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Protein

Gag-Pol polyprotein

Gene

gag-pol

Organism
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

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

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

Gag-Pol polyprotein: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi). Gag-Pol polyprotein may regulate its own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, the polyprotein would promote translation, whereas at high concentration, the polyprotein would encapsidate genomic RNA and then shut off translation.
Matrix protein p17: Targets the polyprotein to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus (By similarity). Matrix protein is part of the pre-integration complex. Implicated in the release from host cell mediated by Vpu. Binds to RNA (By similarity).By similarity
Capsid protein p24: Forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion (PubMed:8648689). 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 (PubMed:12660176). Host restriction factors such as monkey TRIM5-alpha or TRIMCyp bind retroviral capsids and cause premature capsid disassembly, leading to blocks in reverse transcription. Capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species (PubMed:23785198). Host PIN1 apparently facilitates the virion uncoating (By similarity). On the other hand, interactions with PDZD8 or CYPA stabilize the capsid (PubMed:24554657).By similarity4 Publications
Nucleocapsid protein p7: Encapsulates and protects viral dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc fingers. Acts as a nucleic acid chaperone which is involved in rearangement of nucleic acid secondary structure during gRNA retrotranscription. Also facilitates template switch leading to recombination. As part of the polyprotein, participates in gRNA dimerization, packaging, tRNA incorporation and virion assembly.5 Publications
Protease: Aspartyl protease that mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane (PubMed:9573231, PubMed:11932404). Cleavages take place as an ordered, step-wise cascade to yield mature proteins (PubMed:9573231, PubMed:11932404). This process is called maturation (PubMed:9573231, PubMed:11932404). Displays maximal activity during the budding process just prior to particle release from the cell (PubMed:9573231, PubMed:11932404). Also cleaves Nef and Vif, probably concomitantly with viral structural proteins on maturation of virus particles (PubMed:7835426). 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 (PubMed:12660176, PubMed:19914170).PROSITE-ProRule annotationBy similarity3 Publications
Reverse transcriptase/ribonuclease H: 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 tRNA3-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.1 Publication
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.2 Publications

Miscellaneous

Reverse transcriptase/ribonuclease H: 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.

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

  • Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.PROSITE-ProRule annotation EC:3.4.23.16
  • 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. EC:3.1.26.13
  • 3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid. EC:3.1.13.2

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

Protein has several cofactor binding sites:
  • Mg2+By similarityNote: Binds 2 magnesium ions for reverse transcriptase polymerase activity.By similarity
  • Mg2+By similarityNote: Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is a precondition for magnesium binding.By similarity
  • Mg2+By similarityNote: Magnesium ions are required for integrase activity. Binds at least 1, maybe 2 magnesium ions.By similarity

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Protease: The viral protease is inhibited by many synthetic protease inhibitors (PIs), such as amprenavir, atazanavir, indinavir, loprinavir, nelfinavir, ritonavir and saquinavir. Use of protease inhibitors in tritherapy regimens permit more ambitious therapeutic strategies. Reverse transcriptase/ribonuclease H: 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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei221 – 222Cis/trans isomerization of proline peptide bond; by human PPIA/CYPA2
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei513For protease activity; shared with dimeric partnerPROSITE-ProRule annotation1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi697Magnesium; catalytic; for reverse transcriptase activityBy similarity1
Metal bindingi772Magnesium; catalytic; for reverse transcriptase activityBy similarity1
Metal bindingi773Magnesium; catalytic; for reverse transcriptase activityBy similarity1
Sitei988Essential for RT p66/p51 heterodimerizationBy similarity1
Sitei1001Essential for RT p66/p51 heterodimerizationBy similarity1
Metal bindingi1030Magnesium; catalytic; for RNase H activity1
Metal bindingi1065Magnesium; catalytic; for RNase H activity1 Publication1
Metal bindingi1085Magnesium; catalytic; for RNase H activity1
Metal bindingi1136Magnesium; catalytic; for RNase H activity1 Publication1
Metal bindingi1211Magnesium; catalytic; for integrase activityBy similarity1
Metal bindingi1263Magnesium; catalytic; for integrase activityBy similarity1
Metal bindingi1299Magnesium; catalytic; for integrase activityCurated1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri390 – 407CCHC-type 1PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri411 – 428CCHC-type 2PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri1150 – 1191Integrase-typePROSITE-ProRule annotationAdd BLAST42
<p>This subsection of the ‘Function’ section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi1370 – 1417Integrase-typePROSITE-ProRule annotationAdd BLAST48

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

GO - Biological processi

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

Molecular functionAspartyl protease, DNA-binding, DNA-directed DNA polymerase, Endonuclease, Hydrolase, Multifunctional enzyme, Nuclease, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed DNA polymerase, Transferase, Viral nucleoprotein
Biological processActivation of host caspases by virus, DNA integration, DNA recombination, Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host-virus interaction, Modulation of host cell apoptosis by virus, Viral genome integration, Viral penetration into host nucleus, Viral release from host cell, Virion maturation, Virus entry into host cell
LigandLipid-binding, Magnesium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.7.49 2676
3.4.23.16 2676

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-162585 Uncoating of the HIV Virion
R-HSA-162588 Budding and maturation of HIV virion
R-HSA-162592 Integration of provirus
R-HSA-162594 Early Phase of HIV Life Cycle
R-HSA-164516 Minus-strand DNA synthesis
R-HSA-164525 Plus-strand DNA synthesis
R-HSA-164843 2-LTR circle formation
R-HSA-173107 Binding and entry of HIV virion
R-HSA-175474 Assembly Of The HIV Virion
R-HSA-175567 Integration of viral DNA into host genomic DNA
R-HSA-177539 Autointegration results in viral DNA circles
R-HSA-180689 APOBEC3G mediated resistance to HIV-1 infection
R-HSA-180910 Vpr-mediated nuclear import of PICs

SABIO-RK: Biochemical Reaction Kinetics Database

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SABIO-RKi
P04585

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

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Gag-Pol polyprotein
Alternative name(s):
Pr160Gag-Pol
Cleaved into the following 11 chains:
Matrix protein p17
Short name:
MA
Capsid protein p24
Short name:
CA
Spacer peptide 1By similarity
Short name:
SP1
Alternative name(s):
p2
Transframe peptide
Short name:
TF
p6-pol
Short name:
p6*
Alternative name(s):
PR
Retropepsin
Alternative name(s):
Exoribonuclease H (EC:3.1.13.2)
p66 RT
Integrase (EC:2.7.7.-1 Publication, EC:3.1.-.-1 Publication)
Short name:
IN
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:gag-pol
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHuman immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri11706 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiVirusesOrterviralesRetroviridaeOrthoretrovirinaeLentivirus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>Virus hostiHomo sapiens (Human) [TaxID: 9606]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000105453 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Genome
  • UP000002241 Componenti: Genome

