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P04585 (POL_HV1H2) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 178. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Gag-Pol polyprotein
Alternative name(s):
Pr160Gag-Pol

Cleaved into the following 11 chains:

  1. Matrix protein p17
    Short name=MA
  2. Capsid protein p24
    Short name=CA
  3. Spacer peptide p2
  4. Nucleocapsid protein p7
    Short name=NC
  5. Transframe peptide
    Short name=TF
  6. p6-pol
    Short name=p6*
  7. Protease
    EC=3.4.23.16
    Alternative name(s):
    PR
    Retropepsin
  8. Reverse transcriptase/ribonuclease H
    EC=2.7.7.49
    EC=2.7.7.7
    EC=3.1.26.13
    Alternative name(s):
    Exoribonuclease H
    EC=3.1.13.2
    p66 RT
  9. p51 RT
  10. p15
  11. Integrase
    Short name=IN
Gene names
Name:gag-pol
OrganismHuman immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1) [Reference proteome]
Taxonomic identifier11706 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusPrimate lentivirus group
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length1435 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Gag-Pol polyprotein and Gag polyprotein may regulate their own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, Gag-Pol and Gag would promote translation, whereas at high concentration, the polyproteins encapsidate genomic RNA and then shutt off translation. Ref.8 Ref.19 Ref.21 Ref.23 Ref.24 Ref.25

Matrix protein p17 has two main functions: in infected cell, it targets Gag and Gag-pol polyproteins to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus. The second function is to play a role in nuclear localization of the viral genome at the very start of cell infection. Matrix protein is the part of the pre-integration complex. It binds in the cytoplasm the human BAF protein which prevent autointegration of the viral genome, and might be included in virions at the ration of zero to 3 BAF dimer per virion. The myristoylation signal and the NLS thus exert conflicting influences its subcellular localization. The key regulation of these motifs might be phosphorylation of a portion of MA molecules on the C-terminal tyrosine at the time of virus maturation, by virion-associated cellular tyrosine kinase. Implicated in the release from host cell mediated by Vpu. Ref.8 Ref.19 Ref.21 Ref.23 Ref.24 Ref.25

Capsid protein p24 forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry. Interaction with human PPIA/CYPA protects the virus from restriction by human TRIM5-alpha and from an unknown antiviral activity in human cells. This capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species. Ref.8 Ref.19 Ref.21 Ref.23 Ref.24 Ref.25

Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers. Facilitates rearangement of nucleic acid secondary structure during retrotranscription of genomic RNA. This capability is referred to as nucleic acid chaperone activity. Ref.8 Ref.19 Ref.21 Ref.23 Ref.24 Ref.25

The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. Also cleaves Nef and Vif, probably concomitantly with viral structural proteins on maturation of virus particles By similarity. Hydrolyzes host EIF4GI and PABP1 in order to shut off the capped cellular mRNA translation. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response. Ref.8 Ref.19 Ref.21 Ref.23 Ref.24 Ref.25

Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that converts the viral RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA(3)-Lys binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for two polypurine tracts (PPTs) situated at the 5'-end and near the center of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPTs that have not been removed by RNase H as primers. PPTs and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends. Ref.8 Ref.19 Ref.21 Ref.23 Ref.24 Ref.25

Integrase catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein, Vpr and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step, the PIC enters cell nucleus. This process is mediated through integrase and Vpr proteins, and allows the virus to infect a non dividing cell. This ability to enter the nucleus is specific of lentiviruses, other retroviruses cannot and rely on cell division to access cell chromosomes. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The 5'-ends are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination intermediate results, with the 5'-ends of the viral DNA strands and the 3' ends of target DNA strands remaining unjoined, flanking a gap of 5 bp. The last step is viral DNA integration into host chromosome. This involves host DNA repair synthesis in which the 5 bp gaps between the unjoined strands are filled in and then ligated. Since this process occurs at both cuts flanking the HIV genome, a 5 bp duplication of host DNA is produced at the ends of HIV-1 integration. Alternatively, Integrase may catalyze the excision of viral DNA just after strand transfer, this is termed disintegration. Ref.8 Ref.19 Ref.21 Ref.23 Ref.24 Ref.25

Catalytic activity

Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.

Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus.

3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid.

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

Cofactor

Binds 2 magnesium ions for reverse transcriptase polymerase activity By similarity.

Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is a precondition for magnesium binding By similarity.

Magnesium ions for integrase activity. Binds at least 1, maybe 2 magnesium ions By similarity.

Enzyme regulation

The viral protease is inhibited by many synthetic protease inhibitors (PIs), such as amprenavir, atazanavir, indinavir, loprinavir, nelfinavir, ritonavir and saquinavir. RT can be inhibited either by nucleoside RT inhibitors (NRTIs) or by non nucleoside RT inhibitors (NNRTIs). NRTIs act as chain terminators, whereas NNRTIs inhibit DNA polymerization by binding a small hydrophobic pocket near the RT active site and inducing an allosteric change in this region. Classical NRTIs are abacavir, adefovir (PMEA), didanosine (ddI), lamivudine (3TC), stavudine (d4T), tenofovir (PMPA), zalcitabine (ddC), and zidovudine (AZT). Classical NNRTIs are atevirdine (BHAP U-87201E), delavirdine, efavirenz (DMP-266), emivirine (I-EBU), and nevirapine (BI-RG-587). The tritherapies used as a basic effective treatment of AIDS associate two NRTIs and one NNRTI. Use of protease inhibitors in tritherapy regimens permit more ambitious therapeutic strategies.

Subunit structure

Pre-integration complex interacts with human HMGA1. Matrix protein p17 is a trimer. Interacts with gp120 and human BAF. Capsid is a homodimer. Interacts with human PPIA/CYPA. The protease is a homodimer, whose active site consists of two apposed aspartic acid residues. The reverse transcriptase is a heterodimer of p66 RT and p51 RT (RT p66/p51). Heterodimerization of RT is essential for DNA polymerase activity. Despite the sequence identities, p66 RT and p51 RT have distinct folding. Integrase is a homodimer and possibly can form homotetramer. Integrase interacts with human SMARCB1/INI1 and human PSIP1/LEDGF isoform 1 Integrase interacts with human KPNA3; this interaction might play a role in nuclear import of the pre-integration complex. Integrase interacts with human NUP153; this interaction might play a role in nuclear import of the pre-integration complex By similarity. Ref.6 Ref.7 Ref.14 Ref.17 Ref.24

Subcellular location

Matrix protein p17: Virion Potential. Host nucleus By similarity. Host cytoplasm By similarity. Host cell membrane; Lipid-anchor Potential. Note: Following virus entry, the nuclear localization signal (NLS) of the matrix protein participates with Vpr to the nuclear localization of the viral genome. During virus production, the nuclear export activity of the matrix protein counteracts the NLS to maintain the Gag and Gag-Pol polyproteins in the cytoplasm, thereby directing unspliced RNA to the plasma membrane By similarity.

Capsid protein p24: Virion Potential.

Nucleocapsid protein p7: Virion Potential.

Reverse transcriptase/ribonuclease H: Virion Potential.

Integrase: Virion Potential. Host nucleus Potential. Host cytoplasm Potential. Note: Nuclear at initial phase, cytoplasmic at assembly Potential.

Domain

The reverse transcriptase/ribonuclease H (RT) is structured in five subdomains: finger, palm, thumb, connection and RNase H. Within the palm subdomain, the 'primer grip' region is thought to be involved in the positioning of the primer terminus for accommodating the incoming nucleotide. The RNase H domain stabilizes the association of RT with primer-template By similarity.

The tryptophan repeat motif is involved in RT p66/p51 dimerization.

Integrase core domain contains the D-x(n)-D-x(35)-E motif, named for the phylogenetically conserved glutamic acid and aspartic acid residues and the invariant 35 amino acid spacing between the second and third acidic residues. Each acidic residue of the D,D35E motif is independently essential for the 3'-processing and strand transfer activities of purified integrase protein.

Post-translational modification

Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT subunit. Nucleocapsid protein p7 might be further cleaved after virus entry. Ref.11 Ref.16 Ref.20

Capsid protein p24 is phosphorylated.

Matrix protein p17 is tyrosine phosphorylated presumably in the virion by a host kinase. This modification targets the matrix protein to the nucleus.

Miscellaneous

Capsid protein p24 is able to bind macaque TRIM5-alpha or owl monkey TRIMCyp, preventing reverse transcription of the viral genome and succesfull infection of macaque or owl monkey by HIV-1.

The reverse transcriptase is an error-prone enzyme that lacks a proof-reading function. High mutations rate is a direct consequence of this characteristic. RT also displays frequent template switching leading to high recombination rate. Recombination mostly occurs between homologous regions of the two copackaged RNA genomes. If these two RNA molecules derive from different viral strains, reverse transcription will give rise to highly recombinated proviral DNAs.

HIV-1 lineages are divided in three main groups, M (for Major), O (for Outlier), and N (for New, or Non-M, Non-O). The vast majority of strains found worldwide belong to the group M. Group O seems to be endemic to and largely confined to Cameroon and neighboring countries in West Central Africa, where these viruses represent a small minority of HIV-1 strains. The group N is represented by a limited number of isolates from Cameroonian persons. The group M is further subdivided in 9 clades or subtypes (A to D, F to H, J and K).

