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Protein
Submitted name:

Non-structural protein 4a/b

Gene

NS4a/b

Organism
Hepatitis C virus
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Submitted name:
Non-structural protein 4a/bImported
Gene namesi
Name:NS4a/bImported
OrganismiHepatitis C virusImported
Taxonomic identifieri11103 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageFlaviviridaeHepacivirus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A1RX-ray2.50C/D6-24[»]
1N1LX-ray2.60C/D6-24[»]
1RGQX-ray2.90C/D6-24[»]
1RTLX-ray2.75C/D6-24[»]
2A4QX-ray2.45B/D6-24[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO39914.

Family & Domainsi

Family and domain databases

InterProiIPR000745. HCV_NS4a.
[Graphical view]
PfamiPF01006. HCV_NS4a. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

O39914-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
YCLTTGSVVI VGRIILSGKP AIIPDREVLY QAFDEMEECA SHLPYIEHGM
60 70 80
QLAEQFKQKA LGLLQTATKQ AEAAAPVVES KWRALETF
Length:88
Mass (Da):9,750
Last modified:June 1, 2002 - v2
Checksum:iBF7B5198B317B6E0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11Imported
Non-terminal residuei88 – 881Imported

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF007519 Genomic RNA. Translation: AAB62970.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF007519 Genomic RNA. Translation: AAB62970.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A1RX-ray2.50C/D6-24[»]
1N1LX-ray2.60C/D6-24[»]
1RGQX-ray2.90C/D6-24[»]
1RTLX-ray2.75C/D6-24[»]
2A4QX-ray2.45B/D6-24[»]
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

euHCVdbiAF007519.

Miscellaneous databases

EvolutionaryTraceiO39914.

Family and domain databases

InterProiIPR000745. HCV_NS4a.
[Graphical view]
PfamiPF01006. HCV_NS4a. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Crystal structure of the hepatitis C virus NS3 protease domain complexed with a synthetic NS4A cofactor peptide."
    Kim J.L., Morgenstern K.A., Lin C., Fox T., Dwyer M.D., Landro J.A., Chambers S.P., Markland W., Lepre C.A., O'Malley E.T., Harbeson S.L., Rice C.M., Murcko M.A., Caron P.R., Thomson J.A.
    Cell 87:343-355(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 6-24.
  2. "Sequence analysis of hepatitis C virus variants producing discrepant results with two different genotyping assays."
    Prescott L.E., Berger A., Pawlotsky J.M., Conjeevaram P., Pike I., Simmonds P.
    J. Med. Virol. 53:237-244(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  3. "Pyrrolidine-5,5-trans-lactams. 2. The use of X-ray crystal structure data in the optimization of P3 and P4 substituents."
    Andrews D.M., Chaignot H., Coomber B.A., Good A.C., Hind S.L., Johnson M.R., Jones P.S., Mills G., Robinson J.E., Skarzynski T., Slater M.J., Somers D.O.
    Org. Lett. 4:4479-4482(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 6-24.
  4. "Pyrrolidine-5,5-trans-lactams. 4. Incorporation of a P3/P4 urea leads to potent intracellular inhibitors of hepatitis C virus NS3/4A protease."
    Slater M.J., Amphlett E.M., Andrews D.M., Bamborough P., Carey S.J., Johnson M.R., Jones P.S., Mills G., Parry N.R., Somers D.O., Stewart A.J., Skarzynski T.
    Org. Lett. 5:4627-4630(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 6-24.
  5. "Hepatitis C NS3 protease inhibition by peptidyl-alpha-ketoamide inhibitors: kinetic mechanism and structure."
    Liu Y., Stoll V.S., Richardson P.L., Saldivar A., Klaus J.L., Molla A., Kohlbrenner W., Kati W.M.
    Arch. Biochem. Biophys. 421:207-216(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 6-24.
  6. "Synthesis and biological activity of macrocyclic inhibitors of hepatitis C virus (HCV) NS3 protease."
    Chen K.X., Njoroge F.G., Prongay A., Pichardo J., Madison V., Girijavallabhan V.
    Bioorg. Med. Chem. Lett. 15:4475-4478(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 6-24.

Entry informationi

Entry nameiO39914_9HEPC
AccessioniPrimary (citable) accession number: O39914
Entry historyi
Integrated into UniProtKB/TrEMBL: January 1, 1998
Last sequence update: June 1, 2002
Last modified: January 7, 2015
This is version 49 of the entry and version 2 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.