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

Gag-Pol polyprotein :
Integrase :

GO - Cellular componenti

Keywords - Cellular componenti

Capsid protein, Host cell membrane, Host cytoplasm, Host endosome, Host membrane, Host nucleus, Membrane, Virion

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi6S → D: No influence on the PIP2- or concentration-dependent myristyl switch mechanism. 1 Publication1
Mutagenesisi9S → D: No influence on the PIP2- or concentration-dependent myristyl switch mechanism. 1 Publication1
Mutagenesisi18K → A: Replication-defective, induces nuclear mislocalization of matrix protein; when associated with G-22. 1 Publication1
Mutagenesisi22R → G: Replication-defective, induces nuclear mislocalization of matrix protein; when associated with A-18. 1 Publication1
Mutagenesisi27K → A: No effect on subcellular localization of matrix protein; when associated with A-18 and G-22. 1 Publication1
Mutagenesisi67S → D: No influence on the PIP2- or concentration-dependent myristyl switch mechanism. 1 Publication1
Mutagenesisi72S → D: No influence on the PIP2- or concentration-dependent myristyl switch mechanism. 1 Publication1
Mutagenesisi217P → A: 3-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi218V → A: 2.7-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi219H → A or Q: 8-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi220A → G: 44-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi220A → V: 3.4-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi221G → A: 31-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi221G → V: 154-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi222P → A: 36-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi222P → V: More than 150-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi223I → A: 1.2-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi223I → V: 1.0-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi224A → G: 2.3-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi224A → V: 1.7-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi225P → A: 1.6-fold decrease of PPIA-binding affinity. 1 Publication1
Mutagenesisi394N → F or G: Decreases infectivity and replication. 1 Publication1
Mutagenesisi400H → C: Complete loss of infectivity and in vitro chaperone activity. 1 Publication1
Mutagenesisi405C → H: Complete loss of infectivity and DNA synthesis. 1 Publication1
Mutagenesisi421H → C: Partial loss of infectivity. Complete loss of in vitro chaperone activity. 1 Publication1
Mutagenesisi426C → H: Partial loss of infectivity. 1 Publication1
Mutagenesisi1065E → Q: Complete loss of RNase H activity. 1 Publication1
Mutagenesisi1136D → N: Complete loss of RNase H activity. 1 Publication1
Mutagenesisi1159H → C: No effect on integrase activity in vitro. 1 Publication1
Mutagenesisi1163H → C or V: 75% increase of integrase activity in vitro. 1 Publication1
Mutagenesisi1187C → A: Complete loss of integrase activity in vivo. 1 Publication1
Mutagenesisi1190C → A: Complete loss of integrase activity in vivo. 1 Publication1
Mutagenesisi1200Q → C: 75% increase of integrase activity in vitro. 1 Publication1
Mutagenesisi1208W → A: Complete loss of integrase activity in vivo. 1 Publication1
Mutagenesisi1211D → A or V: Complete loss of integrase activity in vivo and in vitro. 3 Publications1
Mutagenesisi1213T → A: No effect on infectivity. 1 Publication1
Mutagenesisi1222V → P: Complete loss of integrase activity. 1 Publication1
Mutagenesisi1228S → A: Complete loss of integrase activity in vivo. 2 Publications1
Mutagenesisi1228S → R: No effect on integrase activity in vitro. 2 Publications1
Mutagenesisi1262T → A: No effect infectivity. 1 Publication1
Mutagenesisi1263D → A or I: Complete loss of integrase activity in vivo and in vitro. 3 Publications1
Mutagenesisi1270G → A: No effect on infectivity. 1 Publication1
Mutagenesisi1282I → P: Complete loss of integrase activity in vivo. 1 Publication1
Mutagenesisi1298V → A: No effect on infectivity. 1 Publication1
Mutagenesisi1299E → G or P: Complete loss of integrase activity in vitro. 3 Publications1
Mutagenesisi1306K → P: Slow down virus replication. 1 Publication1
Mutagenesisi1326A → P: Complete loss of integrase activity in vivo. 1 Publication1
Mutagenesisi1346R → C: 75% increase of integrase activity in vitro. 1 Publication1
Mutagenesisi1382W → A: Complete loss of infectivity. No effect on integrase activity in vitro. 2 Publications1
Mutagenesisi1382W → E: 75% increase of integrase activity in vitro. 2 Publications1

Keywords - Diseasei

AIDS

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3638360

Drug and drug target database

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DrugBanki
DB07892 1-(2-HYDROXYETHYLOXYMETHYL)-6-PHENYL THIOTHYMINE
DB08372 1-[2-(4-ETHOXY-3-FLUOROPYRIDIN-2-YL)ETHYL]-3-(5-METHYLPYRIDIN-2-YL)THIOUREA
DB08681 1-METHYL ETHYL 2-CHLORO-5-[[[(1-METHYLETHOXY)THIOOXO]METHYL]AMINO]-BENZOATE
DB07826 2-[4-chloro-2-(phenylcarbonyl)phenoxy]-N-phenylacetamide
DB08679 2-METHYL-FURAN-3-CARBOTHIOIC ACID [4-CHLORO-3-(3-METHYL-BUT-2-ENYLOXY)-PHENYL]-AMIDE
DB08154 3-chloro-5-[2-chloro-5-(1H-indazol-3-ylmethoxy)phenoxy]benzonitrile
DB07864 4-[(CYCLOPROPYLETHYNYL)OXY]-6-FLUORO-3-ISOPROPYLQUINOLIN-2(1H)-ONE
DB08211 5-bromo-3-(pyrrolidin-1-ylsulfonyl)-1H-indole-2-carboxamide
DB08379 6-(4-chloro-2-fluoro-3-phenoxybenzyl)pyridazin-3(2H)-one
DB08634 6-BENZYL-1-BENZYLOXYMETHYL-5-ISOPROPYL URACIL
DB08188 6-BENZYL-1-ETHOXYMETHYL-5-ISOPROPYL URACIL
DB07871 6-CHLORO-4-(CYCLOHEXYLOXY)-3-ISOPROPYLQUINOLIN-2(1H)-ONE
DB07867 6-CHLORO-4-(CYCLOHEXYLOXY)-3-PROPYLQUINOLIN-2(1H)-ONE
DB07868 6-CHLORO-4-(CYCLOHEXYLSULFANYL)-3-PROPYLQUINOLIN-2(1H)-ONE
DB07869 6-CHLORO-4-(CYCLOHEXYLSULFINYL)-3-PROPYLQUINOLIN-2(1H)-ONE
DB06581 Bevirimat
DB02102 DMP450
DB04609 INHIBITOR Q8467 OF DUPONT MERCK
DB08680 N-[4-CLORO-3-(T-BUTYLOXOME)PHENYL-2-METHYL-3-FURAN-CARBOTHIAMIDE
DB07797 N-[[3-FLUORO-4-ETHOXY-PYRID-2-YL]ETHYL]-N'-[5-CHLORO-PYRIDYL]-THIOUREA
DB07781 N-[[3-FLUORO-4-ETHOXY-PYRID-2-YL]ETHYL]-N'-[5-NITRILOMETHYL-PYRIDYL]-THIOUREA
DB08286 NAPHTHYLOXYACETIC ACID
DB07910 PHENYLALANINDIOL
DB02729 SD146
DB05328 VGV-1
DB02702 XV638

