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Q5EG65

- POLG_HCVGL

UniProt

Q5EG65 - POLG_HCVGL

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Protein

Genome polyprotein

Gene
N/A
Organism
Hepatitis C virus (isolate Glasgow) (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

Enzyme regulationi

Activity of auto-protease NS2-3 is dependent on zinc ions and completely inhibited by EDTA.By similarity

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

GO - Molecular functioni

  1. cysteine-type peptidase activity Source: UniProtKB-KW
  2. ion channel activity Source: UniProtKB-KW
  3. RNA binding Source: UniProtKB-KW
  4. structural molecule activity Source: InterPro

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. clathrin-mediated endocytosis of virus by host cell Source: UniProtKB-KW
  3. evasion or tolerance by virus of host immune response Source: UniProtKB-KW
  4. fusion of virus membrane with host endosome membrane Source: UniProtKB-KW
  5. pore formation by virus in membrane of host cell Source: UniProtKB-KW
  6. protein oligomerization Source: UniProtKB-KW
  7. virion attachment to host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Ion channel, Protease, Ribonucleoprotein, Thiol protease, Viral ion channel

Keywords - Biological processi

Apoptosis, Clathrin-mediated endocytosis of virus by host, Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Interferon antiviral system evasion, Ion transport, Transport, Viral attachment to host cell, Viral penetration into host cytoplasm, Virus endocytosis by host, Virus entry into host cell

Keywords - Ligandi

RNA-binding, Viral nucleoprotein, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 6 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
OrganismiHepatitis C virus (isolate Glasgow) (HCV)
Taxonomic identifieri329389 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageFlaviviridaeHepacivirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]

Subcellular locationi

Chain Core protein p21 : Host endoplasmic reticulum membrane By similarity; Single-pass membrane protein By similarity. Host mitochondrion membrane By similarity; Single-pass type I membrane protein By similarity. Host lipid droplet By similarity
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 (By similarity).By similarity
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 (By similarity).By similarity
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 (By similarity).By similarity
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 (By similarity).By similarity

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
Mutagenesisi180 – 1845ALLSC → VLLLV: Complete loss of processing. 1 Publication

Keywords - Diseasei

Oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed; by hostBy similarity
Chaini2 – 191190Core protein p21PRO_0000037559Add
BLAST
Chaini2 – 177176Core protein p19By similarityPRO_0000037560Add
BLAST
Propeptidei178 – 19114ER anchor for the core protein, removed in mature form by host signal peptidaseBy similarityPRO_0000037561Add
BLAST
Chaini192 – 383192Envelope glycoprotein E1Sequence AnalysisPRO_0000037562Add
BLAST
Chaini384 – 746363Envelope glycoprotein E2Sequence AnalysisPRO_0000037563Add
BLAST
Chaini747 – 80963p7By similarityPRO_0000037564Add
BLAST
Chaini810 – ›829›20Protease NS2-3Sequence AnalysisPRO_0000037565Add
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
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
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

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 and NS2-3) 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
Core protein is ubiquitinated; mediated by UBE3A and leading to core protein subsequent proteasomal degradation.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, 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, 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 (By similarity).By similarity

Protein-protein interaction databases

IntActiQ5EG65. 1 interaction.

Structurei

Secondary structure

1
829
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi414 – 4163
Beta strandi419 – 4213

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GAGX-ray1.80P412-423[»]
ProteinModelPortaliQ5EG65.
SMRiQ5EG65. Positions 2-45.
ModBaseiSearch...
MobiDBiSearch...

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

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 – ›829›16HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

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
Regioni150 – 15910Mitochondrial targeting signalBy similarity
Regioni164 – 1674Important for lipid droplets localizationBy similarity
Regioni265 – 29632Fusion peptideSequence AnalysisAdd
BLAST
Regioni385 – 41127HVR1By similarityAdd
BLAST
Regioni475 – 4817HVR2By similarity
Regioni482 – 49413CD81-binding 1Sequence AnalysisAdd
BLAST
Regioni522 – 55332CD81-binding 2Sequence AnalysisAdd
BLAST
Regioni660 – 67112PKR/eIF2-alpha phosphorylation homology domain (PePHD)Add
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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi476 – 4794Poly-Gly
Compositional biasi796 – 8038Poly-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) and two CD81-binding sites. HVR1 is implicated in the SCARB1-mediated cell entry. HVR2 and CD81-binding sites may be involved in sensitivity and/or resistance to IFN-alpha therapy (By similarity).By similarity

Sequence similaritiesi

Belongs to the hepacivirus polyprotein family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

InterProiIPR002521. HCV_core_C.
IPR002522. HCV_core_N.
IPR002519. HCV_env.
IPR002531. HCV_NS1.
[Graphical view]
PfamiPF01543. HCV_capsid. 1 hit.
PF01542. HCV_core. 1 hit.
PF01539. HCV_env. 1 hit.
PF01560. HCV_NS1. 1 hit.
[Graphical view]
ProDomiPD001388. HCV_env. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Fragment.