Resistance to inhibitors associated with mutations are observed both in viral protease and in reverse transcriptase. Most of the time, single mutations confer only a modest reduction in drug susceptibility. Combination of several mutations is usually required to develop a high-level drug resistance. These mutations are predominantly found in clade B viruses and not in other genotypes. They are listed in this entry which is a representative of clade B.

Sequence similarities

Contains 2 CCHC-type zinc fingers.

Contains 1 integrase catalytic domain.

Contains 1 integrase-type DNA-binding domain.

Contains 1 integrase-type zinc finger.

Contains 1 peptidase A2 domain.

Contains 1 reverse transcriptase domain.

Contains 1 RNase H domain.

Ontologies

Keywords
   Biological processActivation of host caspases by virus
DNA integration
DNA recombination
Host gene expression shutoff by virus
Host translation shutoff by virus
Host-virus interaction
Modulation of host cell apoptosis by virus
Viral genome integration
Viral penetration into host nucleus
Virion maturation
Virus entry into host cell
Virus exit from host cell
   Cellular componentCapsid protein
Host cell membrane
Host cytoplasm
Host membrane
Host nucleus
Membrane
Virion
   Coding sequence diversityRibosomal frameshifting
   DiseaseAIDS
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Magnesium
Metal-binding
RNA-binding
Viral nucleoprotein
Zinc
   Molecular functionAspartyl protease
DNA-directed DNA polymerase
Endonuclease
Hydrolase
Nuclease
Nucleotidyltransferase
Protease
RNA-directed DNA polymerase
Transferase
   PTMLipoprotein
Myristate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processDNA integration

Inferred from electronic annotation. Source: UniProtKB-KW

DNA recombination

Inferred from electronic annotation. Source: UniProtKB-KW

RNA-dependent DNA replication

Traceable author statement. Source: Reactome

entry into host cell

Traceable author statement. Source: Reactome

establishment of integrated proviral latency

Traceable author statement. Source: Reactome

induction by virus of host cysteine-type endopeptidase activity involved in apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

suppression by virus of host translation

Inferred from electronic annotation. Source: UniProtKB-KW

uncoating of virus

Traceable author statement. Source: Reactome

viral entry into host cell

Inferred from electronic annotation. Source: UniProtKB-KW

viral life cycle

Traceable author statement. Source: Reactome

viral penetration into host nucleus

Inferred from electronic annotation. Source: UniProtKB-KW

viral process

Traceable author statement. Source: Reactome

viral release from host cell

Inferred from electronic annotation. Source: UniProtKB-KW

virion assembly

Traceable author statement. Source: Reactome

   Cellular_componenthost cell cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

host cell nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

host cell plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

intracellular

Inferred from electronic annotation. Source: GOC

membrane

Inferred from electronic annotation. Source: UniProtKB-KW

viral nucleocapsid

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA-directed DNA polymerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA-DNA hybrid ribonuclease activity

Inferred from electronic annotation. Source: InterPro

RNA-directed DNA polymerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

aspartic-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

exoribonuclease H activity

Inferred from electronic annotation. Source: UniProtKB-EC

identical protein binding

Inferred from physical interaction PubMed 20227411PubMed 21156026PubMed 22804908PubMed 19914170. Source: IntAct

structural molecule activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself29EBI-3989067,EBI-3989067
PSIP1O7547521EBI-3989067,EBI-1801773From a different organism.
revP697188EBI-3989067,EBI-8540156From a different organism.

Alternative products

This entry describes 2 isoforms produced by ribosomal frameshifting. [Align] [Select]

Note: Translation results in the formation of the Gag polyprotein most of the time. Ribosomal frameshifting at the gag-pol genes boundary occurs at low frequency and produces the Gag-Pol polyprotein. This strategy of translation probably allows the virus to modulate the quantity of each viral protein. Maintenance of a correct Gag to Gag-Pol ratio is essential for RNA dimerization and viral infectivity.
Isoform Gag-Pol polyprotein (identifier: P04585-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: Produced by -1 ribosomal frameshifting.
Isoform Gag polyprotein (identifier: P04591-1)

The sequence of this isoform can be found in the external entry P04591.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by conventional translation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed; by host By similarity
Chain2 – 14351434Gag-Pol polyprotein
PRO_0000223620
Chain2 – 132131Matrix protein p17 By similarity
PRO_0000042439
Chain133 – 363231Capsid protein p24 By similarity
PRO_0000042440
Peptide364 – 37714Spacer peptide p2 By similarity
PRO_0000042441
Chain378 – 43255Nucleocapsid protein p7 By similarity
PRO_0000042442
Peptide433 – 4408Transframe peptide Potential
PRO_0000246716
Chain441 – 48848p6-pol Potential
PRO_0000042443
Chain489 – 58799Protease
PRO_0000038665
Chain588 – 1147560Reverse transcriptase/ribonuclease H
PRO_0000042444
Chain588 – 1027440p51 RT
PRO_0000042445
Chain1028 – 1147120p15
PRO_0000042446
Chain1148 – 1435288Integrase By similarity
PRO_0000042447

Regions

Domain508 – 57770Peptidase A2
Domain631 – 821191Reverse transcriptase
Domain1021 – 1144124RNase H
Domain1201 – 1351151Integrase catalytic
Zinc finger390 – 40718CCHC-type 1
Zinc finger411 – 42818CCHC-type 2
Zinc finger1150 – 119142Integrase-type
DNA binding1370 – 141748Integrase-type
Region217 – 2259PPIA/CYPA-binding loop
Region814 – 8229RT 'primer grip' By similarity
Motif16 – 227Nuclear export signal By similarity
Motif26 – 327Nuclear localization signal By similarity
Motif985 – 100117Tryptophan repeat motif By similarity

Sites

Active site5131For protease activity; shared with dimeric partner By similarity
Metal binding6971Magnesium; catalytic; for reverse transcriptase activity By similarity
Metal binding7721Magnesium; catalytic; for reverse transcriptase activity By similarity
Metal binding7731Magnesium; catalytic; for reverse transcriptase activity By similarity
Metal binding10301Magnesium; catalytic; for RNase H activity
Metal binding10651Magnesium; catalytic; for RNase H activity
Metal binding10851Magnesium; catalytic; for RNase H activity
Metal binding11361Magnesium; catalytic; for RNase H activity
Metal binding12111Magnesium; catalytic; for integrase activity By similarity
Metal binding12631Magnesium; catalytic; for integrase activity By similarity
Site132 – 1332Cleavage; by viral protease By similarity
Site221 – 2222Cis/trans isomerization of proline peptide bond; by human PPIA/CYPA
Site363 – 3642Cleavage; by viral protease By similarity
Site377 – 3782Cleavage; by viral protease By similarity
Site393 – 3942Cleavage; by viral protease Potential
Site426 – 4272Cleavage; by viral protease Potential
Site432 – 4332Cleavage; by viral protease Potential
Site440 – 4412Cleavage; by viral protease By similarity
Site488 – 4892Cleavage; by viral protease By similarity
Site587 – 5882Cleavage; by viral protease By similarity
Site9881Essential for RT p66/p51 heterodimerization By similarity
Site10011Essential for RT p66/p51 heterodimerization By similarity
Site1027 – 10282Cleavage; by viral protease; partial By similarity
Site1147 – 11482Cleavage; by viral protease By similarity

Amino acid modifications

Modified residue1321Phosphotyrosine; by host By similarity
Lipidation21N-myristoyl glycine; by host By similarity