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved; by hostBy similarity
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002236202 – 1435Gag-Pol polyproteinAdd BLAST1434
ChainiPRO_00000424392 – 132Matrix protein p17By similarityAdd BLAST131
ChainiPRO_0000042440133 – 363Capsid protein p24By similarityAdd BLAST231
<p>This subsection of the ‘PTM / Processing’ section describes the position and length of an active peptide in the mature protein.<p><a href='/help/peptide' target='_top'>More...</a></p>PeptideiPRO_0000042441364 – 377Spacer peptide 1By similarityAdd BLAST14
ChainiPRO_0000042442378 – 432Nucleocapsid protein p7By similarityAdd BLAST55
PeptideiPRO_0000246716433 – 440Transframe peptideSequence analysis8
ChainiPRO_0000042443441 – 488p6-polSequence analysisAdd BLAST48
ChainiPRO_0000038665489 – 587ProteaseAdd BLAST99
ChainiPRO_0000042444588 – 1147Reverse transcriptase/ribonuclease HAdd BLAST560
ChainiPRO_0000042445588 – 1027p51 RTAdd BLAST440
ChainiPRO_00000424461028 – 1147p15Add BLAST120
ChainiPRO_00000424471148 – 1435IntegraseBy similarityAdd BLAST288

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi2N-myristoyl glycine; by hostBy similarity1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei132Phosphotyrosine; by hostBy similarity1

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

Gag-Pol polyprotein: 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.PROSITE-ProRule annotation3 Publications
Matrix protein p17: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association (PubMed:17656588).1 Publication
Capsid protein p24: Phosphorylated possibly by host MAPK1; this phosphorylation is necessary for Pin1-mediated virion uncoating.By similarity
Nucleocapsid protein p7: Methylated by host PRMT6, impairing its function by reducing RNA annealing and the initiation of reverse transcription.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei132 – 133Cleavage; by viral proteaseBy similarity2
Sitei363 – 364Cleavage; by viral proteaseBy similarity2
Sitei377 – 378Cleavage; by viral proteaseBy similarity2
Sitei393 – 394Cleavage; by viral proteaseSequence analysis2
Sitei426 – 427Cleavage; by viral proteaseSequence analysis2
Sitei432 – 433Cleavage; by viral proteaseSequence analysis2
Sitei440 – 441Cleavage; by viral proteaseBy similarity2
Sitei488 – 489Cleavage; by viral proteaseBy similarity2
Sitei587 – 588Cleavage; by viral proteaseBy similarity2
Sitei1027 – 1028Cleavage; by viral protease; partialBy similarity2
Sitei1147 – 1148Cleavage; by viral proteaseBy similarity2

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P04585

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

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

Matrix protein p17: Homotrimer; further assembles as hexamers of trimers (PubMed:19327811). Matrix protein p17: Interacts with gp41 (via C-terminus) (By similarity). Matrix protein p17: interacts with host CALM1; this interaction induces a conformational change in the Matrix protein, triggering exposure of the myristate group (PubMed:24500712). Matrix protein p17: interacts with host AP3D1; this interaction allows the polyprotein trafficking to multivesicular bodies during virus assembly (By similarity). Matrix protein p17: Part of the pre-integration complex (PIC) which is composed of viral genome, matrix protein, Vpr and integrase (By similarity). Capsid protein p24: Homodimer; the homodimer further multimerizes as homohexamers or homopentamers (PubMed:19914170). Capsid protein p24: Interacts with human PPIA/CYPA (PubMed:9223641); this interaction stabilizes the capsid. Capsid protein p24: Interacts with human NUP153 (By similarity). Capsid protein p24: Interacts with host PDZD8; this interaction stabilizes the capsid (PubMed:20573829). Capsid protein p24: Interacts with monkey TRIM5; this interaction destabilizes the capsid (PubMed:23785198). Protease: Homodimer, whose active site consists of two apposed aspartic acid residues (PubMed:2162350, PubMed:24132393). Reverse transcriptase/ribonuclease H: 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: Homodimer; possibly can form homotetramer. Integrase: Part of the pre-integration complex (PIC) which is composed of viral genome, matrix protein, Vpr and integrase. Integrase: Interacts with human SMARCB1/INI1 and human PSIP1/LEDGF isoform 1 (PubMed:7801128). Integrase: Interacts with human KPNA3; this interaction might play a role in nuclear import of the pre-integration complex (PubMed:19914170). Integrase: Interacts with human NUP153; this interaction might play a role in nuclear import of the pre-integration complex (By similarity).By similarity10 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
1205538, 127 interactors

Protein interaction database and analysis system

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IntActi
P04585, 6 interactors

Molecular INTeraction database

More...
MINTi
P04585

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P04585

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

Secondary structure

11435
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P04585

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

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SMRi
P04585

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P04585

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini508 – 577Peptidase A2PROSITE-ProRule annotationAdd BLAST70
Domaini631 – 821Reverse transcriptasePROSITE-ProRule annotationAdd BLAST191
Domaini1021 – 1144RNase HPROSITE-ProRule annotationAdd BLAST124
Domaini1201 – 1351Integrase catalyticPROSITE-ProRule annotationAdd BLAST151

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni7 – 31Interaction with Gp41By similarityAdd BLAST25
Regioni8 – 43Interaction with host CALM11 PublicationAdd BLAST36
Regioni12 – 19Interaction with host AP3D1By similarity8
Regioni14 – 33Interaction with membrane phosphatidylinositol 4,5-bisphosphate and RNABy similarityAdd BLAST20
Regioni73 – 77Interaction with membrane phosphatidylinositol 4,5-bisphosphateBy similarity5
Regioni189 – 227Interaction with host PPIA/CYPA and NUP153By similarityAdd BLAST39
Regioni217 – 225PPIA/CYPA-binding loop9
Regioni277 – 363Dimerization/Multimerization of capsid protein p24Add BLAST87
Regioni489 – 493Dimerization of protease1 Publication5
Regioni537 – 543Dimerization of protease1 Publication7
Regioni576 – 588Dimerization of protease1 PublicationAdd BLAST13
Regioni814 – 822RT 'primer grip'By similarity9

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi16 – 22Nuclear export signalBy similarity7
Motifi26 – 32Nuclear localization signalBy similarity7
Motifi985 – 1001Tryptophan repeat motifBy similarityAdd BLAST17

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

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).By similarity
Reverse transcriptase/ribonuclease H: The tryptophan repeat motif is involved in RT p66/p51 dimerization.
Integrase: The 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,D(35)E motif is independently essential for the 3'-processing and strand transfer activities of purified integrase protein.