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

Q5EG65-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSTNPKPQRK TKRNTNRRPQ DVKFPGGGQI VGGVYLLPRR GPRLGVRATR
60 70 80 90 100
KTSERSQPRG RRQPIPKARR PKGRNWAQPG YPWPLYGNEG CGWAGWLPSP
110 120 130 140 150
RGSRPSWGPN DPRRRSRNLG KVIDTLTCGF VDLMGYIPLV GAPLRGAARA
160 170 180 190 200
LAHGVRVLED GVNYATGNLP GCSFSIFLLA LLSCLTVPAS AYQVRNSTGL
210 220 230 240 250
YHVTNDCPNS SIVYEAVDAI LHTPGCVPCV REGNASRCWV AMTPTVATRD
260 270 280 290 300
GRLPTTQLRR HIDLLVGSAT LCSALYVGDL CGSVFLVGQL FTFSPRRHWT
310 320 330 340 350
TQGCNCSIYP GHITGHRMAW DMMMNWSPTT ALVVAQLLRI PQAILDMIAG
360 370 380 390 400
AHWGVLAGMA YFSMVGNWAK VLAVLLLFAG VDAETHVTGG AAARSTLQLA
410 420 430 440 450
GLFQPGAKQN VQLINTNGSW HVNRTALNCN DSLNTGWIAG LFYYHGFNSS
460 470 480 490 500
GCSERLASCR SLTDFDQGWG PISYAGGGGP DHRPYCWHYP PKPCGIVPAK
510 520 530 540 550
SVCGPVYCFT PSPVVVGTTD RSGAPTYSWG ADDTDVFVLN NTRPPLGNWF
560 570 580 590 600
GCTWMNSTGF TKVCGAPPCV IGGVGNNTLH CPTDCFRKHP EATYSRCGSG
610 620 630 640 650
PWLTPRCLVD YPYRLWHYPC TINHSIFKVR MYVGGVEHRL DAACNWTRGE
660 670 680 690 700
RCDLEDRDRS ELSPLLLSTT QWQVLPCSFT TLPALSTGLI HLHQNIVDVQ
710 720 730 740 750
YLYGVGSSIA SWAIKWEYVV LLFLLLADAR VCSCLWMMLL ISQAEAALEN
760 770 780 790 800
LVVLNAASLA GTHGLVSFLV FFCFAWFLRG KWVPGAVYAL YGMWPLLLLL
810 820
LALPQRAYAL DTEVAASCGG VVLVGLMAL
Length:829
Mass (Da):90,587
Last modified:January 23, 2007 - v3
Checksum:i17AD3868F50B4AD4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei829 – 8291

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY885238 Genomic RNA. Translation: AAW78019.1.

Cross-referencesi

Web resourcesi

euHCVdb

The European HCV database

Virus Pathogen Resource

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY885238 Genomic RNA. Translation: AAW78019.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4GAG X-ray 1.80 P 412-423 [» ]
ProteinModelPortali Q5EG65.
SMRi Q5EG65. Positions 2-45.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q5EG65. 1 interaction.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

euHCVdbi AY885238.

Family and domain databases

InterProi IPR002521. HCV_core_C.
IPR002522. HCV_core_N.
IPR002519. HCV_env.
IPR002531. HCV_NS1.
[Graphical view ]
Pfami PF01543. HCV_capsid. 1 hit.
PF01542. HCV_core. 1 hit.
PF01539. HCV_env. 1 hit.
PF01560. HCV_NS1. 1 hit.
[Graphical view ]
ProDomi PD001388. HCV_env. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
ProtoNeti Search...

Publicationsi

  1. "Covalent interactions are not required to permit or stabilize the non-covalent association of hepatitis C virus glycoproteins E1 and E2."
    Patel J., Patel A.H., McLauchlan J.
    J. Gen. Virol. 80:1681-1690(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Hepatitis C virus core protein interacts with a human DEAD box protein DDX3."
    Owsianka A.M., Patel A.H.
    Virology 257:330-340(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION OF CORE PROTEIN WITH HUMAN DDX3X.
  3. "Intramembrane proteolysis promotes trafficking of hepatitis C virus core protein to lipid droplets."
    McLauchlan J., Lemberg M.K., Hope G., Martoglio B.
    EMBO J. 21:3980-3988(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE OF CORE PROTEIN BY THE SIGNAL PEPTIDASE, SUBCELLULAR LOCATION, MUTAGENESIS OF 180-ALA--CYS-184.
  4. "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.
  5. Cited for: REVIEW, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiPOLG_HCVGL
AccessioniPrimary (citable) accession number: Q5EG65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 78 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Documents

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

External Data

Dasty 3