Natural variations

Natural variant4961R → K Confers to resistance to A-77003; when associated with other amino acid changes.
Natural variant4961R → Q Confers to resistance to A-77003.
Natural variant4981L → F Confers resistance to amprenavir, atazanavir, lopinavir; when associated with other amino acid changes.
Natural variant4981L → I Confers resistance to indinavir, lopinavir, ritonavir and saquinavir; when associated with other amino acid changes.
Natural variant4981L → R Confers resistance to indinavir and lopinavir; when associated with other amino acid changes.
Natural variant4981L → V Confers resistance to indinavir and lopinavir; when associated with other amino acid changes.
Natural variant4981L → Y Confers resistance to atazanavir; when associated with other amino acid changes.
Natural variant5031I → V Confers resistance to tipranavir.
Natural variant5041G → E Confers resistance to lopinavir, ritonavir and saquinavir; when associated with other amino acid changes.
Natural variant5081K → I Confers resistance to lopinavir.
Natural variant5081K → M Confers resistance to indinavir, lopinavir and nelfinavir; when associated with other amino acid changes.
Natural variant5081K → R Confers resistance to indinavir, lopinavir and ritonavir; when associated with other amino acid changes.
Natural variant5111L → I Confers resistance to BILA 2185 BS.
Natural variant5121L → I Confers resistance to amprenavir, indinavir, lopinavir, ritonavir and saquinavir; when associated with other amino acid changes.
Natural variant5181D → N Confers resistance to nelfinavir; when associated with other amino acid changes.
Natural variant5201V → I Confers resistance to A-77003, amprenavir, atazanavir, indinavir, kynostatin, lopinavir, ritonavir and saquinavir; when associated with other amino acid changes.
Natural variant5211L → F Confers resistance to atazanavir nelfinavir and ritonavir; when associated with other amino acid changes.
Natural variant5221E → Q Confers resistance to lopinavir; when associated with other amino acid changes.
Natural variant5231E → D Confers resistance to tipranavir.
Natural variant5241M → I Confers resistance to nelfinavir and ritonavir; when associated with other amino acid changes.
Natural variant5241M → L Confers resistance to ritonavir; when associated with other amino acid changes.
Natural variant5251S → D Confers resistance to indinavir and tipranavir; when associated with other amino acid changes.
Natural variant5291R → K Confers resistance to tipranavir.
Natural variant5331K → I Confers resistance to DMD-323; when associated with other amino acid changes.
Natural variant5341M → F Confers resistance to A-77003.
Natural variant5341M → I Confers resistance to A-77003, amprenavir, atazanavir, indinavir, kynostatin, lopinavir, ritonavir, saquinavir and telinavir; when associated with other amino acid changes.
Natural variant5341M → L Confers resistance to A-77003, amprenavir, indinavir, lopinavir, ritonavir and saquinavir; when associated with other amino acid changes.
Natural variant5351I → V Confers resistance to amprenavir, lopinavir, kynostatin, ritonavir and saquinavir; when associated with other amino acid changes.
Natural variant5361G → V Confers resistance to A-77003, amprenavir, indinavir, ritonavir, saquinavir and telinavir; when associated with other amino acid changes.
Natural variant5381I → L Confers resistance to atazanavir; when associated with other amino acid changes.
Natural variant5381I → V Confers resistance to amprenavir, lopinavir and ritonavir; when associated with other amino acid changes.
Natural variant5411F → L Confers resistance to lopinavir and telinavir; when associated with other amino acid changes.
Natural variant5411F → Y Confers resistance to indinavir, ritonavir and saquinavir; when associated with other amino acid changes.
Natural variant5421I → A Confers resistance to lopinavir.
Natural variant5421I → L Confers resistance to amprenavir and lopinavir; when associated with other amino acid changes.
Natural variant5421I → M Confers resistance to amprenavir and lopinavir.
Natural variant5421I → S Confers resistance to lopinavir.
Natural variant5421I → T Confers resistance to lopinavir; when associated with other amino acid changes.
Natural variant5421I → V Confers resistance to indinavir, lopinavir, ritonavir and saquinavir; when associated with other amino acid changes.
Natural variant5431K → R Confers resistance to nelfinavir.
Natural variant5451R → K Confers resistance to nelfinavir.
Natural variant5461Q → E Confers resistance to lopinavir and ritonavir; when associated with other amino acid changes.
Natural variant5481D → E Confers resistance to tripanavir.
Natural variant5491Q → H Confers resistance to lopinavir; when associated with other amino acid changes.
Natural variant5511L → P Confers resistance to atazanavir, indinavir, lopinavir, ritonavir and saquinavir; when associated with other amino acid changes.
Natural variant5511L → T Confers resistance to lopinavir.
Natural variant5531E → Q Confers resistance to lopinavir; when associated with other amino acid changes.
Natural variant5541I → F Confers resistance to indinavir, ritonavir and saquinavir; when associated with other amino acid changes.
Natural variant5571H → Y Confers resistance to lopinavir; when associated with other amino acid changes.
Natural variant5591A → I Confers resistance to lopinavir; when associated with other amino acid changes.
Natural variant5591A → L Confers resistance to lopinavir; when associated with other amino acid changes.
Natural variant5591A → T Confers resistance to A-77003, indinavir, lopinavir, nelfinavir and tripanavir; when associated with other amino acid changes.
Natural variant5591A → V Confers resistance to amprenavir, atazanavir, indinavir, kynostatin, lopinavir, nelfinavir, ritonavir, saquinavir and telinavir; when associated with other amino acid changes.
Natural variant5611G → S Confers resistance to indinavir, nelfinavir, ritonavir and saquinavir; when associated with other amino acid changes.
Natural variant5651V → I Confers resistance to indinavir, nelfinavir, ritonavir and saquinavir; when associated with other amino acid changes.
Natural variant5701V → A Confers resistance to A-77003, indinavir, lopinavir, nelfinavir, ritonavir and saquinavir; when associated with other amino acid changes.
Natural variant5701V → F Confers resistance to lopinavir and ritonavir; when associated with other amino acid changes.
Natural variant5701V → I Confers resistance to A-77003 and kynostatin; when associated with other amino acid changes.
Natural variant5701V → S Confers resistance to lopinavir and ritonavir.
Natural variant5701V → T Confers resistance to indinavir, lopinavir, ritonavir and saquinavir; when associated with other amino acid changes.
Natural variant5721I → A Confers resistance to atazanavir, indinavir, lopinavir, nelfinavir, ritonavir and saquinavir; when associated with other amino acid changes.
Natural variant5721I → V Confers resistance to amprenavir, atazanavir, indinavir, kynostatin, lopinavir, nelfinavir, ritonavir, saquinavir and telinavir; when associated with other amino acid changes.
Natural variant5761N → D Confers resistance to nelfinavir; when associated with other amino acid changes.
Natural variant5761N → S Confers resistance to atazanavir, indinavir and nelfinavir; when associated with other amino acid changes.
Natural variant5771L → M Confers resistance to atazanavir; when associated with other amino acid changes.
Natural variant5781L → M Confers resistance to indinavir, lopinavir, nelfinavir, ritonavir and saquinavir; when associated with other amino acid changes.
Natural variant5791T → S Confers resistance to lopinavir, ritonavir and saquinavir; when associated with other amino acid changes.
Natural variant5811I → L Confers resistance to indinavir.
Natural variant6281M → L Confers resistance to zidovudine; when associated with other amino acid changes.
Natural variant6311E → A Confers resistance to lamivudine.
Natural variant6311E → D Confers resistance to zidovudine; when associated with other amino acid changes.
Natural variant6391P → R Confers resistance to stavudine.
Natural variant6411N → D Confers resistance to stavudine.
Natural variant6491A → V Confers multi-NRTI resistance; when associated with other amino acid changes.
Natural variant6521K → R Confers resistance to abacavir, adefovir, didenosine, lamivudine, stavudine, tenofir and zidovuline; when associated with other amino acid changes.
Natural variant6541D → A Confers resistance to zidovudine.
Natural variant6541D → E Confers multi-NRTI resistance.
Natural variant6541D → G Confers multi-NRTI resistance.
Natural variant6541D → N Confers resistance to zidovudine.
Natural variant6541D → S Confers multi-NRTI resistance.
Natural variant6551S → G Confers multi-NRTI resistance; when associated with other amino acid changes.
Natural variant6551S → N Confers multi-NRTI resistance.
Natural variant6551S → Y Confers multi-NRTI resistance.
Natural variant6561T → A Confers resistance to lamivudine and stavudine.
Natural variant6561T → D Confers resistance to lamivudine, stavudine and rarely to zalcitabine.
Natural variant6561T → G Confers resistance to didanosine, zalcitabine and zidovudine.
Natural variant6561T → N Confers resistance to lamivudine and stavudine.
Natural variant6571K → E Confers resistance to adefovir and lamivudine.
Natural variant6571K → R Confers resistance to zidovudine; when associated with other amino acid changes.
Natural variant6571K → S Confers resistance to didanosine and stavudine.
Natural variant6611L → I Confers resistance to HBY 097.
Natural variant6611L → V Confers resistance to abacavir, didanosine, HBY 097 and zalcitabine; when associated with other amino acid changes.
Natural variant6621V → I Confers multi-NRTI resistance; when associated with other amino acid changes.
Natural variant6621V → L Confers resistance to HBY 097.
Natural variant6621V → M Confers resistance to stavudine and zalcitabine.
Natural variant6621V → T Confers resistance to d4C, didanosine, stavudine and zalcitabine.
Natural variant6641F → L Confers multi-NRTI resistance; when associated with other amino acid changes.
Natural variant6751W → G Confers resistance to pyrophosphate analog PFA.
Natural variant6751W → S Confers resistance to pyrophosphate analog PFA.
Natural variant6761E → G Confers resistance to pyrophosphate analog PFA.
Natural variant6761E → K Confers resistance to pyrophosphate analog PFA.
Natural variant6791L → I Confers resistance to pyrophosphate analog PFA.
Natural variant6871L → I Confers resistance to nevirapine and efavirenz.
Natural variant6881K → E Confers resistance to atevirdine, efavirenz, nevirapine and zidovudine.
Natural variant6881K → P Confers resistance to TMC125; when associated with E-142.
Natural variant6881K → Q Confers resistance to efavirenz; when associated with I-19.
Natural variant6901K → E Confers resistance to atevirdine; when associated with other amino acid changes.
Natural variant6901K → N Confers resistance to atevirdine, efavirenz, emivirine and nevirapine; when associated with other amino acid changes.
Natural variant6901K → R Confers resistance to emivirine and trovirdine; when associated with other D-179 and C-181.
Natural variant6931V → A Confers resistance to nevirapine.
Natural variant6931V → I Confers resistance to HBY 097.
Natural variant6931V → M Confers resistance to delavirdine, efavirenz and nevirapine.
Natural variant6951V → I Confers resistance to efavirenz, emivirine, nevirapine and trovirdine; when associated with other amino acid changes.
Natural variant7021Y → F Confers resistance to abacavir; when associated with other amino acid changes.
Natural variant7031F → Y Confers multi-NRTI resistance; when associated with other amino acid changes.
Natural variant7051V → I Confers resistance to zidovudine; when associated with other amino acid changes.
Natural variant7061P → S Confers resistance to lodenosine.
Natural variant7221I → L Confers resistance to delavirdine, efavirenz and nevirapine; when associated with I-239.
Natural variant7221I → M Confers resistance to delavirdine, efavirenz and nevirapine; when associated with I-239.
Natural variant7221I → T Confers resistance to delavirdine, efavirenz and nevirapine; when associated with I-239.
Natural variant7251E → K Confers resistance to emivirine.
Natural variant7321Q → M Confers both multi-NRTI and multi-NNRTI resistance.
Natural variant7381Q → M Confers multi-NRTI resistance; when associated with other amino acid changes.
Natural variant7431S → A Confers resistance to pyrophosphate analog PFA.
Natural variant7441P → S Confers resistance to lamivudine.
Natural variant7481Q → L Confers resistance to pyrophosphate analog PFA.
Natural variant7661V → D Confers resistance to efavirenz, tivirapine and trovirdine; when associated with other amino acid changes.
Natural variant7681Y → C Confers multi-NNRTI resistance.
Natural variant7711M → I Confers resistance to lamivudine and emtricitabine.
Natural variant7711M → T Confers resistance to abacavir, didanosine, emtricitabine, lamivudine and zalcitabine.
Natural variant7711M → V Confers resistance to lamivudine.
Natural variant7751Y → C Confers resistance to nevirapine.
Natural variant7751Y → H Confers resistance to atevirdine, efavirenz, loviride and zidovudine.
Natural variant7751Y → L Confers resistance to efavirenz.
Natural variant7761V → I Confers resistance to HBY 097.
Natural variant7771G → A Confers resistance to efavirenz and nevirapine.
Natural variant7771G → C Confers resistance to efavirenz and nevirapine.
Natural variant7771G → E Confers resistance to efavirenz, nevirapine and quinoxaline.
Natural variant7771G → Q Confers resistance to efavirenz, HBY 097 and nevirapine.
Natural variant7771G → S Confers resistance to efavirenz and nevirapine.
Natural variant7771G → T Confers resistance to efavirenz, HBY 097 and nevirapine.
Natural variant7771G → V Confers resistance to efavirenz and nevirapine.
Natural variant7951H → Y Confers resistance to lamivudine, pyrophosphate analog PFA and zidovudine.
Natural variant7971L → W Confers resistance to zidovudine.
Natural variant7981R → K Confers resistance to lamivudine and zidovudine.
Natural variant8011L → F Confers resistance to ph-AZT and zidovudine.
Natural variant8021T → F Confers resistance to zidovudine; when associated with other amino acid changes.
Natural variant8021T → Y Confers resistance to zidovudine; when associated with other amino acid changes.
Natural variant8061K → E Confers resistance to zidovudine.
Natural variant8061K → Q Confers resistance to zidovudine; when associated with other amino acid changes.
Natural variant8061K → R Confers resistance to lamivudine, stavudine, zalcicabine and zidovudine.
Natural variant8121P → H Confers resistance to efavirenz, emivirine, HBY 097 and quinoxaline; when associated with A-17.
Natural variant8231P → L Confers resistance to atevirdine and delavirdine.
Natural variant8251K → T Confers resistance to atevirdine and zidovudine; when associated with other amino acid changes.
Natural variant8701L → I Confers resistance to delavirdine, efavirenz and nevirapine.
Natural variant9051Y → F Confers resistance to delavirdine and nevirapine.
Natural variant9201G → D Confers resistance to abacavir, lamivudine and zidovudine.
Natural variant9201G → E Confers resistance to abacavir, lamivudine and zidovudine.
Natural variant9731T → I Confers resistance to abacavir, lamivudine and zidovudine.