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri390 – 407CCHC-type 1PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri411 – 428CCHC-type 2PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri1150 – 1191Integrase-typePROSITE-ProRule annotationAdd BLAST42

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

Database of Orthologous Groups

More...
OrthoDBi
VOG09000135

Family and domain databases

Conserved Domains Database

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CDDi
cd05482 HIV_retropepsin_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.10.200, 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

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001969 Aspartic_peptidase_AS
IPR000721 Gag_p24
IPR017856 Integrase-like_N
IPR036862 Integrase_C_dom_sf_retrovir
IPR001037 Integrase_C_retrovir
IPR001584 Integrase_cat-core
IPR003308 Integrase_Zn-bd_dom_N
IPR000071 Lentvrl_matrix_N
IPR012344 Matrix_HIV/RSV_N
IPR001995 Peptidase_A2_cat
IPR021109 Peptidase_aspartic_dom_sf
IPR034170 Retropepsin-like_cat_dom
IPR018061 Retropepsins
IPR008916 Retrov_capsid_C
IPR008919 Retrov_capsid_N
IPR010999 Retrovr_matrix
IPR012337 RNaseH-like_sf
IPR002156 RNaseH_domain
IPR036397 RNaseH_sf
IPR000477 RT_dom
IPR010659 RVT_connect
IPR010661 RVT_thumb
IPR001878 Znf_CCHC
IPR036875 Znf_CCHC_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00540 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

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00234 HIV1MATRIX

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00343 ZnF_C2HC, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF46919 SSF46919, 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

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50175 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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

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

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

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by ribosomal frameshifting. AlignAdd to basket
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) [UniParc]FASTAAdd to basket

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.

