorylate the hepatitis C virus NS5A protein."
    Coito C., Diamond D.L., Neddermann P., Korth M.J., Katze M.G.
    J. Virol. 78:3502-3513(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION OF NS5A.
  12. "Genetic variability of hepatitis C virus in chronically infected patients with viral breakthrough during interferon-ribavirin therapy."
    Vuillermoz I., Khattab E., Sablon E., Ottevaere I., Durantel D., Vieux C., Trepo C., Zoulim F.
    J. Med. Virol. 74:41-53(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAINS ISDR AND V3 REGIONS.
  13. "Systematic identification of hepatocellular proteins interacting with NS5A of the hepatitis C virus."
    Ahn J., Chung K.-S., Kim D.-U., Won M., Kim L., Kim K.-S., Nam M., Choi S.-J., Kim H.-C., Yoon M., Chae S.-K., Hoe K.-L.
    J. Biochem. Mol. Biol. 37:741-748(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION OF NS5A WITH CELLULAR PROTEINS.
  14. "The SH3 binding motif of HCV NS5A protein interacts with Bin1 and is important for apoptosis and infectivity."
    Nanda S.K., Herion D., Liang T.J.
    Gastroenterology 130:794-809(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION OF NS5A WITH HUMAN BIN1, FUNCTION OF NS5A.
  15. "Up-regulation of fatty acid synthase promoter by hepatitis C virus core protein: genotype-3a core has a stronger effect than genotype-1b core."
    Jackel-Cram C., Babiuk L.A., Liu Q.
    J. Hepatol. 46:999-1008(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION OF CORE PROTEIN, FUNCTION OF CORE PROTEIN.
  16. "Properties of the hepatitis C virus core protein: a structural protein that modulates cellular processes."
    McLauchlan J.
    J. Viral Hepat. 7:2-14(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  17. Cited for: REVIEW, SUBCELLULAR LOCATION.
  18. "An RNA-binding protein, hnRNP A1, and a scaffold protein, septin 6, facilitate hepatitis C virus replication."
    Kim C.S., Seol S.K., Song O.-K., Park J.H., Jang S.K.
    J. Virol. 81:3852-3865(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HNRNPA1 AND SEPT6.
  19. "The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site."
    Love R.A., Parge H.E., Wickersham J.A., Hostomsky Z., Habuka N., Moomaw E.W., Adachi T., Hostomska Z.
    Cell 87:331-342(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1027-1215.
  20. "Complex of NS3 protease and NS4A peptide of BK strain hepatitis C virus: a 2.2-A resolution structure in a hexagonal crystal form."
    Yan Y., Li Y., Munshi S., Sardana V., Cole J.L., Sardana M., Steinkuehler C., Tomei L., de Francesco R., Kuo L.C., Chen Z.
    Protein Sci. 7:837-847(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1027-1206 AND 1678-1691.
  21. "Crystal structure of RNA helicase from genotype 1b hepatitis C virus. A feasible mechanism of unwinding duplex RNA."
    Cho H.-S., Ha N.-C., Kang L.-W., Chung K.M., Back S.H., Jang S.K., Oh B.-H.
    J. Biol. Chem. 273:15045-15052(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1216-1650.
  22. "Molecular views of viral polyprotein processing revealed by the crystal structure of the hepatitis C virus bifunctional protease-helicase."
    Yao N., Reichert P., Taremi S.S., Prosise W.W., Weber P.C.
    Structure 7:1353-1363(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1013-1657.
  23. "The solution structure of the N-terminal proteinase domain of the hepatitis C virus (HCV) NS3 protein provides new insights into its activation and catalytic mechanism."
    Barbato G., Cicero D.O., Nardi M.C., Steinkuehler C., Cortese R., De Francesco R., Bazzo R.
    J. Mol. Biol. 289:371-384(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1027-1206.
  24. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2420-2950.
  25. "Crystal structure of the RNA-dependent RNA polymerase from hepatitis C virus reveals a fully encircled active site."
    Lesburg C.A., Cable M.B., Ferrari E., Hong Z., Mannarino A.F., Weber P.C.
    Nat. Struct. Biol. 6:937-943(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2414-2989.
  26. "Crystal structure of the RNA-dependent RNA polymerase of hepatitis C virus."
    Ago H., Adachi T., Yoshida A., Yamamoto M., Habuka N., Yatsunami K., Miyano M.
    Structure 7:1417-1426(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2420-2999.
  27. "Structural analysis of the hepatitis C virus RNA polymerase in complex with ribonucleotides."
    Bressanelli S., Tomei L., Rey F.A., De Francesco R.
    J. Virol. 76:3482-3492(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2420-2955.
  28. "Non-nucleoside analogue inhibitors bind to an allosteric site on HCV NS5B polymerase. Crystal structures and mechanism of inhibition."
    Wang M., Ng K.K.-S., Cherney M.M., Chan L., Yannopoulos C.G., Bedard J., Morin N., Nguyen-Ba N., Alaoui-Ismaili M.H., Bethell R.C., James M.N.G.
    J. Biol. Chem. 278:9489-9495(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2420-2989 IN COMPLEX WITH A NON-NUCLEOSIDE INHIBITOR.
  29. "Crystallographic identification of a noncompetitive inhibitor binding site on the hepatitis C virus NS5B RNA polymerase enzyme."
    Love R.A., Parge H.E., Yu X., Hickey M.J., Diehl W., Gao J., Wriggers H., Ekker A., Wang L., Thomson J.A., Dragovich P.S., Fuhrman S.A.
    J. Virol. 77:7575-7581(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 2420-2995 IN COMPLEX WITH AN INHIBITOR.

Entry informationi

Entry nameiPOLG_HCVBK
AccessioniPrimary (citable) accession number: P26663
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 167 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

Cell culture adaptation of the virus leads to mutations in NS5A, reducing its inhibitory effect on replication.By similarity
Core protein 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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3