Experimental info

Mutagenesis2171P → A: 3-fold decrease of PPIA-binding affinity. Ref.9
Mutagenesis2181V → A: 2.7-fold decrease of PPIA-binding affinity. Ref.9
Mutagenesis2191H → A or Q: 8-fold decrease of PPIA-binding affinity. Ref.9
Mutagenesis2201A → G: 44-fold decrease of PPIA-binding affinity. Ref.9
Mutagenesis2201A → V: 3.4-fold decrease of PPIA-binding affinity. Ref.9
Mutagenesis2211G → A: 31-fold decrease of PPIA-binding affinity. Ref.9
Mutagenesis2211G → V: 154-fold decrease of PPIA-binding affinity. Ref.9
Mutagenesis2221P → A: 36-fold decrease of PPIA-binding affinity. Ref.9
Mutagenesis2221P → V: More than 150-fold decrease of PPIA-binding affinity. Ref.9
Mutagenesis2231I → A: 1.2-fold decrease of PPIA-binding affinity. Ref.9
Mutagenesis2231I → V: 1.0-fold decrease of PPIA-binding affinity. Ref.9
Mutagenesis2241A → G: 2.3-fold decrease of PPIA-binding affinity. Ref.9
Mutagenesis2241A → V: 1.7-fold decrease of PPIA-binding affinity. Ref.9
Mutagenesis2251P → A: 1.6-fold decrease of PPIA-binding affinity. Ref.9
Mutagenesis3941N → F or G: Decreases infectivity and replication. Ref.22
Mutagenesis4001H → C: Complete loss of infectivity and in vitro chaperone activity. Ref.15
Mutagenesis4051C → H: Complete loss of infectivity and DNA synthesis. Ref.15
Mutagenesis4211H → C: Partial loss of infectivity. Complete loss of in vitro chaperone activity. Ref.15
Mutagenesis4261C → H: Partial loss of infectivity. Ref.15
Mutagenesis10651E → Q: Complete loss of RNase H activity. Ref.13
Mutagenesis11361D → N: Complete loss of RNase H activity. Ref.13
Mutagenesis11591H → C: No effect on integrase activity in vitro. Ref.4
Mutagenesis11631H → C or V: 75% increase of integrase activity in vitro. Ref.4
Mutagenesis11871C → A: Complete loss of integrase activity in vivo. Ref.5
Mutagenesis11901C → A: Complete loss of integrase activity in vivo. Ref.5
Mutagenesis12001Q → C: 75% increase of integrase activity in vitro. Ref.4
Mutagenesis12081W → A: Complete loss of integrase activity in vivo. Ref.5
Mutagenesis12111D → A or V: Complete loss of integrase activity in vivo and in vitro. Ref.4 Ref.5 Ref.10
Mutagenesis12131T → A: No effect on infectivity. Ref.5
Mutagenesis12221V → P: Complete loss of integrase activity. Ref.5
Mutagenesis12281S → A: Complete loss of integrase activity in vivo. Ref.4 Ref.5
Mutagenesis12281S → R: No effect on integrase activity in vitro. Ref.4 Ref.5
Mutagenesis12621T → A: No effect infectivity. Ref.5
Mutagenesis12631D → A or I: Complete loss of integrase activity in vivo and in vitro. Ref.4 Ref.5 Ref.10
Mutagenesis12701G → A: No effect on infectivity. Ref.5
Mutagenesis12821I → P: Complete loss of integrase activity in vivo. Ref.5
Mutagenesis12981V → A: No effect on infectivity. Ref.5
Mutagenesis12991E → G or P: Complete loss of integrase activity in vitro. Ref.4 Ref.5 Ref.10
Mutagenesis13061K → P: Slow down virus replication. Ref.5
Mutagenesis13261A → P: Complete loss of integrase activity in vivo. Ref.5
Mutagenesis13461R → C: 75% increase of integrase activity in vitro. Ref.4
Mutagenesis13821W → A: Complete loss of infectivity. No effect on integrase activity in vitro. Ref.4 Ref.5
Mutagenesis13821W → E: 75% increase of integrase activity in vitro. Ref.4 Ref.5

Secondary structure

.............................................................................................................................................................................................................................................. 1435
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Gag-Pol polyprotein [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 8487B36BDEAC5FE4

FASTA1,435162,042
        10         20         30         40         50         60 
MGARASVLSG GELDRWEKIR LRPGGKKKYK LKHIVWASRE LERFAVNPGL LETSEGCRQI 

        70         80         90        100        110        120 
LGQLQPSLQT GSEELRSLYN TVATLYCVHQ RIEIKDTKEA LDKIEEEQNK SKKKAQQAAA 

       130        140        150        160        170        180 
DTGHSNQVSQ NYPIVQNIQG QMVHQAISPR TLNAWVKVVE EKAFSPEVIP MFSALSEGAT 

       190        200        210        220        230        240 
PQDLNTMLNT VGGHQAAMQM LKETINEEAA EWDRVHPVHA GPIAPGQMRE PRGSDIAGTT 

       250        260        270        280        290        300 
STLQEQIGWM TNNPPIPVGE IYKRWIILGL NKIVRMYSPT SILDIRQGPK EPFRDYVDRF 

       310        320        330        340        350        360 
YKTLRAEQAS QEVKNWMTET LLVQNANPDC KTILKALGPA ATLEEMMTAC QGVGGPGHKA 