« Hide
        10         20         30         40         50
MGARASVLSG GELDRWEKIR LRPGGKKKYK LKHIVWASRE LERFAVNPGL
60 70 80 90 100
LETSEGCRQI LGQLQPSLQT GSEELRSLYN TVATLYCVHQ RIEIKDTKEA
110 120 130 140 150
LDKIEEEQNK SKKKAQQAAA DTGHSNQVSQ NYPIVQNIQG QMVHQAISPR
160 170 180 190 200
TLNAWVKVVE EKAFSPEVIP MFSALSEGAT PQDLNTMLNT VGGHQAAMQM
210 220 230 240 250
LKETINEEAA EWDRVHPVHA GPIAPGQMRE PRGSDIAGTT STLQEQIGWM
260 270 280 290 300
TNNPPIPVGE IYKRWIILGL NKIVRMYSPT SILDIRQGPK EPFRDYVDRF
310 320 330 340 350
YKTLRAEQAS QEVKNWMTET LLVQNANPDC KTILKALGPA ATLEEMMTAC
360 370 380 390 400
QGVGGPGHKA RVLAEAMSQV TNSATIMMQR GNFRNQRKIV KCFNCGKEGH
410 420 430 440 450
TARNCRAPRK KGCWKCGKEG HQMKDCTERQ ANFLREDLAF LQGKAREFSS
460 470 480 490 500
EQTRANSPTR RELQVWGRDN NSPSEAGADR QGTVSFNFPQ VTLWQRPLVT
510 520 530 540 550
IKIGGQLKEA LLDTGADDTV LEEMSLPGRW KPKMIGGIGG FIKVRQYDQI
560 570 580 590 600
LIEICGHKAI GTVLVGPTPV NIIGRNLLTQ IGCTLNFPIS PIETVPVKLK
610 620 630 640 650
PGMDGPKVKQ WPLTEEKIKA LVEICTEMEK EGKISKIGPE NPYNTPVFAI
660 670 680 690 700
KKKDSTKWRK LVDFRELNKR TQDFWEVQLG IPHPAGLKKK KSVTVLDVGD
710 720 730 740 750
AYFSVPLDED FRKYTAFTIP SINNETPGIR YQYNVLPQGW KGSPAIFQSS
760 770 780 790 800
MTKILEPFRK QNPDIVIYQY MDDLYVGSDL EIGQHRTKIE ELRQHLLRWG
810 820 830 840 850
LTTPDKKHQK EPPFLWMGYE LHPDKWTVQP IVLPEKDSWT VNDIQKLVGK
860 870 880 890 900
LNWASQIYPG IKVRQLCKLL RGTKALTEVI PLTEEAELEL AENREILKEP
910 920 930 940 950
VHGVYYDPSK DLIAEIQKQG QGQWTYQIYQ EPFKNLKTGK YARMRGAHTN
960 970 980 990 1000
DVKQLTEAVQ KITTESIVIW GKTPKFKLPI QKETWETWWT EYWQATWIPE
1010 1020 1030 1040 1050
WEFVNTPPLV KLWYQLEKEP IVGAETFYVD GAANRETKLG KAGYVTNRGR
1060 1070 1080 1090 1100
QKVVTLTDTT NQKTELQAIY LALQDSGLEV NIVTDSQYAL GIIQAQPDQS
1110 1120 1130 1140 1150
ESELVNQIIE QLIKKEKVYL AWVPAHKGIG GNEQVDKLVS AGIRKVLFLD
1160 1170 1180 1190 1200
GIDKAQDEHE KYHSNWRAMA SDFNLPPVVA KEIVASCDKC QLKGEAMHGQ
1210 1220 1230 1240 1250
VDCSPGIWQL DCTHLEGKVI LVAVHVASGY IEAEVIPAET GQETAYFLLK
1260 1270 1280 1290 1300
LAGRWPVKTI HTDNGSNFTG ATVRAACWWA GIKQEFGIPY NPQSQGVVES
1310 1320 1330 1340 1350
MNKELKKIIG QVRDQAEHLK TAVQMAVFIH NFKRKGGIGG YSAGERIVDI
1360 1370 1380 1390 1400
IATDIQTKEL QKQITKIQNF RVYYRDSRNP LWKGPAKLLW KGEGAVVIQD
1410 1420 1430
NSDIKVVPRR KAKIIRDYGK QMAGDDCVAS RQDED
Note: Produced by -1 ribosomal frameshifting.
Length:1,435
Mass (Da):162,042
Last modified:January 23, 2007 - v4
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i8487B36BDEAC5FE4
GO
Isoform Gag polyprotein (identifier: P04591-1) [UniParc]FASTAAdd to basket
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.
Length:500
Mass (Da):55,930
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti496R → K Confers to resistance to A-77003; when associated with other amino acid changes. 1
Natural varianti496R → Q Confers to resistance to A-77003. 1
Natural varianti498L → F Confers resistance to amprenavir, atazanavir, lopinavir; when associated with other amino acid changes. 1
Natural varianti498L → I Confers resistance to indinavir, lopinavir, ritonavir and saquinavir; when associated with other amino acid changes. 1
Natural varianti498L → R Confers resistance to indinavir and lopinavir; when associated with other amino acid changes. 1
Natural varianti498L → V Confers resistance to indinavir and lopinavir; when associated with other amino acid changes. 1
Natural varianti498L → Y Confers resistance to atazanavir; when associated with other amino acid changes. 1
Natural varianti503I → V Confers resistance to tipranavir. 1
Natural varianti504G → E Confers resistance to lopinavir, ritonavir and saquinavir; when associated with other amino acid changes. 1
Natural varianti508K → I Confers resistance to lopinavir. 1
Natural varianti508K → M Confers resistance to indinavir, lopinavir and nelfinavir; when associated with other amino acid changes. 1
Natural varianti508K → R Confers resistance to indinavir, lopinavir and ritonavir; when associated with other amino acid changes. 1
Natural varianti511L → I Confers resistance to BILA 2185 BS. 1
Natural varianti512L → I Confers resistance to amprenavir, indinavir, lopinavir, ritonavir and saquinavir; when associated with other amino acid changes. 1
Natural varianti518D → N Confers resistance to nelfinavir; when associated with other amino acid changes. 1
Natural varianti520V → I Confers resistance to A-77003, amprenavir, atazanavir, indinavir, kynostatin, lopinavir, ritonavir and saquinavir; when associated with other amino acid changes. 1
Natural varianti521L → F Confers resistance to atazanavir nelfinavir and ritonavir; when associated with other amino acid changes. 1
Natural varianti522E → Q Confers resistance to lopinavir; when associated with other amino acid changes. 1
Natural varianti523E → D Confers resistance to tipranavir. 1
Natural varianti524M → I Confers resistance to nelfinavir and ritonavir; when associated with other amino acid changes. 1
Natural varianti524M → L Confers resistance to ritonavir; when associated with other amino acid changes. 1
Natural varianti525S → D Confers resistance to indinavir and tipranavir; when associated with other amino acid changes. 1
Natural varianti529R → K Confers resistance to tipranavir. 1
Natural varianti533K → I Confers resistance to DMD-323; when associated with other amino acid changes. 1
Natural varianti534M → F Confers resistance to A-77003. 1
Natural varianti534M → I Confers resistance to A-77003, amprenavir, atazanavir, indinavir, kynostatin, lopinavir, ritonavir, saquinavir and telinavir; when associated with other amino acid changes. 1
Natural varianti534M → L Confers resistance to A-77003, amprenavir, indinavir, lopinavir, ritonavir and saquinavir; when associated with other amino acid changes. 1
Natural varianti535I → V Confers resistance to amprenavir, lopinavir, kynostatin, ritonavir and saquinavir; when associated with other amino acid changes. 1
Natural varianti536G → V Confers resistance to A-77003, amprenavir, indinavir, ritonavir, saquinavir and telinavir; when associated with other amino acid changes. 1
Natural varianti538I → L Confers resistance to atazanavir; when associated with other amino acid changes. 1
Natural varianti538I → V Confers resistance to amprenavir, lopinavir and ritonavir; when associated with other amino acid changes. 1
Natural varianti541F → L Confers resistance to lopinavir and telinavir; when associated with other amino acid changes. 1
Natural varianti541F → Y Confers resistance to indinavir, ritonavir and saquinavir; when associated with other amino acid changes. 1
Natural varianti542I → A Confers resistance to lopinavir. 1
Natural varianti542I → L Confers resistance to amprenavir and lopinavir; when associated with other amino acid changes. 1
Natural varianti542I → M Confers resistance to amprenavir and lopinavir. 1
Natural varianti542I → S Confers resistance to lopinavir. 1
Natural varianti542I → T Confers resistance to lopinavir; when associated with other amino acid changes. 1
Natural varianti542I → V Confers resistance to indinavir, lopinavir, ritonavir and saquinavir; when associated with other amino acid changes. 1
Natural varianti543K → R Confers resistance to nelfinavir. 1
Natural varianti545R → K Confers resistance to nelfinavir. 1
Natural varianti546Q → E Confers resistance to lopinavir and ritonavir; when associated with other amino acid changes. 1
Natural varianti548D → E Confers resistance to tripanavir. 1
Natural varianti549Q → H Confers resistance to lopinavir; when associated with other amino acid changes. 1
Natural varianti551L → P Confers resistance to atazanavir, indinavir, lopinavir, ritonavir and saquinavir; when associated with other amino acid changes. 1
Natural varianti551L → T Confers resistance to lopinavir. 1
Natural varianti553E → Q Confers resistance to lopinavir; when associated with other amino acid changes. 1
Natural varianti554I → F Confers resistance to indinavir, ritonavir and saquinavir; when associated with other amino acid changes. 1
Natural varianti557H → Y Confers resistance to lopinavir; when associated with other amino acid changes. 1
Natural varianti559A → I Confers resistance to lopinavir; when associated with other amino acid changes. 1
Natural varianti559A → L Confers resistance to lopinavir; when associated with other amino acid changes. 1
Natural varianti559A → T Confers resistance to A-77003, indinavir, lopinavir, nelfinavir and tripanavir; when associated with other amino acid changes. 1
Natural varianti559A → V Confers resistance to amprenavir, atazanavir, indinavir, kynostatin, lopinavir, nelfinavir, ritonavir, saquinavir and telinavir; when associated with other amino acid changes. 1
Natural varianti561G → S Confers resistance to indinavir, nelfinavir, ritonavir and saquinavir; when associated with other amino acid changes. 1
Natural varianti565V → I Confers resistance to indinavir, nelfinavir, ritonavir and saquinavir; when associated with other amino acid changes. 1
Natural varianti570V → A Confers resistance to A-77003, indinavir, lopinavir, nelfinavir, ritonavir and saquinavir; when associated with other amino acid changes. 1
Natural varianti570V → F Confers resistance to lopinavir and ritonavir; when associated with other amino acid changes. 1
Natural varianti570V → I Confers resistance to A-77003 and kynostatin; when associated with other amino acid changes. 1