       370        380        390        400        410        420 
RVLAEAMSQV TNSATIMMQR GNFRNQRKIV KCFNCGKEGH TARNCRAPRK KGCWKCGKEG 

       430        440        450        460        470        480 
HQMKDCTERQ ANFLREDLAF LQGKAREFSS EQTRANSPTR RELQVWGRDN NSPSEAGADR 

       490        500        510        520        530        540 
QGTVSFNFPQ VTLWQRPLVT IKIGGQLKEA LLDTGADDTV LEEMSLPGRW KPKMIGGIGG 

       550        560        570        580        590        600 
FIKVRQYDQI LIEICGHKAI GTVLVGPTPV NIIGRNLLTQ IGCTLNFPIS PIETVPVKLK 

       610        620        630        640        650        660 
PGMDGPKVKQ WPLTEEKIKA LVEICTEMEK EGKISKIGPE NPYNTPVFAI KKKDSTKWRK 

       670        680        690        700        710        720 
LVDFRELNKR TQDFWEVQLG IPHPAGLKKK KSVTVLDVGD AYFSVPLDED FRKYTAFTIP 

       730        740        750        760        770        780 
SINNETPGIR YQYNVLPQGW KGSPAIFQSS MTKILEPFRK QNPDIVIYQY MDDLYVGSDL 

       790        800        810        820        830        840 
EIGQHRTKIE ELRQHLLRWG LTTPDKKHQK EPPFLWMGYE LHPDKWTVQP IVLPEKDSWT 

       850        860        870        880        890        900 
VNDIQKLVGK LNWASQIYPG IKVRQLCKLL RGTKALTEVI PLTEEAELEL AENREILKEP 

       910        920        930        940        950        960 
VHGVYYDPSK DLIAEIQKQG QGQWTYQIYQ EPFKNLKTGK YARMRGAHTN DVKQLTEAVQ 

       970        980        990       1000       1010       1020 
KITTESIVIW GKTPKFKLPI QKETWETWWT EYWQATWIPE WEFVNTPPLV KLWYQLEKEP 

      1030       1040       1050       1060       1070       1080 
IVGAETFYVD GAANRETKLG KAGYVTNRGR QKVVTLTDTT NQKTELQAIY LALQDSGLEV 

      1090       1100       1110       1120       1130       1140 
NIVTDSQYAL GIIQAQPDQS ESELVNQIIE QLIKKEKVYL AWVPAHKGIG GNEQVDKLVS 

      1150       1160       1170       1180       1190       1200 
AGIRKVLFLD GIDKAQDEHE KYHSNWRAMA SDFNLPPVVA KEIVASCDKC QLKGEAMHGQ 

      1210       1220       1230       1240       1250       1260 
VDCSPGIWQL DCTHLEGKVI LVAVHVASGY IEAEVIPAET GQETAYFLLK LAGRWPVKTI 

      1270       1280       1290       1300       1310       1320 
HTDNGSNFTG ATVRAACWWA GIKQEFGIPY NPQSQGVVES MNKELKKIIG QVRDQAEHLK 

      1330       1340       1350       1360       1370       1380 
TAVQMAVFIH NFKRKGGIGG YSAGERIVDI IATDIQTKEL QKQITKIQNF RVYYRDSRNP 

      1390       1400       1410       1420       1430 
LWKGPAKLLW KGEGAVVIQD NSDIKVVPRR KAKIIRDYGK QMAGDDCVAS RQDED 

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Isoform Gag polyprotein [UniParc].

See P04591.

References

[1]"Complete nucleotide sequences of functional clones of the AIDS virus."
Ratner L., Fisher A., Jagodzinski L.L., Mitsuya H., Liou R.-S., Gallo R.C., Wong-Staal F.
AIDS Res. Hum. Retroviruses 3:57-69(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]Ogata N., Alter H.J., Miller R.H., Purcell R.H.
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]Chappey C.
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[4]"Site-directed mutagenesis of HIV-1 integrase demonstrates differential effects on integrase functions in vitro."
Leavitt A.D., Shiue L., Varmus H.E.
J. Biol. Chem. 268:2113-2119(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF HIS-1159; HIS-1163; GLN-1200; ASP-1211; SER-1228; ASP-1263; GLU-1299; ARG-1346 AND TRP-1382.
[5]"Human immunodeficiency virus type 1 integrase: effect on viral replication of mutations at highly conserved residues."
Cannon P.M., Wilson W., Byles E., Kingsman S.M., Kingsman A.J.
J. Virol. 68:4768-4775(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-1187; CYS-1190; TRP-1208; ASP-1211; THR-1213; VAL-1222; SER-1228; THR-1262; ASP-1263; GLY-1270; ILE-1282; VAL-1298; GLU-1299; LYS-1306; ALA-1326 AND TRP-1382.
Strain: Isolate WI3.
[6]"Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B."
Luban J., Bossolt K.L., Franke E.K., Kalpana G.V., Goff S.P.
Cell 73:1067-1078(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION OF CAPSID WITH HUMAN PPIA/CYPA.
[7]"Binding and stimulation of HIV-1 integrase by a human homolog of yeast transcription factor SNF5."
Kalpana G.V., Marmon S., Wang W., Crabtree G.R., Goff S.P.
Science 266:2002-2006(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION OF INTEGRASE WITH HUMAN SMARCB1/INI1.
[8]"Cyclophilin A is required for an early step in the life cycle of human immunodeficiency virus type 1 before the initiation of reverse transcription."
Braaten D., Franke E.K., Luban J.
J. Virol. 70:3551-3560(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF CAPSID.
[9]"Molecular recognition in the HIV-1 capsid/cyclophilin A complex."
Yoo S., Myszka D.G., Yeh C., McMurray M., Hill C.P., Sundquist W.I.
J. Mol. Biol. 269:780-795(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF PRO-217; VAL-218; HIS-219; ALA-220; GLY-221; PRO-222; ILE-223; ALA-224 AND PRO-225.
[10]"Mutations in the human immunodeficiency virus type 1 integrase D,D(35)E motif do not eliminate provirus formation."
Gaur M., Leavitt A.D.
J. Virol. 72:4678-4685(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASP-1211; ASP-1263 AND GLU-1299.
[11]"Organization of HIV-1 pol is critical for Pol polyprotein processing."
Chang Y.Y., Yu S.L., Syu W.J.
J. Biomed. Sci. 6:333-341(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
[12]"Maintenance of the Gag/Gag-Pol ratio is important for human immunodeficiency virus type 1 RNA dimerization and viral infectivity."
Shehu-Xhilaga M., Crowe S.M., Mak J.
J. Virol. 75:1834-1841(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: GAG/GAG-POL RATIO.
[13]"Mutations in the ribonuclease H active site of HIV-RT reveal a role for this site in stabilizing enzyme-primer-template binding."
Cristofaro J.V., Rausch J.W., Le Grice S.F., DeStefano J.J.
Biochemistry 41:10968-10975(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITES OF RNASE H, MUTAGENESIS OF GLU-1065 AND ASP-1136.
[14]"Catalysis of cis/trans isomerization in native HIV-1 capsid by human cyclophilin A."
Bosco D.A., Eisenmesser E.Z., Pochapsky S., Sundquist W.I., Kern D.
Proc. Natl. Acad. Sci. U.S.A. 99:5247-5252(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: CIS/TRANS ISOMERIZATION OF CAPSID.
[15]"Subtle alterations of the native zinc finger structures have dramatic effects on the nucleic acid chaperone activity of human immunodeficiency virus type 1 nucleocapsid protein."
Guo J., Wu T., Kane B.F., Johnson D.G., Henderson L.E., Gorelick R.J., Levin J.G.
J. Virol. 76:4370-4378(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF HIS-400; CYS-405; HIS-421 AND CYS-426.
[16]"The dimer interfaces of protease and extra-protease domains influence the activation of protease and the specificity of GagPol cleavage."
Pettit S.C., Gulnik S., Everitt L., Kaplan A.H.
J. Virol. 77:366-374(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
[17]"The barrier-to-autointegration factor is a component of functional human immunodeficiency virus type 1 preintegration complexes."
Lin C.W., Engelman A.
J. Virol. 77:5030-5036(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION OF MATRIX PROTEIN P17 WITH HUMAN BAF.
[18]"Structural organization of authentic, mature HIV-1 virions and cores."
Briggs J.A., Wilk T., Welker R., Krausslich H.G., Fuller S.D.
EMBO J. 22:1707-1715(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: QUARTERNARY STRUCTURE OF CAPSID.
[19]"Cleavage of eIF4G by HIV-1 protease: effects on translation."
Perales C., Carrasco L., Ventoso I.
FEBS Lett. 533:89-94(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF PROTEASE.
[20]"In vitro processing of HIV-1 nucleocapsid protein by the viral proteinase: effects of amino acid substitutions at the scissile bond in the proximal zinc finger sequence."
Tozser J., Shulenin S., Louis J.M., Copeland T.D., Oroszlan S.
Biochemistry 43:4304-4312(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE OF NUCLEOCAPSID PROTEIN P7.
[21]"Human immunodeficiency virus type 1 Gag polyprotein modulates its own translation."
Anderson E.C., Lever A.M.
J. Virol. 80:10478-10486(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[22]"Characterization of human immunodeficiency virus type 1 (HIV-1) containing mutations in the nucleocapsid protein at a putative HIV-1 protease cleavage site."
Thomas J.A., Shulenin S., Coren L.V., Bosche W.J., Gagliardi T.D., Gorelick R.J., Oroszlan S.
Virology 354:261-270(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASN-394.
[23]"Dissecting the protein-RNA and RNA-RNA interactions in the nucleocapsid-mediated dimerization and isomerization of HIV-1 stemloop 1."
Hagan N.A., Fabris D.
J. Mol. Biol. 365:396-410(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF NUCLEOCAPSID PROTEIN P7.
[24]"Importin alpha3 interacts with HIV-1 integrase and contributes to HIV-1 nuclear import and replication."
Ao Z., Danappa Jayappa K., Wang B., Zheng Y., Kung S., Rassart E., Depping R., Kohler M., Cohen E.A., Yao X.
J. Virol. 84:8650-8663(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF INTEGRASE, INTERACTION OF INTEGRASE WITH HUMAN KPNA3.
[25]"HIV- 1 protease inhibits Cap- and poly(A)-dependent translation upon eIF4GI and PABP cleavage."
Castello A., Franco D., Moral-Lopez P., Berlanga J.J., Alvarez E., Wimmer E., Carrasco L.
PLoS ONE 4:E7997-E7997(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF PROTEASE.
[26]"Evidence that HIV-1 reverse transcriptase employs the DNA 3' end directed primary/secondary RNase H cleavage mechanism during synthesis and strand transfer."
Purohit V., Balakrishnan M., Kim B., Bambara R.A.
J. Biol. Chem. 280:40534-40543(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF REVERSE TRANSCRIPTASE AND RNASE H.
[27]"Proteolytic processing and particle maturation."
Vogt V.M.
Curr. Top. Microbiol. Immunol. 214:95-131(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[28]"Structural biology of HIV."
Turner B.G., Summers M.F.
J. Mol. Biol. 285:1-32(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[29]"Mechanisms of retroviral recombination."
Negroni M., Buc H.
Annu. Rev. Genet. 35:275-302(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[30]"Retroviral proteases."
Dunn B.M., Goodenow M.M., Gustchina A., Wlodawer A.
Genome Biol. 3:REVIEWS3006.1-REVIEWS3006.7(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[31]"Role of HIV-1 Gag domains in viral assembly."
Scarlata S., Carter C.
Biochim. Biophys. Acta 1614:62-72(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[32]"Human cell proteins and human immunodeficiency virus DNA integration."
Turlure F., Devroe E., Silver P.A., Engelman A.
Front. Biosci. 9:3187-3208(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[33]"Cyclophilin, TRIM5, and innate immunity to HIV-1."
Sokolskaja E., Luban J.
Curr. Opin. Microbiol. 9:404-408(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[34]"X-ray analysis of HIV-1 proteinase at 2.7-A resolution confirms structural homology among retroviral enzymes."
Lapatto R., Blundell T., Hemmings A., Overington J., Wilderspin A., Wood S., Merson J.R., Whittle P.J., Danley D.E., Geoghegan K.F., Hawrylik S.J., Lee S.E., Scheld K.G., Hobart P.M.
Nature 342:299-302(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 489-587.
[35]"Novel binding mode of highly potent HIV-proteinase inhibitors incorporating the (R)-hydroxyethylamine isostere."
Krohn A., Redshaw S., Ritchie J.C., Graves B.J., Hatada M.H.
J. Med. Chem. 34:3340-3342(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 489-587 IN COMPLEX WITH THE INHIBITOR RO 32-8959.
[36]"Structural characterization of a 39-residue synthetic peptide containing the two zinc binding domains from the HIV-1 p7 nucleocapsid protein by CD and NMR spectroscopy."
Omichinski J.G., Clore G.M., Sakaguchi K., Appella E., Gronenborn A.M.
FEBS Lett. 292:25-30(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 390-406.
[37]"Crystal structure of a complex of HIV-1 protease with a dihydroxyethylene-containing inhibitor: comparisons with molecular modeling."
Thanki N., Rao J.K., Foundling S.I., Howe W.J., Moon J.B., Hui J.O., Tomasselli A.G., Heinrikson R.L., Thaisrivongs S., Wlodawer A.
Protein Sci. 1:1061-1072(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 489-587 IN COMPLEX WITH A DIHYDROXYETHYLENE-CONTAINING INHIBITOR.
[38]"Conformational behaviour of the active and inactive forms of the nucleocapsid NCp7 of HIV-1 studied by 1H NMR."
Morellet N., de Rocquigny H., Mely Y., Jullian N., Demene H., Ottmann M., Gerard D., Darlix J.L., Fournie-Zaluski M.-C., Roques B.P.
J. Mol. Biol. 235:287-301(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 390-430.
[39]"Rational design of potent, bioavailable, nonpeptide cyclic ureas as HIV protease inhibitors."
Lam P.Y.S., Jadhav P.K., Eyermann C.J., Hodge C.N., Ru Y., Bacheler L.T., Meek J.L., Otto M.J., Rayner M.M., Wong Y.N., Chang C.-H., Weber P.C., Jackson D.A., Sharpe T.R., Erickson-Viitanen S.
Science 263:380-384(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 489-587 IN COMPLEX WITH THE INHIBITOR XK263.
[40]"Crystals of HIV-1 reverse transcriptase diffracting to 2.2 A resolution."
Stammers D.K., Somers D.O., Ross C.K., Kirby I., Ray P.H., Wilson J.E., Norman M., Ren J.S., Esnouf R.M., Garman E.F., Jones E.Y., Stuart D.I.
J. Mol. Biol. 242:586-588(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 588-1147.
[41]"Refined solution structure of p17, the HIV matrix protein."
Matthews S., Barlow P., Clark N., Kingsman S., Kingsman A., Campbell I.
Biochem. Soc. Trans. 23:725-729(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-132.
[42]"The structure of HIV-1 reverse transcriptase complexed with 9-chloro-TIBO: lessons for inhibitor design."
Ren J.S., Esnouf R.M., Hopkins A.L., Ross C.K., Jones E.Y., Stammers D.K., Stuart D.I.
Structure 3:915-926(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 588-1027.
[43]"Mechanism of inhibition of HIV-1 reverse transcriptase by non-nucleoside inhibitors."
Esnouf R.M., Ren J.S., Ross C.K., Jones E.Y., Stammers D.K., Stuart D.I.
Nat. Struct. Biol. 2:303-308(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 588-1147.
[44]"Complexes of HIV-1 reverse transcriptase with inhibitors of the HEPT series reveal conformational changes relevant to the design of potent non-nucleoside inhibitors."
Hopkins A.L., Ren J.S., Esnouf R.M., Willcox B.E., Jones E.Y., Ross C.K., Miyasaka T., Walker R.T., Tanaka H., Stammers D.K., Stuart D.I.
J. Med. Chem. 39:1589-1600(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 588-1027.
[45]"Improved cyclic urea inhibitors of the HIV-1 protease: synthesis, potency, resistance profile, human pharmacokinetics and X-ray crystal structure of DMP 450."
Hodge C.N., Aldrich P.E., Bacheler L.T., Chang C.-H., Eyermann C.J., Garber S.S., Grubb M., Jackson D.A., Jadhav P.K., Korant B.D., Lam P.Y.S., Maurin M.B., Meek J.L., Otto M.J., Rayner M.M., Reid C., Sharpe T.R., Shum L., Winslow D.L., Erickson-Viitanen S.