Natural varianti570V → S Confers resistance to lopinavir and ritonavir. 1
Natural varianti570V → T Confers resistance to indinavir, lopinavir, ritonavir and saquinavir; when associated with other amino acid changes. 1
Natural varianti572I → A Confers resistance to atazanavir, indinavir, lopinavir, nelfinavir, ritonavir and saquinavir; when associated with other amino acid changes. 1
Natural varianti572I → V Confers resistance to amprenavir, atazanavir, indinavir, kynostatin, lopinavir, nelfinavir, ritonavir, saquinavir and telinavir; when associated with other amino acid changes. 1
Natural varianti576N → D Confers resistance to nelfinavir; when associated with other amino acid changes. 1
Natural varianti576N → S Confers resistance to atazanavir, indinavir and nelfinavir; when associated with other amino acid changes. 1
Natural varianti577L → M Confers resistance to atazanavir; when associated with other amino acid changes. 1
Natural varianti578L → M Confers resistance to indinavir, lopinavir, nelfinavir, ritonavir and saquinavir; when associated with other amino acid changes. 1
Natural varianti579T → S Confers resistance to lopinavir, ritonavir and saquinavir; when associated with other amino acid changes. 1
Natural varianti581I → L Confers resistance to indinavir. 1
Natural varianti628M → L Confers resistance to zidovudine; when associated with other amino acid changes. 1
Natural varianti631E → A Confers resistance to lamivudine. 1
Natural varianti631E → D Confers resistance to zidovudine; when associated with other amino acid changes. 1
Natural varianti639P → R Confers resistance to stavudine. 1
Natural varianti641N → D Confers resistance to stavudine. 1
Natural varianti649A → V Confers multi-NRTI resistance; when associated with other amino acid changes. 1
Natural varianti652K → R Confers resistance to abacavir, adefovir, didenosine, lamivudine, stavudine, tenofir and zidovuline; when associated with other amino acid changes. 1
Natural varianti654D → A Confers resistance to zidovudine. 1
Natural varianti654D → E Confers multi-NRTI resistance. 1
Natural varianti654D → G Confers multi-NRTI resistance. 1
Natural varianti654D → N Confers resistance to zidovudine. 1
Natural varianti654D → S Confers multi-NRTI resistance. 1
Natural varianti655S → G Confers multi-NRTI resistance; when associated with other amino acid changes. 1
Natural varianti655S → N Confers multi-NRTI resistance. 1
Natural varianti655S → Y Confers multi-NRTI resistance. 1
Natural varianti656T → A Confers resistance to lamivudine and stavudine. 1
Natural varianti656T → D Confers resistance to lamivudine, stavudine and rarely to zalcitabine. 1
Natural varianti656T → G Confers resistance to didanosine, zalcitabine and zidovudine. 1
Natural varianti656T → N Confers resistance to lamivudine and stavudine. 1
Natural varianti657K → E Confers resistance to adefovir and lamivudine. 1
Natural varianti657K → R Confers resistance to zidovudine; when associated with other amino acid changes. 1
Natural varianti657K → S Confers resistance to didanosine and stavudine. 1
Natural varianti661L → I Confers resistance to HBY 097. 1
Natural varianti661L → V Confers resistance to abacavir, didanosine, HBY 097 and zalcitabine; when associated with other amino acid changes. 1
Natural varianti662V → I Confers multi-NRTI resistance; when associated with other amino acid changes. 1
Natural varianti662V → L Confers resistance to HBY 097. 1
Natural varianti662V → M Confers resistance to stavudine and zalcitabine. 1
Natural varianti662V → T Confers resistance to d4C, didanosine, stavudine and zalcitabine. 1
Natural varianti664F → L Confers multi-NRTI resistance; when associated with other amino acid changes. 1
Natural varianti675W → G Confers resistance to pyrophosphate analog PFA. 1
Natural varianti675W → S Confers resistance to pyrophosphate analog PFA. 1
Natural varianti676E → G Confers resistance to pyrophosphate analog PFA. 1
Natural varianti676E → K Confers resistance to pyrophosphate analog PFA. 1
Natural varianti679L → I Confers resistance to pyrophosphate analog PFA. 1
Natural varianti687L → I Confers resistance to nevirapine and efavirenz. 1
Natural varianti688K → E Confers resistance to atevirdine, efavirenz, nevirapine and zidovudine. 1
Natural varianti688K → P Confers resistance to TMC125; when associated with E-142. 1
Natural varianti688K → Q Confers resistance to efavirenz; when associated with I-19. 1
Natural varianti690K → E Confers resistance to atevirdine; when associated with other amino acid changes. 1
Natural varianti690K → N Confers resistance to atevirdine, efavirenz, emivirine and nevirapine; when associated with other amino acid changes. 1
Natural varianti690K → R Confers resistance to emivirine and trovirdine; when associated with other D-179 and C-181. 1
Natural varianti693V → A Confers resistance to nevirapine. 1
Natural varianti693V → I Confers resistance to HBY 097. 1
Natural varianti693V → M Confers resistance to delavirdine, efavirenz and nevirapine. 1
Natural varianti695V → I Confers resistance to efavirenz, emivirine, nevirapine and trovirdine; when associated with other amino acid changes. 1
Natural varianti702Y → F Confers resistance to abacavir; when associated with other amino acid changes. 1
Natural varianti703F → Y Confers multi-NRTI resistance; when associated with other amino acid changes. 1
Natural varianti705V → I Confers resistance to zidovudine; when associated with other amino acid changes. 1
Natural varianti706P → S Confers resistance to lodenosine. 1
Natural varianti722I → L Confers resistance to delavirdine, efavirenz and nevirapine; when associated with I-239. 1
Natural varianti722I → M Confers resistance to delavirdine, efavirenz and nevirapine; when associated with I-239. 1
Natural varianti722I → T Confers resistance to delavirdine, efavirenz and nevirapine; when associated with I-239. 1
Natural varianti725E → K Confers resistance to emivirine. 1
Natural varianti732Q → M Confers both multi-NRTI and multi-NNRTI resistance. 1
Natural varianti738Q → M Confers multi-NRTI resistance; when associated with other amino acid changes. 1
Natural varianti743S → A Confers resistance to pyrophosphate analog PFA. 1
Natural varianti744P → S Confers resistance to lamivudine. 1
Natural varianti748Q → L Confers resistance to pyrophosphate analog PFA. 1
Natural varianti766V → D Confers resistance to efavirenz, tivirapine and trovirdine; when associated with other amino acid changes. 1
Natural varianti768Y → C Confers multi-NNRTI resistance. 1
Natural varianti771M → I Confers resistance to lamivudine and emtricitabine. 1
Natural varianti771M → T Confers resistance to abacavir, didanosine, emtricitabine, lamivudine and zalcitabine. 1
Natural varianti771M → V Confers resistance to lamivudine. 1
Natural varianti775Y → C Confers resistance to nevirapine. 1
Natural varianti775Y → H Confers resistance to atevirdine, efavirenz, loviride and zidovudine. 1
Natural varianti775Y → L Confers resistance to efavirenz. 1
Natural varianti776V → I Confers resistance to HBY 097. 1
Natural varianti777G → A Confers resistance to efavirenz and nevirapine. 1
Natural varianti777G → C Confers resistance to efavirenz and nevirapine. 1
Natural varianti777G → E Confers resistance to efavirenz, nevirapine and quinoxaline. 1
Natural varianti777G → Q Confers resistance to efavirenz, HBY 097 and nevirapine. 1
Natural varianti777G → S Confers resistance to efavirenz and nevirapine. 1
Natural varianti777G → T Confers resistance to efavirenz, HBY 097 and nevirapine. 1
Natural varianti777G → V Confers resistance to efavirenz and nevirapine. 1
Natural varianti795H → Y Confers resistance to lamivudine, pyrophosphate analog PFA and zidovudine. 1
Natural varianti797L → W Confers resistance to zidovudine. 1
Natural varianti798R → K Confers resistance to lamivudine and zidovudine. 1
Natural varianti801L → F Confers resistance to ph-AZT and zidovudine. 1
Natural varianti802T → F Confers resistance to zidovudine; when associated with other amino acid changes. 1
Natural varianti802T → Y Confers resistance to zidovudine; when associated with other amino acid changes. 1
Natural varianti806K → E Confers resistance to zidovudine. 1
Natural varianti806K → Q Confers resistance to zidovudine; when associated with other amino acid changes. 1
Natural varianti806K → R Confers resistance to lamivudine, stavudine, zalcicabine and zidovudine. 1
Natural varianti812P → H Confers resistance to efavirenz, emivirine, HBY 097 and quinoxaline; when associated with A-17. 1
Natural varianti823P → L Confers resistance to atevirdine and delavirdine. 1
Natural varianti825K → T Confers resistance to atevirdine and zidovudine; when associated with other amino acid changes. 1
Natural varianti870L → I Confers resistance to delavirdine, efavirenz and nevirapine. 1
Natural varianti905Y → F Confers resistance to delavirdine and nevirapine. 1
Natural varianti920G → D Confers resistance to abacavir, lamivudine and zidovudine. 1
Natural varianti920G → E Confers resistance to abacavir, lamivudine and zidovudine. 1
Natural varianti973T → I Confers resistance to abacavir, lamivudine and zidovudine. 1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
K03455 Genomic RNA Translation: AAB50259.1 Sequence problems.
AF033819 Genomic RNA Translation: AAC82598.2 Sequence problems.