Chem. Biol. 3:301-314(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 489-587 IN COMPLEX WITH COMPLEX WITH DMP450.
[46]"Three-dimensional solution structure of the HIV-1 protease complexed with DMP323, a novel cyclic urea-type inhibitor, determined by nuclear magnetic resonance spectroscopy."
Yamazaki T., Hinck A.P., Wang Y.X., Nicholson L.K., Torchia D.A., Wingfield P., Stahl S.J., Kaufman J.D., Chang C.-H., Domaille P.J., Lam P.Y.S.
Protein Sci. 5:495-506(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 489-587 IN COMPLEX WITH THE INHIBITOR DMP323.
[47]"Unique features in the structure of the complex between HIV-1 reverse transcriptase and the bis(heteroaryl)piperazine (BHAP) U-90152 explain resistance mutations for this nonnucleoside inhibitor."
Esnouf R.M., Ren J.S., Hopkins A.L., Ross C.K., Jones E.Y., Stammers D.K., Stuart D.I.
Proc. Natl. Acad. Sci. U.S.A. 94:3984-3989(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 588-1130.
[48]"Cyclic urea amides: HIV-1 protease inhibitors with low nanomolar potency against both wild type and protease inhibitor resistant mutants of HIV."
Jadhav P.K., Ala P.J., Woerner F.J., Chang C.-H., Garber S.S., Anton E.D., Bacheler L.T.
J. Med. Chem. 40:181-191(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 489-587.
[49]"Toward a universal inhibitor of retroviral proteases: comparative analysis of the interactions of LP-130 complexed with proteases from HIV-1, FIV, and EIAV."
Kervinen J., Lubkowski J., Zdanov A., Bhatt D., Dunn B.M., Hui K.Y., Powell D.J., Kay J., Wlodawer A., Gustchina A.
Protein Sci. 7:2314-2323(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 489-587 IN COMPLEX WITH THE INHIBITOR LP-130.
[50]"Nonpeptide cyclic cyanoguanidines as HIV-1 protease inhibitors: synthesis, structure-activity relationships, and X-ray crystal structure studies."
Jadhav P.K., Woerner F.J., Lam P.Y., Hodge C.N., Eyermann C.J., Man H.W., Daneker W.F., Bacheler L.T., Rayner M.M., Meek J.L., Erickson-Viitanen S., Jackson D.A., Calabrese J.C., Schadt M.C., Chang C.-H.
J. Med. Chem. 41:1446-1455(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 489-587.
[51]"Counteracting HIV-1 protease drug resistance: structural analysis of mutant proteases complexed with XV638 and SD146, cyclic urea amides with broad specificities."
Ala P.J., Huston E.E., Klabe R.M., Jadhav P.K., Lam P.Y.S., Chang C.-H.
Biochemistry 37:15042-15049(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 489-587.
[52]"Molecular recognition of cyclic urea HIV-1 protease inhibitors."
Ala P.J., DeLoskey R.J., Huston E.E., Jadhav P.K., Lam P.Y.S., Eyermann C.J., Hodge C.N., Schadt M.C., Lewandowski F.A., Weber P.C., McCabe D.D., Duke J.L., Chang C.-H.
J. Biol. Chem. 273:12325-12331(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 489-587.
[53]"Hydrophilic peptides derived from the transframe region of Gag-Pol inhibit the HIV-1 protease."
Louis J.M., Dyda F., Nashed N.T., Kimmel A.R., Davies D.R.
Biochemistry 37:2105-2110(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 490-587 IN COMPLEX WITH A TRIPEPTIDE INHIBITOR.
[54]"3'-azido-3'-deoxythymidine drug resistance mutations in HIV-1 reverse transcriptase can induce long range conformational changes."
Ren J.S., Esnouf R.M., Hopkins A.L., Jones E.Y., Kirby I., Keeling J., Ross C.K., Larder B.A., Stuart D.I., Stammers D.K.
Proc. Natl. Acad. Sci. U.S.A. 95:9518-9523(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 588-1130.
[55]"Crystal structures of HIV-1 reverse transcriptase in complex with carboxanilide derivatives."
Ren J.S., Esnouf R.M., Hopkins A.L., Warren J., Balzarini J., Stuart D.I., Stammers D.K.
Biochemistry 37:14394-14403(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 588-1147 IN COMPLEX WITH CARBOXANILIDE DERIVATIVES.
[56]"Structural and kinetic analysis of drug resistant mutants of HIV-1 protease."
Mahalingam B., Louis J.M., Reed C.C., Adomat J.M., Krouse J., Wang Y.-F., Harrison R.W., Weber I.T.
Eur. J. Biochem. 263:238-245(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 501-599.
[57]"Crystal structure of the HIV-1 integrase catalytic core and C-terminal domains: a model for viral DNA binding."
Chen J.C., Krucinski J., Miercke L.J., Finer-Moore J.S., Tang A.H., Leavitt A.D., Stroud R.M.
Proc. Natl. Acad. Sci. U.S.A. 97:8233-8238(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1199-1435.
[58]"1.9 A X-ray study shows closed flap conformation in crystals of tethered HIV-1 PR."
Pillai B., Kannan K.K., Hosur M.V.
Proteins 43:57-64(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 489-587.
[59]"Structural mechanisms of drug resistance for mutations at codons 181 and 188 in HIV-1 reverse transcriptase and the improved resilience of second generation non-nucleoside inhibitors."
Ren J.S., Nichols C.E., Bird L.E., Chamberlain P.P., Weaver K.L., Short S.A., Stuart D.I., Stammers D.K.
J. Mol. Biol. 312:795-805(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 588-1147 IN COMPLEX WITH INHIBITORS.
[60]"Effects of remote mutation on the autolysis of HIV-1 PR: X-ray and NMR investigations."
Kumar M., Kannan K.K., Hosur M.V., Bhavesh N.S., Chatterjee A., Mittal R., Hosur R.V.
Biochem. Biophys. Res. Commun. 294:395-401(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 489-587.
[61]"Solution structure of the RNase H domain of the HIV-1 reverse transcriptase in the presence of magnesium."
Pari K., Mueller G.A., DeRose E.F., Kirby T.W., London R.E.
Biochemistry 42:639-650(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1014-1147.
[62]"Crystal structures of HIV-1 reverse transcriptases mutated at codons 100, 106 and 108 and mechanisms of resistance to non-nucleoside inhibitors."
Ren J.S., Nichols C.E., Chamberlain P.P., Weaver K.L., Short S.A., Stammers D.K.
J. Mol. Biol. 336:569-578(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 588-1147 IN COMPLEX WITH INHIBITORS.
[63]"Design of non-nucleoside inhibitors of HIV-1 reverse transcriptase with improved drug resistance properties. 2."
Freeman G.A., Andrews C.W. III, Hopkins A.L., Lowell G.S., Schaller L.T., Cowan J.R., Gonzales S.S., Koszalka G.W., Hazen R.J., Boone L.R., Ferris R.G., Creech K.L., Roberts G.B., Short S.A., Weaver K.L., Reynolds D.J., Milton J., Ren J.S. expand/collapse author list , Stuart D.I., Stammers D.K., Chan J.H.
J. Med. Chem. 47:5923-5936(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 588-1147 IN COMPLEX WITH INHIBITORS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K03455 Genomic RNA. Translation: AAB50259.1. Sequence problems.
AF033819 Genomic RNA. Translation: AAC82598.2. Sequence problems.
RefSeqNP_057849.4. NC_001802.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A30X-ray2.00A/B489-587[»]
1BV7X-ray2.00A/B489-587[»]
1BV9X-ray2.00A/B489-587[»]
1BVENMR-A/B489-587[»]
1BVGNMR-A/B489-587[»]
1BWAX-ray1.90A/B489-587[»]
1BWBX-ray1.80A/B489-587[»]
1C0TX-ray2.70A588-1146[»]
B588-1026[»]
1C0UX-ray2.52A588-1146[»]
B588-1026[»]
1C1BX-ray2.50A588-1146[»]
B588-1026[»]
1C1CX-ray2.50A588-1146[»]
B588-1026[»]
1DMPX-ray2.00A/B489-587[»]
1DTQX-ray2.80A588-1146[»]
B588-1026[»]
1DTTX-ray3.00A588-1146[»]
B588-1026[»]
1E6JX-ray3.00P143-352[»]
1EP4X-ray2.50A588-1146[»]
B588-1026[»]
1ESKNMR-A390-429[»]
1EX4X-ray2.80A/B1199-1435[»]
1EXQX-ray1.60A/B1204-1356[»]
1FB7X-ray2.60A489-587[»]
1FK9X-ray2.50A588-1130[»]
B588-1027[»]
1FKOX-ray2.90A588-1130[»]
B588-1027[»]
1FKPX-ray2.90A588-1129[»]
B588-1026[»]
1G6LX-ray1.90A489-587[»]
1HIVX-ray2.00A/B489-587[»]
1HVHX-ray1.80A/B489-587[»]
1HVRX-ray1.80A/B489-587[»]
1HWRX-ray1.80A/B489-587[»]
1HXBX-ray2.30A/B489-587[»]
1JKHX-ray2.50A588-1147[»]
B588-1027[»]
1JLAX-ray2.50A588-1147[»]
B588-1027[»]
1JLBX-ray3.00A588-1147[»]
B588-1027[»]
1JLCX-ray3.00A588-1147[»]
B588-1027[»]
1JLEX-ray2.80A588-1147[»]
B588-1027[»]
1JLFX-ray2.60A588-1147[»]
B588-1027[»]
1JLGX-ray2.60A588-1147[»]
B588-1027[»]
1JLQX-ray3.00A588-1146[»]
B588-1026[»]
1KLMX-ray2.65A588-1147[»]
B588-1027[»]
1LV1X-ray2.10A489-587[»]
1LW0X-ray2.80A588-1147[»]
B588-1027[»]
1LW2X-ray3.00A588-1147[»]
B588-1027[»]
1LWCX-ray2.62A588-1147[»]
B588-1027[»]
1LWEX-ray2.81A588-1147[»]
B588-1027[»]
1LWFX-ray2.80A588-1147[»]
B588-1027[»]
1NCPNMR-N390-406[»]
1O1WNMR-A1014-1147[»]
1ODWX-ray2.10A/B489-587[»]
1ODYX-ray2.00A/B489-587[»]
1QBRX-ray1.80A/B489-587[»]
1QBSX-ray1.80A/B489-587[»]
1QBTX-ray2.10A/B489-587[»]
1QBUX-ray1.80A/B489-587[»]
1REVX-ray2.60A588-1147[»]
B588-1027[»]
1RT1X-ray2.55A588-1147[»]
B588-1027[»]
1RT2X-ray2.55A588-1147[»]
B588-1027[»]
1RT3X-ray3.00A588-1147[»]
B588-1027[»]
1RT4X-ray2.90A588-1147[»]
B588-1027[»]
1RT5X-ray2.90A588-1147[»]
B588-1027[»]
1RT6X-ray2.80A588-1147[»]
B588-1027[»]
1RT7X-ray3.00A588-1147[»]
B588-1027[»]
1RTDX-ray3.20B/D588-1027[»]
1RTHX-ray2.20A588-1146[»]
B588-1026[»]
1RTIX-ray3.00A588-1146[»]
B588-1026[»]
1RTJX-ray2.35A588-1147[»]
B588-1027[»]
1S1TX-ray2.40A588-1147[»]
B588-1027[»]
1S1UX-ray3.00A588-1147[»]
B588-1027[»]
1S1VX-ray2.60A588-1147[»]
B588-1027[»]
1S1WX-ray2.70A588-1147[»]
B588-1027[»]
1S1XX-ray2.80A588-1147[»]
B588-1027[»]
1T05X-ray3.00B588-1016[»]
1TAMNMR-A1-132[»]
1TKTX-ray2.60A588-1147[»]
B588-1027[»]
1TKXX-ray2.85A588-1147[»]
B588-1027[»]
1TKZX-ray2.81A588-1147[»]
B588-1027[»]
1TL1X-ray2.90A588-1147[»]
B588-1027[»]
1TL3X-ray2.80A588-1146[»]
B588-1026[»]
1VRTX-ray2.20A588-1146[»]
B588-1026[»]
1VRUX-ray2.40A588-1146[»]
B588-1026[»]
2HNDX-ray2.50A591-1123[»]
B594-1014[»]
2HNYX-ray2.50A591-1123[»]
B594-1014[»]
2HNZX-ray3.00A591-1123[»]
2KODNMR-A/B276-363[»]
2NPHX-ray1.65A/B489-587[»]
2OPPX-ray2.55A591-1132[»]
B592-1018[»]
2OPQX-ray2.80A591-1124[»]
B592-1015[»]
2OPRX-ray2.90A589-1135[»]
B593-1018[»]
2OPSX-ray2.30A589-1130[»]
B593-1027[»]
2RF2X-ray2.40A588-1147[»]
B588-1027[»]
2RKIX-ray2.30A588-1147[»]
B588-1027[»]
2WHHX-ray1.69A489-587[»]
2WOMX-ray3.20A588-1147[»]
B588-1027[»]
2WONX-ray2.80A588-1147[»]
B588-1027[»]
2YNFX-ray2.36A588-1147[»]
B588-1015[»]
2YNGX-ray2.12A588-1147[»]
B588-1015[»]
2YNHX-ray2.90A588-1147[»]
B588-1015[»]
2YNIX-ray2.49A588-1147[»]
B588-1015[»]
3AO2X-ray1.80A/B1197-1359[»]
3C6TX-ray2.70A588-1147[»]
B588-1027[»]
3C6UX-ray2.70A588-1147[»]
B588-1027[»]
3DI6X-ray2.65A588-1148[»]
B588-1027[»]
3DLEX-ray2.50A588-1147[»]
B588-1027[»]
3DLGX-ray2.20A588-1147[»]
B588-1027[»]
3DM2X-ray3.10A588-1147[»]
B588-1027[»]
3DMJX-ray2.60A588-1147[»]
B588-1027[»]
3DOKX-ray2.90A588-1147[»]
B588-1027[»]
3DOLX-ray2.50A588-1147[»]
B588-1027[»]
3DOXX-ray2.00A489-587[»]
3DRPX-ray2.60A588-1147[»]
B588-1027[»]
3DRRX-ray2.89A588-1147[»]
B588-1027[»]
3DRSX-ray3.15A588-1147[»]
B588-1027[»]
3DYAX-ray2.30A588-1148[»]
B588-1027[»]
3E01X-ray2.95A588-1148[»]
B588-1027[»]
3FFIX-ray2.60A588-1147[»]
B588-1027[»]
3I0RX-ray2.98A588-1147[»]
B588-1027[»]
3I0SX-ray2.70A588-1147[»]
B588-1027[»]
3KJVX-ray3.10A588-1147[»]
B588-1027[»]
3KK1X-ray2.70A588-1147[»]
B588-1027[»]
3KK2X-ray2.90A588-1147[»]
B588-1027[»]
3KK3X-ray2.90A588-1147[»]
B588-1027[»]
3KT2X-ray1.65A489-587[»]
3KT5X-ray1.80A489-587[»]
3LAKX-ray2.30A/B588-1147[»]
3LALX-ray2.51A/B588-1147[»]
3LAMX-ray2.76A/B588-1147[»]
3LANX-ray2.55A/B588-1147[»]
3LP0X-ray2.79A588-1147[»]
B588-1027[»]
3LP1X-ray2.23A588-1147[»]
B588-1027[»]
3LP2X-ray2.80A588-1147[»]
B588-1027[»]
3M8PX-ray2.67A588-1148[»]
B588-1027[»]
3M8QX-ray2.70A588-1148[»]
B588-1027[»]
3MECX-ray2.30A588-1147[»]
B588-1027[»]
3MEDX-ray2.50A588-1147[»]
B588-1027[»]
3MEEX-ray2.40A588-1147[»]
B588-1027[»]
3MEGX-ray2.80A588-1147[»]
B588-1027[»]
3MIMX-ray1.76A/B489-587[»]
3N3IX-ray2.50A489-587[»]
3NBPX-ray2.95A588-1148[»]
B588-1027[»]
3PHVX-ray2.70A489-587[»]
3QINX-ray1.70A1014-1148[»]
3QIOX-ray1.40A1014-1148[»]
3QIPX-ray2.09A588-1147[»]
B588-1027[»]
3T19X-ray2.60A/B588-1147[»]
3T1AX-ray2.40A/B588-1147[»]
3TAMX-ray2.51A588-1147[»]
B588-1027[»]
4B3OX-ray3.30A588-1145[»]
B588-1027[»]
4B3PX-ray4.84A588-1145[»]
B588-1027[»]
4B3QX-ray5.00A588-1145[»]
B588-1027[»]
4I7FX-ray2.50A588-1147[»]
B588-1027[»]
4KV8X-ray2.30A588-1147[»]
B588-1027[»]
4NCGX-ray2.58A588-1147[»]
B585-1027[»]
ProteinModelPortalP04585.
SMRP04585. Positions 1-432, 489-1144, 1148-1417.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP04585. 2 interactions.
MINTMINT-111862.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID155348.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
SABIO-RKP04585.