NCBI Reference Sequences

More...
RefSeqi
NP_057849.4, NC_001802.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
155348

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
vg:155348

Keywords - Coding sequence diversityi

Ribosomal frameshifting

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

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

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

HIV drug resistance mutations
hivdb

HIV drug resistance database

BioAfrica HIV proteomics resource

Pol entry

BioAfrica HIV proteomics resource

RT (p51) entry

BioAfrica HIV proteomics resource

RNase H (p15) entry

BioAfrica HIV proteomics resource

PR (p15) entry

BioAfrica HIV proteomics resource

IN (p31) entry

BioAfrica: HIV bioinformatics in Africa

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K03455 Genomic RNA Translation: AAB50259.1 Sequence problems.
AF033819 Genomic RNA Translation: AAC82598.2 Sequence problems.
RefSeqiNP_057849.4, NC_001802.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
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-ray2.70A588-1147[»]
B588-1027[»]
1C0UX-ray2.52A588-1147[»]
B588-1027[»]
1C1BX-ray2.50A588-1147[»]
B588-1428[»]
1C1CX-ray2.50A588-1147[»]
B588-1027[»]
1DMPX-ray2.00A/B489-587[»]
1DTQX-ray2.80A588-1147[»]
B588-1027[»]
1DTTX-ray3.00A588-1147[»]
B588-1027[»]
1E6JX-ray3.00P143-352[»]
1EP4X-ray2.50A588-1147[»]
B588-1027[»]
1ESKNMR-A390-430[»]
1EX4X-ray2.80A/B1199-1435[»]
1EXQX-ray1.60A/B1203-1356[»]
1FB7X-ray2.60A489-587[»]
1FK9X-ray2.50A588-1130[»]
B588-1027[»]
1FKOX-ray2.90A588-1130[»]
B588-1027[»]
1FKPX-ray2.90A588-1130[»]
B588-1027[»]
1G6LX-ray1.90A484-587[»]
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-ray3.00A588-1147[»]
B588-1027[»]
1KLMX-ray2.65A588-1147[»]
B588-1027[»]
1LV1X-ray2.10A484-587[»]
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-ray2.20A588-1147[»]
B588-1027[»]
1RTIX-ray3.00A588-1147[»]
B588-1027[»]
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-ray2.80A588-1147[»]
B588-1027[»]
1VRTX-ray2.20A588-1147[»]
B588-1027[»]
1VRUX-ray2.40A588-1147[»]
B588-1027[»]
2HNDX-ray2.50A591-1124[»]
2HNYX-ray2.50A591-1124[»]
2HNZX-ray3.00A591-1124[»]
B594-1015[»]
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-ray2.00A484-587[»]
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-ray1.65A484-587[»]
3KT5X-ray1.80A484-587[»]
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[»]
3N3IX-ray2.50A484-587[»]
3NBPX-ray2.95A588-1148[»]
B588-1027[»]
3PHVX-ray2.70A489-587[»]
3QINX-ray1.70A1014-1103[»]
A1142-1148[»]
3QIOX-ray1.40A1014-1148[»]
3QIPX-ray2.09A588-1147[»]
B588-1027[»]
3T19X-ray2.60A/B588-1147[»]
3T1AX-ray2.40A/B588-1147[»]
3TAMX-ray2.51A590-1147[»]
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[»]
4KSEX-ray2.68B588-1017[»]
4KV8X-ray2.30A588-1147[»]
B588-1027[»]
4NCGX-ray2.58A588-1147[»]
B585-1027[»]
4Q1WX-ray1.85A/B496-587[»]
4Q1XX-ray1.90A/B496-587[»]
4Q1YX-ray1.50A/B496-587[»]
4Q5MX-ray1.79A484-587[»]
4QLHX-ray2.45A489-592[»]
4U1HX-ray1.59C180-188[»]
4U1IX-ray1.92C180-188[»]
4U1JX-ray1.38C180-188[»]
4U7QX-ray1.70A/B496-587[»]
4U7VX-ray1.38A/B496-587[»]
5DGUX-ray1.22A/B496-587[»]
5DGWX-ray1.62A/B496-587[»]
5EU7X-ray2.64A/B1204-1356[»]
5HRNX-ray1.75A1197-1359[»]
5HRPX-ray1.81A1197-1359[»]
5HRRX-ray1.88A1197-1359[»]
5HRSX-ray1.86A1197-1359[»]
5IM7X-ray2.50E/F308-316[»]
5J2MX-ray2.43A588-1147[»]
B588-1027[»]
5J2NX-ray2.90A588-1147[»]
B588-1027[»]
5J2PX-ray2.53A588-1147[»]
B588-1027[»]
5J2QX-ray2.79A588-1147[»]
B588-1027[»]
5K14X-ray2.40A588-1147[»]
5KAOX-ray1.80A/B489-587[»]
5T82NMR-A824-905[»]
5TC2X-ray1.84A/B1366-1420[»]
5VZ6X-ray2.60A585-1147[»]
B585-1027[»]
5XOSX-ray1.70C880-888[»]
5XOTX-ray2.79C880-888[»]
5YRSX-ray1.76A/B489-587[»]
6BSGX-ray2.44A588-1144[»]
B588-1027[»]
6BSHX-ray2.65A588-1144[»]
B588-1027[»]
6BSIX-ray3.25A588-1144[»]
B588-1027[»]
6BSJX-ray2.89A588-1144[»]
B588-1027[»]
ProteinModelPortaliP04585
SMRiP04585
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1205538, 127 interactors
IntActiP04585, 6 interactors
MINTiP04585

Chemistry databases

BindingDBiP04585
ChEMBLiCHEMBL3638360
DrugBankiDB07892 1-(2-HYDROXYETHYLOXYMETHYL)-6-PHENYL THIOTHYMINE
DB08372 1-[2-(4-ETHOXY-3-FLUOROPYRIDIN-2-YL)ETHYL]-3-(5-METHYLPYRIDIN-2-YL)THIOUREA
DB08681 1-METHYL ETHYL 2-CHLORO-5-[[[(1-METHYLETHOXY)THIOOXO]METHYL]AMINO]-BENZOATE
DB07826 2-[4-chloro-2-(phenylcarbonyl)phenoxy]-N-phenylacetamide
DB08679 2-METHYL-FURAN-3-CARBOTHIOIC ACID [4-CHLORO-3-(3-METHYL-BUT-2-ENYLOXY)-PHENYL]-AMIDE
DB08154 3-chloro-5-[2-chloro-5-(1H-indazol-3-ylmethoxy)phenoxy]benzonitrile
DB07864 4-[(CYCLOPROPYLETHYNYL)OXY]-6-FLUORO-3-ISOPROPYLQUINOLIN-2(1H)-ONE
DB08211 5-bromo-3-(pyrrolidin-1-ylsulfonyl)-1H-indole-2-carboxamide
DB08379 6-(4-chloro-2-fluoro-3-phenoxybenzyl)pyridazin-3(2H)-one
DB08634 6-BENZYL-1-BENZYLOXYMETHYL-5-ISOPROPYL URACIL
DB08188 6-BENZYL-1-ETHOXYMETHYL-5-ISOPROPYL URACIL
DB07871 6-CHLORO-4-(CYCLOHEXYLOXY)-3-ISOPROPYLQUINOLIN-2(1H)-ONE
DB07867 6-CHLORO-4-(CYCLOHEXYLOXY)-3-PROPYLQUINOLIN-2(1H)-ONE
DB07868 6-CHLORO-4-(CYCLOHEXYLSULFANYL)-3-PROPYLQUINOLIN-2(1H)-ONE
DB07869 6-CHLORO-4-(CYCLOHEXYLSULFINYL)-3-PROPYLQUINOLIN-2(1H)-ONE
DB06581 Bevirimat
DB02102 DMP450
DB04609 INHIBITOR Q8467 OF DUPONT MERCK
DB08680 N-[4-CLORO-3-(T-BUTYLOXOME)PHENYL-2-METHYL-3-FURAN-CARBOTHIAMIDE
DB07797 N-[[3-FLUORO-4-ETHOXY-PYRID-2-YL]ETHYL]-N'-[5-CHLORO-PYRIDYL]-THIOUREA
DB07781 N-[[3-FLUORO-4-ETHOXY-PYRID-2-YL]ETHYL]-N'-[5-NITRILOMETHYL-PYRIDYL]-THIOUREA
DB08286 NAPHTHYLOXYACETIC ACID
DB07910 PHENYLALANINDIOL
DB02729 SD146
DB05328 VGV-1
DB02702 XV638

Proteomic databases

PRIDEiP04585

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi155348
KEGGivg:155348

Phylogenomic databases

OrthoDBiVOG09000135

Enzyme and pathway databases

BRENDAi2.7.7.49 2676
3.4.23.16 2676
ReactomeiR-HSA-162585 Uncoating of the HIV Virion
R-HSA-162588 Budding and maturation of HIV virion
R-HSA-162592 Integration of provirus
R-HSA-162594 Early Phase of HIV Life Cycle
R-HSA-164516 Minus-strand DNA synthesis
R-HSA-164525 Plus-strand DNA synthesis
R-HSA-164843 2-LTR circle formation
R-HSA-173107 Binding and entry of HIV virion
R-HSA-175474 Assembly Of The HIV Virion
R-HSA-175567 Integration of viral DNA into host genomic DNA
R-HSA-177539 Autointegration results in viral DNA circles
R-HSA-180689 APOBEC3G mediated resistance to HIV-1 infection
R-HSA-180910 Vpr-mediated nuclear import of PICs
SABIO-RKiP04585

Miscellaneous databases

EvolutionaryTraceiP04585

Protein Ontology

More...
PROi
PR:P04585

Family and domain databases

CDDicd05482 HIV_retropepsin_like, 1 hit
Gene3Di1.10.10.200, 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
InterProiView protein in InterPro
IPR001969 Aspartic_peptidase_AS
IPR000721 Gag_p24
IPR017856 Integrase-like_N
IPR036862 Integrase_C_dom_sf_retrovir
IPR001037 Integrase_C_retrovir
IPR001584 Integrase_cat-core
IPR003308 Integrase_Zn-bd_dom_N
IPR000071 Lentvrl_matrix_N
IPR012344 Matrix_HIV/RSV_N
IPR001995 Peptidase_A2_cat
IPR021109 Peptidase_aspartic_dom_sf
IPR034170 Retropepsin-like_cat_dom
IPR018061 Retropepsins
IPR008916 Retrov_capsid_C
IPR008919 Retrov_capsid_N
IPR010999 Retrovr_matrix
IPR012337 RNaseH-like_sf
IPR002156 RNaseH_domain
IPR036397 RNaseH_sf
IPR000477 RT_dom
IPR010659 RVT_connect
IPR010661 RVT_thumb
IPR001878 Znf_CCHC
IPR036875 Znf_CCHC_sf
PfamiView protein in Pfam
PF00540 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
PRINTSiPR00234 HIV1MATRIX
SMARTiView protein in SMART
SM00343 ZnF_C2HC, 2 hits
SUPFAMiSSF46919 SSF46919, 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
PROSITEiView protein in PROSITE
PS50175 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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPOL_HV1H2
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P04585
Secondary accession number(s): O09777, Q9WJC5
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: December 5, 2018
This is version 227 of the entry and version 4 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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