Family and domain databases

Gene3D1.10.10.200. 1 hit.
1.10.1200.30. 1 hit.
1.10.150.90. 1 hit.
1.10.375.10. 1 hit.
2.30.30.10. 1 hit.
2.40.70.10. 1 hit.
3.30.420.10. 2 hits.
4.10.60.10. 1 hit.
InterProIPR001969. Aspartic_peptidase_AS.
IPR000721. Gag_p24.
IPR001037. Integrase_C_retrovir.
IPR001584. Integrase_cat-core.
IPR017856. Integrase_Zn-bd_dom-like_N.
IPR003308. Integrase_Zn-bd_dom_N.
IPR000071. Lentvrl_matrix_N.
IPR012344. Matrix_N_HIV/RSV.
IPR018061. Pept_A2A_retrovirus_sg.
IPR001995. Peptidase_A2_cat.
IPR021109. Peptidase_aspartic_dom.
IPR008916. Retrov_capsid_C.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix_N.
IPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
IPR000477. RT_dom.
IPR010659. RVT_connect.
IPR010661. RVT_thumb.
IPR001878. Znf_CCHC.
[Graphical view]
PfamPF00540. Gag_p17. 1 hit.
PF00607. Gag_p24. 1 hit.
PF00552. IN_DBD_C. 1 hit.
PF02022. Integrase_Zn. 1 hit.
PF00075. RNase_H. 1 hit.
PF00665. rve. 1 hit.
PF00077. RVP. 1 hit.
PF00078. RVT_1. 1 hit.
PF06815. RVT_connect. 1 hit.
PF06817. RVT_thumb. 1 hit.
PF00098. zf-CCHC. 2 hits.
[Graphical view]
PRINTSPR00234. HIV1MATRIX.
SMARTSM00343. ZnF_C2HC. 2 hits.
[Graphical view]
SUPFAMSSF46919. SSF46919. 1 hit.
SSF47353. SSF47353. 1 hit.
SSF47836. SSF47836. 1 hit.
SSF47943. SSF47943. 1 hit.
SSF50122. SSF50122. 1 hit.
SSF50630. SSF50630. 1 hit.
SSF53098. SSF53098. 2 hits.
SSF57756. SSF57756. 1 hit.
PROSITEPS50175. ASP_PROT_RETROV. 1 hit.
PS00141. ASP_PROTEASE. 1 hit.
PS50994. INTEGRASE. 1 hit.
PS51027. INTEGRASE_DBD. 1 hit.
PS50879. RNASE_H. 1 hit.
PS50878. RT_POL. 1 hit.
PS50158. ZF_CCHC. 2 hits.
PS50876. ZF_INTEGRASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP04585.

Entry information

Entry namePOL_HV1H2
AccessionPrimary (citable) accession number: P04585
Secondary accession number(s): O09777, Q9WJC5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 178 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references